



@article {3295,
	title = {Adsorbed fibrinogen enhances production of bone- and angiogenic-related factors by monocytes/macrophages},
	journal = {Tissue Engineering - Part A},
	volume = {20},
	year = {2014},
	note = {Cited By (since 1996):1Export Date: 21 November 2014},
	month = {2014},
	pages = {250 - 263},
	abstract = {Macrophages are phagocytic cells with great importance in guiding multiple stages of inflammation and tissue repair. By producing a large number of biologically active molecules, they can affect the behavior of other cells and events, such as the foreign body response and angiogenesis. Since protein adsorption to biomaterials is crucial for the inflammatory process, we addressed the ability of the pro-inflammatory molecule fibrinogen (Fg) to modulate macrophage behavior toward tissue repair/regeneration. For this purpose, we used chitosan (Ch) as a substrate for Fg adsorption. Freshly isolated human monocytes were seeded on Ch substrates alone or previously adsorbed with Fg, and allowed to differentiate into macrophages for 10 days. Cell adhesion and morphology, formation of foreign body giant cells (FBGC), and secretion of a total of 80 cytokines and growth factors were evaluated. Both substrates showed similar numbers of adherent macrophages along differentiation as compared with RGD-coated surfaces, which were used as positive controls. Fg did not potentiate FBGC formation. In addition, actin cytoskeleton staining revealed the presence of punctuate F-actin with more elongated and interconnecting cells on Ch substrates. Antibody array screening and quantification of inflammation- and wound-healing-related factors indicated an overall reduction in Ch-based substrates versus RGD-coated surfaces. At late times, most inflammatory agents were down-regulated in the presence of Fg, in contrast to growth factor production, which was stimulated by Fg. Importantly, on Ch+Fg substrates, fully differentiated macrophages produced significant amounts of macrophage inflammatory protein-1delta (MIP-1δ), platelet-derived growth factor-BB, bone morphogenetic protein (BMP)-5, and BMP-7 compared with Ch alone. In addition, other important factors involved in bone homeostasis and wound healing, such as growth hormone, transforming growth factor-β3, and insulin-like growth factor-binding proteins, as well as several angiogenic mediators, including endocrine gland-derived vascular endothelial factor, fibroblast growth factor-7, and placental growth factor, were significantly promoted by Fg. This work provides a new perspective on the inflammatory response in the context of bone repair/regeneration mediated by a pro-inflammatory protein (Fg) adsorbed onto a biomaterial (Ch) that does not otherwise exhibit osteogenic properties. {\textcopyright} Copyright 2014, Mary Ann Liebert, Inc.},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84891526984\&partnerID=40\&md5=bf455ae8d2df37fe5c29d41156c8096a},
	author = {Maciel, J. and Oliveira, M.I. and Colton, E. and McNally, A.K. and Oliveira, C. and Anderson, J.M. and Barbosa, M.A.}
}
@article {3311,
	title = {The effect of hyaluronan-based delivery of stromal cell-derived factor-1 on the recruitment of MSCs in degenerating intervertebral discs},
	journal = {Biomaterials},
	volume = {35},
	year = {2014},
	note = {Export Date: 21 November 2014},
	month = {2014},
	pages = {8144 - 8153},
	abstract = {Intervertebral disc (IVD) degeneration is the leading cause of low back pain and disability in the active population. Transplantation of mesenchymal stem cells (MSCs) in a hydrogel carrier can induce regenerative effects in degenerated IVDs. Moreover, it was found that degenerative discs release chemoattractants effective in MSC recruitment. Based on these findings, we hypothesized that an injectable hydrogel that can enhance the number of migrated MSCs in the IVD and provide a suitable matrix for their survival and differentiation would be ideal. The purpose of this study was to evaluate the potential of a thermoreversible hyaluronan-poly(N-isopropylacrylamide) (HAP) hydrogel as chemoattractant delivery system to recruit human MSCs in degenerative IVDs. The results demonstrate that HAP hydrogels containing stromal cell derived factor-1 (SDF-1) significantly increased the number of MSCs migrating into nucleotomized discs compared with discs treated with only HAP or SDF-1 in solution. HAP hydrogels releasing SDF-1 enhanced both the number of recruited cells and their migration distance in the IVD tissue. Furthermore, this phenomenon was dependent on MSC donor age. In conclusion, HAP SDF-1 is effective for the recruitment of stem cells in the IVD, thus opening new possibilities for the development of regenerative therapies based on endogenous cell migration. {\textcopyright} 2014 Elsevier Ltd.},
	keywords = {Intervertebral disc, Mesenchymal Stem Cells, Recruitment, Stromal cell derived factor-1, Thermoreversible hyaluronan hydrogel},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84903746142\&partnerID=40\&md5=1366ab2e3399d0a363aab2e356bbdf96},
	author = {Pereira, C.L. and Gon{\c c}alves, R.M. and Peroglio, M. and Pattappa, G. and D{\textquoteright}Este, M. and Eglin, D. and Barbosa, M.A. and Alini, M. and Grad, S.}
}
@booklet {3260,
	title = {Impact of 3-D printed PLA- and chitosan-based scaffolds on human monocyte/macrophage responses: Unraveling the effect of 3-D structures on inflammation},
	howpublished = {Acta Biomaterialia},
	volume = {10},
	year = {2014},
	note = {Cited By (since 1996):2Export Date: 21 November 2014},
	month = {2014},
	pages = {613 - 622},
	abstract = {Recent studies have pointed towards a decisive role of inflammation in triggering tissue repair and regeneration, while at the same time it is accepted that an exacerbated inflammatory response may lead to rejection of an implant. Within this context, understanding and having the capacity to regulate the inflammatory response elicited by 3-D scaffolds aimed for tissue regeneration is crucial. This work reports on the analysis of the cytokine profile of human monocytes/macrophages in contact with biodegradable 3-D scaffolds with different surface properties, architecture and controlled pore geometry, fabricated by 3-D printing technology. Fabrication processes were optimized to create four different 3-D platforms based on polylactic acid (PLA), PLA/calcium phosphate glass or chitosan. Cytokine secretion and cell morphology of human peripheral blood monocytes allowed to differentiate on the different matrices were analyzed. While all scaffolds supported monocyte/macrophage adhesion and stimulated cytokine production, striking differences between PLA-based and chitosan scaffolds were found, with chitosan eliciting increased secretion of tumor necrosis factor (TNF)-α, while PLA-based scaffolds induced higher production of interleukin (IL)-6, IL-12/23 and IL-10. Even though the material itself induced the biggest differences, the scaffold geometry also impacted on TNF-α and IL-12/23 production, with chitosan scaffolds having larger pores and wider angles leading to a higher secretion of these pro-inflammatory cytokines. These findings strengthen the appropriateness of these 3-D platforms to study modulation of macrophage responses by specific parameters (chemistry, topography, scaffold architecture). {\textcopyright} 2013 Acta Materialia Inc.},
	keywords = {3-D scaffolds, Human macrophages, Inflammation, Rapid prototyping, Tissue engineering},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84896505907\&partnerID=40\&md5=948f87b684be751bc6eb444e28ce6025},
	author = {Almeida, C.R. and Serra, T. and Oliveira, M.I. and Planell, J.A. and Barbosa, M.A. and Navarro, M.}
}
@article {3270,
	title = {Macrophages stimulate gastric and colorectal cancer invasion through EGFR Y 1086, c-Src, Erk1/2 and Akt phosphorylation and smallGTPase activity},
	journal = {Oncogene},
	volume = {33},
	year = {2014},
	note = {Cited By (since 1996):2Export Date: 21 November 2014},
	month = {2014},
	pages = {2123 - 2133},
	abstract = {The interactions between cancer cells and their microenvironment are crucial for malignant progression, as they modulate invasion-related activities. Tumor-associated macrophages are generally considered allies in the process of tumor progression in several types of cancer, although their role on gastric and colorectal carcinomas is still poorly understood. In this report, we studied the influence of primary human macrophages on gastric and colorectal cancer cells, considering invasion, motility/migration, proteolysis and activated intracellular signaling pathways. We demonstrated that macrophages stimulate cancer cell invasion, motility and migration, and that these effects depend on matrix metalloproteinase (MMP) activity and on the activation of epidermal growth factor receptor (EGFR) (at the residue Y 1086), PLC-γ (phospholipase C-gamma) and Gab1 (GRB2-associated binding protein-1), as evidenced by siRNA (small interference RNA) experiments. Epidermal growth factor (EGF)-immunodepletion impaired macrophage-mediated cancer cell invasion and motility, suggesting that EGF is the pro-invasive and pro-motile factor produced by macrophages. Macrophages also induced gastric and colorectal cancer cell phosphorylation of Akt, c-Src and ERK1/2, and led to an increase of RhoA and Cdc42 activity. Interestingly, whereas macrophage-mediated cancer cell c-Src and ERK1/2 phosphorylation occurred downstream EGFR activation, Akt phosphorylation seems to be a parallel event, taking place in an EGFR-independent manner. The involvement of EGF, EGFR-downstream signaling partners and MMPs in macrophage-mediated invasion provides novel insights into the molecular crosstalk established between cancer cells and macrophages, opening new perspectives for the design of new and more efficient therapeutic strategies to counteract cancer cell invasion. {\textcopyright} 2014 Macmillan Publishers Limited.},
	keywords = {cancer cell invasion, colon cancer, Gastric cancer, invasion-related signaling pathways, Macrophages, tumor microenvironment},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84899425243\&partnerID=40\&md5=beff5192ff42940c75fef8b48ebd3ae7},
	author = {Cardoso, A.P. and Pinto, M.L. and Pinto, A.T. and Oliveira, M.I. and Pinto, M.T. and Gon{\c c}alves, R. and Relvas, J.B. and Figueiredo, C. and Seruca, R. and Mantovani, A. and Mareel, M. and Barbosa, M.A. and Oliveira, M.J.}
}
@article {3291,
	title = {Neonatal human dermal fibroblasts immobilized in RGD-alginate induce angiogenesis},
	journal = {Cell Transplantation},
	volume = {23},
	year = {2014},
	note = {Export Date: 21 November 2014},
	month = {2014},
	pages = {945 - 957},
	abstract = {Promoting angiogenesis in a damaged tissue is a major challenge for tissue regeneration. Recent findings in tissue engineering suggest that fibroblasts (FBs) play an important role in orchestrating the angiogenic process. Fibroblasts maintain the structural integrity of connective tissue by continuously secreting growth factors and extracellular matrix precursors, which are essential for endothelial cell (EC) adhesion and spreading, thus playing a crucial role in angiogenesis. We hypothesized that FBs immobilized in alginate gels grafted with the RGD peptidic sequence could influence the recruitment of ECs to improve vascularization. In this work, the modulation of immobilized human FBs within the 3D synthetic extracellular matrix was assessed. Experiments using cocultures of ECs and FBs in indirect contact as well as angiogenic assays were performed to assess the influence of FBs immobilized in RGD-alginate in ECs{\textquoteright} viability, stabilization, sprouting, and assembly into capillary-like structures. This study demonstrates the ability of FBs immobilized within RGD-alginate microspheres to modulate and support capillary-like structures{\textquoteright} assembly. These findings indicate that the microenvironment created by these stromal cells in the scaffold modulates capillary morphogenesis, thus stimulating angiogenesis in situ and can potentially be used in regenerative medicine in clinical scenarios where vascularization is essential. {\textcopyright} 2014 Cognizant Comm. Corp.},
	keywords = {Alginate, angiogenesis, Endothelial cells (ECs), Fibroblasts (FBs), RGD peptide: Injectable biomaterials},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84905231059\&partnerID=40\&md5=8ca92aea469585cbf168cb6fbad9d3ad},
	author = {Guerreiro, S.G. and Oliveira, M.J. and Barbosa, M.A. and Soares, R. and Granja, P.L.}
}
@article {3277,
	title = {Production, characterization and biocompatibility of marine collagen matrices from an alternative and sustainable source: The sea urchin Paracentrotus lividus},
	journal = {Marine Drugs},
	volume = {12},
	year = {2014},
	note = {Export Date: 21 November 2014},
	month = {2014},
	pages = {4912 - 4933},
	abstract = {Collagen has become a key-molecule in cell culture studies and in the tissue engineering field. Industrially, the principal sources of collagen are calf skin and bones which, however, could be associated to risks of serious disease transmission. In fact, collagen derived from alternative and riskless sources is required, and marine organisms are among the safest and recently exploited ones. Sea urchins possess a circular area of soft tissue surrounding the mouth, the peristomial membrane (PM), mainly composed by mammalian-like collagen. The PM of the edible sea urchin Paracentrotus lividus therefore represents a potential unexploited collagen source, easily obtainable as a food industry waste product. Our results demonstrate that it is possible to extract native collagen fibrils from the PM and produce suitable substrates for in vitro system. The obtained matrices appear as a homogeneous fibrillar network (mean fibril diameter 30-400 nm and < 2 μm) and display remarkable mechanical properties in term of stiffness (146 {\textpm} 48 MPa) and viscosity (60.98 {\textpm} 52.07 GPa{\textperiodcentered}s). In vitro tests with horse pbMSC show a good biocompatibility in terms of overall cell growth. The obtained results indicate that the sea urchin P. lividus can be a valuable low-cost collagen source for mechanically resistant biomedical devices.},
	keywords = {Biocompatibility, Collagen matrix, Mesenchimal stromal cells, Native fibril, Sea urchin collagen, Tissue regeneration},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84908025685\&partnerID=40\&md5=58774d56d0d60e6bc725ae6ecacaa068},
	author = {Di Benedetto, C. and Barbaglio, A. and Martinello, T. and Alongi, V. and Fassini, D. and Cullor{\`a}, E. and Patruno, M. and Bonasoro, F. and Barbosa, M.A. and Carnevali, M.D.C. and Sugni, M.}
}
@article {3285,
	title = {Selective albumin-binding surfaces modified with a thrombin-inhibiting peptide},
	journal = {Acta Biomaterialia},
	volume = {10},
	year = {2014},
	note = {Export Date: 21 November 2014},
	month = {2014},
	pages = {1227 - 1237},
	abstract = {Blood-contacting medical devices have been associated with severe clinical complications, such as thrombus formation, triggered by the activation of the coagulation cascade due to the adsorption of certain plasma proteins on the surface of biomaterials. Hence, the coating of such surfaces with antithrombotic agents has been used to increase biomaterial haemocompatibility. Biomaterial-induced clotting may also be decreased by albumin adsorption from blood plasma in a selective and reversible way, since this protein is not involved in the coagulation cascade. In this context, this paper reports that the immobilization of the thrombin inhibitor D-Phe-Pro-D-Arg-D-Thr-CONH 2 (fPrt) onto nanostructured surfaces induces selective and reversible adsorption of albumin, delaying the clotting time when compared to peptide-free surfaces. fPrt, synthesized with two glycine residues attached to the N-terminus (GGfPrt), was covalently immobilized onto self-assembled monolayers (SAMs) having different ratios of carboxylate-hexa(ethylene glycol)- and tri(ethylene glycol)-terminated thiols (EG6-COOH/EG3) that were specifically designed to control GGfPrt orientation, exposure and density at the molecular level. In solution, GGfPrt was able to inactivate the enzymatic activity of thrombin and to delay plasma clotting time in a concentration-dependent way. After surface immobilization, and independently of its concentration, GGfPrt lost its selectivity to thrombin and its capacity to inhibit thrombin enzymatic activity against the chromogenic substrate n-p-tosyl-Gly-Pro-Arg-p-nitroanilide. Nevertheless, surfaces with low concentrations of GGfPrt could delay the capacity of adsorbed thrombin to cleave fibrinogen. In contrast, GGfPrt immobilized in high concentrations was found to induce the procoagulant activity of the adsorbed thrombin. However, all surfaces containing GGfPrt have a plasma clotting time similar to the negative control (empty polystyrene wells), showing resistance to coagulation, which is explained by its capacity to adsorb albumin in a selective and reversible way. This work opens new perspectives to the improvement of the haemocompatibility of blood-contacting medical devices. {\textcopyright} 2013 Acta Materialia Inc. Published by Elsevier Ltd. All rights reserved.},
	keywords = {Albumin, Blood compatibility, Clotting, Surface modification, Thrombin},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84895067841\&partnerID=40\&md5=8486186625f8f4f1cbc538bb3e34dd82},
	author = {Freitas, S.C. and Maia, S. and Figueiredo, A.C. and Gomes, P. and Pereira, P.J.B. and Barbosa, M.A. and Martins, M.C.L.}
}
@article {2759,
	title = {Adsorbed fibrinogen leads to improved bone regeneration and correlates with differences in the systemic immune response},
	journal = {Acta Biomaterialia},
	volume = {9},
	year = {2013},
	note = {Export Date: 23 May 2013Source: ScopusArticle in Press},
	month = {07/2013},
	pages = {7209-7217},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84876834487\&partnerID=40\&md5=2d00f0bc55f461c9c979548276f0e53d},
	author = {Santos, S.G. and Lamghari, M. and Almeida, C.R. and Oliveira, M.I. and Neves, N. and Ribeiro, A.C. and Barbosa, J.N. and Barros, R. and Maciel, J. and Martins, M.C.L. and Gon{\c c}alves, R.M. and Barbosa, M.A.}
}
@article {2880,
	title = {Endothelialization of chitosan porous conduits via immobilization of a recombinant fibronectin fragment (rhFNIII7-10)},
	journal = {Acta Biomaterialia},
	volume = {9},
	year = {2013},
	note = {Export Date: 12 December 2013Source: Scopus},
	month = {2013///},
	pages = {5643 - 5652},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84873199566\&partnerID=40\&md5=f548695261ada2fc57ece26bff1f45d0},
	author = {Amaral, I.F. and Neiva, I. and Ferreira da Silva, F. and Sousa, S.R. and Piloto, A.M. and Lopes, C.D.F. and Barbosa, M.A. and Kirkpatrick, C.J. and P{\^e}go, A.P.}
}
@article {2776,
	title = {Fibrinogen promotes resorption of chitosan by human osteoclasts},
	journal = {Acta Biomaterialia},
	volume = {9},
	year = {2013},
	note = {Export Date: 23 May 2013Source: ScopusArticle in Press},
	month = {2013///},
	pages = {6553-6562},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84873739793\&partnerID=40\&md5=5114933c69d12bf99e9785aca23b3011},
	author = {Torres, A.L. and Santos, S.G. and Oliveira, M.I. and Barbosa, M.A.}
}
@article {2830,
	title = {Macrophage polarization following chitosan implantation},
	journal = {Biomaterials},
	volume = {34},
	year = {2013},
	note = {Export Date: 12 December 2013Source: Scopus},
	month = {2013///},
	pages = {9952 - 9959},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84885383515\&partnerID=40\&md5=a152c1c59bf410d725b5e4ce4eeed18f},
	author = {Vasconcelos, D.P. and Fonseca, A.C. and Costa, M. and Amaral, I.F. and Barbosa, M.A. and {\'A}guas, A.P. and Barbosa, J.N.}
}
@booklet {2867,
	title = {Macrophages stimulate gastric and colorectal cancer invasion through EGFR Y1086, c-Src, Erk1/2 and Akt phosphorylation and smallGTPase activity},
	howpublished = {Oncogene},
	year = {2013},
	note = {Cited By (since 1996):1Export Date: 12 December 2013Source: ScopusArticle in Press},
	month = {2013///},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84876908646\&partnerID=40\&md5=bcc2929bb93817db3dc0e3421c420722},
	author = {Cardoso, A.P. and Pinto, M.L. and Pinto, A.T. and Oliveira, M.I. and Pinto, M.T. and Gon{\c c}alves, R. and Relvas, J.B. and Figueiredo, C. and Seruca, R. and Mantovani, A. and Mareel, M. and Barbosa, M.A. and Oliveira, M.J.}
}
@article {2847,
	title = {Modulation of stability and mucoadhesive properties of chitosan microspheres for therapeutic gastric application},
	journal = {International Journal of Pharmaceutics},
	volume = {454},
	year = {2013},
	note = {Cited By (since 1996):1Export Date: 12 December 2013Source: Scopus},
	month = {2013///},
	pages = {116 - 124},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84884163785\&partnerID=40\&md5=1d040067777b023c63bb769260b66dcd},
	author = {Fernandes, M. and Gon{\c c}alves, I.C. and Nardecchia, S. and Amaral, I.F. and Barbosa, M.A. and Martins, M.C.L.}
}
@booklet {2190,
	title = {Bioengineered surfaces to improve the blood compatibility of biomaterials through direct thrombin inactivation},
	howpublished = {Acta BiomaterialiaActa Biomater.},
	year = {2012},
	note = {Export Date: 21 November 2012Source: ScopusArticle in Pressdoi: 10.1016/j.actbio.2012.07.020Language of Original Document: EnglishCorrespondence Address: Martins, M.C.L.; INEB - Instituto de Engenharia Biom{\'e}dica, Universidade do Porto, Rua do Campo Alegre 823, 415email: cmartins@ineb.up.pt},
	month = {2012///},
	abstract = {Thrombus formation, due to thrombin generation, is a major problem affecting blood-contacting medical devices. This work aimed to develop a new strategy to improve the hemocompatibility of such devices by the immobilization of a naturally occurring thrombin inhibitor into a nanostructured surface. Boophilin, a direct thrombin inhibitor from the cattle tick Rhipicephalus microplus, was produced as a recombinant protein in Pichia pastoris. Boophilin was biotinylated and immobilized on biotin-terminated self-assembled monolayers (SAM) via neutravidin. In order to maintain its proteinase inhibitory capacity after surface immobilization, boophilin was biotinylated after the formation of a boophilin-thrombin complex to minimize the biotinylation of the residues involved in thrombin-boophilin interaction. The extent of boophilin biotinylation was determined using matrix-assisted laser desorption/ionization-time of flight/time of flight mass spectrometry. Boophilin immobilization and thrombin adsorption were quantified using quartz crystal microbalance with dissipation. Thrombin competitive adsorption from human serum was assessed using                        125I-thrombin. Thrombin inhibition and plasma clotting time were determined using spectrophotometric techniques. Boophilin-coated SAM were able to promote thrombin adsorption in a selective way, inhibiting most of its activity and delaying plasma coagulation in comparison with boophilin-free surfaces, demonstrating boophilin{\textquoteright}s potential to improve the hemocompatibility of biomaterials used in the production of blood-contacting devices. {\textcopyright} 2012 Acta Materialia Inc.
},
	keywords = {Coagulation, Hemocompatibility, Protein adsorption, Surface functionalization, Thrombin},
	isbn = {17427061 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84865246462\&partnerID=40\&md5=278b2e7d1427a6032eba9ecbd01c3872},
	author = {Freitas, S.C. and Cereija, T.B. and Figueiredo, A.C. and Os{\'o}rio, H. and Pereira, P.J.B. and Barbosa, M.A. and Martins, M.C.L.}
}
@article {2203,
	title = {Biosynthesis of highly pure poly-γ-glutamic acid for biomedical applications},
	journal = {Journal of Materials Science: Materials in MedicineJ. Mater. Sci. Mater. Med.},
	volume = {23},
	year = {2012},
	note = {Export Date: 21 November 2012Source: ScopusCODEN: JSMMEdoi: 10.1007/s10856-012-4639-xPubMed ID: 22532096Language of Original Document: EnglishCorrespondence Address: Pereira, C.L.; INEB-Instituto de Engenharia Biom{\'e}dica, Universidade Do Porto, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: Catarina.pereira@ineb.up.ptChemicals/CAS: chitosan, 9012-76-4; glutamic acid, 11070-68-1, 138-15-8, 56-86-0, 6899-05-4; polyglutamic acid, 24991-23-9, 25513-46-6; Biocompatible Materials; Polyglutamic Acid, 25513-46-6; poly(gamma-glutamic acid)References: Ratner, B.D., Hoffman, A.S., Shoen, F.J., Lemons, J.E., (2004) Natural Materials. Biomaterials Science-an Introduction to Materials in Medicine, , 2nd ed. San Diego, CA: Academic Press;Buescher, J.M., Margaritis, A., Microbial biosynthesis of polyglutamic acid biopolymer and applications in the biopharmaceutical, biomedical and food industries (2007) Critical Reviews in Biotechnology, 27 (1), pp. 1-19. , DOI 10.1080/07388550601166458, PII 773236840; 
Kang, H.-S., Park, S.-H., Lee, Y.-G., Son, T.-I., Polyelectrolyte complex hydrogel composed of chitosan and poly(γ-glutamic acid) for biological application: Preparation, physical properties, and cytocompatibility (2007) Journal of Applied Polymer Science, 103 (1), pp. 386-394. , DOI 10.1002/app.24623; 
Lin, Y.-H., Chung, C.-K., Chen, C.-T., Liang, H.-F., Chen, S.-C., Sung, H.-W., Preparation of nanoparticles composed of chitosan/poly-γ-glutamic acid and evaluation of their permeability through Caco-2 cells (2005) Biomacromolecules, 6 (2), pp. 1104-1112. , DOI 10.1021/bm049312a; 
Sanda, F., Fujiyama, T., Endo, T., Chemical synthesis of polygamma-glutamic acid by polycondensation of gamma-glutamic acid dimer: Synthesis and reaction of poly gamma-glutamic acid methyl ester (2000) J Polym Sci, Part A: Polym Chem, 39, pp. 732-741; 
Ashiuchi, M., Shimanouchi, K., Nakamura, H., Kamei, T., Soda, K., Park, C., Sung, M.-H., Misono, H., Enzymatic synthesis of high-molecular-mass poly-γ-glutamate and regulation of its stereochemistry (2004) Applied and Environmental Microbiology, 70 (7), pp. 4249-4255. , DOI 10.1128/AEM.70.7.4249-4255.2004; 
Shih, I.-L., Van, Y.-T., The production of poly-(γ-glutamic acid) from microorganisms and its various applications (2001) Bioresource Technology, 79 (3), pp. 207-225. , DOI 10.1016/S0960-8524(01)00074-8, PII S0960852401000748; 
Prodhomme, E.J.F., Tutt, A.L., Glennie, M.J., Bugg, T.D.H., Multivalent Conjugates of Poly-γ-D-glutamic Acid from Bacillus licheniformis with Antibody F(ab{\textquoteright}) and Glycopeptide Ligands (2003) Bioconjugate Chemistry, 14 (6), pp. 1148-1155. , DOI 10.1021/bc020019m; 
Schneerson, R., Kubler-Kielb, J., Liu, T.-Y., Dai, Z.-D., Leppla, S.H., Yergey, A., Backlund, P., Robbins, J.B., Poly(γ-D-glutamic acid) protein conjugates induce IgG antibodies in mice to the capsule of Bacillus anthracis: A potential addition to the anthrax vaccine (2003) Proceedings of the National Academy of Sciences of the United States of America, 100 (15), pp. 8945-8950. , DOI 10.1073/pnas.1633512100; 
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Sung, M.-H., Park, C., Kim, C.-J., Poo, H., Soda, K., Ashiuchi, M., Natural and edible biopolymer poly-γ-glutamic acid: Synthesis, production, and applications (2005) Chemical Record, 5 (6), pp. 352-366. , DOI 10.1002/tcr.20061; 
Kunioka, M., Biosynthesis and chemical reactions of poly(amino acid)s from microorganisms (1997) Applied Microbiology and Biotechnology, 47 (5), pp. 469-475. , DOI 10.1007/s002530050958; 
Ashiuchi, M., Soda, K., Misono, H., A poly-γ-glutamate synthetic system of Bacillus subtilis IFO 3336: Gene cloning and biochemical analysis of poly-γ-glutamate produced by Escherichia coli clone cells (1999) Biochemical and Biophysical Research Communications, 263 (1), pp. 6-12. , DOI 10.1006/bbrc.1999.1298; 
Park, C., Choi, J.-C., Choi, Y.-H., Nakamura, H., Shimanouchi, K., Horiuchi, T., Misono, H., Sung, M.-H., Synthesis of super-high-molecular-weight poly-γ-glutamic acid by Bacillus subtilis subsp. chungkookjang (2005) Journal of Molecular Catalysis B: Enzymatic, 35 (4-6), pp. 128-133. , DOI 10.1016/j.molcatb.2005.06.007; 
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Hsieh, C.-Y., Tsai, S.-P., Wang, D.-M., Chang, Y.-N., Hsieh, H.-J., Preparation of γ-PGA/chitosan composite tissue engineering matrices (2005) Biomaterials, 26 (28), pp. 5617-5623. , DOI 10.1016/j.biomaterials.2005.02.012, PII S0142961205001614; 
Richard, A., Margaritis, A., Rheology, oxygen transfer, and molecular weight characteristics of poly(glutamic acid) fermentation by Bacillus subtilis (2003) Biotechnology and Bioengineering, 82 (3), pp. 299-305. , DOI 10.1002/bit.10568; 
Peng, S.-F., Yang, M.-J., Su, C.-J., Chen, H.-J., Lee, P.-W., Wei, M.-C., Effects of incorporation of poly(gamma-glutamic acid) in chitosan/DNA complex nanoparticles on cellular uptake and transfection efficiency (2009) Biomaterials, 30, pp. 1797-1808; 
Lin, Y.-H., Mi, F.-L., Chen, C.-T., Chang, W.-C., Peng, S.-F., Liang, H.-F., Sung, H.-W., Preparation and characterization of nanoparticles shelled with chitosan for oral insulin delivery (2007) Biomacromolecules, 8 (1), pp. 146-152. , DOI 10.1021/bm0607776; 
Lee, P.-W., Peng, S.-F., Su, C.-J., Mi, F.-L., Chen, H.-L., Wei, M.-C., Lin, H.-J., Sung, H.-W., The use of biodegradable polymeric nanoparticles in combination with a low-pressure gene gun for transdermal DNA delivery (2008) Biomaterials, 29 (6), pp. 742-751. , DOI 10.1016/j.biomaterials.2007.10.034, PII S014296120700837X; 
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Keresztessy, Z., Bodn{\'a}r, M., Ber, E., Hajdu, I., Zhang, M., Hartmann, J., Self-assembling chitosan/poly-γ-glutamic acid nanoparticles for targeted drug delivery (2009) Colloid Polym Sci, 287 (7), pp. 759-765; 
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Berger, J., Reist, M., Mayer, J.M., Felt, O., Gurny, R., Structure and interactions in chitosan hydrogels formed by complexation or aggregation for biomedical applications (2004) European Journal of Pharmaceutics and Biopharmaceutics, 57 (1), pp. 35-52. , DOI 10.1016/S0939-6411(03)00160-7; 
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},
	month = {2012///},
	pages = {1583 - 1591},
	abstract = {The remarkable properties of poly-aminoacids, mainly their biocompatibility and biodegradability, have prompted an increasing interest in these polymers for biomedical applications. Poly-γ-glutamic acid (γ-PGA) is one of the most interesting poly-aminoacids with potential applications as a biomaterial. Here we describe the production and characterization of γ-PGA by Bacillus subtilis natto. The γ-PGA was produced with low molecular weight (10-50 kDa), high purity grade (>99 \%) and a D-/L-glutamate ratio of 50-60/50-40 \%. To evaluate the feasibility of using this γ-PGA as a biomaterial, chitosan (Ch)/γ-PGA nanoparticles were prepared by the coacervation method at pH ranging from 3.0 to 5.0, with dimensions in the interval 214-221 nm with a poly-dispersion index of ca. 0.2. The high purity of γ-PGA produced by this method, which is firstly described here, renders this biopolymer suitable for biomedical applications. Moreover, the Ch/γ-PGA nanocomplexes developed in this investigation can be combined with biologically active substances for their delivery in the organism. The fact that the assembly between Ch and γ-PGA relies on electrostatic interactions enables addition of other molecules that can be released into the medium through changes from acidic to physiological pH, without loss in biological activity. {\textcopyright} Springer Science+Business Media, LLC 2012.},
	keywords = {Amino acids, animal cell, article, Bacillus subtilis, Bacillus subtilis natto, Bioactivity, Biocompatibility, Biocompatible Materials, biodegradability, Biodegradable polymers, Biodegradation, Biologically active substances, biomaterial, Biomedical applications, biomedicine, biosynthesis, chitosan, circular dichroism, complex formation, controlled study, dispersion, Electrophoresis, Polyacrylamide Gel, feasibility study, Functional polymers, gamma polyglutamic acid, Glutamic acid, High purity, Low molecular weight, Medical applications, molecular interaction, molecular weight, Nanocomplexes, nanoparticle, nonhuman, pH, Physiological pH, polyglutamic acid, Potential applications, priority journal, purification, Spectroscopy, Fourier Transform Infrared, static electricity, Stereoisomerism, unclassified drug},
	isbn = {09574530 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84863314791\&partnerID=40\&md5=d0d618bb2684c8e80e984cfe35f3eb77},
	author = {Pereira, C.L. and Antunes, J.C. and Gon{\c c}alves, R.M. and Ferreira-da-Silva, F. and Barbosa, M.A.}
}
@article {2180,
	title = {Chitosan drives anti-inflammatory macrophage polarisation and pro-inflammatory dendritic cell stimulation.},
	journal = {European cells \& materialsEur Cell Mater},
	volume = {24},
	year = {2012},
	note = {Export Date: 21 November 2012Source: ScopusPubMed ID: 22828991Language of Original Document: EnglishCorrespondence Address: Oliveira, M.I.Chemicals/CAS: chitosan, 9012-76-4; Antigens, CD86; Biocompatible Materials; Chitosan, 9012-76-4; Histocompatibility Antigens Class II; IL10 protein, human; Interleukin-10, 130068-27-8; Transforming Growth Factor beta1; Tumor Necrosis Factor-alpha},
	month = {2012///},
	pages = {136 - 152; discussion 152-153},
	abstract = {Macrophages and dendritic cells (DC) share the same precursor and play key roles in immunity. Modulation of their behaviour to achieve an optimal host response towards an implanted device is still a challenge. Here we compare the differentiation process and polarisation of these related cell populations and show that they exhibit different responses to chitosan (Ch), with human monocyte-derived macrophages polarising towards an anti-inflammatory phenotype while their DC counterparts display pro-inflammatory features. Macrophages and DC, whose interactions with biomaterials are frequently analysed using fully differentiated cells, were cultured directly on Ch films, rather than exposed to the polymer after complete differentiation. Ch was the sole stimulating factor and activated both macrophages and DC, without leading to significant T cell proliferation. After 10 d on Ch, macrophages significantly down-regulated expression of pro-inflammatory markers, CD86 and MHCII. Production of pro-inflammatory cytokines, particularly TNF-α, decreased with time for cells cultured on Ch, while anti-inflammatory IL-10 and TGF-β1, significantly increased. Altogether, these results suggest an M2c polarisation. Also, macrophage matrix metalloproteinase activity was augmented and cell motility was stimulated by Ch. Conversely, DC significantly enhanced CD86 expression, reduced IL-10 secretion and increased TNF-α and IL-1β levels. Our findings indicate that cells with a common precursor may display different responses, when challenged by the same biomaterial. Moreover, they help to further comprehend macrophage/DC interactions with Ch and the balance between pro- and anti-inflammatory signals associated with implant biomaterials. We propose that an overall pro-inflammatory reaction may hide the expression of anti-inflammatory cytokines, likely relevant for tissue repair/regeneration.},
	keywords = {antibody specificity, Antigens, CD86, article, Biocompatible Materials, biomaterial, biosynthesis, CD86 antigen, Cell culture, cell differentiation, cell motion, Cell Movement, Cells, Cultured, chitosan, cytology, dendritic cell, Dendritic Cells, drug effect, flow cytometry, Histocompatibility Antigens Class II, HLA antigen class 2, human, Humans, IL10 protein, human, immunology, interleukin 10, Interleukin-10, macrophage, Macrophages, metabolism, monocyte, Monocytes, Organ Specificity, transforming growth factor beta1, tumor necrosis factor alpha, Tumor Necrosis Factor-alpha},
	isbn = {14732262 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84868253478\&partnerID=40\&md5=5a496411709ccbe5d3d70de13b58b08a},
	author = {Oliveira, M.I. and Santos, S.G. and Oliveira, M.J. and Torres, A.L. and Barbosa, M.A.}
}
@article {2187,
	title = {The effect of adsorbed fibronectin and osteopontin on macrophage adhesion and morphology on hydrophilic and hydrophobic model surfaces},
	journal = {Acta BiomaterialiaActa Biomater.},
	volume = {8},
	year = {2012},
	note = {Export Date: 21 November 2012Source: Scopusdoi: 10.1016/j.actbio.2012.06.010Language of Original Document: EnglishCorrespondence Address: Barbosa, M.A.; INEB - Instituto de Engenharia Biom{\'e}dica, Universidade Do Porto, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: mbarbosa@ineb.up.ptChemicals/CAS: fibronectin, 86088-83-7; gold, 7440-57-5; osteopontin, 106441-73-0References: Anderson, J.M., Biological responses to materials (2001) Annu Rev Mater Res, 31, pp. 81-110;Horbett, T.A., Brash, J.L., Proteins at interfaces: Current issues and future prospects (1987) Proteins at Interfaces, pp. 1-33; 
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Martins, M.C., Fonseca, C., Barbosa, M.A., Ratner, B.D., Albumin adsorption on alkanethiols self-assembled monolayers on gold electrodes studied by chronopotentiometry (2003) Biomaterials, 24, pp. 3697-3706; 
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MacIel, J., Martins, M.C.L., Barbosa, M.A., The stability of self-assembled monolayers with time and under biological conditions (2010) J Biomed Mater Res, 94, pp. 833-843; 
Martins, M.C., Ratner, B.D., Barbosa, M.A., Protein adsorption on mixtures of hydroxyl- and methyl-terminated alkanethiols self-assembled monolayers (2003) J Biomed Mater Res, 67, pp. 158-171; 
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Martins, M.C.L., Curtin, S.A., Freitas, S.C., Salgueiro, P., Ratner, B.D., Barbosa, M.A., Molecularly designed surfaces for blood deheparinization using an immobilized heparin-binding peptide (2009) J Biomed Mater Res, 88, pp. 162-173; 
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Goncalves, R., Martins, M.C.L., Oliveira, M.J., Almeida-Porada, G., Barbosa, M.A., Bioactivity of immobilized EGF on self-assembled monolayers: Optimization of the immobilization process (2010) J Biomed Mater Res, 94, pp. 576-585; 
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},
	month = {2012///},
	pages = {3669 - 3677},
	abstract = {Macrophages play a crucial role in the host response to biomaterials. Here we investigated the effect of adsorbed fibronectin (FN) and osteopontin (OPN), two important proteins for tissue repair, on macrophage adhesion and morphology. Since cell-biomaterial interactions are modulated via proteins adsorbed onto biomaterial surfaces, FN and OPN were adsorbed on model self-assembled monolayers (SAMs) of alkanethiols on gold with different functional terminal groups (CH                        3, OH and tetra(ethylene-glycol)). The initial interaction of inflammatory cells with a biomaterial is crucial for the ensuing phases of an inflammatory reaction. For this reason short-term cultures of primary human macrophages were performed. To account for the competitive adsorption of other proteins serum was added to the culture medium and the effect compared with serum-free medium cultures. In the presence of serum hydrophilic surfaces increased macrophage adhesion. In particular, FN induced a higher cell density, while OPN tended to decrease it. In serum-free medium cell adhesion was greater on hydrophobic surfaces, except for OPN-coated SAMs. Importantly, FN no longer enhanced macrophage adhesion, while OPN maintained its inhibitory effect. Cell polarization studies indicated that macrophage morphology variations induced by surface chemistry are overcome by pre-adsorbed OPN. Taken together our results show that in the presence of serum macrophage adhesion is promoted by FN hydrophilic surfaces, but impaired on OPN-coated surfaces. The effects of inhibited macrophage adhesion on macrophage fusion, and its relevance to the initial stages of the inflammatory response to biomaterials are discussed. {\textcopyright} 2012 Acta Materialia Inc. Published by Elsevier Ltd. All rights reserved.
},
	keywords = {alkane, article, biomaterial, Biomaterials, cell adhesion, cell density, cell interaction, cell structure, controlled study, culture medium, cytoskeleton, Fibronectin, functional group, gold, human, human cell, hydrophilicity, hydrophobicity, inflammatory cell, macrophage, Macrophages, nanomaterial, Osteopontin, priority journal, self assembled monolayer, Self-assembled monolayers, Tetra, thiol, tissue repair},
	isbn = {17427061 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84865455542\&partnerID=40\&md5=9d34fb780e9ce53b424143b0f3eefb97},
	author = {Maciel, J. and Oliveira, M.I. and Gonalves, R.M. and Barbosa, M.A.}
}
@article {2183,
	title = {The effect of octadecyl chain immobilization on the hemocompatibility of poly (2-hydroxyethyl methacrylate)},
	journal = {BiomaterialsBiomaterials},
	volume = {33},
	year = {2012},
	note = {Export Date: 21 November 2012Source: ScopusCODEN: BIMADdoi: 10.1016/j.biomaterials.2012.07.007Language of Original Document: EnglishCorrespondence Address: Sperling, C.; Max Bergmann Center of Biomaterials Dresden, Leibniz Institute of Polymer Research Dresden, Hohe Str. 6, 01069 Dresden, Germany; email: sperling@ipfdd.deChemicals/CAS: isocyanate, 71000-82-3, 75-13-8; polymacon, 25053-81-0, 25249-16-5, 98932-78-6References: Gorbet, M.B., Sefton, M.V., Biomaterial-associated thrombosis: roles of coagulation factors, complement, platelets and leukocytes (2004) Biomaterials, 25, pp. 5681-5703;Cao, L., Sukavaneshvar, S., Ratner, B.D., Horbett, T.A., Glow discharge plasma treatment of polyethylene tubing with tetraglyme results in ultralow fibrinogen adsorption and greatly reduced platelet adhesion (2006) J Biomed Mater Res A, 79, pp. 788-803; 
Tanaka, M., Motomura, T., Kawada, M., Anzai, T., Kasori, Y., Shiroya, T., Blood compatible aspects of poly(2-methoxyethylacrylate) (PMEA)-relationship between protein adsorption and platelet adhesion on PMEA surface (2000) Biomaterials, 21, pp. 1471-1481; 
Martins, C.L., Ratner, B.D., Barbosa, M.A., Protein adsorption on mixtures of hydroxyl- and methylterminated alkanethiols self-assembled monolayers (2003) J Biomed Mater Res, 67 A, pp. 158-171; 
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},
	month = {2012///},
	pages = {7677 - 7685},
	abstract = {Albumin-scavenging surfaces decorated with n-alkyl chains represent an established strategy for blood-contacting applications. To evaluate this concept, a set of poly (2-hydroxyethyl methacrylate) (pHEMA) films modified with different amounts of octadecyl isocyanate (C18) was investigated in an in vitro hemocompatibility assay using freshly drawn human whole blood. In addition, the hydrogel materials were thoroughly characterized with respect to changes in wettability and elasticity, which accompanied the gradual chemical modification of pHEMA. An increase of the surface C18 content induced enhanced hydrophobicity and stiffness. Immobilization of C18 chains was found to substantially reduce the coagulation activation and the complement activation by the pHEMA films. Platelet adhesion and degranulation (PF4 release) were similar on the modified and the unmodified pHEMA. Platelet adhesion to pHEMA hydrogels was lower than the polytetrafluoroethylene reference. We conclude that the immobilization of octadecyl chains improved the hemocompatibility of pHEMA materials under conditions that might be encountered in low shear blood flow. {\textcopyright} 2012 Elsevier Ltd.},
	keywords = {Adhesion, Albumin, article, Biological materials, Biomaterials, Blood, Blood flow, Chemical modification, Coagulation, controlled study, Degranulation, Elasticity, Haemocompatibility, Hemocompatibility, human, hydrogel, in vitro study, In-vitro, isocyanate, Octadecyl, octadecyl isocyanate, PHEMA, Platelet adhesion, Platelets, Poly(2-hydroxyethyl methacrylate), PolyHEMA, polymacon, priority journal, Protein adsorption, thrombocyte adhesion, unclassified drug, wettability, Whole blood},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84865188580\&partnerID=40\&md5=81a8750115106c3d6e9fa2de862d9f70},
	author = {Fischer, M. and Baptista, C.P. and Gon{\c c}alves, I.C. and Ratner, B.D. and Sperling, C. and Werner, C. and Martins, C.L. and Barbosa, M.A.}
}
@booklet {2179,
	title = {Endothelialization of chitosan porous conduits via immobilization of a recombinant fibronectin fragment (rhFNIII                    7-10)
},
	howpublished = {Acta BiomaterialiaActa Biomater.},
	year = {2012},
	note = {Export Date: 21 November 2012Source: ScopusArticle in Pressdoi: 10.1016/j.actbio.2012.10.029Language of Original Document: EnglishCorrespondence Address: Amaral, I.F.; INEB - Instituto de Engenharia Biom{\'e}dica, Universidade do Porto, Rua do Campo Alegre, 823, 41email: iamaral@ineb.up.pt},
	month = {2012///},
	abstract = {The present study aimed to develop a pre-endothelialized chitosan (CH) porous hollowed scaffold for application in spinal cord regenerative therapies. CH conduits with different degrees of acetylation (DA; 4\% and 15\%) were prepared, characterized (microstructure, porosity and water uptake) and functionalized with a recombinant fragment of human fibronectin (rhFNIII                        7-10). Immobilized rhFNIII 
                        7-10 was characterized in terms of amount ( 
                        125I-radiolabelling), exposure of cell-binding domains (immunofluorescence) and ability to mediate endothelial cell (EC) adhesion and cytoskeletal rearrangement. Functionalized conduits revealed a linear increase in immobilized rhFNIII 
                        7-10 with rhFNIII 
                        7-10 concentration, and, for the same concentration, higher amounts of rhFNIII 
                        7-10 on DA 4\% compared with DA 15\%. Moreover, rhFNIII 
                        7-10 concentrations as low as 5 and 20 μg ml 
},
	keywords = {Protein conformation, Protein radiolabelling, Spinal cord injury, Surface grafting, Three-dimensional scaffolds},
	isbn = {17427061 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84868680582\&partnerID=40\&md5=6599fd2565f4511b94e944978afc8073},
	author = {Amaral, I.F. and Neiva, I. and Ferreira da Silva, F. and Sousa, S.R. and Piloto, A.M. and Lopes, C.D.F. and Barbosa, M.A. and Kirkpatrick, C.J. and P{\^e}go, A.P.}
}
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Liippo, J., Toriseva, M., K{\"a}h{\"a}ri, V.-M., Natural killer cell in wound healing (2009) Natural Killer Cells - Basic Science and Clinical Application, pp. 519-525. , eds M. Lotze \& A. Thomson, New York, NY: Academic Press; 
Soderstrom, K., Stein, E., Colmenero, P., Purath, U., Muller-Ladner, U., De Matos, C.T., Tarner, I.H., Engleman, E.G., Natural killer cells trigger osteoclastogenesis and bone destruction in arthritis (2010) Proc. Natl Acad. Sci. USA, 107, pp. 13028-13033. , doi:10.1073/pnas.1000546107
},
	month = {2012///},
	pages = {261 - 271},
	abstract = {An exacerbated inflammatory response questions biomaterial biocompatibility, but on the other hand, inflammation has a central role in the regulation of tissue regeneration. Therefore, it may be argued that an {\textquoteright}ideal{\textquoteright} inflammatory response is crucial to achieve efficient tissue repair/regeneration. Natural killer (NK) cells, being one of the first populations arriving at an injury site, can have an important role in regulating bone repair/regeneration, particularly through interactions with mesenchymal stem/stromal cells (MSCs). Here, we studied how biomaterials designed to incorporate inflammatory signals affected NK cell behaviour and NK cell-MSC interactions. Adsorption of the pro-inflammatory molecule fibrinogen (Fg) to chitosan films led to a 1.5-fold increase in adhesion of peripheral blood human NK cells, without an increase in cytokine secretion. Most importantly, it was found that NK cells are capable of stimulating a threefold increase in human bone marrow MSC invasion, a key event taking place in tissue repair, but did not affect the expression of the differentiation marker alkaline phosphatase (ALP). Of significant importance, this NK cell-mediated MSC recruitment was modulated by Fg adsorption. Designing novel biomaterials leading to rational modulation of the inflammatory response is proposed as an alternative to current bone regeneration strategies. {\textcopyright} 2011 The Royal Society.},
	keywords = {Adhesion, Adsorption, alkaline phosphatase, article, Biocompatibility, biomaterial, Biomaterials, blood cell, Bone, bone marrow cell, Bone Regeneration, Bone repair, cell adhesion, Cell culture, cell differentiation, cell function, cell interaction, cell invasion, Cells, chitosan, Chitosan film, cytokine, Cytokine secretions, Differentiation markers, fibrinogen, gamma interferon, human, Human bone marrow, human cell, Inflammation, Inflammatory response, Mesenchymal Stem Cells, mesenchymal stroma cell, Mesenchymal stromal cells, natural killer cell, Natural killer cells, NK cells, ossification, Pathology, Peripheral blood, Phosphatases, protein expression, Tissue, Tissue regeneration, tissue repair},
	isbn = {17425689 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84856583891\&partnerID=40\&md5=8a6b58ebb9ee4c20099877008acde805},
	author = {Almeida, C.R. and Vasconcelos, D.P. and Gon{\c c}alves, R.M. and Barbosa, M.A.}
}
@article {2214,
	title = {Mesenchymal stem cell recruitment by stromal derived factor-1-delivery systems based on chitosan/poly(γ-glutamic acid) polyelectrolyte complexes},
	journal = {European Cells and MaterialsEur. Cells and Mater.},
	volume = {23},
	year = {2012},
	note = {Export Date: 21 November 2012Source: ScopusLanguage of Original Document: EnglishCorrespondence Address: Gon{\c c}alves, R. M.; INEB, R. Campo Alegre, 823, Porto 4150-180, Portugal; email: raquelg@ineb.up.ptChemicals/CAS: chitosan, 9012-76-4; polyglutamic acid, 24991-23-9, 25513-46-6; Biocompatible Materials; CXCL12 protein, human; Chemokine CXCL12; Chitosan, 9012-76-4; Membranes, Artificial; Polyglutamic Acid, 25513-46-6; poly(gamma-glutamic acid)References: Almeida, C.R., Vasconcelos, D.P., Gon{\c c}alves, R., Barbosa, M.A., Enhanced me s enchymal stromal cell recruitment via Natural Killer cells by incorporation of inflammatory signals in biomaterials (2012) J R Soc Interface, 9, pp. 261-271;Amersham, Iodine-125. A guide to radioiodination techniques (1993) Amersham Life Science, , (I.-A.g.t.r. Techniques, Ed). Amersham, Little Chalfort, UK; 
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},
	month = {2012///},
	pages = {249 - 261},
	abstract = {Human mesenchymal stem cells (hMSCs) have an enormous potential for tissue engineering and cell-based therapies. With a potential of differentiation into multiple lineages and immune-suppression, these cells play a key role in tissue remodelling and regeneration. Here a method of hMSC recruitment is described, based on the incorporation of a chemokine in Chitosan (Ch)/ Poly(γ-glutamic acid) (γ-PGA) complexes. Ch is a nontoxic, cationic polysaccharide widely investigated. γ-PGA is a hydrophilic, non-toxic, biodegradable and negatively charged poly-amino acid. Ch and γ-PGA, being oppositely charged, can be combined through electrostatic interactions. These biocompatible structures can be used as carriers for active substances and can be easily modulated in order to control the delivery of drugs, proteins, DNA, etc. Using the layer-by-layer method, Ch and γ-PGA were assembled into polyelectrolyte multilayers films (PEMs) with thickness of 120 nm. The chemokine stromal-derived factor-1 (SDF-1) was incorporated in these complexes and was continuously released during 120 h. The method of SDF-1 incorporation is of crucial importance for polymers assembly into PEMs and for the release kinetics of this chemokine. The Ch/γ-PGA PEMs with SDF-1 were able to recruit hMSCs, increasing the cell migration up to 6 fold to a maximum of 16.2 {\textpm} 4.9 cells/mm                        2. The controlled release of SDF-1 would be of great therapeutic value in the process of hMSC homing to injured tissues. This is the first study suggesting Ch/γ-PGA PEMs as SDF-1 reservoirs to recruit hMSCs, describing an efficient method of chemokine incorporation that allows a sustained released up to 5 days and that can be easily scaled-up.
},
	keywords = {adsorption kinetics, article, artificial membrane, Biocompatible Materials, biomaterial, cell differentiation, cell migration, cell motion, Cell Movement, Cell recruitment, chemistry, Chemokine CXCL12, chitosan, controlled study, CXCL12 protein, human, cytology, drug adsorption, drug delivery system, Drug Delivery Systems, drug derivative, drug effect, ellipsometry, enzyme linked immunosorbent assay, human, human cell, human tissue, Humans, in vitro study, isotope labeling, Layer-by-layer, Membranes, Artificial, Mesenchymal stem cell, Mesenchymal Stem Cells, metabolism, methodology, poly(gamma glutamic acid), poly(gamma-glutamic acid), Poly(γ-glutamic acid), polyglutamic acid, Protein delivery, static electricity, stromal cell derived factor 1, sustained drug release},
	isbn = {14732262 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84864582297\&partnerID=40\&md5=2fe4a066582cc820d2a8f9dd64fde21b},
	author = {Gon{\c c}alves, R.M. and Antunes, J.C. and Barbosa, M.A.}
}
@article {2232,
	title = {Interactions of leukocytes and platelets with poly(lysine/leucine) immobilized on tetraethylene glycol-terminated self-assembled monolayers},
	journal = {Acta BiomaterialiaActa Biomater.},
	volume = {7},
	year = {2011},
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},
	month = {2011///},
	pages = {1949 - 1955},
	abstract = {Surfaces that bind heparin are important for biomaterials for blood deheparinization. In our recent work it was demonstrated that a polypeptide composed of l-lysine and l-leucine (pKL), after immobilization onto tetra(ethylene glycol) terminated self-assembled monolayers (EG4-SAMs), can bind heparin from blood plasma in a selective, concentration-dependent way. During this work the effect of this peptide on platelet adhesion and activation and leukocyte adhesion was studied. The surface charge of these nanostructured surfaces was evaluated in order to correlate the effect of positively charged amine groups and hydrophobic methyl groups on the behavior of platelets and leukocyte adhesion. The results demonstrated that the presence of pKL decreased leukocyte adhesion to EG4-SAMs at all concentrations used. This effect is even more pronounced when surfaces were pre-immersed in heparinized plasma. In contrast, there is an increase in platelet adhesion and activation with increased percentage immobilized pKL. This effect is enhanced when surfaces were pre-immersed in heparinized plasma. However, adsorbed pKL in very low amounts does not induce platelet adhesion and activation compared with EG4, even when pre-immersed in plasma. Since only low pKL amounts are necessary to induce heparin selectivity, these results are promising for the development of heparin-binding biomaterials for blood deheparinization. {\textcopyright} 2011 Acta Materialia Inc. Published by Elsevier Ltd. All rights reserved.},
	keywords = {article, Blood Platelets, Cell Communication, Cell Shape, Ethylene Glycol, heparin, heparin binding protein, Humans, hydrophobicity, Imidazoles, Immobilized Proteins, leucine, leukocyte, leukocyte adherence, Leukocytes, methyl group, nanomaterial, plasma, Platelet Adhesiveness, Platelets, Polyethylene Glycols, polylysine, polypeptide, priority journal, Proteins, self assembled monolayer, Self-assembled monolayers, static electricity, Surface charge, Surface Properties, Tetra, thrombocyte, thrombocyte adhesion},
	isbn = {17427061 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-79953868334\&partnerID=40\&md5=2cb5b44223fe6e8106b513b80689103d},
	author = {Martins, M.C.L. and Ochoa-Mendes, V. and Ferreira, G. and Barbosa, J.N. and Curtin, S.A. and Ratner, B.D. and Barbosa, M.A.}
}
@article {2215,
	title = {Layer-by-layer self-assembly of chitosan and poly(γ-glutamic acid) into polyelectrolyte complexes},
	journal = {BiomacromoleculesBiomacromolecules},
	volume = {12},
	year = {2011},
	note = {Cited By (since 1996): 3Export Date: 21 November 2012Source: ScopusCODEN: BOMAFdoi: 10.1021/bm2008235PubMed ID: 22032302Language of Original Document: EnglishCorrespondence Address: Antunes, J.C.; INEB - Instituto de Engenharia Biom{\'e}dica, Porto, Portugal; email: joana.antunes@ineb.up.ptChemicals/CAS: chitosan, 9012-76-4; glutamic acid, 11070-68-1, 138-15-8, 56-86-0, 6899-05-4; Biocompatible Materials; Chitosan, 9012-76-4; Electrolytes; Polyglutamic Acid, 25513-46-6; Viscoelastic Substances; poly(gamma-glutamic acid)References: Bertrand, P., Jonas, A., Laschewsky, A., Legras, R., Ultrathin polymer coatings by complexation of polyelectrolytes at interfaces: Suitable materials, structure and properties (2000) Macromol. Rapid Commun., 21, pp. 319-348;Schonhoff, M., Layered polyelectrolyte complexes: Physics of formation and molecular properties (2003) J. Phys.: Condens. Matter, 15, pp. R1781-R1808; 
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},
	month = {2011///},
	pages = {4183 - 4195},
	abstract = {Chitosan (Ch) is a nontoxic and biocompatible polysaccharide extensively used in biomedical applications. Ch, as a polycation, can be combined with anionic polymers by layer-bylayer (LbL) self-assembly, giving rise to multilayered complexed architectures. These structures can be used in tissue engineering strategies, as drug delivery systems, or artificial matrices mimicking the extracellular microenvironment. In this work, Ch was combined with poly(γ-glutamic acid) (γ-PGA). γ-PGA is a polyanion, which was microbially produced, and is known for its low immunogenic reaction and low cytotoxicity. Multilayered ultrathin films were assembled by LbL, with a maximum of six layers. The interaction between both polymers was analyzed by: ellipsometry, quartz crystal microbalance with dissipation, Fourier transform infrared spectroscopy, atomic force microscopy, and zeta potential measurements. Ch/γ-PGA polyelectrolyte multilayers (PEMs) revealed no cytotoxicity according to ISO 10993-5. Overall, this study demonstrates that Ch can interact electrostatically with γ-PGA forming multilayered films. Furthermore, this study provides a comprehensive characterization of Ch/γ-PGA PEM structures, elucidating the contribution of each layer for the nanostructured films. These model surfaces can be useful substrates to study cell-biomaterial interactions in tissue regeneration. {\textcopyright} 2011 American Chemical Society.},
	keywords = {Amino acids, Anionic polymers, article, Atomic force microscopy, Atomic spectroscopy, Biocompatible Materials, Biocompatible polysaccharides, Biomaterials, Biomedical applications, Cell-biomaterial interactions, chemical interaction, chitosan, controlled study, Cytotoxicity, Drug delivery, drug delivery system, Drug Delivery Systems, Electrolytes, ellipsometry, enzyme activity, Extracellular, Fourier transform infrared spectroscopy, Glutamic acid, immunogenicity, infrared spectroscopy, Layer by layer self assembly, Medical applications, microenvironment, Microenvironments, Microscopy, Atomic Force, Model surface, Models, Molecular, Multi-layered, Multi-layered films, Multilayers, nanofilm, Nanostructured Films, polyanion, Polyanions, Polycations, polyelectrolyte, Polyelectrolyte complexes, Polyelectrolyte multilayer, Polyelectrolytes, Polyethylenes, polyglutamic acid, Polymers, priority journal, Programmed control systems, Quartz, quartz crystal microbalance, Quartz crystal microbalance with dissipation, Self assembly, Tissue, Tissue engineering, Tissue regeneration, Ultrathin films, Viscoelastic Substances, Zeta potential, Zeta potential measurements},
	isbn = {15257797 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84856258191\&partnerID=40\&md5=8ba447b7a45e8004e5b3aa3d5cff2404},
	author = {Antunes, J.C. and Pereira, C.L. and Molinos, M. and Ferreira-da-Silva, F. and Dessi, M. and Gloria, A. and Ambrosio, L. and Gonca̧lves, R.M. and Barbosa, M.A.}
}
@article {2237,
	title = {Pectin-based injectable biomaterials for bone tissue engineering},
	journal = {BiomacromoleculesBiomacromolecules},
	volume = {12},
	year = {2011},
	note = {Cited By (since 1996): 6Export Date: 21 November 2012Source: ScopusCODEN: BOMAFdoi: 10.1021/bm101110xPubMed ID: 21302960Language of Original Document: EnglishCorrespondence Address: Munarin, F.; Biomatlab, Bioengineering Department, Politecnico di Milano, Piazza Leonardo da Vinci 32, 20133, Milan, Italy; email: fabiola.munarin@mail.polimi.itChemicals/CAS: arginylglycylaspartic acid, 99896-85-2; osteocalcin, 136461-80-8; pectin, 9000-69-5; Biocompatible Materials; Oligopeptides; Pectins; arginyl-glycyl-aspartic acid, 99896-85-2; pectin, 9000-69-5References: Brown, M.J., Lester, J.N., (1980) Appl. Environ. Microbiol., 40, pp. 179-185;Knox, J.P., (2008) Curr. Opin. Plant Biol., 1, pp. 308-313; 
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},
	month = {2011///},
	pages = {568 - 577},
	abstract = {A variety of natural polymers and proteins are considered to be 3D cell culture structures able to mimic the extracellular matrix (ECM) to promote bone tissue regeneration. Pectin, a natural polysaccharide extracted from the plant cell walls and having a chemical structure similar to alginate, provides interesting properties as artificial ECM. In this work, for the first time, pectin, modified with an RGD-containing oligopeptide or not, is used as an ECM alternative to immobilize cells for bone tissue regeneration. The viability, metabolic activity, morphology, and osteogenic differentiation of immobilized MC3T3-E1 preosteoblats demonstrate the potential of this polysaccharide to keep immobilized cells viable and differentiating. Preosteoblasts immobilized in both types of pectin microspheres maintained a constant viability up to 29 days and were able to differentiate. The grafting of the RGD peptide on pectin backbone induced improved cell adhesion and proliferation within the microspheres. Furthermore, not only did cells grow inside but also theywere able to spread out from themicrospheres and to organize themselves in 3D structures producing a mineralized extracellular matrix. These promising results suggest that pectin can be proposed as an injectable cell vehicle for bone tissue regeneration. {\textcopyright} 2011 American Chemical Society.},
	keywords = {3-D Cell culture, 3D Structure, 3T3 Cells, Adhesion, Alginate, animal cell, Animals, arginylglycylaspartic acid, article, Biocompatible Materials, Biopolymers, Bone, Bone and Bones, Bone Regeneration, bone tissue, Bone tissue engineering, Bone tissue regeneration, carbohydrate analysis, cell adhesion, Cell culture, cell differentiation, cell growth, cell metabolism, cell proliferation, cell spreading, cell structure, cell viability, Cells, Chemical modification, Chemical structure, controlled study, Cryoelectron Microscopy, Extracellular matrices, extracellular matrix, gene expression, immobilized cell, Immobilized cells, Injectable biomaterials, Injections, MC3T3-E1, Metabolic activity, Mice, Microscopy, Electron, Scanning, microsphere, Microspheres, Mineralized extracellular matrixes, mouse, Natural polysaccharide, nonhuman, Oligopeptides, osteoblast, osteocalcin, Osteogenic differentiation, pectin, Pectins, Plant cell culture, Plant cell wall, Preosteoblasts, priority journal, RGD peptide, Three dimensional, Tissue engineering},
	isbn = {15257797 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-79955409005\&partnerID=40\&md5=277a7d5e91116f9a03f144aabda0dd96},
	author = {Munarin, F. and Guerreiro, S.G. and Grellier, M.A. and Tanzi, M.C. and Barbosa, M.A. and Petrini, P. and Granja, P.L.}
}
@article {2281,
	title = {Adhesion of human leukocytes on mixtures of hydroxyl- and methyl-terminated self-assembled monolayers: Effect of blood protein adsorption},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {93},
	year = {2010},
	note = {Cited By (since 1996): 4Export Date: 21 November 2012Source: ScopusCODEN: JBMRCdoi: 10.1002/jbm.a.32480PubMed ID: 19484768Language of Original Document: EnglishCorrespondence Address: Barbosa, J. N.; Divis{\~a}o de Biomateriais, INEB-Instituto de Engenharia Biom{\'e}dica, Universidade do Porto, Porto 4150-180, Portugal; email: judite@ineb.up.ptChemicals/CAS: Blood Proteins; Gold, 7440-57-5; Hydroxyl Radical, 3352-57-6References: Brodbeck, W.G., Nakayama, Y., Matsuda, T., Colton, E., Ziats, N.P., Anderson, J.M., Biomaterial surface chemistry dictates adherent monocyte/macrophage cytokine expression in vitro (2002) Cytokine, 18, pp. 311-319;Kao, W.Y.J., Evaluation of leukocyte adhesion on polyurethanes: The effects of shear stress and blood proteins (2000) Biomaterials, 21, pp. 2295-2303; 
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},
	month = {2010///},
	pages = {12 - 19},
	abstract = {The adhesion of human leukocytes to nanostructured surfaces with different chemical properties and the effect of protein adsorption were investigated. Selfassembled monolayers (SAMs) prepared with mixtures of methyl- and hydroxyl-terminated alkanethiols in different percentages on gold were used. The surfaces were preimmersed in distinct protein solutions (human serum albumin, human fibrinogen, and autologous plasma). Adherent leukocytes were analyzed both by light and SEM. SAMs submitted to pre-immersion in plasma presented higher numbers of adherent leukocytes in the pure OH-terminated SAM, whereas methyl-terminated surfaces accounted for the lowest number of adherent cells. We observed a general increase in the number of adherent human leukocytes as the percentage of OH groups on the surface of the SAMs increased for all the pre-immersion conditions investigated. The number of adherent human leukocytes is highly influenced by the pre-immersion conditions used, and this observation is particularly relevant in the case of the methyl-terminated SAMs. The results obtained demonstrate that surface chemistry has a major influence in leukocyte adhesion to biomaterials, and that pre-immersion in protein solutions has a determinant effect in leukocyte adhesion. {\textcopyright} 2009 Wiley Periodicals, Inc.},
	keywords = {Adherent cells, Adhesion, Adsorption, Alkanethiols, article, Biological materials, biomaterial, Blood protein adsorption, Blood Proteins, cell adhesion, Cell Count, Chemical properties, gold, human, human cell, Human leukocytes, Human serum albumins, Humans, hydroxyl group, Hydroxyl Radical, Hydroxyl-terminated, immersion, Inflammatory response, leukocyte adherence, Leukocyte adhesion, Leukocytes, Nanostructured materials, Nanostructured surface, Nanostructured surfaces, OH group, Protein adsorption, protein blood level, Protein solution, Proteins, Sams, Scanning electron microscopy, Self assembled monolayers, Self-assembled monolayers, SEM, Surface chemistry, Surface Properties},
	isbn = {15493296 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-77649225392\&partnerID=40\&md5=0b35403e1b98581c557435b6cf7a8286},
	author = {Barbosa, J.N. and Martins, M.C.L. and Freitas, S.C. and Gon{\c c}alves, I.C. and {\'A}guas, A.P. and Barbosa, M.A.}
}
@article {2268,
	title = {Bioactivity of immobilized EGF on self-assembled monolayers: Optimization of the immobilization process},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {94},
	year = {2010},
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Garcia, R., Franklin, R.A., Mccubrey, J.A., EGF induces cell motility and multi-drug resistance gene expression in breast cancer cells (2006) Cell Cycle, 5, pp. 2820-2826
},
	month = {2010///},
	pages = {576 - 585},
	abstract = {Last trends in Biomaterials focus the mimic of cellular environments capable to control cellular responses. Epidermal growth factor (EGF) is a pleiotropic cytokine known to regulate cell proliferation, differentiation, and death. This study aims to optimize the immobilization of EGF on 11-mercapto-1-undecyl-tetra(ethylene)glycol (EG4) - self-assembled monolayers (SAMs) and to establish a new model surface to study EGF-mediated signaling. Gold substrates were modified with a monolayer of EG4 and N,N'- carbonyldiimidazole (CDI) was used to activate hydroxyl terminated groups of EG4-SAMs. EGF was then immobilized on activated EG4-SAMs at pH 7.4, 4{\textdegree}C, and 100 rpm. Different immobilization reaction times were tested as well as different CDI concentrations to optimize the reaction conditions and obtain a range of immobilized EGF concentrations on the surfaces. Surface characterization of EGF-SAMs was performed using radiolabeling, water contact angle measurements, X-ray photoelectron spectroscopy, and ELISA. Phosphorylation of EGFR on BT-20 breast cancer cell line by EGF-SAMs was tested by immunostaining. EGF was successfully immobilized on EG4-SAMs, at 4{\textdegree}C and pH 7.4 in a range of concentrations from 3.6 {\textpm} 0.8 to 17.6 {\textpm} 1.5 ng/cm                        2. The concentration of EGF increases with immobilization time and with the CDI concentration reaching the maximum for surfaces activated with 30 mg/mL of CDI after 48 h. The bioactivity of EGF-SAMs was confirmed by immunostaining of phospho-EGFR of BT-20 cells. This study described EGF immobilization on EG4-SAMs at different concentrations, which could be important surface models to study specific protein interactions at the molecular level evolving EGF-family of proteins. {\textcopyright} 2010 Wiley Periodicals, Inc. J.
},
	keywords = {Adsorption, Angle measurement, article, Biocompatible Materials, Biological materials, Breast cancer cells, cancer cell culture, Carbonyldiimidazole, Cell culture, Cell immobilization, Cell Line, Tumor, cell proliferation, Cellular environment, Cellular response, Concentration (process), Concentration of, Contact angle, controlled study, Cytokines, EGF, Electron energy levels, enzyme linked immunosorbent assay, Enzyme-Linked Immunosorbent Assay, epidermal growth factor, Epidermal growth factors, Ethylene, Glycols, gold, Gold substrates, human, human cell, Humans, Hydroxyl-terminated, Imidazoles, Immobilization process, Immobilization reaction, immunofluorescence, immunohistochemistry, Immunostaining, Molecular levels, Nanostructured materials, Nanostructured surface, Nanostructured surfaces, New model, Optimization, Phosphorylation, Photoelectron spectroscopy, Polyethylene Glycols, Protein adsorption, protein immobilization, protein interaction, protein phosphorylation, Proteins, Radiolabeling, Radioligand Assay, Reaction conditions, reaction optimization, Receptor, Epidermal Growth Factor, Sams, self assembled monolayer, Self assembled monolayers, Self-assembled monolayers, Sulfhydryl Compounds, Surface characterization, Surface functionalization, Surface models, Surface Properties, Water contact angle measurement, X ray photoelectron spectroscopy},
	isbn = {15493296 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-77953815323\&partnerID=40\&md5=7b54d717bbba475933dd86cc62659acc},
	author = {Gon{\c c}alves, R. and Martins, M.C.L. and Oliveira, M.J. and Almeida-Porada, G. and Barbosa, M.A.}
}
@article {2274,
	title = {Characterization of polymeric solutions as injectable vehicles for hydroxyapatite microspheres},
	journal = {AAPS PharmSciTechAAPS PharmSciTech},
	volume = {11},
	year = {2010},
	note = {Cited By (since 1996): 1Export Date: 21 November 2012Source: Scopusdoi: 10.1208/s12249-010-9447-3PubMed ID: 20490958Language of Original Document: EnglishCorrespondence Address: Oliveira, S. M.; Dep. de Eng. Mec{\^a}nica e Gest{\~a}o Industrial, Escola Superior de Tecnologia e Gest{\~a}o de Viseu, Campus Polit{\'e}cnico de Repeses, 3504-510, Viseu, Portugal; email: soliveira@estv.ipv.ptChemicals/CAS: alginic acid, 28961-37-7, 29894-36-8, 9005-32-7, 9005-38-3; carboxymethylcellulose, 8050-38-2, 9000-11-7, 9004-32-4, 9050-04-8; hydroxyapatite, 1306-06-5, 51198-94-8; hydroxypropylmethylcellulose, 9004-65-3; Biocompatible Materials; Capsules; Durapatite, 1306-06-5; Excipients; Polymers; Solutions; VehiclesReferences: Verlaan, J.J., Oner, F.C., Dhert, W.J., Anterior spinal column augmentation with injectable bone cements (2006) Biomat, 27 (3), pp. 290-301;Chenite, A., Chaput, C., Wang, D., Combes, C., Buschmann, M.D., Hoemann, C.D., Novel injectable neutral solutions of chitosan form biodegradable gels in situ (2000) Biomat, 21 (21), pp. 2155-2161; 
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},
	month = {2010///},
	pages = {852 - 858},
	abstract = {A polymeric solution and a reinforcement phase can work as an injectable material to fill up bone defects. However, the properties of the solution should be suitable to enable the transport of that extra phase. Additionally, the use of biocompatible materials is a requirement for tissue regeneration. Thus, we intended to optimize a biocompatible polymeric solution able to carry hydroxyapatite microspheres into bone defects using an orthopedic injectable device. To achieve that goal, polymers usually regarded as biocompatible were selected, namely sodium carboxymethylcellulose, hydroxypropylmethylcellulose, and Na-alginate (ALG). The rheological properties of the polymeric solutions at different concentrations were assessed by viscosimetry before and after moist heat sterilization. In order to correlate rheological properties with injectability, solutions were tested using an orthopedic device applied for minimal invasive surgeries. Among the three polymers, ALG solutions presented the most suitable properties for our goal and a non-sterile ALG 6\% solution was successfully used to perform preliminary injection tests of hydroxyapatite microspheres. Sterile ALG 7.25\% solution was found to closely match non-sterile ALG 6\% properties and it was selected as the optimal vehicle. Finally, sterile ALG 7.25\% physical stability was studied at different temperatures over a 3-month period. It was observed that its rheological properties presented minor changes when stored at 25{\textdegree}C or at 4{\textdegree}C. {\textcopyright} 2010 American Association of Pharmaceutical Scientists.},
	keywords = {Alginate, alginic acid, article, Biocompatibility, Biocompatible Materials, Capsules, Carboxymethylcellulose, Drug Compounding, Durapatite, Excipients, hydroxyapatite, Hydroxypropylmethylcellulose, Injectability, injection, Injections, instrument sterilization, microsphere, Microspheres, minimally invasive surgery, molecular weight, orthopedic equipment, Polymers, priority journal, Solutions, Vehicles, viscometry},
	isbn = {15309932 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-77954819260\&partnerID=40\&md5=e8503462fa39dcc285aef7e07f765eef},
	author = {Oliveira, S.M. and Almeida, I.F. and Costa, P.C. and Barrias, C.C. and Ferreira, M.R.P. and Bahia, M.F. and Barbosa, M.A.}
}
@article {2279,
	title = {The effect of immobilization of thrombin inhibitors onto self-assembled monolayers on the adsorption and activity of thrombin},
	journal = {BiomaterialsBiomaterials},
	volume = {31},
	year = {2010},
	note = {Cited By (since 1996): 7Export Date: 21 November 2012Source: ScopusCODEN: BIMADdoi: 10.1016/j.biomaterials.2010.01.097PubMed ID: 20153046Language of Original Document: EnglishCorrespondence Address: Martins, M.C.L.; INEB - Instituto de Engenharia Biom{\'e}dica, Divis{\~a}o de Biomateriais, Universidade do Porto, Rua do Campo Alegre 823, 4150-180 Porto, Portugal; email: cmartins@ineb.up.ptChemicals/CAS: thrombin, 9002-04-4; Albumins; Gold, 7440-57-5; Immobilized Proteins; Iodine Radioisotopes; Peptides; Solutions; Thrombin, 3.4.21.5References: Gorbet, M.B., Sefton, M.V., Biomaterial-associated thrombosis: roles of coagulation factors, complement, platelets and leukocytes (2004) Biomaterials, 25 (26), pp. 5681-5703;Ratner, B.D., Hoffman, A.F., Schoen, F.J., Lemons, J.L., (2004) Biomaterials science - an introduction to materials in medicine. 2nd ed., , Elsevier Academic Press, San Diego, CA, USA; 
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},
	month = {2010///},
	pages = {3772 - 3780},
	abstract = {Thrombus formation is the major problem associated with biomaterials for blood contact medical devices. The immobilization of inhibitors to thrombin, a serine protease that plays a central role on the coagulation system, on the surface of biomaterials should be a good strategy to avoid blood clotting and increase their hemocompatibility. The aim of this work is the design of a nanostructured surface with capacity to adsorb and inactivate thrombin. The pentapeptide sequence d-Phenylalanine-Proline-Arginine-Proline-Glycine (fPRPG), that was described as a thrombin inhibitor, was immobilized onto tetra(ethylene glycol) terminated self-assembled monolayers (EG4-SAMs). Surface containing different amounts of fPRPG were prepared using different concentrations of N,N'-Carbonyldiimidazole (CDI) during immobilization. The efficiency of fPRPG immobilization was followed using ellipsometry, contact angle measurements, Infrared reflection absorption spectroscopy (IRRAS) and X-ray photoelectron spectroscopy (XPS). Thrombin adsorption was quantified using radiolabelled thrombin and its activity in solution and after adsorption on the developed surfaces was assessed using a chromogenic assay. It was found that, although the immobilization of fPRPG on to EG4-SAMs does not increase its selectivity to thrombin, the activity of the adsorbed thrombin was inhibited in a peptide concentration dependent way. We concluded that SAMs with fPRPG immobilized in high amounts can be used as thrombin-inhibitor surfaces, which is a good step on the development of new surfaces for blood contact devices. {\textcopyright} 2010 Elsevier Ltd. All rights reserved.},
	keywords = {Absorption spectroscopy, Adsorption, adsorption kinetics, Albumins, Amino Acid Sequence, Amino acids, Angle measurement, article, Biomaterials, Blood, Blood clotting, Blood contact, Carbonyldiimidazole, Coagulation, Coagulation system, concentration (parameters), Concentration-dependent, Contact angle, D-phenylalanine, ellipsometry, Ethylene, Ethylene Glycol, ethylene glycol derivative, gold, Hemocompatibility, Humans, imidazole derivative, Immobilized Proteins, Infrared reflection absorption spectroscopy, infrared spectroscopy, Iodine Radioisotopes, isotope labeling, Medical Devices, monolayer culture, nanoanalysis, Nanostructured surface, peptide, Peptide immobilization, Peptides, phenylalanylprolylarginylprolylglycine, Phosphatases, priority journal, Protein adsorption, protein assembly, protein function, protein immobilization, quantitative study, Sams, Self assembled monolayers, Self-assembled monolayers, Serine protease, Solubility, Solutions, Spectroscopy, Fourier Transform Infrared, Surface functionalization, Surface Properties, Tetra, tetra(ethylene glycol), Thrombin, thrombin inhibitor, Thrombin inhibitors, Thrombus formation, unclassified drug, X ray photoelectron spectroscopy},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-77649271932\&partnerID=40\&md5=f7180daf23d326319cf6d8dbf0eac77c},
	author = {Freitas, S.C. and Barbosa, M.A. and Martins, M.C.L.}
}
@article {2280,
	title = {Evaluation of the effect of the degree of acetylation on the inflammatory response to 3D porous chitosan scaffolds},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {93},
	year = {2010},
	note = {Cited By (since 1996): 3Export Date: 21 November 2012Source: ScopusCODEN: JBMRCdoi: 10.1002/jbm.a.32499PubMed ID: 19484769Language of Original Document: EnglishCorrespondence Address: Barbosa, J. N.; INEB - Instituto de Engenharia Biom{\'e}dica, Divis{\~a}o de Biomateriais, Universidade do Porto, Rua do Campo Alegre 823, 4150-180 Porto, Portugal; email: judite@ineb.up.ptChemicals/CAS: chitosan, 9012-76-4; Chitosan, 9012-76-4References: Sefton, M.V., Babensee, J.E., Woodhouse, K.A., Innate and adaptative immune responses in tissue engineering (2008) Semin Immunol, 20, pp. 83-85;VandeVord, P.J., Matthew, H.W.T., DeSilva, S.P., Mayton, L., Wu, B., Wooley, P.H., Evaluation of the biocompatibility of a chitosan scaffold in mice (2002) J Biomed Mater Res, 59, pp. 585-590; 
Anderson, J.M., Biological responses to materials (2001) Annu Rev Mater Res, 31, pp. 81-110; 
Babensee, J.E., Anderson, J.M., McIntire, L.V., Mikos, A.G., Host response to tissue engineered devices (1998) Adv Drug Deliv Rev, 33, pp. 111-139; 
Ueno, H., Mori, T., Fujinaga, T., Topical formulations and wound healing applications of chitosan (2001) Adv Drug Deliv Rev, 52, pp. 105-115; 
Kim, I.Y., Seo, S.J., Moon, H.S., Yoo, M.K., Park, I.Y., Kim, B.C., Cho, C.S., Chitosan and its derivatives for tissue engineering applications (2008) Biotechnol Adv, 26, pp. 1-21; 
Tomihata, K., Ikada, Y., In vitro and in vivo degradation of films of chitin and its deacetylated derivatives (1997) Biomaterials, 18, pp. 567-575; 
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Amaral, I.F., Lamghari, M., Sousa, S.R., Sampaio, P., Barbosa, M.A., Rat bone marrow stromal cell osteogenic differentiation and fibronectin adsorption on chitosan membranes: The effect of the degree of acetylation (2005) J Biomed Mater Res, 75 A, pp. 387-397. , Part A; 
Ueno, H., Murakami, M., Okumura, M., Kadosawa, T., Uede, T., Fujinaga, T., Chitosan accelerates the production of osteopontin from polymorphonuclear leukocytes (2001) Biomaterials, 22, pp. 1667-1673
},
	month = {2010///},
	pages = {20 - 28},
	abstract = {The effect of the degree of acetylation (DA) of 3D chitosan (Ch) scaffolds on the inflammatory reaction was investigated. Chitosan porous scaffolds with DAs of 4 and 15\% were implanted using a subcutaneous air-pouch model of inflammation. The initial acute inflammatory response was evaluated 24 and 48 h after implantation. To characterize the initial response, the recruitment and adhesion of inflammatory cells to the implant site was studied. The fibrous capsule formation and the infiltration of inflammatory cells within the scaffolds were evaluated for longer implantation times (2 and 4 weeks). Chitosan with DA 15\% attracted the highest number of leukocytes to the implant site. High numbers of adherent inflammatory cells were also observed in this material. For longer implantation periods Ch scaffolds with a DA of 15\% induced the formation of a thick fibrous capsule and a high infiltration of inflammatory cells within the scaffold. Our results indicate that the biological response to implanted Ch scaffolds was influenced by the DA. Chitosan with a DA of 15\% induce a more intense inflammatory response when compared with DA 4\% Ch. Because inflammation and healing are interrelated, this result may provide clues for the relative importance of acetyl and amine functional groups in tissue repair and regeneration. {\textcopyright} 2009 Wiley Periodicals, Inc.},
	keywords = {acetic acid derivative, Acetylation, Acute inflammatory response, amine, Amine functional groups, animal cell, animal experiment, animal tissue, Animals, article, Biological materials, Biological response, Biomaterials, cell adhesion, cell infiltration, Chitin, chitosan, Chitosan scaffold, Degree of acetylation, Fibrous capsule, Fibrous capsule formation, freeze drying, Functional groups, Hydrogels, implant, implantation, Implantation periods, Implants, Experimental, Inflammation, Inflammatory cells, Inflammatory reaction, Inflammatory response, leukocyte count, Leukocytes, male, Mice, Mice, Inbred BALB C, Microscopy, Electron, Scanning, mouse, nonhuman, Pathology, porosity, Porous scaffold, Prosthesis Implantation, Relative importance, Scaffolds, Subcutaneous Tissue, Surface Properties, Three dimensional, Tissue regeneration, tissue repair, Tissue response, Tissue responses, Tissue Scaffolds},
	isbn = {15493296 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-77649219383\&partnerID=40\&md5=58781af29b82f3108ded649c4776e428},
	author = {Barbosa, J.N. and Amaral, I.F. and {\'A}guas, A.P. and Barbosa, M.A.}
}
@article {2264,
	title = {Immobilization of human mesenchymal stem cells within RGD-grafted alginate microspheres and assessment of their angiogenic potential},
	journal = {BiomacromoleculesBiomacromolecules},
	volume = {11},
	year = {2010},
	note = {Cited By (since 1996): 18Export Date: 21 November 2012Source: ScopusCODEN: BOMAFdoi: 10.1021/bm100264aPubMed ID: 20690708Language of Original Document: EnglishCorrespondence Address: Granja, P. L.; INEB-Instituto de Engenharia Biom{\'e}dica, Rua do Campo Alegre No. 823, 4150-180 Porto, Portugal; email: pgranja@ineb.up.ptMolecular Sequence Numbers: GENBANK: BC021289, NM_000088, NM_002046;Chemicals/CAS: alginic acid, 28961-37-7, 29894-36-8, 9005-32-7, 9005-38-3; alkaline phosphatase, 9001-78-9; arginylglycylaspartic acid, 99896-85-2; Alginates; Alkaline Phosphatase, 3.1.3.1; Collagen Type I; DNA Primers; Oligopeptides; arginyl-glycyl-aspartic acid, 99896-85-2References: Temenoff, J.S., Mikos, A.G., Injectable biodegradable materials for orthopedic tissue engineering (2000) Biomaterials, 21, pp. 2405-2412;Barralet, J.E., Wang, L., Lawson, M., Triffitt, J.T., Cooper, P.R., Shelton, R.M., Comparison of bone marrow cell growth on 2D and 3D alginate hydrogels (2005) J. Mater. Sci.: Mater. Med., 16, pp. 515-519; 
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Yu, J., Gu, Y., Du, K.T., Mihardja, S., Sievers, R.E., Lee, R.J., The effect of injected RGD modified alginate on angiogenesis and left ventricular function in a chronic rat infarct model (2009) Biomaterials, 30, pp. 751-756
},
	month = {2010///},
	pages = {1956 - 1964},
	abstract = {In this work, human mesenchymal stem cells (hMSC) immobilized in RGD-coupled alginate microspheres, with a binary composition of high and low molecular weight alginate, were investigated. Cells immobilized within RGD-alginate microspheres (during 21 days) showed metabolic activity, with an overall viability higher than 90\%, short cell extensions, and, when induced, they were able to differentiate into the osteogenic lineage. In osteogenic conditions (comparing to basal conditions), immobilized cells presented alkaline phosphatase (ALP) activity and an upregulation of ALP, collagen type I, and Runx 2 expression. Moreover, mineralization was also detected in immobilized cells under osteogenic stimulus. In addition, it was demonstrated for the first time that MSCs immobilized in this 3D matrix were able to enhance the ability of neighboring endothelial cells to form tubelike structures. Overall, these findings represent a step forward in the development of injectable stem cell carriers for bone tissue engineering. {\textcopyright} 2010 American Chemical Society.},
	keywords = {Alginate, Alginates, alginic acid, alkaline phosphatase, Alkaline phosphatase activity, angiogenesis, arginylglycylaspartic acid, article, Basal conditions, Base Sequence, Binary composition, bone development, Bone tissue engineering, Cell culture, cell differentiation, Cell extension, Cell immobilization, cell metabolism, cell structure, cell viability, collagen type 1, Collagen type I, controlled study, DNA Primers, Endothelial Cells, endothelium cell, enzyme activity, human, human cell, Human mesenchymal stem cells, Humans, immobilized cell, Immobilized cells, Low molecular weight, matrix, Mesenchymal stem cell, Mesenchymal Stem Cells, Metabolic activity, Microscopy, Electron, Scanning, microsphere, Microspheres, molecular weight, Neovascularization, Physiologic, nucleotide sequence, Oligopeptides, osteoblast, Osteogenic, Phosphatases, priority journal, protein expression, quantitative analysis, Reverse Transcriptase Polymerase Chain Reaction, stem cell, Stem cells, three dimensional imaging, Tissue engineering, transcription factor RUNX2, umbilical vein, Up-regulation, upregulation},
	isbn = {15257797 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-77955575798\&partnerID=40\&md5=d2d378c63dc49de9324e8dddb24ff2e9},
	author = {Bidarra, S.J. and Barrias, C.C. and Barbosa, M.A. and Soares, R. and Granja, P.L.}
}
@article {2255,
	title = {The stability of self-assembled monolayers with time and under biological conditions},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {94},
	year = {2010},
	note = {Cited By (since 1996): 7Export Date: 21 November 2012Source: ScopusCODEN: JBMRCdoi: 10.1002/jbm.a.32746PubMed ID: 20336761Language of Original Document: EnglishCorrespondence Address: Barbosa, M. A.; Divis{\~a}o de Biomateriais, INEB - Instituto de Engenharia Biom{\'e}dica, Universidade do Porto, Rua do Campo Alegre 823, Porto 4150-180, Portugal; email: mbarbosa@ineb.up.ptChemicals/CAS: sulfur, 13981-57-2, 7704-34-9; Culture Media; Ethanol, 64-17-5; Sulfhydryl Compounds; Sulfur, 7704-34-9; Water, 7732-18-5References: Mrksich, M., Whitesides, G.M., Using self-assembled monolayers to understand the interactions of man- Made surfaces with proteins and cells (1996) Annual Review of Biophysics and Biomolecular Structure, 25, pp. 55-78;Mrksich, M., Dike, L.E., Tien, J., Ingber, D.E., Whitesides, G.M., Using microcontact printing to pattern the attachment of mammalian cells to self-assembled monolayers of alkanethiolates on transparent films of gold and silver (1997) Exp Cell Res, 235, pp. 305-313; 
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Willey, T.M., Vance, A.L., Van Buuren, T., Bostedt, C., Terminello, L.J., Fadley, C.S., Rapid degradation of alkanethiol-based self-assembled monolayers on gold in ambient laboratory conditions (2005) Surf Sci, 576, pp. 188-196; 
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},
	month = {2010///},
	pages = {833 - 843},
	abstract = {The stability of self-assembled monolayers (SAMs) of different functionalities (CH                        3
},
	keywords = {Animals, article, Binding energy, Biological conditions, Biological studies, Body fluids, Cattle, Cell culture, Culture Media, Ethanol, Female, Fetal bovine serum, In-cell, materials testing, measurement, molecular stability, Nitrogen chamber, nonhuman, Organic polymers, Oxidation, Oxidation-Reduction, Oxidized sulfur, Photodegradation, Photoelectron spectroscopy, Sams, self assembled monolayer, Self assembled monolayers, Self-assembled monolayers, Stability, Storage condition, Sulfhydryl Compounds, Sulfur, Surface Properties, Water, wettability, X ray photoelectron spectroscopy, XPS, XPS spectra},
	isbn = {15493296 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-77954806701\&partnerID=40\&md5=9c561e8b43c045cdeb8d80a42148c6ca},
	author = {Maciel, J. and Martins, M.C.L. and Barbosa, M.A.}
}
@article {2275,
	title = {Targeted gene delivery into peripheral sensorial neurons mediated by self-assembled vectors composed of poly(ethylene imine) and tetanus toxin fragment c},
	journal = {Journal of Controlled ReleaseJ. Control. Release},
	volume = {143},
	year = {2010},
	note = {Cited By (since 1996): 13Export Date: 21 November 2012Source: ScopusCODEN: JCREEdoi: 10.1016/j.jconrel.2010.01.018PubMed ID: 20093157Language of Original Document: EnglishCorrespondence Address: P{\^e}go, A.P.; INEB-Instituto de Engenharia Biom{\'e}dica, Divis{\~a}o de Biomateriais, Universidade do Porto, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: apego@ineb.up.ptChemicals/CAS: DNA, 9007-49-2; macrogol, 25322-68-3; polyethyleneimine, 74913-72-7; DNA, 9007-49-2; Imines; Peptide Fragments; Polyethylenes; Tetanus Toxin; poly(ethylene imine); tetanus toxin fragment CReferences: Rodriguez, F.J., Valero-Cabre, A., Navarro, X., Regeneration and functional recovery following peripheral nerve injury (2004) Drug Discov. Today, 1 (2), pp. 177-185;Sahenk, Z., Neurotrophins and peripheral neuropathies (2006) Brain Pathol., 16 (4), pp. 311-319; 
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},
	month = {2010///},
	pages = {350 - 358},
	abstract = {A simple, safe and efficient system that can specifically transfect peripheral sensorial neurons can bring new answers to address peripheral neuropathies. A multi-component non-viral gene delivery vector targeted to peripheral nervous system cells was developed, using poly(ethylene imine) (PEI) as starting material. A binary DNA/polymer complex based on thiolated PEI (PEISH) was optimized, considering complex size and zeta potential and the ability to transfect a sensorial neuron cell line (ND7/23). The 50. kDa non-toxic fragment from tetanus toxin (HC), which has been previously shown to interact specifically with peripheral neurons and to undergo retrograde transport, was grafted to the complex core via a bifunctional PEG (HC-PEG) reactive for the thiol moieties present in the complex surface. Several formulations of HC-PEG ternary complexes were tested for targeting, by assessing the extent of cellular internalization and levels of transfection, in both the ND7/23 and NIH 3 T3 (fibroblast) cell lines. Targeted gene transfer to the neuronal cell line was observed for the complex formulations containing 5 and 7.5. Μg of HC-PEG. Finally, our results demonstrate that the developed ternary vectors are able to transfect primary cultures of dorsal root ganglion dissociated neurons in a targeted manner and elicit the expression of a relevant neurotrophic factor. {\textcopyright} 2010 Elsevier B.V.},
	keywords = {Aberrations, animal cell, Animals, article, Bifunctional, Cell culture, Cell Line, Tumor, Cell lines, cell strain 3T3, Cells, Cultured, Cellular internalization, Chemical modification, Complex cores, Complex formulations, Complex surface, controlled study, DNA, DNA protein complex, Dorsal root ganglia, Efficient systems, embryo, Ethylene, Female, Gene transfer, genetic transfection, Imines, internalization, macrogol, Mice, mouse, Multicomponents, nanoparticle, nanoparticles, neuroblastoma cell, Neuronal cell, Neurons, neurotrophic factor, Neurotrophic factors, NIH 3T3 Cells, Nitrogen compounds, Non-viral, Non-viral gene delivery, nonhuman, Nonviral, nonviral gene delivery system, Nucleic acids, Particle Size, Peptide Fragments, Peripheral nervous system, Peripheral neuropathy, Plasmids, Polyethylene Glycols, Polyethylene oxides, Polyethyleneimine, Polyethylenes, Primary culture, priority journal, process optimization, protein expression, rat, Rats, Rats, Wistar, Regenerative Medicine, Self-assembled, sensory nerve cell, spinal ganglion, Starting materials, Targeted, Targeted gene delivery, Ternary complex, Ternary vectors, Tetanus toxin, tetanus toxin fragment c, Transfection, unclassified drug, Zeta potential},
	isbn = {01683659 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-77952239026\&partnerID=40\&md5=077b03d49cf392defc3d0c77f2f249d1},
	author = {Oliveira, H. and Fernandez, R. and Pires, L.R. and Martins, M.C.L. and Sim{\~o}es, S. and Barbosa, M.A. and P{\^e}go, A.P.}
}
@article {2323,
	title = {The correlation between the adsorption of adhesive proteins and cell behaviour on hydroxyl-methyl mixed self-assembled monolayers},
	journal = {BiomaterialsBiomaterials},
	volume = {30},
	year = {2009},
	note = {Cited By (since 1996): 41Export Date: 21 November 2012Source: ScopusCODEN: BIMADdoi: 10.1016/j.biomaterials.2008.09.048PubMed ID: 18952279Language of Original Document: EnglishCorrespondence Address: Barrias, C.C.; INEB - Instituto de Engenharia Biom{\'e}dica, Divis{\~a}o de Biomateriais, Universidade do Porto, R. Campo Alegre 823, 4150-180 Porto, Portugal; email: ccbarrias@ineb.up.ptChemicals/CAS: fibronectin, 86088-83-7; gold, 7440-57-5; thiol derivative, 13940-21-1; Biocompatible Materials; Fibronectins; VitronectinReferences: Wilson, C.J., Clegg, R.E., Leavesley, D.I., Pearcy, M.J., Mediation of biomaterial-cell interactions by adsorbed proteins: a review (2005) Tissue Eng, 11, pp. 1-18;Garc{\'\i}a, A.J., Vega, M.D., Boettiger, D., Modulation of cell proliferation and differentiation through substrate-dependent changes in fibronectin conformation (1999) Mol Biol Cell, 10, pp. 785-798; 
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},
	month = {2009///},
	pages = {307 - 316},
	abstract = {The objective of this study was to compare the biological effects of two key cell-adhesive proteins, fibronectin (FN) and vitronectin (VN), upon adsorption onto molecularly-designed model surfaces. Single-component and mixed self-assembled monolayers (SAMs) of alkanethiols on gold with OH and CH                        3 terminal groups were prepared at 100\%, 65\%, 36\% and 0\% of OH at the surface, to generate a range of surfaces with a simple chemistry and a wettability gradient. FN and VN were adsorbed under non-competitive (single-protein solutions) and competitive (multi-protein solutions) conditions, and compared at different levels: adsorbed amount (radiolabelling), elution, functional presentation of cell-binding domains (ELISA), and role in mediating cell adhesion (antibody-based assay). The observed trends were related to mesenchymal stem cell response in terms of adhesion and overall cell morphology. Under non-competitive conditions, adsorption of both proteins increased with surface hydrophobicity. The presence of competitive proteins significantly decreased the adsorbed amounts, although both proteins were still detected in all SAMs. Adsorption of FN followed a trend similar to that of non-competitive conditions, while adsorption of VN was higher on 100\%OH-SAMs. Concerning elution, retention of adsorbed VN was always higher than that of FN. For both proteins, functional presentation of cell-binding domains was more effective on the more hydrophilic 100\%OH-SAMs. This fact, coupled to the ability of this type of SAMs to selectively recruit and retain VN in the presence of competitive serum proteins, seems to correlate with the better cell response observed on these surfaces, as compared with hydrophobic 0\%OH(100\%CH
                        3)-SAMs. {\textcopyright} 2008 Elsevier Ltd. All rights reserved.
},
	keywords = {Adhesion, Adhesiveness, Adsorption, alkane, Animals, article, Biocompatible Materials, Biological Assay, bone marrow, Cattle, cell adhesion, Cell culture, Cell Movement, Cells, Cells, Cultured, cytology, cytoskeleton, Electric currents, Electron energy levels, enzyme linked immunosorbent assay, Fibronectin, Fibronectins, Focal adhesions, Functional groups, Functionalization, gold, human, human cell, Humans, hydrophilicity, hydrophobicity, Hydroxylation, isotope labeling, Mesenchymal stem cell, Mesenchymal Stem Cells, Microscopy, Confocal, Missile bases, Molecular interactions, monoclonal antibody, priority journal, Protein adsorption, protein analysis, protein binding, Protein Structure, Tertiary, Proteins, Self assembled monolayers, Self-assembled monolayers, stem cell, Stem cells, Surface Properties, thiol derivative, Vitronectin},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-55249093830\&partnerID=40\&md5=132fa4efe300c4f76764942bfe3bce30},
	author = {Barrias, C.C. and Martins, M.C.L. and Almeida-Porada, G. and Barbosa, M.A. and Granja, P.L.}
}
@article {2305,
	title = {The effect of the co-immobilization of human osteoprogenitors and endothelial cells within alginate microspheres on mineralization in a bone defect},
	journal = {BiomaterialsBiomaterials},
	volume = {30},
	year = {2009},
	note = {Cited By (since 1996): 38Export Date: 21 November 2012Source: ScopusCODEN: BIMADdoi: 10.1016/j.biomaterials.2009.02.033PubMed ID: 19299013Language of Original Document: EnglishCorrespondence Address: Grellier, M.; INSERM, U577, Universit{\'e} Victor Segalen Bordeaux 2, UMR-S577, F-33076 Bordeaux Cedex, France; email: maritie.grellier@inserm.frChemicals/CAS: alginic acid, 28961-37-7, 29894-36-8, 9005-32-7, 9005-38-3; alkaline phosphatase, 9001-78-9; arginylglycylaspartic acid, 99896-85-2; osteocalcin, 136461-80-8; Alginates; Glucuronic Acid, 576-37-4; Hexuronic Acids; alginic acid, 9005-32-7References: Oreffo, R.O., Triffitt, J.T., Future potentials for using osteogenic stem cells and biomaterials in orthopedics (1999) Bone, 25 (2 SUPPL), pp. 5S-9S;Lubiatowski, P., Kruczynski, J., Gradys, A., Trzeciak, T., Jaroszewski, J., Articular cartilage repair by means of biodegradable scaffolds (2006) Transplant Proc, 38 (1), pp. 320-322; 
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},
	month = {2009///},
	pages = {3271 - 3278},
	abstract = {Bone regeneration seems to be dependant on cell communication between osteogenic and endothelial cells arising from surrounding blood vessels. This study aims to determine whether endothelial cells can regulate the osteogenic potential of osteoprogenitor cells in vitro and in vivo, in a long bone defect, when co-immobilized in alginate microspheres. Alginate is a natural polymer widely used as a biomaterial for cell encapsulation. Human osteoprogenitors (HOP) from bone marrow mesenchymal stem cells were immobilized alone or together with human umbilical vein endothelial cells (HUVEC) inside irradiated, oxidized and RGD-grafted alginate microspheres. Immobilized cells were cultured in dynamic conditions and cell metabolic activity increased during three weeks. The gene expression of alkaline phosphatase and osteocalcin, both specific markers of the osteoblastic phenotype, and mineralization deposits were upregulated in co-immobilized HOPs and HUVECs, comparing to the immobilization of monocultures. VEGF secretion was also increased when HOPs were co-immobilized with HUVECs. Microspheres containing co-cultures were further implanted in a bone defect and bone formation was analysed by μCT and histology at 3 and 6 weeks post-implantation. Mineralization was observed inside and around the implanted microspheres containing the immobilized cells. However, when HOPs were co-immobilized with HUVECs, mineralization significantly increased. These findings demonstrate that co-immobilization of osteogenic and endothelial cells within RGD-grafted alginate microspheres provides a promising strategy for bone tissue engineering. {\textcopyright} 2009 Elsevier Ltd. All rights reserved.},
	keywords = {adult, aged, Alginate, Alginates, alginic acid, alkaline phosphatase, animal tissue, Animals, arginylglycylaspartic acid, article, Bioactivity, Biopolymers, Blood vessel prostheses, Blood Vessels, Bone, Bone and Bones, bone defect, Bone defects, Bone formations, Bone marrow mesenchymal stem cells, bone mineralization, Bone Regeneration, Bone regenerations, bone tissue, Bone tissue engineerings, Calcification, Physiologic, Cell communications, Cell culture, Cell encapsulations, cell function, cell growth, Cell immobilization, Cell membranes, cell metabolism, Cells, Cultured, Co immobilizations, Co-culture, coculture, computer assisted tomography, controlled study, Defects, Dynamic conditions, Endothelial Cells, endothelium cell, gene expression, gene expression regulation, Glucuronic Acid, Grafting (chemical), Hexuronic Acids, histology, human, human cell, Human umbilical vein endothelial cells, Humans, Humulus, immobilized cell, Immobilized cells, in vitro study, in vivo study, In-vitro, In-vivo, irradiation, long bone, Long bones, Mesenchymal stem cell, Metabolic activities, Mice, Mice, Nude, microsphere, Microspheres, Middle Aged, Mineralogy, monoculture, mouse, nonhuman, osteoblast, osteocalcin, Osteogenic, Osteogenic potentials, Osteoprogenitor cells, Osteoprogenitors, Oxidation, Peptides, phenotype, Post implantations, priority journal, Self assembly, Sodium compounds, stem cell transplantation, Stem cells, Tissue engineering, umbilical vein, upregulation, Vascular endothelial growth factor (VEGF), X ray analysis, Young Adult},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-67349213598\&partnerID=40\&md5=0190ab2a91dc0dc3527ffd9f86fabf63},
	author = {Grellier, M. and Granja, P.L. and Fricain, J.-C. and Bidarra, S.J. and Renard, M. and Bareille, R. and Bourget, C. and Am{\'e}d{\'e}e, J. and Barbosa, M.A.}
}
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Oliveira, S.M., Turner, G., Mijares, D., Amaral, I.F., Barbosa, M.A., Teixeira, C.C., (2007) Engineering endochondral bone: In vivo studies
},
	month = {2009///},
	pages = {625 - 634},
	abstract = {Chitosan scaffolds have been shown to possess biological and mechanical properties suitable for tissue engineering and clinical applications. In the present work, chitosan sponges were evaluated regarding their ability to support cartilage cell proliferation and maturation, which are the first steps in endochondral bone formation. Chitosan sponges were seeded with chondrocytes isolated from chicken embryo sterna. Chondrocyte/chitosan constructs were cultured for 20 days, and treated with retinoic acid (RA) to induce chondrocyte maturation and matrix synthesis. At different time points, samples were collected for microscopic, histological, biochemical, and mechanical analyses. Results show chondrocyte attachment, proliferation, and abundant matrix synthesis, completely obliterating the pores of the sponges. RA treatment caused chondrocyte hypertrophy, characterized by the presence of type X collagen in the extracellular matrix and increased alkaline phosphatase activity. In addition, hypertrophy markedly changed the mechanical properties of the chondrocyte/chitosan constructs. In conclusion, we have developed chitosan sponges with adequate pore structure and mechanical properties to serve as a support for hypertrophic chondrocytes. In parallel studies, we have evaluated the ability of this mature cartilage scaffold to induce endochondral ossification. {\textcopyright} Copyright 2009, Mary Ann Liebert, Inc. 2009.},
	keywords = {alkaline phosphatase, Alkaline phosphatase activity, animal, animal cell, animal tissue, Animals, article, biomechanics, Body fluids, Bone, Bone and Bones, Bone formation, Cartilage, cartilage cell, Cell culture, cell damage, cell hypertrophy, cell isolation, cell maturation, Cell membranes, cell proliferation, Cells, Cultured, chick embryo, Chicken embryo, Chitin, chitosan, Chitosan scaffold, Chondrocyte, Chondrocyte maturation, Chondrocytes, Clinical application, collagen type 10, Collagen Type X, controlled study, cytology, DNA, drug effect, embryo, enchondral ossification, Endochondral ossification, enzyme activity, enzymology, Extracellular matrices, extracellular matrix, gene expression profiling, Hypertrophic chondrocytes, in vitro study, In-vitro, Ligaments, Matrix synthesis, Mechanical analysis, Mechanical properties, metabolism, methodology, nonhuman, Pathology, physiology, Porifera, porosity, priority journal, retinoic acid, Retinoic acids, Scaffolds, sponge (Porifera), Sterna, sternum, synthesis, Time points, Tissue engineering, tissue scaffold, Tissue Scaffolds, Tretinoin, Type X collagen},
	isbn = {19373341 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-64549143844\&partnerID=40\&md5=310f8e62d4dd51ccb9399db171440148},
	author = {Oliveira, S.M. and Amaral, I.F. and Barbosa, M.A. and Teixeira, C.C.}
}
@article {2317,
	title = {Engineering endochondral bone: In vivo studies},
	journal = {Tissue Engineering - Part ATissue Eng. Part A},
	volume = {15},
	year = {2009},
	note = {Cited By (since 1996): 14Export Date: 21 November 2012Source: Scopusdoi: 10.1089/ten.tea.2008.0052Language of Original Document: EnglishCorrespondence Address: Teixeira, C. C.; Department of Basic Science and Craniofacial Biology, College of Dentistry, New York University, 345 East. 24th St., New York, NY 10010; email: ct40@nyu.eduChemicals/CAS: chitosan, 9012-76-4; Chitosan, 9012-76-4; MineralsReferences: Yelin, E., Callahan, L.F., The economic cost and social and psychological impact of musculoskeletal conditions. National Arthritis Data Work Groups (1995) Arthritis Rheum, 38, p. 1351;Service, R.F. Tissue engineers build new bone. Science 289,1498, 2000Dupraz, A., Delecrin, J., Moreau, A., Pilet, P., Passuti, N., Long-term bone response to particulate injectable ceramic (1998) J Biomed Mater Res, 42, p. 368; 
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},
	month = {2009///},
	pages = {635 - 643},
	abstract = {The use of biomaterials to replace lost bone has been a common practice for decades. More recently, the demands for bone repair and regeneration have pushed research into the use of cultured cells and growth factors in association with these materials. Here we report a novel approach to engineer new bone using a transient cartilage scaffold to induce endochondral ossification. Chondrocyte/chitosan scaffolds (both a transient cartilage scaffold- experimental-and a permanent cartilage scaffold-control) were prepared and implanted subcutaneously in nude mice. Bone formation was evaluated over a period of 5 months. Mineralization was assessed by Faxitron, micro computed tomography, backscatter electrons, and Fourier transform infrared spectroscopy analyses. Histological analysis provided further information on tissue changes in and around the implanted scaffolds. The deposition of ectopic bone was detected in the surface of the experimental implants as early as 1 month after implantation. After 3 months, bone trabeculae and bone marrow cavities were formed inside the scaffolds. The bone deposited was similar to the bone of the mice vertebra. Interestingly, no bone formation was observed in control implants. In conclusion, an engineered transient cartilage template carries all the signals necessary to induce endochondral bone formation in vivo. {\textcopyright} Copyright 2009, Mary Ann Liebert, Inc. 2009.},
	keywords = {animal, animal experiment, animal tissue, Animals, article, Biological materials, Biomaterials, Bone, Bone and Bones, Bone formation, bone marrow, bone mineralization, Bone repair, bone transplantation, Calcification, Physiologic, Cartilage, cartilage cell, chick embryo, chitosan, Chondrocytes, Computerized tomography, controlled study, Cultured cell, cytology, drug effect, Ectopic bones, ectopic tissue, electron, enchondral ossification, Endochondral ossification, Fourier transform infrared spectroscopy, Growth (materials), Growth factor, Histological analysis, histology, implantation, in vivo study, In-control, In-vivo, infrared spectroscopy, Ligaments, male, metabolism, methodology, Mice, Mice, Nude, micro-computed tomography, Microcomputed tomography, Microscopy, Electron, Scanning, mineral, Minerals, mouse, Mus, Mus musculus, nonhuman, Nude mice, nude mouse, ossification, physiology, priority journal, Prosthesis Implantation, Scaffolds, Scanning electron microscopy, Spectroscopic analysis, Spectroscopy, Spectroscopy, Fourier Transform Infrared, Tissue changes, Tissue engineering, tissue scaffold, Tissue Scaffolds, Tomography, trabecular bone, vertebra},
	isbn = {19373341 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-64549096039\&partnerID=40\&md5=d389cb8b10be8945007a5b6996b8896f},
	author = {Oliveira, S.M. and Mijares, D.Q. and Turner, G. and Amaral, I.F. and Barbosa, M.A. and Teixeira, C.C.}
}
@article {2297,
	title = {Fibronectin-mediated endothelialisation of chitosan porous matrices},
	journal = {BiomaterialsBiomaterials},
	volume = {30},
	year = {2009},
	note = {Cited By (since 1996): 8Export Date: 21 November 2012Source: ScopusCODEN: BIMADdoi: 10.1016/j.biomaterials.2009.06.056PubMed ID: 19615736Language of Original Document: EnglishCorrespondence Address: Amaral, I.F.; INEB - Instituto de Engenharia Biom{\'e}dica, Divis{\~a}o de Biomateriais, Universidade do Porto, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: iamaral@ineb.up.ptChemicals/CAS: chitosan, 9012-76-4; fibronectin, 86088-83-7; Biocompatible Materials; Chitosan, 9012-76-4; FibronectinsReferences: Moon, J.J., West, J.L., Vascularization of engineered tissues: approaches to promote angiogenesis in biomaterials (2008) Current Topics in Medicinal Chemistry, 8 (4), pp. 300-310;Blitterswijk, C.A., Moroni, L., Rouwkema, J., Siddappa, R., Sohier, J., Tissue engineering - an introduction (2008) Tissue engineering, , Blitterswijk C.A. (Ed), Elsevier; 
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},
	month = {2009///},
	pages = {5465 - 5475},
	abstract = {Chitosan (Ch) porous matrices were investigated regarding their ability to be colonized by human microvascular endothelial cells (HPMEC-ST1.6R cell line) and macrovascular endothelial cells namely HUVECs. Specifically we assessed if previous incubation of Ch in a fibronectin (FN) solution was effective in promoting endothelial cell (EC) adhesion to Ch matrices with different degrees of acetylation (DAs). Upon FN physiadsorption, marked differences were found between the two DAs investigated, namely DA 4\% and 15\%. While cell adhesion was impaired on Ch with DA 15\%, ECs were able to not only adhere to Ch with DA 4\%, but also to spread and colonize the scaffolds, with retention of the EC phenotype and angiogenic potential. To explain the observed differences between the two DAs, protein adsorption studies using                        125I-FN and immunofluorescent labelling of FN cell-binding domains were carried out. In agreement with the higher cell numbers found, scaffolds with DA 4\% revealed a higher number of exposed FN cell-binding domains as well as greater ability to adsorb FN and to retain and exchange adsorbed FN in the presence of competitive proteins. These findings suggest that the DA is a key parameter modulating EC adhesion to FN-coated Ch by influencing the adsorbed protein layer. {\textcopyright} 2009 Elsevier Ltd. All rights reserved.
},
	keywords = {Acetylation, Adhesion, Adsorption, angiogenesis, article, Biocompatible Materials, Blood vessel prostheses, cell adhesion, Cell culture, cell invasion, Cell Line, Cell lines, Cell membranes, Cell number, cell proliferation, Cell size, cell spreading, cell survival, Cell-binding domain, Chitin, Chitin/chitosan, chitosan, colony formation, controlled study, Degrees of acetylation, Electric conductivity measurement, Electric currents, Endothelial cell, Endothelial Cells, Endothelialisation, endothelium, endothelium cell, epithelization, Fibronectin, Fibronectins, human, human cell, Human microvascular endothelial cells, Humans, immunofluorescence test, Key parameters, Labels, materials testing, Matrix algebra, Neovascularization, Physiologic, phenotype, porosity, Porous matrixs, priority journal, Protein adsorption, Protein layers, Scaffold, Scaffolds, Self assembly, Tissue engineering, tissue scaffold, umbilical vein},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-68549107574\&partnerID=40\&md5=9babb57c1a4f2ae6eb7e7e0643bffe48},
	author = {Amaral, I.F. and Unger, R.E. and Fuchs, S. and Mendon{\c c}a, A.M. and Sousa, S.R. and Barbosa, M.A. and P{\^e}go, A.P. and Kirkpatrick, C.J.}
}
@article {2296,
	title = {Improving chitosan-mediated gene transfer by the introduction of intracellular buffering moieties into the chitosan backbone},
	journal = {Acta BiomaterialiaActa Biomater.},
	volume = {5},
	year = {2009},
	note = {Cited By (since 1996): 17Export Date: 21 November 2012Source: Scopusdoi: 10.1016/j.actbio.2009.04.021PubMed ID: 19427930Language of Original Document: EnglishCorrespondence Address: P{\^e}go, A.P.; INEB-Instituto de Engenharia Biom{\'e}dica, Divis{\~a}o de Biomateriais, Universidade do Porto, Rua do Campo Alegre 823, 4150-180 Porto, Portugal; email: apego@ineb.up.ptChemicals/CAS: DNA, 9007-49-2; chitosan, 9012-76-4; imidazole, 1467-16-9, 288-32-4; Biocompatible Materials; Buffers; Chitosan, 9012-76-4; DNA, 9007-49-2; Drug CarriersReferences: Kirkpatrick, C.J., Fuchs, S., Peters, K., Brochhausen, C., Hermanns, M.I., Unger, R.E., Visions for regenerative medicine: interface between scientific fact and science fiction (2006) Artif Organs, 30, pp. 822-827;Sim{\~o}es, S., Filipe, A., Faneca, H., Mano, M., Penacho, N., Duzgunes, N., Cationic liposomes for gene delivery (2005) Expert Opin Drug Deliv, 2, pp. 237-254; 
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},
	month = {2009///},
	pages = {2995 - 3006},
	abstract = {Chitosan was functionalized with imidazole moieties (CHimi) with the aim of improving its buffering capacity and promoting the endosomal escape ability of chitosan-DNA complexes, ultimately increasing their transfection efficiency. 5.6\%, 12.9\% and 22.1\% of the glucosamine residues of chitosan were substituted. Complexes with different molar ratios of primary amines to DNA phosphate anion (N/P) were prepared by a coacervation method. For an N/P \&gt; 3, CHimi polymers are able to complex electrostatically with DNA and condense it into positively charged nanostructures (average size 260 nm and zeta potential +16 mV at pH 5.5). In the concentration range 2.5-100 μg ml},
	keywords = {article, beta galactosidase, Biocompatible Materials, Buffers, Cell Line, cell transport, Chemical structure, chitosan, coacervation, complex formation, controlled study, Cytotoxicity, Diffusion, DNA, Drug Carriers, Drug Compounding, endosome, Gene delivery, Gene transfer, genetic transfection, human, human cell, Humans, imidazole, Kidney, materials testing, nanomaterial, nanoparticle, priority journal, protein expression, proton transport, Tissue engineering, Transfection},
	isbn = {17427061 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-70349162856\&partnerID=40\&md5=fb6672dd0cf06d6ced21eec115b597d2},
	author = {Moreira, C. and Oliveira, H. and Pires, L.R. and Sim{\~o}es, S. and Barbosa, M.A. and P{\^e}go, A.P.}
}
@article {2291,
	title = {Induction of notch signaling by immobilization of jagged-1 on self-assembled monolayers},
	journal = {BiomaterialsBiomaterials},
	volume = {30},
	year = {2009},
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},
	month = {2009///},
	pages = {6879 - 6887},
	abstract = {Notch signaling is a key mechanism during mammal development and stem cell regulation. This study aims to target and control Notch signaling by ligands immobilization using self-assembled monolayers (SAMs) as model surfaces. Non-fouling substrates were prepared by immersion of gold substrates in (1-Mercapto-11-undecyl)tetra(ethylene glycol) thiol solutions. These surfaces were activated with N,N'-carbonyldiimidazole (CDI) at different concentrations (0, 0.03, 0.3, 3 and 30 mg/ml) and an anti-human IgG, Fc specific fragment antibody (Ab) was covalently bound to EG4-SAMs to guarantee the correct exposure of the Notch ligand Jagged-1/Fc chimera (Jag-1). The presence of Ab and Jag-1 was confirmed by radiolabeling, X-ray photoelectron spectroscopy (XPS), ellipsometry and ELISA. The biological activity of Jag-1-Ab-SAMs was assessed by real-time PCR for Hes-1 family gene expression, a Notch pathway target gene, in HL-60 cell line. Results have shown an increase of the amount of immobilized Ab with increasing surface activator concentrations. Jag-1 concentration also increases with Ab concentration. Interestingly, a higher Jagged-1 exposure and fold increase in Hes-1 expression were obtained for surfaces activated with the lowest concentration of CDI (0.03 mg/ml). These results illustrate the great importance of ligands orientation and exposure, when compared with density. This investigation brings new insights into Notch signaling mechanisms. In particular, Jag-1-Ab-SAMs have shown to be adequate model surfaces to study Notch pathway activation and may provide a basis to develop new interfaces in biomaterials to control Notch mechanism in different cell systems. {\textcopyright} 2009 Elsevier Ltd.},
	keywords = {Activator concentration, Adequate models, Adsorption, Animals, article, Bioactivity, Biological activities, Biological materials, biomaterial, Calcium-Binding Proteins, Carbonyldiimidazole, Cell culture, Cell Line, Cell membranes, cell strain HL 60, Cell system, Chemical activation, Concentration (process), Concentration of, controlled study, Covalently bound, Ethylene, Ethylene Glycol, gene expression, gold, Gold substrates, HL-60 cell line, human, human cell, Human IgG, Humans, Immunoassay, immunoglobulin Fc fragment, Immunoglobulin G, immunoglobulin G antibody, Intercellular Signaling Peptides and Proteins, Jagged1, Ligands, Mammalia, Membrane Proteins, Model surface, Molecular Structure, Nanostructured materials, Nanostructured surfaces, Nonfouling, Notch receptor, Notch signaling, Photoelectron spectroscopy, priority journal, Protein adsorption, protein immobilization, Radiolabeling, Real-time PCR, Receptors, Fc, Receptors, Notch, Recombinant Fusion Proteins, Sams, self assembled monolayer, Self assembled monolayers, Self-assembled monolayers, signal transduction, Signaling, stem cell, Surface Properties, Target genes, Tetra, transcription factor HES 1, X ray photoelectron spectroscopy},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-70350188310\&partnerID=40\&md5=6c55d29cf8ae55288f3e87880171ec70},
	author = {Gon{\c c}alves, R.M. and Martins, M.C.L. and Almeida-Porada, G. and Barbosa, M.A.}
}
@article {2325,
	title = {Molecularly designed surfaces for blood deheparinization using an immobilized heparin-binding peptide},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {88},
	year = {2009},
	note = {Cited By (since 1996): 12Export Date: 21 November 2012Source: ScopusCODEN: JBMRCdoi: 10.1002/jbm.a.31849PubMed ID: 18286636Language of Original Document: EnglishCorrespondence Address: Martins, M. C. L.; INEB - Instituto de Engenharia Biom{\'e}dica, Divis{\~a}o de Biomaterials, Universidade do Porto, Rua do Campo Alegre, 823, 4150-180, Porto, Portugal; email: cmartins@ineb.up.ptChemicals/CAS: carbonyldiimidazole, 530-62-1; heparin, 37187-54-5, 8057-48-5, 8065-01-8, 9005-48-5; imidazole, 1467-16-9, 288-32-4; leucine, 61-90-5, 7005-03-0; lysine, 56-87-1, 6899-06-5, 70-54-2; tetraethylene glycol, 112-60-7; Ethylene Glycol, 107-21-1; Heparin, 9005-49-6; Leucine, 61-90-5; Lysine, 56-87-1; PeptidesReferences: Dailey J. Blood. Ipswich, MA, USA: Medical Consulting Group; 1998Section, V., Chronic intermittent haemodialysis and prevention of clotting in the extracorporal system (2002) Nephrol Dialysis Transplant, 17, pp. 63-71;Zhang, Y.H., Singh, V.K., Yang, V.C., Novel approach for optimizing the capacity and efficacy of a protamine filter for clinical extracorporeal heparin removal (1998) Asaio J, 44, pp. M368-M373; 
Tao, W., Deyo, D.J., Brunston, R.L., Vertrees, R.A., Zwischenberger, J.B., Extracorporeal heparin adsorption following cardiopulmonary bypass with a heparin removal device - An alternative to protamine (1998) Critical Care Med, 26, pp. 1096-1102; 
Ameer, G.A., Barabino, G., Sasisekharan, R., Harmon, W., Cooney, C.L., Langer, R., Ex vivo evaluation of a Taylor-Couette flow, immobilized heparinase I device for clinical application (1999) Proc Natl Acad Sci USA, 96, pp. 2350-2355; 
Ostuni, E., Yan, L., Whitesides, G.M., The interaction of proteins and cells with self-assembled monolayers of alkanethiolates on gold and silver (1999) Colloids Surf B-Biointerfaces, 15, pp. 3-30; 
Mrksich, M., Whitesides, G.M., Using self-assembled monolayers that present oligo(ethylene glycol) groups to control the interactions of proteins with surfaces. Poly(Ethylene Glycol) (1997) ACS Symposium Series, 680, pp. 361-373; 
Cardin, A.D., Weintraub, H.J.R., Molecular modeling of proteinglycosaminoglycan interactions (1989) Arteriosclerosis, 9, pp. 21-32; 
Kricheldorf, H.R., (1987) α-Amino Acid N-Carboxyanhydrides and Related Heterocycles, , New York: Springer Verlag;; 
Martins, M.C.L., Ratner, B.D., Barbosa, M.A., Protein adsorption on mixtures of hydroxyl- and methylterminated alkanethiols self-assembled monolayers (2003) J Biomed Mater Res A, 67, pp. 158-171; 
Lee, H.J., Nedelkov, D., Corn, R.M., Surface plasmon resonance imaging measurements of antibody arrays for the multiplexed detection of low molecular weight protein biomarkers (2006) Anal Chem, 78, pp. 6504-6510; 
Roeges, N.P.G., (1994) A Guide to the Complete Interpretation of Infrared Spectra of Organic Structures, , England: Wiley;; 
Li, L.Y., Chen, S.F., Zheng, J., Ratner, B.D., Jiang, S.Y., Protein adsorption on oligo(ethylene glycol)-terminated alkanethiolate self-assembled monolayers: The molecular basis for non-fouling behavior (2005) J Phys Chem B, 109, pp. 2934-2941; 
Beamson, G., High, B.D., (1992) Resolution XPS of Organic Polymers, , Chichester: Wiley;; 
Sousa, S.R., Moradas, F.P., Saramago, B., Viseu, M.L., Barbosa, M.A., Human serum albumin adsorption on TiO2 from single protein solutions and from plasma (2004) Langmuir, 20, pp. 9745-9754; 
Socrates, G., (2001) Infrared and Raman Characteristic Group Frequencies: Tables and Charts, , Chichester: Wiley;; 
Capila, I., Linhardt, R.J., Heparin - Protein interactions (2002) Angewandte Chemie-Int Ed, 41, pp. 391-112; 
Snell, C.R.F.G., Kinetics and thermodynamics of the alpha Helix - β Transconformation of poly(L-lysine) and L-leucine copolymers. A compensation phenomenon (1973) Biochemistry, 12, pp. 1017-1025; 
Hearn, M.T.W., 1,1'-Carbonyldiimidazole-mediated immobilization of enzymes and affinity ligands (1987) Methods Enzymol, 135, pp. 102-117; 
Stollner, D., Scheller, F.W., Warsinke, A., Activation of cellulose membranes with 1,1'-carbonyldiimidazole or 1-cyano-4-dimethylaminopyridinium tetrafluoroborate as a basis for the development of immunosensors (2002) Anal Biochem, 304, pp. 157-165
},
	month = {2009///},
	pages = {162 - 173},
	abstract = {Systemic heparinization, used during haemodialysis to prevent blood clotting on the extracorporeal circuit, leads to a high incidence of hemorrhagic complications. The adverse reactions associated with heparin neutralization using protamine sulphate justify the development of an alternative system for blood deheparinization. The main objective of this work is to design nanostructured surfaces with the capacity to bind heparin from blood in a selective way. A heparin-binding polypeptide, composed of L-lysine and L-leucine (pKL), was synthesized and immobilized, in different concentrations, onto self-assembled monolayers (SAMs) terminated with tetra(ethylene-glycol) (EG4 SAMs). Immobilization was performed using a fixed concentration of pKL after surface activation to different degrees using a range of CDI (N,N'-carbonyldiimidazole) concentrations. Results demonstrated that the presence of pKL increases heparin adsorption to EG4-SAMs, independently of the pKL concentration and the way of immobilization (adsorption or covalent bound). Selectivity towards heparin was successfully achieved on SAMs with low concentrations of immobilized pKL (9-17\% of pKL). Surfaces were characterized using ellipsometry, contact angle measurements, Fourier transform infrared reflection absorption spectroscopy (IRAS), atomic force microscopy, and X-ray photoelectron spectroscopy. Heparin adsorption was assessed using IRAS and N-sulphonate-                        35S-heparin. Therefore, this study could give a good contribution for the design of blood deheparinization devices. {\textcopyright} 2008 Wiley Periodicals, Inc.
},
	keywords = {Absorption spectroscopy, Adsorption, Alternative systems, Amines, Amino acids, Angle measurement, article, Atomic force microscopy, Atomic forces, Atomic spectroscopy, Binding peptides, Blood, Blood clotting, Carbonyl diimidazole, Carbonyldiimidazole, Contact angle, deheparinization, device, Dialysis, Electron energy levels, ellipsometry, Ethylene, Ethylene Glycol, Fourier Transform Infrared, Fourier transforms, Glycols, Haemodialysis, heparin, heparin binding protein, Heparinization, High incidences, Humans, imidazole, immobilization, infrared spectroscopy, leucine, Low concentrations, lysine, Methods, Missile bases, Monolayers, nanomaterial, Nanostructured surfaces, Nanostructures, Peptide immobilization, Peptides, Photoelectron spectroscopy, Polysaccharides, Protein adsorption, protein binding, Renal Dialysis, Self assembled monolayers, Self-assembled monolayers, Sulphate, Surface activations, Surface functionalization, Surface Properties, surface property, tetraethylene glycol, unclassified drug, X ray photoelectron spectroscopy, X-ray photoelectron spectroscopies},
	isbn = {15493296 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-57449118932\&partnerID=40\&md5=8f442ccbde0273f4ed4e04024a75fd37},
	author = {Martins, M.C.L. and Curtin, S.A. and Freitas, S.C. and Salgueiro, P. and Ratner, B.D. and Barbosa, M.A.}
}
@book {2320,
	title = {Morphology and mechanical properties of injectable ceramic microspheres},
	series = {Key Engineering MaterialsKey Eng Mat},
	volume = {396-398},
	year = {2009},
	note = {Cited By (since 1996): 1Export Date: 21 November 2012Source: ScopusCODEN: KEMAEdoi: 10.4028/0-87849-353-0.691Language of Original Document: EnglishCorrespondence Address: Oliveira, S. M.; ESTV, Departamento de Engenharia Mec{\^a}nica, Instituto Polit{\'e}cnico de Viseu, Viseu, PortugalReferences: Barrias, C.C., Ribeiro, C.C., Lamghari, M., Miranda, C.S., Barbosa, M.A., Proliferation, activity, and osteogenic differentiation of bone marrow stromal cells cultured on calcium titanium phosphate microspheres (2005) Journal of Biomedical Materials Research, 72 A (1), pp. 57-66;Barrias, C.C., Ribeiro, C.C., Barbosa, M.A., Adhesion and proliferation of human osteoblastic cells seeded on injectable hydroxyapatite microspheres (2004) Bioceramics, 16, pp. 254-262,877-880; 
Ribeiro, C.C., Barrias, C.C., Barbosa, M.A., Calcium phosphate-alginate microspheres as enzyme delivery matrices (2004) Biomaterials, 25 (18), pp. 4363-4373; 
Silva, R.V., Camilli, J.A., Bertran, C.A., Moreira, N.H., The use of hydroxyapatite and autogenous cancellous bone grafts to repair bone defects in rats (2005) International Journal of Oral and Maxillofacial Surgery, 34 (2), pp. 178-184; 
Boyan, B.D., Lossd{\"o}rfer, S., Wang, L., Zhao, G., Lohmann, C.H., Cochran, D.L., Schwartz, Z., Osteoblasts generate an osteogenic microenvironment when grown on surfaces with rough microtopographies (2003) Eur Cell Mater, 6, pp. 22-27; 
Cardoso, O.N., Sotto Mayor, T., Pinto, A.M.F.R., Campos, J.B.L.M., Axial dispersion of particles in a slugging column - the role of the laminar wake of the bubbles (2003) Chemical Engineering Science, 58 (18), pp. 4159-4172; 
Gauthier, O., Bouler, J.M., Weiss, P., Bosco, J., Aguado, E., Daculsi, G., Short-term effects of mineral particle sizes on cellular degradation activity after implantation of injectable calcium phosphate biomateriais and the consequences for bone substitution (1999) Bone, 25 (2), pp. 71S-74S; 
Xu, H.H., Weir, M.D., Burguera, E.F., Fraser, A.M., Injectable and macroporous calcium phosphate cement scaffold (2006) Biomaterials, 27 (24), pp. 4279-4287; 
Ginebra, M.P., Rilliard, A., Fernandez, E., Elvira, C., San Roman, J., Planell, J.A., Mechanical and rheological improvement of a calcium phosphate cement by the addition of a polymeric drug (2001) J Biomed Mater Res, 57 (1), pp. 113-118
},
	month = {2009///},
	pages = {691 - 694},
	abstract = {The aim of this study was to analyze the effect of starting powder granulometry and sintering conditions on the morphological structure and mechanical properties of injectable hydroxyapaptite (HAp) microspheres. The mechanical properties of the microspheres were evaluated, to investigate if their integrity could be maintained during the injection process. To obtain microspheres, HAp powders were dispersed in a sodium alginate solution and spherical particles were prepared by droplet extrusion under a co-axial air stream, coupled with ionotropic gelation in the presence of Ca                        2+. This was followed by a sintering process at various temperatures and times. The morphology of microspheres was observed under SEM, diameter measurements were performed in an optical microscope and the compression strength was evaluated using a texture analyzer. Finally, microspheres prepared using lower granulometry HAp powders and sintered at 1200{\textdegree}C for 1 hour presented the best properties and were selected as the most suitable for the envisaged application.
},
	keywords = {Air streams, Apatite, Calcium, Ceramic microspheres, Co-axial, Coagulation, Compression strengths, Diameter measurements, Gelation, Granulometry, hydroxyapatite, Injectable, Injection process, Ionotropic gelations, Mechanical properties, Microspheres, Morphological structures, Morphology and mechanical properties, Optical microscopes, Powders, SEM, Sintering, Sintering conditions, Sintering process, Sodium, Sodium alginates, Spherical particles, Starting powders, Texture analyzers},
	isbn = {10139826 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-58849147162\&partnerID=40\&md5=5bf4364653a3ad10b5ab28c1a01568ab},
	author = {Oliveira, S.M. and Barrias, C.C. and Ribeiro, C.C. and Almeida, I.F. and Bahia, M.F. and Barbosa, M.A.}
}
@article {2298,
	title = {Protein adsorption and clotting time of pHEMA hydrogels modified with C18 ligands to adsorb albumin selectively and reversibly},
	journal = {BiomaterialsBiomaterials},
	volume = {30},
	year = {2009},
	note = {Cited By (since 1996): 9Export Date: 21 November 2012Source: ScopusCODEN: BIMADdoi: 10.1016/j.biomaterials.2009.06.025PubMed ID: 19595453Language of Original Document: EnglishCorrespondence Address: Gon{\c c}alves, I.C.; INEB - Instituto de Engenharia Biom{\'e}dica, Divis{\~a}o de Biomateriais, Universidade do Porto, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: icastro@ineb.up.ptChemicals/CAS: fibrinogen, 9001-32-5; human serum albumin, 9048-49-1; polymacon, 25053-81-0, 25249-16-5, 98932-78-6; polystyrene, 9003-53-6; Biocompatible Materials; Coated Materials, Biocompatible; Hydrogels; Polyhydroxyethyl Methacrylate, 25249-16-5; Serum AlbuminReferences: Kottkemarchant, K., Anderson, J.M., Umemura, Y., Marchant, R.E., Effect of albumin coating on the in vitro blood compatibility of dacron arterial prostheses (1989) Biomaterials, 10 (3), pp. 147-155;Ji, J., Feng, L.X., Barbosa, M.A., Stearyl poly(ethylene oxide) grafted surfaces for preferential adsorption of albumin (2001) Biomaterials, 22 (22), pp. 3015-3023; 
Keogh, J.R., Eaton, J.W., Albumin-binding surfaces for biomaterials (1994) The Journal of Laboratory and Clinical Medicine, 124 (4), pp. 537-545; 
Keogh, J.R., Velander, F.F., Eaton, J.W., Albumin-binding surfaces for implantable devices (1992) Journal of Biomedical Materials Research, 26 (4), pp. 441-456; 
Martins, M.C.L., Wang, D., Ji, J., Feng, L., Barbosa, M.A., Albumin and fibrinogen adsorption on Cibacron blue F3G-A immobilised onto PU-PHEMA (polyurethane-poly(hydroxyethylmethacrylate)) surfaces (2003) Journal of Biomaterials Science Polymer Edition, 14 (5), pp. 439-455; 
McFarland, C.D., De Filippis, C., Jenkins, M., Tunstell, A., Rhodes, N.P., Williams, D.F., Albumin-binding surfaces: in vitro activity (1998) Journal of Biomaterials Science Polymer Edition, 9 (11), pp. 1227-1239; 
Munro, M.S., Quattrone, A.J., Ellsworth, S.R., Kulkarni, P., Eberhart, R.C., Alkyl substituted polymers with enhanced albumin affinity (1981) Transactions American Society for Artificial Internal Organs, 27, pp. 499-503; 
Tsai, C.C., Huo, H.H., Kulkarni, P., Eberhart, R.C., Biocompatible coatings with high albumin affinity (1990) ASAIO Transactions, 36 (3), pp. 307-310; 
Wang, D.A., Chen, B.L., Ji, J., Feng, L.X., Selective adsorption of serum albumin on biomedical polyurethanes modified by a poly(ethylene oxide) coupling-polymer with Cibacron blue (F3G-A) endgroups (2002) Bioconjugate Chemistry, 13 (4), pp. 792-803; 
Gon{\c c}alves, I.C., Martins, M.C.L., Barbosa, M.A., Naeemi, E., Ratner, B.D., Selective protein adsorption modulates platelet adhesion and activation to oligo(ethylene glycol)-terminated self-assembled monolayers with C18 ligands (2009) Journal of Biomedical Materials Research Part A, 89 A (3), pp. 642-653; 
Bain, C.D., Troughton, E.B., Tao, Y.T., Evall, J., Whitesides, G.M., Nuzzo, R.G., Formation of monolayer films by the spontaneous assembly of organic thiols from solution onto gold (1989) Journal of the American Chemical Society, 111 (1), pp. 321-335; 
Kwok, S.C., Mourad, P.D., Crum, L.A., Ratner, B.D., Surface modification of polymers with self-assembled molecular structures: multitechnique surface characterization (2000) Biomacromolecules, 1, pp. 139-148; 
Goncalves, I.C., Martins, M.C.L., Barbosa, M.A., Ratner, B.D., Protein adsorption on 18-alkyl chains immobilized on hydroxyl-terminated self-assembled monolayers (2005) Biomaterials, 26 (18), pp. 3891-3899; 
Ratner, B.D., Hoffman, A.F., Schoen, F.J., Lemons, J.L., (2004) Biomaterials science - an introduction to materials in medicine. 2nd ed., , Elsevier Academic Press, San Diego, CA, USA; 
Ratner, B.D., Miller, I.F., Interaction of urea with poly(2-hydroxyethyl methacrylate) hydrogels (1972) Journal of Polymer Science Part a-1-Polymer Chemistry, 10 (8), pp. 2425-2445; 
Horbett, T.A., Techniques for protein adsorption studies (1986) Techniques of biocompatibility testing, pp. 183-214. , Williams D.F. (Ed), Harcover: CRC Press; 
Cao, L., Chang, M., Lee, C.Y., Castner, D.G., Sukavaneshvar, S., Ratner, B.D., Plasma-deposited tetraglyme surfaces greatly reduce total blood protein adsorption, contact activation, platelet adhesion, platelet procoagulant activity, and in vitro thrombus deposition (2007) Journal of Biomedical Materials Research Part A, 81 (4), pp. 827-837; 
Stovbun, E.V., Kuzaev, A.I., Baturin, S.M., (1996) Polymer Science Series A, 38, pp. 691-695; 
Tanaka, M., Motomura, T., Kawada, M., Anzai, T., Yuu, K., Shiroya, T., Blood compatible aspects of poly(2-methoxyethylacrylate) (PMEA) - relationship between protein adsorption and platelet adhesion on PMEA surface (2000) Biomaterials, 21 (14), pp. 1471-1481; 
Castner, D.G., Ratner, B.D., Hirao, A., Nakahama, S., Characterization of poly(2-hydroxyethyl methacrylate) (PHEMA) by XPS (1996) Surface Science Spectra, 4 (1-4), p. 14; 
L{\'o}pez, G.P., Ratner, B.D., Rapoza, R.J., Horbett, T.A., Plasma deposition of ultrathin films of poly(2-hydroxyethyl methacrylate): surface analysis and protein adsorption measurements (1993) Macromolecules, 26 (13), pp. 3247-3253; 
Martins, M.C.L., Wang, D., Ji, J., Feng, L., Barbosa, M.A., Albumin and fibrinogen adsorption on PU-PHEMA surfaces (2003) Biomaterials, 24 (12), pp. 2067-2076; 
Tsukagoshi, T., Kondo, Y., Yoshino, N., Protein adsorption on polymer-modified silica particle surface (2007) Colloids and Surfaces B Biointerfaces, 54 (1), pp. 101-107; 
Ratner, B.D., Biomedical applications of hydrogels: review and critical appraisal (1981) Biocompatibility of clinical implant materials, , Williams D.F. (Ed), CRC Press; 
H{\"o}{\"o}k, F., V{\"o}r{\"o}s, J., Rodahl, M., Kurrat, R., B{\"o}ni, P., Ramsden, J.J., A comparative study of protein adsorption on titanium oxide surfaces using in situ ellipsometry, optical waveguide lightmode spectroscopy, and quartz crystal microbalance/dissipation (2002) Colloids and Surfaces B Biointerfaces, 24 (2), pp. 155-170; 
Stryer, L., (1998) Biochemistry. 4th ed., , WH Freeman, New York; 
Garrett, Q., Chatelier, R.C., Griesser, H.J., Milthorpe, B.K., Effect of charged groups on the adsorption and penetration of proteins onto and into carboxymethylated poly(HEMA) hydrogels (1998) Biomaterials, 19 (23), pp. 2175-2186; 
Mequanint, K., Sheardown, H., 2-Methacryloyloxyethyl N-butylcarbamate: a new co-monomer for synthesis of polyurethane hydrogels with improved mechanical properties for biomedical applications (2005) Journal of Biomaterials Science Polymer Edition, 16 (10), pp. 1303-1318; 
Horbett, T.A., Adsorption of proteins from plasma to a series of hydrophilic-hydrophobic copolymers. II. Compositional analysis with the prelabeled protein technique (1981) Journal of Biomedical Materials Research, 15 (5), pp. 673-695; 
Feng, L., Andrade, J.D., Protein adsorption on low-temperature isotropic carbon. 3. isotherms, competitivity, desorption and exchange of human albumin and fibrinogen (1994) Biomaterials, 15 (5), pp. 323-333; 
Pitt, W.G., Cooper, S.L., Albumin adsorption on alkyl chain derivatized polyurethanes. 1. The effect of C-18 alkylation (1988) Journal of Biomedical Materials Research, 22 (5), pp. 359-382; 
Markiewski, M.M., Nilsson, B., Ekdahl, K.N., Mollnes, T.E., Lambris, J.D., Complement and coagulation: strangers or partners in crime? (2007) Trends in Immunology, 28 (4), pp. 184-192; 
Zhang, Z., Zhang, M., Chen, S., Horbett, T.A., Ratner, B.D., Jiang, S., Blood compatibility of surfaces with superlow protein adsorption (2008) Biomaterials, 29 (32), pp. 4285-4291; 
Grunkemeier, J.M., Tsai, W.B., Horbett, T.A., Hemocompatibility of treated polystyrene substrates: contact activation, platelet adhesion, and procoagulant activity of adherent platelets (1998) Journal of Biomedical Materials Research, 41 (4), pp. 657-670; 
Gorbet, M.B., Sefton, M.V., Biomaterial-associated thrombosis: roles of coagulation factors, complement, platelets and leukocytes (2004) Biomaterials, 25 (26), pp. 5681-5703
},
	month = {2009///},
	pages = {5541 - 5551},
	abstract = {This work intended to create a nanostructured biomaterial that would bind albumin in a selective and reversible way in order to inhibit the adsorption of other blood proteins and therefore minimize activation of coagulation. Different levels of C18 ligand have been immobilized on poly(2-hydroxyethyl methacrylate) (pHEMA). We hypothesize that samples with intermediate amounts of C18 ligand would allow albumin to recognize them and bind through its hydrophobic pockets specific for long chain fatty acids. Surface characterization has confirmed increasing amounts of C18 ligand on pHEMA as the percentage of C18 in solution increases, with maximum coverage achieved in 10\% C18 samples. Adsorption from pure albumin solution revealed a small decrease in albumin adsorption from pHEMA to 1\% C18 and 2.5\% C18 samples, but on surfaces with 5\% or higher C18 the amount of adsorbed albumin increased as the percentage of C18 increased. Competitive adsorption studies in the presence of both albumin and fibrinogen, and in the presence of all plasma proteins showed that 1\% C18 and 2.5\% C18 were the only surfaces selective for albumin, and that the presence of all plasma proteins may even potentiate albumin adsorption. Reversibility studies demonstrated that both 2.5\% C18 and 5\% C18 samples exchange                        125I-albumin selectively in the presence of both unlabeled albumin and plasma, but 2.5\% C18 samples presented higher exchangeability rates (58\%). Clotting times using recalcified plasma revealed that samples with none or small amounts of C18 (pHEMA to 5\% C18) did not shorten the clotting time compared to the negative control (polystyrene), indicating low activation of the intrinsic coagulation cascade. {\textcopyright} 2009 Elsevier Ltd. All rights reserved.
},
	keywords = {Adsorption, article, Biocompatible Materials, Biomaterials, blood clotting time, Blood Coagulation Tests, Body fluids, Clotting time, Coagulation, Coated Materials, Biocompatible, concentration response, controlled study, Fatty acids, fibrinogen, human serum albumin, hydrogel, Hydrogels, hydrophilicity, Ligands, long chain fatty acid, materials testing, Plasmas, PolyHEMA, Polyhydroxyethyl Methacrylate, polymacon, Polymer blends, polystyrene, Polystyrenes, priority journal, Protein adsorption, protein binding, Proteins, Serum Albumin, Surface modification, surface property, Surface treatment},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-68549112719\&partnerID=40\&md5=aa1dd37881210211ef398092a3be6174},
	author = {Gon{\c c}alves, I.C. and Martins, M.C.L. and Barbosa, M.A. and Ratner, B.D.}
}
@article {2309,
	title = {Selective protein adsorption modulates platelet adhesion and activation to oligo(ethylene glycol)-terminated self-assembled monolayers with C18 ligands},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {89},
	year = {2009},
	note = {Cited By (since 1996): 11Export Date: 21 November 2012Source: ScopusCODEN: JBMRCdoi: 10.1002/jbm.a.32011PubMed ID: 18442116Language of Original Document: EnglishCorrespondence Address: Gon{\c c}alves, I. C.; INEB-Instituto de Engenharia Biom{\'e}dica, Laborat{\'o}rio de Biomateriais, Universidade do Porto, Run do Campo Alegre, 823, 4150-180 Porto, Portugal; email: icastro@ineb.up.ptChemicals/CAS: fibrinogen, 9001-32-5; glutaraldehyde, 111-30-8, 37245-61-7; human serum albumin, 9048-49-1; Carbon, 7440-44-0; Ethylene Glycol, 107-21-1; Ligands; Serum AlbuminReferences: Nath, N., Hyun, J., Ma, H., Chilkoti, A., Surface engineering strategies for control of protein and cell interactions (2004) Surf Sci, 570, pp. 98-110;Mao, C., Qiu, Y.Z., Sang, H.B., Mei, H., Zhu, A.P., Shen, J., Lin, S.C., Various approaches to modify biomaterial surfaces for improving hemocompatibility (2004) Adv Colloid Interface Sci, 110, pp. 5-17; 
Gorbet, M.B., Sefton, M.V., Biomaterial-associated thrombosis: Roles of coagulation factors, complement, platelets and leukocytes (2004) Biomaterials, 25, pp. 5681-5703; 
Kottkemarchant, K., Anderson, J.M., Umemura, Y., Marchant, R.E., Effect of albumin coating on the in vitro blood compatibility of dacron arterial prostheses (1989) Biomaterials, 10, pp. 147-155; 
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},
	month = {2009///},
	pages = {642 - 653},
	abstract = {This study focuses on the selective binding of albumin to a nanostructured surfaces to inhibit other blood proteins from adsorbing thereby reducing platelet adhesion and activation. Tetra (ethylene-glycol)-terminated self- assembled monolayers (EG4 SAMs) with different percentages of CI 8 ligands on the surface were characterized by contact angle measurements, X-ray photoelectron microscopy, infrared reflection-absorption spectroscopy, and ellipsometry. A specific surface (2.5\% C18 SAM) was found to be selective for human serum albumin (HSA) in the presence of both albumin and fibrinogen (HFG). The importance of this concentration of C18 ligands was stressed in reversibility studies since that surface exchanged almost all the preadsorbed HSA by HSA in solution, but not by HFG. The effect of protein adsorption in the subsequent adhesion and activation of platelets was studied by pre-immersing the surfaces in albumin and plasma before contact with platelets. Scanning electron microscopy and glutaraldehyde induced fluorescence technique images showed that as surfaces got more hydrophobic due to the immobilization of C18 ligands, the number of adherent platelets increased and their morphology changed from round to fully spread. Pre-immersion in HSA led to an 80{\textdegree}/o decrease in platelet adhesion and reduction of activation. Pre-immersion in 1\% plasma was only relevant in 2.5\% CI 8 SAMs since this was the only surface that demonstrated less adhesion of platelets comparing with buffer pre-immersion. However, they still adsorb more platelets then when HSA was preadsorbed. This was confirmed in competition studies between HSA and plasma that suggested that other plasma proteins were also adsorbing to this surface. {\textcopyright} 2008 Wiley Periodicals, Inc.},
	keywords = {Absorption spectroscopy, Acoustic microscopes, Adhesion, Adsorption, Albumin, Aldehydes, Angle measurement, article, Biological materials, Biomaterials, Blood Platelets, Blood protein, Blood substitutes, Carbon, Cell Shape, chemical composition, Concentration of, Contact angle, controlled study, Ethylene, Ethylene Glycol, ethylene glycol derivative, fibrinogen, Fluorescence technique, glutaraldehyde, gold nanoparticle, human, human serum albumin, Human serum albumins, Humans, hydrophobicity, Infrared reflection absorption spectroscopy, infrared spectroscopy, ligand, Ligands, Nanostructured surface, normal human, Oligo(ethylene glycol), Photoelectron spectroscopy, plasma, Plasma diagnostics, Plasma protein, Plasmas, Platelet adhesion, Platelet Adhesiveness, Platelets, Protein adsorption, protein binding, Proteins, Sams, Scanning electron microscopy, Selective binding, Selective protein adsorption, self assembled monolayer, Self assembled monolayers, Self-assembled monolayers, Serum Albumin, Specific surface, Spectrophotometry, Infrared, Surface Properties, surface property, thrombocyte activation, thrombocyte adhesion, thrombocyte shape, X ray photoelectron spectroscopy, X-ray photoelectron microscopy},
	isbn = {15493296 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-66249128976\&partnerID=40\&md5=0be21ad44fe5cf556598975ea1655bed},
	author = {Gon{\c c}alves, I.C. and Martins, M.C.L. and Barbosa, M.A. and Naeemi, E. and Ratner, B.D.}
}
@article {2336,
	title = {Injectability of a bone filler system based on hydroxyapatite microspheres and a vehicle with in situ gel-forming ability},
	journal = {Journal of Biomedical Materials Research - Part B Applied BiomaterialsJ. Biomed. Mater. Res. Part B Appl. Biomater.},
	volume = {87},
	year = {2008},
	note = {Cited By (since 1996): 9Export Date: 21 November 2012Source: ScopusCODEN: JBMRGdoi: 10.1002/jbm.b.31066PubMed ID: 18437700Language of Original Document: EnglishCorrespondence Address: Oliveira, S. M.; Escola Superior de Tecnologia de Viseu (ESTV), Dep. de Eng. Mec{\^a}nica e Gest{\~a}o Industrial, 3504-510 Viseu, Portugal; email: serafim@ineb.up.ptChemicals/CAS: alginic acid, 28961-37-7, 29894-36-8, 9005-32-7, 9005-38-3; calcium carbonate, 13397-26-7, 13701-58-1, 14791-73-2, 471-34-1; gluconolactonase, 9012-44-6, 9012-73-1; hydroxyapatite, 1306-06-5, 51198-94-8; Bone Substitutes; Durapatite, 1306-06-5; GelsTradenames: Captal S, Plasma BiotalManufacturers: Plasma BiotalReferences: Ribeiro, C.C., Barrias, C.C., Barbosa, M.A., Calcium phosphate-alginate microspheres as enzyme delivery matrices (2004) Biomaterials, 25, pp. 4363-4373;Grabowski, G.A., Leslie, N., Wenstrup, R., Enzyme therapy for Gaucher disease: The first 5 years (1998) Blood Rev, 12, pp. 115-133; 
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},
	month = {2008///},
	pages = {49 - 58},
	abstract = {The aim of this study was to test the injectability of a bone filler system based on the combination of ceramic microspheres with a gel-like vehicle, for noninvasive surgery. Porous hydroxyapatite microspheres with a uniform size and an average diameter of 535 {\textpm} 38 μm were prepared, and their compression strength and friability were tested. The sodium-alginate solution with a concentration of 7.25\% (w/v) was used as the vehicle. To promote its in situ gelation, calcium carbonate and D-gluconic-δ-lactone were added to the solution. Microspheres were mixed with the vehicle at different percentages (20-40 wt \%). Gelation times in the range of 8-20 min, were obtained, depending on the formulation. Mixtures of HAp microspheres with alginate solution at 7.25\% originating a gel in 11 min present an adequate handling time to perform an injection. Their injectability was evaluated using an injection device commonly employed in vertebroplasty surgical procedures, coupled to a texturometer in compression mode. Using an extrusion rate of 0.1 mm/s, the force required to extrude any of the mixtures tested was lower than 100 N. For an extrusion rate of 1 mm/s mixtures with 40 wt \% of microspheres were very difficult to inject. Mixtures with 35 wt \% of microspheres presented the best compromise between injectability and compression strength of the gelled system. MicroCT analysis revealed a homogeneous distribution of the microspheres inside the vehicle, as well as full interconnection of the intra-microspheres spaces. The compression strength for the gelled systems ranged from 80 kPa (gel itself) to 600 kPa (composite with 40 Wt \% of microspheres). {\textcopyright} 2008 Wiley Periodicals, Inc.},
	keywords = {Alginate, alginic acid, Apatite, article, Average diameter, bioengineering, Bone, bone filler system, Bone Substitutes, Calcium, Calcium carbonate, Ceramic, Ceramic microspheres, Coagulation, Colloids, compression, Compression mode, Compression strengths, Compressive Strength, Computerized tomography, Concentration (process), Data compression, Durapatite, Extrusion, Extrusion rates, Fillers, Forming, Gel-forming ability, Gelation, Gels, gluconolactonase, Handling time, Homogeneous distribution, hydrogel, hydroxyapatite, In situ gelation, in situ hybridization, In-situ, Injectability, injection, Injection (oil wells), Micro-CT, microsphere, Microspheres, Mixtures, non invasive procedure, Particle Size, Porous hydroxyapatite, Sodium, Surgery, Surgical procedures, Uniform size, Vehicles, Vertebroplasty},
	isbn = {15524973 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-52449123139\&partnerID=40\&md5=cc648bad01cb2c6aa01d885acac10e8a},
	author = {Oliveira, S.M. and Barrias, C.C. and Almeida, I.F. and Costa, P.C. and Pena Ferreira, M.R. and Bahia, M.F. and Barbosa, M.A.}
}
@article {2350,
	title = {Microstructure, mechanical properties and chemical degradation of brazed AISI 316 stainless steel/alumina systems},
	journal = {Materials Science and Engineering AMater. Sci. Eng. A},
	volume = {480},
	year = {2008},
	note = {Cited By (since 1996): 11Export Date: 21 November 2012Source: Scopusdoi: 10.1016/j.msea.2007.07.015Language of Original Document: EnglishCorrespondence Address: Paiva, O.C.; Instituto Superior de Engenharia do Porto (ISEP), Rua Dr. Antonio Bernardino Almeida 431, 4200-072 Porto, Portugal; email: omp@isep.ipp.ptReferences: Schwartz, M.M., (1990) Ceramic Joining, pp. 75-140. , Schwartz M.M. (Ed), ASM International, Ohio;Nicholas, M.G., (1986) Br. Ceram. Trans. J., 85, pp. 144-146; 
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},
	month = {2008///},
	pages = {306 - 315},
	abstract = {The main aims of the present study are simultaneously to relate the brazing parameters with: (i) the correspondent interfacial microstructure, (ii) the resultant mechanical properties and (iii) the electrochemical degradation behaviour of AISI 316 stainless steel/alumina brazed joints. Filler metals on such as Ag-26.5Cu-3Ti and Ag-34.5Cu-1.5Ti were used to produce the joints. Three different brazing temperatures (850, 900 and 950 {\textdegree}C), keeping a constant holding time of 20 min, were tested. The objective was to understand the influence of the brazing temperature on the final microstructure and properties of the joints. The mechanical properties of the metal/ceramic (M/C) joints were assessed from bond strength tests carried out using a shear solicitation loading scheme. The fracture surfaces were studied both morphologically and structurally using scanning electron microscopy (SEM), energy dispersive spectroscopy (EDS) and X-ray diffraction analysis (XRD). The degradation behaviour of the M/C joints was assessed by means of electrochemical techniques. It was found that using a Ag-26.5Cu-3Ti brazing alloy and a brazing temperature of 850 {\textdegree}C, produces the best results in terms of bond strength, 234 {\textpm} 18 MPa. The mechanical properties obtained could be explained on the basis of the different compounds identified on the fracture surfaces by XRD. On the other hand, the use of the Ag-34.5Cu-1.5Ti brazing alloy and a brazing temperature of 850 {\textdegree}C produces the best results in terms of corrosion rates (lower corrosion current density), 0.76 {\textpm} 0.21 μA cm},
	keywords = {Active metal brazing, Alumina, Bond strength (materials), Brazing, Electrochemical degradation, Filler metals, fracture, Interface composition, Metal/ceramic joining, Metallic matrix composites, morphology, Processing parameters, Shear strength, Stainless steel},
	isbn = {09215093 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-41149104604\&partnerID=40\&md5=6dfded1210945bb66208633744939f64},
	author = {Paiva, O.C. and Barbosa, M.A.}
}
@article {2359,
	title = {Osteoblast adhesion and morphology on TiO                    2 depends on the competitive preadsorption of albumin and fibronectin
},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {84},
	year = {2008},
	note = {Cited By (since 1996): 34Export Date: 21 November 2012Source: ScopusCODEN: JBMRCdoi: 10.1002/jbm.a.31201PubMed ID: 17607748Language of Original Document: EnglishCorrespondence Address: Sousa, S.R.; INEB - Instituto de Engenharia Biom{\'e}dica, Laborat{\'o}rio de Biomaterials, R. do Campo Alegre, 823, 4150-180 Porto, Portugal; email: ssousa@ibmc.up.ptChemicals/CAS: fibronectin, 86088-83-7; human serum albumin, 9048-49-1; hydrogen peroxide, 7722-84-1; iodine 125, 14158-31-7, 22822-81-7; titanium dioxide, 1317-70-0, 1317-80-2, 13463-67-7, 51745-87-0; Albumins; Coloring Agents; Fibronectins; Iodine Radioisotopes; Neutral Red, 553-24-2; titanium dioxide, 13463-67-7; Titanium, 7440-32-6References: Anselme, K., Osteoblast adhesion on biomaterials (2000) Biomaterials, 21, pp. 667-681;Tidwell, C.D., Ertel, S.I., Ratner, B.D., Tarasevich, B.J., Atre, S., Allara, D.L., Endothelial cell growth and protein adsorption on terminally functionalized, self-assembled monolayers of alkane-thiolates on gold (1997) Langmuir, 13, pp. 3404-3413; 
Malmsten, M., Lassen, B., Competitive adsorption at hydrophobic surfaces from binary protein systems (1994) J Colloid Interface Sci, 166, pp. 490-498; 
Koenig, A.L., Gambillara, V., Grainger, D.W., Correlating fibronectin adsorption with endothelial cell adhesion and signaling on polymer substrates (2003) J Biomed Mater Res A, 64, pp. 20-37; 
Horbett, T.A., The role of adsorbed proteins in animal cell adhesion (1994) Colloids Surf B, 2, pp. 225-240; 
Huang, H.H., Ho, C.T., Lee, T.H., Lee, T.L., Liao, K.K., Chen, F.L., Effect of surface roughness of ground titanium on initial cell adhesion (2004) Biomol Eng, 21, pp. 93-97; 
Vitte, J., Benoliel, A.M., Pierres, A., Bongrand, P., Is there a predictable relationship between surface physical-chemical properties and cell behaviour at the interface? (2004) Eur Cell Mater, 7, pp. 52-63; 
Tsai, W.B., Grunkemeier, J.M., McFarland, C.D., Horbett, T.A., Platelet adhesion to polystyrene-based surfaces preadsorbed with plasmas selectively depleted in fibrinogen, fibronectin, vitronectin, or von Willebrand{\textquoteright}s factor (2002) J Biomed Mater Res, 60, pp. 348-359; 
Grainger, D.W., Pavon-Djavid, G., Migonney, V., Josefowicz, M., Assessment of fibronectin conformation adsorbed to polytetrafluoroethylene surfaces from serum protein mixtures and correlation to support of cell attachment in culture (2003) J Biomater Sci Polym Ed, 14, pp. 973-988; 
Goncalves, I.C., Martins, M.C.L., Barbosa, M.A., Ratner, B.D., Protein adsorption on 18-alkyl chains immobilized on hydroxyl-terminated self-assembled monolayers (2005) Biomaterials, 26, pp. 3891-3899; 
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Iodine-125. A Guide to Radioiodination Techniques. Little Chalfont, UK: Amersham Life Science; 1993. p 64Lima, J., Sousa, S.R., Ferreira, A., Barbosa, M.A., Interactions between calcium, phosphate, and albumin on the surface of titanium (2001) J Biomed Mater Res, 55, pp. 45-53; 
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},
	month = {2008///},
	pages = {281 - 290},
	abstract = {This study aims at assessing the influence of the competitive preadsorption of human serum albumin (HSA) and human plasma fibronectin (FN) from binary solutions and 10\% plasma on MC3T3-E1 osteoblast adhesion and morphology on two types of TiO                        2 substrates. One was commercially pure titanium with a titanium oxide layer formed in an H
                        2O
                        2 solution and the other TiO
                        2 sputtered on Si (Sousa et al., Langmuir 2004; 20:9745-9754.). The strategy applied in the present investigation was to compare osteoblast adhesion to surfaces preadsorbed with HSA, FN, HSA/FN = 1, HSA/FN = 200, and 10\% plasma. The adsorption of proteins was evaluated measuring the amount and the effectiveness of binding with radiolabeled proteins, 
                        125I-FN and 
                        125I-HSA. Our results indicated that MC3T3-E1 osteoblast adhesion correlates well with the amounts of FN and HSA adsorbed on TiO
                        2 surfaces. Also, we found that fewer osteoblasts adhered to both substrates preadsorbed with HSA, HSA/FN = 200, and 10\% plasma, after 4 and 24 h, than to the surfaces preadsorbed with FN and HSA/FN = 1. For the latter, FN was able to compensate the inhibitory effect of HSA on osteoblast adhesion. Therefore, the presence of lower amounts of coadsorbed albumin may improve presentation of FN in a more integrin-recognized conformation, suggesting that some degree of molecular packing prevents loss of integrin-binding activity. FN reversibility does not seem to be dependent on the HSA/FN adsorption mass ratio in solution, suggesting that FN competitively adsorbs to TiO
                        2 in a favorable conformation and does not suffers subsequent conformational changes allowing exchange with other FN molecules in solution. {\textcopyright} 2007 Wiley Periodicals, Inc.
},
	keywords = {2, 3T3 Cells, Adsorption, Albumins, animal cell, Animals, article, binding kinetics, cell adhesion, Coloring Agents, Competitive protein adsorption, controlled study, cytoskeleton, Data Interpretation, Statistical, Fibronectin, Fibronectins, FN, HSA, human serum albumin, hydrogen peroxide, iodine 125, Iodine Radioisotopes, isotope labeling, Mice, Microscopy, Confocal, mouse, neutral red, nonhuman, osteoblast, Osteoblast adhesion, Osteoblasts, Protein radiolabeling, Proteins, Radiology, Solutions, Sterilization, surface property, TiO, Titanium, Titanium dioxide},
	isbn = {15493296 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-38049002555\&partnerID=40\&md5=dd5a4dee91d3fe1e9eb9a6ba31553c0a},
	author = {Sousa, S.R. and Lamghari, M. and Sampaio, P. and Moradas-Ferreira, P. and Barbosa, M.A.}
}
@article {2381,
	title = {Attachment, spreading and short-term proliferation of human osteoblastic cells cultured on chitosan films with different degrees of acetylation},
	journal = {Journal of Biomaterials Science, Polymer EditionJ. Biomater. Sci. Polym. Ed.},
	volume = {18},
	year = {2007},
	note = {Cited By (since 1996): 22Export Date: 21 November 2012Source: ScopusCODEN: JBSEEdoi: 10.1163/156856207780425068Language of Original Document: EnglishCorrespondence Address: Amaral, I.F.; INEB - Instituto de Engenharia Biom{\'e}dica, Laborat{\'o}rio de Biomateriais, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: iamaral@ineb.up.ptChemicals/CAS: chitosan, 9012-76-4; Biocompatible Materials; Chitosan, 9012-76-4References: Vacanti, C.A., Bonassar, L.J., Vacanti, J.P., (2000) Principles of Tissue Engineering, p. 671. , R. P. Lanza, R. Langer and J. Vacanti Eds, p, Academic Press, San Diego, CA;Bruder, S.P., Caplan, A.I., (2000) Principles of Tissue Engineering, p. 683. , R. P. Lanza, R. Langer and J. Vacanti Eds, p, Academic Press, San Diego, CA; 
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},
	month = {2007///},
	pages = {469 - 485},
	abstract = {Chitosan (Ch) is being actively investigated as a non-protein template for the growth of an increasing number of anchorage-dependent cells, including chondrocytes and bone cells. In the present work, Ch films with degrees of N-acetylation (DAs) in the range of 4 to 49\% were evaluated with respect to the attachment, spreading and short-term proliferation of osteoblasts, using human osteoblastic MG-63 cells. The films were characterized in terms of surface morphology and surface charge by atomic force microscopy and streaming potential measurements, respectively. Cell attachment was assessed after 3 and 24 h of cell culture. After 24 h of incubation, cell attachment was found to be dependent on the DA, lower DAs favouring cell adhesion. With time, cell spreading and cytoskeleton organization were only attained for DAs <= 13\%. Regarding cell proliferation, cells grown on films with the lowest DA (4\%) revealed a higher specific growth rate as compared to those grown on films with higher DAs. Films with a DA of 49\% failed to sustain cell proliferation. In addition, a longer lag-phase was observed on Ch, as compared to TCPS, in accordance to an observed delay of cell spreading. The present findings revealed that differences in the DA as small as 9\% may be critical in terms of the osteoblast response to two-dimensional Ch-based matrices. {\textcopyright} 2007 VSP.},
	keywords = {Acetylation, AFM, article, Atomic force microscopy, Biocompatible Materials, biofilm, Biofilms, biomaterial, bone cell, cartilage cell, cell adhesion, cell anchorage, Cell culture, cell growth, Cell Line, Tumor, cell proliferation, Cell Shape, cell spreading, cell survival, Chemical structure, chemistry, Chitin, chitosan, comparative study, controlled study, cytoskeleton, Degree of acetylation, drug effect, Growth kinetics, human, human cell, Humans, incubation time, metabolism, Microscopy, Atomic Force, osteoblast, Osteoblast-like cells, Osteoblasts, Pathology, priority journal, Surface charge, Surface Properties, surface property, Surface treatment, tumor cell line, Zeta potential},
	isbn = {09205063 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-34347375992\&partnerID=40\&md5=437b9ed270e859425b76aa3655c611be},
	author = {Amaral, I.F. and Cordeiro, A.L. and Sampaio, P. and Barbosa, M.A.}
}
@book {2385,
	title = {Characterization of hydroxyapatite sputtered films doped with titanium},
	series = {Key Engineering MaterialsKey Eng Mat},
	volume = {330-332 I},
	year = {2007},
	note = {Cited By (since 1996): 1Export Date: 21 November 2012Source: ScopusCODEN: KEMAELanguage of Original Document: EnglishCorrespondence Address: Ribeiro, A.R.; INEB-Instituto de Engenharia Biom{\'e}dica, Laborat{\'o}rio de Biomateriais, Universidade do Porto, Rua Campo Alegre, 823, 4150-180 Porto, Portugal; email: arr@ineb.up.ptReferences: Bhat, (2002) Biomaterials, , Narosa Publishing House/Kluwer Academic Publishers, India;Feddes B, Vredenberg AM. Wolke JGC, Jansen JA.: Surface and Coatings Technology 185 (2-3) (2004), p. 346Gisep, A., (2002) Injury-International Journal of the Care of the Injured, 33 (SUPPL. 2), p. 88; 
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Barrias, C.C., Ribeiro, C.C., Rodriguez, D., S{\'a} Miranda, C., Barbosa, M.A., (2005) Key Engineering Materials, 284-286, p. 689; 
Ribeiro, C.C., Barrias, C.C., Barbosa, M.A., (2004) Biomaterials, 25, p. 4363; 
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},
	month = {2007///},
	pages = {649 - 652},
	abstract = {In the present work, thin films of hydroxyapatite (HAp), titanium, and hydroxyapatite doped with different titanium concentrations were obtained by sputtering and characterized using several analytical techniques. These films are intended to be used as model surfaces on protein adsorption studies in order to better understand the role of titanium ions in biological processes.},
	keywords = {Adsorption, Biofilms, Doping (additives), hydroxyapatite, Hydroxyapatite sputtered films, Model surfaces, Proteins, Sputtering, Titanium, Titanium ions},
	isbn = {10139826 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-33846300257\&partnerID=40\&md5=7946215d8f37e0e216b57336b89f0f02},
	author = {Ribeiro, A.R. and Piedade, A.P. and Ribeiro, C.C. and Vieira, M.T. and Barbosa, M.A.}
}
@article {2386,
	title = {A novel dry active electrode for EEG recording},
	journal = {IEEE Transactions on Biomedical EngineeringIEEE Trans. Biomed. Eng.},
	volume = {54},
	year = {2007},
	note = {Cited By (since 1996): 24Export Date: 21 November 2012Source: ScopusArt. No.: 23CODEN: IEBEAdoi: 10.1109/TBME.2006.884649PubMed ID: 17260869Language of Original Document: EnglishCorrespondence Address: Fonseca, C.; INEB Instituto de Engenharia Biom{\'e}dica, Laborat{\'o}rio de Biomateriais, Universidade Do Porto, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: cfonseca@ibmc.up.ptChemicals/CAS: Biocompatible Materials; Titanium, 7440-32-6; titanium dioxide, 13463-67-7References: Portnoy, W., David, R., Akers, L., Insulated ECG electrodes (1974) Biomedical Electrode Technology, , H. A. Miller and D. C. Harrison, Eds. New York: Academic;Nishimura, S., Tomita, Y., Horiuchi, T., Clinical application of an active electrode using an operational amplifier (1992) IEEE Trans. Biomed. Eng, 39 (10), pp. 1090-1099. , Oct; 
Taheri, A., Knight, R., Smith, R., A dry electrode for EEG recording (1994) Electroencephalogr. Clin. Neurophysiol, 90, pp. 376-383; 
Searle, A., Kirkup, L., A direct comparison of wet, dry and insulating bioelectric recording electrodes (2000) Physiol. Meas, 22, pp. 71-83; 
Fonseca, C., Vaz, F., Barbosa, M.A., Electrochemical behaviour of titanium coated stainless steel by R.F. sputtering in synthetic sweat solutions for electrode applications (2004) Corrosion Sci, 46 (12), pp. 3005-3018; 
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Perez, J., Vilarinho, P., Kholkin, A., High-quality Pbzr0.52Ti0. 48O3 films prepared by modified sol-gel route at low temperature (2004) Thin Solid Films, 449 (1-2), pp. 20-24; 
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Ferree, T., Luu, P., Russell, G., Tucker, D., Scalp electrode impedance, infection risk and EEG data quality (2001) Clin. Neurophysiol, 112 (3), pp. 536-544
},
	month = {2007///},
	pages = {162 - 165},
	abstract = {The design and testing of a "dry" active electrode for electroencephalographic recording is described. A comparative study between the EEG signals recorded in human volunteers simultaneously with the classical Ag-AgCl and "dry" active electrodes was carried out and the reported preliminary results are consistent with a better performance of these devices over the conventional Ag-AgCl electrodes. {\textcopyright} 2007 IEEE.},
	keywords = {article, Biocompatible Materials, Bioelectric phenomena, Bioelectric signal recording, bioenergy, biomedical electrodes, Biomedical engineering, Data recording, Dry electrodes, Electric Impedance, Electrochemical electrodes, electrode, Electrodes, electroencephalogram, Electroencephalographic recording, electroencephalography, Equipment Design, Equipment Failure Analysis, Feasibility Studies, Pilot Projects, signal transduction, Silver compounds, Titanium},
	isbn = {00189294 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-33846389173\&partnerID=40\&md5=0273ef7699807f6e20f95dd6bacb3c9b},
	author = {Fonseca, C. and Silva Cunha, J.P. and Martins, R.E. and Ferreira, V.M. and Marques De S{\'a}, J.P. and Barbosa, M.A. and Martins Da Silva, A.}
}
@article {2376,
	title = {Upregulation of bone cell differentiation through immobilization within a synthetic extracellular matrix},
	journal = {BiomaterialsBiomaterials},
	volume = {28},
	year = {2007},
	note = {Cited By (since 1996): 39Export Date: 21 November 2012Source: ScopusCODEN: BIMADdoi: 10.1016/j.biomaterials.2007.04.028PubMed ID: 17532040Language of Original Document: EnglishCorrespondence Address: Evangelista, M.B.; INEB-Instituto de Engenharia Biom{\'e}dica, Laborat{\'o}rio de Biomateriais, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: mbe@ineb.up.ptChemicals/CAS: alginic acid, 28961-37-7, 29894-36-8, 9005-32-7, 9005-38-3; alkaline phosphatase, 9001-78-9; arginylglycylaspartic acid, 99896-85-2; DNA, 9007-49-2; osteocalcin, 136461-80-8; Alginates; alginic acid, 9005-32-7; Alkaline Phosphatase, EC 3.1.3.1; arginyl-glycyl-aspartic acid, 99896-85-2; Glucuronic Acid, 576-37-4; Hexuronic Acids; Oligopeptides; Osteocalcin, 104982-03-8References: de Vos, P., de Haan, B., Wolters, G.H.J., VanSchilfgaarde, R., Factors influencing the adequacy of microencapsulation of rat pancreatic islets (1996) Transplantation, 62 (7), pp. 888-893;Brissova, M., Lacik, I., Powers, A.C., Anilkumar, A.V., Wang, T., Control and measurement of permeability for design of microcapsule cell delivery system (1998) J Biomed Mater Res, 39 (1), pp. 61-70; 
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},
	month = {2007///},
	pages = {3644 - 3655},
	abstract = {There is a need for new therapeutic strategies to treat bone defects caused by trauma, disease or tissue loss. Injectable systems for cell transplantation have the advantage of allowing the use of minimally invasive surgical procedures, and thus for less discomfort to patients. In the present study, it is hypothesized that Arg-Gly-Asp (RGD)-coupled in a binary (low and high molecular weight) injectable alginate composition is able to influence bone cell differentiation in a three-dimensional (3D) structure. Viability, metabolic activity, cytoskeleton organization, ultrastructure and differentiation (alkaline phosphatase (ALP), von Kossa, alizarin red stainings and osteocalcin quantification) of immobilized cells were assessed. Cells within RGD-modified alginate microspheres were able to establish more interactions with the synthetic extracellular matrix as visualized by confocal laser scanning microscope and transmission electron microscopy imaging, and presented a much higher level of differentiation (more intense ALP and mineralization stainings and higher levels of osteocalcin secretion) when compared to cells immobilized within unmodified alginate microspheres. These findings demonstrate that peptides covalently coupled to alginate were efficient in influencing cell behavior within this 3D system, and may provide adequate preparation of osteoblasts for cell transplantation. {\textcopyright} 2007 Elsevier Ltd. All rights reserved.},
	keywords = {3T3 Cells, Alginate, Alginates, alginic acid, alkaline phosphatase, animal cell, Animals, arginylglycylaspartic acid, article, Bone, bone cell, Bone Regeneration, calvaria, cell adhesion, cell differentiation, Cell encapsulation, Cell immobilization, cell metabolism, cell proliferation, cell survival, cell ultrastructure, cell viability, confocal laser microscopy, controlled study, cytology, cytoskeleton, DNA, DNA content, ECM (extracellular matrix), enzyme activity, extracellular matrix, Glucuronic Acid, Hexuronic Acids, hydrogel, immobilized cell, metabolism, Mice, Microscopy, Confocal, Microscopy, Electron, Transmission, microsphere, Microspheres, nonhuman, Oligopeptides, osteoblast, Osteoblasts, osteocalcin, Patient treatment, priority journal, rat, RGD peptide, structure analysis, three dimensional imaging, Tissue engineering, transmission electron microscopy, Transplantation (surgical)},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-34249870130\&partnerID=40\&md5=4476a4b1ee80320328c1bf37054037bb},
	author = {Evangelista, M.B. and Hsiong, S.X. and Fernandes, R. and Sampaio, P. and Kong, H.-J. and Barrias, C.C. and Salema, R. and Barbosa, M.A. and Mooney, D.J. and Granja, P.L.}
}
@book {2414,
	title = {Calcium phosphate microspheres for localised delivery of a therapeutic enzyme},
	series = {Key Engineering MaterialsKey Eng Mat},
	volume = {309-311 II},
	year = {2006},
	note = {Export Date: 21 November 2012Source: ScopusCODEN: KEMAELanguage of Original Document: EnglishCorrespondence Address: Barrias, C.C.; INEB - Instituto de Engenharia Biom{\'e}dica, Laborat{\'o}rio de Biomateriais, R. Campo Alegre 823, 4150-180 Porto, Portugal; email: ccbarrias@ineb.up.ptReferences: Barrias, C.C., Ribeiro, C.C., Barbosa, M.A., (2004) Key Eng. Mater., 254-256, p. 877;Barrias, C.C., Ribeiro, C.C., Lamghari, M., Miranda, C.S., Barbosa, M.A., (2005) J. Biomed. Mater. Res. A, 72 A, p. 57; 
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},
	month = {2006///},
	pages = {903 - 906},
	abstract = {The ability of calcium titanium phosphate (CTP) and hydroxyapatite (HAp) microspheres to reversibly adsorb the enzyme glucocerebrosidase (GCR) while preserving its biological activity, and efficiently deliver it to Gaucher disease (GD) fibroblasts was investigated. CTP microspheres adsorbed ca. 3.6-fold more GCR than HAp microspheres. The activity of adsorbed GCR was higher than the free enzyme in the case of CTP microspheres and lower when HAp was used. GCR release from both types of microspheres was characterized by the initial elution of a large percentage of enzyme followed by a delayed release that extended for at least 30 days. Released GCR was internalized by GD fibroblasts increasing their intracellular enzymatic activity. In cells treated with the same amount of GCR-loaded CTP microspheres or free-GCR a higher intracellular activity was detected in the former case, suggesting an improved efficacy.},
	keywords = {Adsorption, Biocompatibility, biological activity, Biomaterials, Calcium Compounds, Calcium titanium phosphate, Calcium titanium phosphate (CTP), Cells, Enzyme adsorption, Enzymes, hydroxyapatite, Microspheres},
	isbn = {10139826 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-33645396489\&partnerID=40\&md5=de3cf8530e8c690b254fed782b964340},
	author = {Barrias, C.C. and Ribeiro, C.C. and Martins, M.C.L. and Barbosa, M.A. and Rodrigues, D. and Miranda, M.C.S.}
}
@article {2409,
	title = {Cellulose phosphates as biomaterials. In vitro biocompatibility studies},
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	year = {2006},
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},
	month = {2006///},
	pages = {728 - 739},
	abstract = {Grafting of phosphate groups has been investigated as a means to render biomedical polymers able to induce the formation of an apatite layer. In the present investigation, regenerated cellulose hydrogels were surface modified by phosphorylation using a previously reported method. The in vitro biocompatibility of materials with varying phosphate contents was evaluated in cultured human bone marrow stromal cells (HBMSC), in terms of cytotoxicity, cell attachment, proliferation and immunohistochemistry. Negatively charged cellulose phosphates were neutralized in the form of the calcium salt before contact with cells. Cellulose phosphates were not cytotoxic, independently of the phosphate content. Unmodified regenerated cellulose hydrogels showed good rates of HBMSC attachment and proliferation. On the contrary, negatively charged, highly hydrophilic, phosphorylated surfaces showed poor HBMSC attachment and proliferation, as well as poor alkaline phosphatase-specific activity and expression of osteocalcin and type I collagen. Differences found are discussed in terms of surface chemical functionality, hydrophilicity and charge. {\textcopyright} 2005 Elsevier B.V. All rights reserved.},
	keywords = {Biocompatibility, Biomaterials, Cell attachment, Cell culture, Cellulose, Cellulose derivatives, Cellulose phosphates, Cytotoxicity, Grafting (chemical), Human bone marrow stromal cells, Hydrogels, hydrophilicity, immunohistochemistry, In vitro, Phosphorylation, Proliferation, Regenerated cellulose hydrogels, toxicity},
	isbn = {13815148 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-33745266092\&partnerID=40\&md5=52325c348b6bd4139bbfb3dbc0419bd8},
	author = {Granja, P.L. and J{\'e}so, B.D. and Bareille, R. and Rouais, F. and Baquey, C. and Barbosa, M.A.}
}
@article {2392,
	title = {Fibrinogen adsorption, platelet adhesion and activation on mixed hydroxyl-/methyl-terminated self-assembled monolayers},
	journal = {BiomaterialsBiomaterials},
	volume = {27},
	year = {2006},
	note = {Cited By (since 1996): 70Export Date: 21 November 2012Source: ScopusCODEN: BIMADdoi: 10.1016/j.biomaterials.2006.06.010PubMed ID: 16842847Language of Original Document: EnglishCorrespondence Address: Martins, M.C.L.; INEB - Instituto de Engenharia Biom{\'e}dica, Laborat{\'o}rio de Biomateriais, Universidade do Porto, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: cmartins@ibmc.up.ptChemicals/CAS: fibrinogen, 9001-32-5; glutaraldehyde, 111-30-8, 37245-61-7; gold, 7440-57-5; thiol derivative, 13940-21-1; Alkanes; Biocompatible Materials; Fibrinogen, 9001-32-5; hydroxide ion, 14280-30-9; Hydroxides; Sulfhydryl CompoundsReferences: Savage, B., Ruggeri, Z.M., Selective recognition of adhesive sites in surface-bound fibrinogen by glycoprotein-iib-iiia on nonactivated platelets (1991) J Biol Chem, 266 (17), pp. 11227-11233;Tsai, W.B., Grunkemeier, J.M., McFarland, C.D., Horbett, T.A., Platelet adhesion to polystyrene-based surfaces preadsorbed with plasmas selectively depleted in fibrinogen, fibronectin, vitronectin, or von Willebrand{\textquoteright}s factor (2002) J Biomed Mater Res, 60 (3), pp. 348-359; 
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},
	month = {2006///},
	pages = {5357 - 5367},
	abstract = {The effect of surface wettability on fibrinogen adsorption, platelet adhesion and platelet activation was investigated using self-assembled monolayers (SAMs) containing different ratios of longer chain methyl- and shorter chain hydroxyl-terminated alkanethiols (C15CH3 vs. C11OH) on gold. Protein adsorption studies were performed using radiolabeled human fibrinogen (HFG). Platelet adhesion and activation studies with and without pre-adsorbed fibrinogen, albumin and plasma were assessed using scanning electron microscopy (SEM) and a glutaraldehyde-induced fluorescence technique (GIFT). Results demonstrated a linear decrease of HFG adsorption with the increase of OH groups on the monolayer (increase of the hydrophilicity). Platelet adhesion and activation also decrease with increase of hydrophilicity of surface. Concerning SAMs pre-immersed in proteins, fibrinogen adsorption was related with high platelet adhesion and activation. The passivant effect of albumin on platelet adhesion and activation was only demonstrated on SAMs contained C11OH. When all the blood proteins are present (plasma) platelet adhesion was almost absent on SAMs with 65\% and 100\% C11OH. This could be explained by the higher albumin affinity of the SAMs with 65\% C11OH and the lower total protein adsorption associated with SAMs with 100\% C11OH. {\textcopyright} 2006 Elsevier Ltd. All rights reserved.},
	keywords = {Adsorption, Albumin, alkane derivative, Alkanes, article, binding affinity, Biocompatible Materials, Blood Platelets, Cells, Cultured, Chemical reactions, controlled study, Crystallization, fibrinogen, Fluorescence, fluorescence analysis, glutaraldehyde, gold, human, human cell, Humans, hydrophilicity, Hydroxides, hydroxyl group, materials testing, methyl group, Methylation, monolayer culture, Monolayers, normal human, Organic compounds, plasma, Plasma protein, Platelet activation, Platelet adhesion, Platelet Adhesiveness, priority journal, Protein adsorption, protein binding, Proteins, Radiolabeled human fibrinogen (HFG), Scanning electron microscopy, Self assembled, SEM, Sulfhydryl Compounds, surface property, thiol derivative, thrombocyte adhesion, wettability},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-33746216936\&partnerID=40\&md5=c2c54ad0448df431fbd884394915eb51},
	author = {Rodrigues, S.N. and Gon{\c c}alves, I.C. and Martins, M.C.L. and Barbosa, M.A. and Ratner, B.D.}
}
@article {2399,
	title = {Functionalization of chitosan membranes through phosphorylation: Atomic force microscopy, wettability, and cytotoxicity studies},
	journal = {Journal of Applied Polymer ScienceJ. Appl. Polym. Sci.},
	volume = {102},
	year = {2006},
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},
	month = {2006///},
	pages = {276 - 284},
	abstract = {Grafting negatively charged groups such as phosphates is a well-known strategy for inducing the deposition of apatite-like layers under simulated physiological conditions. In this investigation, chitosan was phosphorylated in an attempt to enhance its osteoconduction. Chitosan membranes were phosphorylated at 30{\textdegree}C with the H                        3PO
                        4/ Et 
                        3PO
                        4/P
                        2O
                        5/butanol reaction system for periods up to 48 h. This method is an alternative to the phosphoric acid/ urea/dimethylformamide phosphorylation method, which involves the use of much higher temperatures. In this study, the effects of the phosphorylation reaction time on the surface morphology and surface free energy of phosphorylated membranes were investigated with atomic force microscopy and static-contact-angle measurements, respectively. In addition, the modified membranes were evaluated with respect to their cytotoxiciry toward bone cells through the incubation of human osteoblastic cells with extracts of the materials for two different periods: 24 and 120 h. The results revealed a reduction of the average surface roughness at the nanometer scale with increasing phosphorylation reaction time. Wettability studies showed an increase in the polar component of the surface free energy with increasing reaction time as a result of the increase in the phosphate surface concentration. Cytotoxicity studies revealed no cytotoxic effect of phosphorylated membranes on osteoblastic cells, regardless of the incubation period. {\textcopyright} 2006 Wiley Periodicals, Inc.
},
	keywords = {Atomic force microscopy, Atomic force microscopy (AFM), Biocompatibility, Biological applications, Biological applications of polymers, Biomaterials, Chitin, chitosan, Chitosan membranes, grafting, Grafting (chemical), Osteoblastic cells, Phosphorylation, Polymeric membranes, polysaccharide, Polysaccharides, surface property, toxicity, Urea},
	isbn = {00218995 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-33749478403\&partnerID=40\&md5=c365a50e3e767b1da90ad4ccd331440b},
	author = {Amaral, I.F. and Granja, P.L. and Melo, L.V. and Saramago, B. and Barbosa, M.A.}
}
@article {2420,
	title = {The influence of functional groups of self-assembled monolayers on fibrous capsule formation and cell recruitment},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {76},
	year = {2006},
	note = {Cited By (since 1996): 13Export Date: 21 November 2012Source: ScopusCODEN: JBMRCdoi: 10.1002/jbm.a.30602Language of Original Document: EnglishCorrespondence Address: Barbosa, J.N.; INEB-Instituto de Engenharia Biom{\'e}dica, Laborat{\'o}rio de Biomateriais, Rua do Campo Alegre 823, 4150-180 Porto, Portugal; email: judite@ibmc.up.ptChemicals/CAS: gold, 7440-57-5; thiol derivative, 13940-21-1; Biocompatible Materials; Gold, 7440-57-5; Sulfhydryl CompoundsReferences: Babensee, J.E., Anderson, J.M., McIntire, L.V., Mikos, A.G., Host response to tissue engineered devices (1998) Adv Drug Deliv Rev, 33, pp. 111-139;Anderson, J.M., In vivo biocompatibility of implantable delivery systems and biomaterials (1994) Eur J Pharm Biopharm, 40, pp. 1-8; 
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},
	month = {2006///},
	pages = {737 - 743},
	abstract = {The contribution of the surface chemistry of an implant to the thickness of the fibrous capsule formed after implantation was herein investigated. For that, self-assembled monolayers (SAMs) of alkanethiols on gold with different terminal functional groups (COOH, OH, and CH                        3) were used. These surfaces were implanted in subcutaneous air pouches of BALB/c mice and the ensuing fibrous capsules were evaluated and compared with the initial inflammatory response caused by the implant. The thickness of the fibrous capsules that are under organization around the implant was measured 1 week after implantation by histology. Inflammatory exudates were collected from the air pouches 24 h after the implantation of SAMs and were analyzed by flow cytometry. A significant increase in the thickness of fibrous capsules was seen around implanted CH
                        3-terminated SAMs, and also in gold surfaces, in comparison with the air pouch wall of sham-operated mice and of COOH- and OH-covered SAMs. The CH
                        3-coated implants also recruited higher numbers of inflammatory cells; this enhancement involved a significant number of Mac-1
                        + cells. Our data indicate that implant surfaces coated with CH
                        3 induce thick fibrous capsules and this may be the result of the stronger inflammatory effect of CH
                        3 in comparison with COOH or OH chemical groups. {\textcopyright} 2005 Wiley Periodicals, Inc.
},
	keywords = {animal, animal cell, animal experiment, animal model, animal tissue, Animals, article, Bagg albino mouse, Biocompatible Materials, biomaterial, chemistry, controlled study, flow cytometry, functional group, gold, histology, implantation, Inflammation, male, Mice, Mice, Inbred BALB C, Monolayers, mouse, nonhuman, Self assembly, Self-assembled monolayers, Sulfhydryl Compounds, Surface chemistry, thiol derivative, tissue reaction, Tissue responses},
	isbn = {15493296 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-33745564665\&partnerID=40\&md5=6cbc5f976e86764eea35724a4af706f9},
	author = {Barbosa, J.N. and Madureira, P. and Barbosa, M.A. and {\'A}guas, A.P.}
}
@article {2408,
	title = {Leptin effect on RANKL and OPG expression in MC3T3-E1 osteoblasts},
	journal = {Journal of Cellular BiochemistryJ. Cell. Biochem.},
	volume = {98},
	year = {2006},
	note = {Cited By (since 1996): 17Export Date: 21 November 2012Source: ScopusCODEN: JCEBDdoi: 10.1002/jcb.20853PubMed ID: 16479591Language of Original Document: EnglishCorrespondence Address: Lamghari, M.; INEB-Instituto de Engenharia Biom{\'e}dica, Laborat{\'o}rio de Biomateriais, Rua Campo Alegre 823, 4150-180, Porto, Portugal; email: lamghari@ineb.up.ptChemicals/CAS: osteoclast differentiation factor, 200145-93-3; osteoprotegerin, 205944-50-9; Alkaline Phosphatase, EC 3.1.3.1; Carrier Proteins; Glycoproteins; leptin receptor; Leptin; Membrane Glycoproteins; Osteoprotegerin; RANK Ligand; Receptor Activator of Nuclear Factor-kappa B; Receptors, Cell Surface; Receptors, Cytoplasmic and Nuclear; Receptors, Tumor Necrosis Factor; RNA, Messenger; Tnfrsf11a protein, mouse; Tnfrsf11b protein, mouse; Tnfsf11 protein, mouseReferences: Burguera, B., Hofbauer, L.C., Thomas, T., Gori, F., Evans, G.L., Khosla, S., Riggs, B.L., Turner, R.T., Leptin reduces ovariectomy-induced bone loss in rats (2001) Endocrinology, 142, pp. 3546-3553;Cornish, J., Callon, K.E., Bava, U., Lin, C., Naot, D., Hill, B.L., Grey, A.B., Reid, I.R., Leptin directly regulates bone cell function in vitro and reduces bone fragility in vivo (2002) J Endocrinol, 175, pp. 405-415; 
Ducy, P., Amling, M., Takeda, S., Priemel, M., Schilling, A.F., Beil, F.T., Shen, J., Karsenty, G., Leptin inhibits bone formation through a hypothalamic relay: A central control of bone mass (2000) Cell, 100, pp. 197-207; 
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Holloway, W.R., Collier, F.M., Aitken, C.J., Myers, D.E., Hodge, J.M., Malakellis, M., Gough, T.J., Nicholson, G.C., Leptin inhibits osteoclast generation (2002) J Bone Miner Res, 17, pp. 200-209; 
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Kanematsu, M., Yoshimura, K., Takaoki, M., Sato, A., Vector-averaged gravity regulates gene expression of receptor activator of NF-κB (RANK) ligand and osteoprotegerin in bone marrow stromal cells via cyclic AMP/protein kinase A pathway (2002) Bone, 30, pp. 553-558; 
Lacely, D.L., Timms, E., Tan, H.L., Dunstan, C.R., Burgess, T., Elliott, R., Colombero, A., Boyle, W.J., Osteoproteferin ligand is a cytokine that regulates osteoclast differentiation and activation (1998) Cell, 93, pp. 165-167; 
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Lee, S.K., Lorenzo, J.A., Regulation of receptor activator of nuclear factor-κB ligand and osteoprotegerin mRNA expression by parathyroid hormone is predominantly mediated by the protein kinase a pathway in murine bone marrow cultures (2002) Bone, 31, pp. 252-259; 
Lee, Y.J., Park, J.H., Ju, S.K., You, K.H., Ko, J.S., Kim, H.M., Leptin receptor isoform expression in rat osteoblasts and their functional analysis (2002) FEBS Lett, 528, pp. 43-47; 
Liu, J., Yang, H., Liu, W., Cao, X., Feng, X., Sp1 and Sp3 regulate the basal transcription of receptor activator of nuclear factor kappa B ligand gene in osteoblasts and bone marrow stromal cells (2005) J Cell Biochem, 96 (4), pp. 716-727; 
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Reseland, J.E., Syversen, U., Bakke, I., Ovigstad, G., Eide, L.G., Hjertner, O., Gordeladze, J.O., Drevon, C.A., Leptin is expressed in and secreted from primary cultures of human osteoblasts and promotes bone mineralization (2001) J Bone Miner Res, 16, pp. 1426-11414; 
Rubin, J., Ackert-Bicknell, C., Zhu, L., Fan, X., Murphy, T., Nanes, M., Marcus, R., Rosen, C., Insulin like growth factor-I (IGF-I) regulates osteoprotegerin (OPG) and RANK ligand (RANKL) in vitro and osteoprotogerin in vivo (2002) J Clin Endocrinal Metab, 87, pp. 4273-4279; 
Rubin, J., Murphy, T., Fan, X., Goldschmidt, M., Taylor, W., Mechanical strain inhibits RANKL expression through activation of ERK1/2 in bone marrow stromal cells (2002) J Bone Miner Res, 17, pp. 1452-1460; 
Simonet, W.S., Lacey, D.L., Dunstan, C.R., Kelley, M., Chang, M.S., Luthy, R., Nguyen, H.Q., Boyle, W.J., Osteoprotegerin: A novel secreted protein involved in the regulation of bone density (1997) Cell, 89, pp. 309-319; 
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Suda, T., Ueno, Y., Fujii, K., Shinki, T., Vitamin D and bone (2003) J Cell Biochem, 88, pp. 259-266; 
Thomas, T., Gori, F., Khosla, S., Jensen, M.D., Burguera, B., Riggs, B.L., Leptin acts on human marrow stromal cells to enhance differentiation to osteoblasts and to inhibit differentiation to adipocytes (1999) Endocrinology, 140, pp. 1630-1638; 
Udagawa, N., Takahashi, N., Yasuda, H., Mizuno, A., Itoh, K., Ueno, Y., Shinki, T., Suda, T., Osteoprotegerin produced by osteoblasts is an important regulator in osteoclast development and function (2000) Endocrinology, 141, pp. 3478-3484; 
Wamoto, I., Fujino, T., Douchi, T., The leptin receptor in human osteoblasts and the direct effect of leptin on bone metabolism (2004) Gynecol Endocrinol, 19, pp. 97-104; 
Yasuda, H., Shima, N., Nakagawa, N., Yamaguchi, K., Kinosaki, M., Mochizuki, S., Tomoyasu, A., Suda, T., Osteoclast differentiation factor is a ligand for osteoprotegerin/ osteoclastogenesis-inhibitory factor and is identical to TRANCE/RANKL (1998) Proc Natl Acad Sci USA, 95, pp. 3597-3602
},
	month = {2006///},
	pages = {1123 - 1129},
	abstract = {Recent studies have suggested that leptin hormone may play a pivotal role on bone remodeling through a direct effect by modulating positively the OPG/RANKL balance. Here, we investigate the effect of leptin hormone on RANKL and OPG expression in MC3T3-E1 osteoblasts using RT-PCR and ELISA measurements. We have at first identified the expression of Ob-Rb and Ob-Ra leptin receptor isoforms in MC3T3-E1 and observed that these cells respond to mrleptin treatments. We then investigated the effect of mrleptin on RANKL and OPG expression. We show that mrleptin dose-dependently regulated the expression of RANKL mRNA with complete inhibition observed at concentrations higher than 12 ng/ml. This effect was confirmed with sRANKL protein measurements. However, the exposure of MC3T3-E1 to mrleptin had no effect on OPG mRNA. Taken together, these results suggest that leptin modulates positively OPG/RANKL balance by inhibiting the expression of RANKL gene. {\textcopyright} 2006 Wiley-Liss, Inc.},
	keywords = {alkaline phosphatase, animal cell, Animals, article, bone remodeling, Carrier Proteins, Cell Line, enzyme linked immunosorbent assay, gene expression, gene expression regulation, Glycoproteins, hormone action, leptin, leptin receptor, leptin receptor a, leptin receptor b, MC3T3-E1, Membrane Glycoproteins, messenger RNA, Mice, mouse, nonhuman, Ob-Ra, Ob-Rb, OPG, osteoblast, Osteoblasts, osteoclast differentiation factor, Osteoprotegerin, priority journal, protein expression, RANK Ligand, RANKL, Receptor Activator of Nuclear Factor-kappa B, Receptors, Cell Surface, Receptors, Cytoplasmic and Nuclear, Receptors, Tumor Necrosis Factor, reverse transcription polymerase chain reaction, RNA extraction, RNA, Messenger, unclassified drug},
	isbn = {07302312 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-33746452603\&partnerID=40\&md5=f5eb37e7159ced26f3b7e756d59bc1bb},
	author = {Lamghari, M. and Tavares, L. and Camboa, N. and Barbosa, M.A.}
}
@article {2421,
	title = {Three-dimensional culture of human osteoblastic cells in chitosan sponges: The effect of the degree of acetylation},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {76},
	year = {2006},
	note = {Cited By (since 1996): 19Export Date: 21 November 2012Source: ScopusCODEN: JBMRCdoi: 10.1002/jbm.a.30522PubMed ID: 16270345Language of Original Document: EnglishCorrespondence Address: Amaral, I.F.; INEB-Instituto de Engenharia Biom{\'e}dica, Laborat{\'o}rio de Biomateriais, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: iamaral@ineb.up.ptChemicals/CAS: alkaline phosphatase, 9001-78-9; chitosan, 9012-76-4; collagen, 9007-34-5; Alkaline Phosphatase, EC 3.1.3.1; Chitosan, 9012-76-4; Collagen, 9007-34-5References: Bruder, S.P., Caplan, A.I., Bone regeneration through cellular engineering (2000) Principles of Tissue Engineering, pp. 683-696. , Lanza RP, Langer R, Vacanti J, editors. San Diego: Academic Press;Anselme, K., Osteoblast adhesion on biomaterials (2000) Biomaterials, 21, pp. 667-681; 
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},
	month = {2006///},
	pages = {335 - 346},
	abstract = {In this investigation, the effect of the degree of acetylation (DA) of chitosan on the behavior of human osteoblastic MG-63 cells cultured in three-dimensional chitosan matrices was assessed. Chitosan sponges with DAs in the range of 4 to 49\% were prepared and characterized in terms of microstructure, porosity, and pore size. Collagen sponges were used as 3D control. Cell proliferation was determined using the MTT assay while the retention of the osteoblastic phenotype was monitored by assaying alkaline phosphatase activity. Cell morphology, cytoskeletal organization, and viability were assessed using different microscopy techniques. Chitosan sponges showed a similar microstructure regardless the DA, except for the highest DA used, where a more heterogeneous pore distribution was observed. In terms of cell proliferation, alkaline phosphatase activity and cell viability, cells cultured in chitosan scaffolds performed as well as in the 3D control regardless the DA, except for the highest DA used, where an inhibitory effect on cell proliferation was found. However, while in sponges with DAs <= 13\% cells attached and spread displaying long cell filopodia and numerous cell-to-cell contacts, in sponges with higher DAs cells tended to remain spherical and grow into spheroid-like cellular aggregates. In the present study, the DA played a key role in determining the affinity of osteoblastic cells towards the substrates, possibly by influencing the nature of the initial adsorbed protein layer. {\textcopyright} 2005 Wiley Periodicals, Inc.},
	keywords = {Acetylation, Aggregates, alkaline phosphatase, article, Bone Regeneration, bone tissue, Bone tissue engineering, Cell culture, Cell Culture Techniques, Cell filopodia, cell growth, cell proliferation, Cell Shape, cell structure, cell survival, cell viability, chitosan, Collagen, confocal microscopy, controlled study, Cytoskeletal organization, cytoskeleton, Degree of acetylation (DA), enzyme activity, gel permeation chromatography, human, human cell, Humans, infrared spectroscopy, Microstructure, morphology, osteoblast, Osteoblastic cells, Osteoblasts, Phosphatase activity, porosity, Proteins, Scaffold, Scaffolds, Scanning electron microscopy, Substrates, Tissue engineering},
	isbn = {00219304 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-33645101773\&partnerID=40\&md5=5adc6336963ec1c8a83d8ec89943159d},
	author = {Amaral, I.F. and Sampaio, P. and Barbosa, M.A.}
}
@article {2418,
	title = {The uptake of titanium ions by hydroxyapatite particles - Structural changes and possible mechanisms},
	journal = {BiomaterialsBiomaterials},
	volume = {27},
	year = {2006},
	note = {Cited By (since 1996): 44Export Date: 21 November 2012Source: ScopusCODEN: BIMADdoi: 10.1016/j.biomaterials.2005.09.043PubMed ID: 16256192Language of Original Document: EnglishCorrespondence Address: Ribeiro, C.C.; INEB - Instituto de Engenharia Biom{\'e}dica, Laborat{\'o}rio de Biomateriais, Rua do Campo Alegre 823, Porto 4150-180, Portugal; email: cribeiro@ineb.up.ptChemicals/CAS: hydroxyapatite, 1306-06-5, 51198-94-8; titanium, 7440-32-6; Biocompatible Materials; Durapatite, 1306-06-5; Ions; Solutions; titanium phosphate, 17017-57-1; Titanium, 7440-32-6References: Fowler, B.O., Infrared studies of apatites. II Preparation of normal and isotopically substituted calcium, strontium, and barium hydroxyapatites and spectra-structure-composition correlations (1974) Inorg Chem, 13, pp. 207-214;Legeros, R.Z., Daculsi, G., Orly, I., Abergas, T., Torres, W., Solution mediated transformation of octacalcium phosphate (OCP) to apatite (1989) Scann Microsc, 3, pp. 129-138; 
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},
	month = {2006///},
	pages = {1749 - 1761},
	abstract = {In order to understand the effect of titanium ions on the molecular structure of hydroxyapatite (HAp), HAp powders were incubated in solutions with different titanium concentrations. After incubation, the powders obtained were analysed using different techniques, namely X-ray diffraction (XRD), Fourier transform infrared spectroscopy (FT-IR), differential thermal analysis (DTA), X-ray photoelectron spectroscopy (XPS), and energy dispersive spectroscopy (EDS). The results suggest that, depending on the concentration of titanium in solution, two different mechanisms of interaction with HAp occur. For concentrations equal to or smaller than 200 ppm, the titanium uptake by the solid seems to be primarily due to incorporation in the lattice. For higher concentrations, a dissolution-precipitation process seems to occur, leading to formation of a titanium phosphate compound. {\textcopyright} 2005 Elsevier Ltd. All rights reserved.},
	keywords = {article, Biocompatible Materials, concentration response, differential scanning calorimetry, drug mechanism, drug structure, Durapatite, Energy dispersive spectroscopy, Fourier transform infrared spectroscopy, hydroxyapatite, Incubation, infrared spectroscopy, Ions, Lattice constants, particulate matter, powder, Precipitation (chemical), priority journal, Solutions, Spectroscopy, Spectroscopy, Fourier Transform Infrared, temperature, Titanium, Titanium ions, Titanium phosphate, X ray diffraction, X ray diffraction analysis, X ray photoelectron spectroscopy, X-Ray Diffraction},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-28744435342\&partnerID=40\&md5=d3c05375129c7b4a53ec5a0c4b4271d3},
	author = {Ribeiro, C.C. and Gibson, I. and Barbosa, M.A.}
}
@article {2447,
	title = {Biological evaluation of calcium alginate microspheres as a vehicle for the localized delivery of a therapeutic enzyme},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {74},
	year = {2005},
	note = {Cited By (since 1996): 12Export Date: 21 November 2012Source: ScopusCODEN: JBMRCdoi: 10.1002/jbm.a.30348PubMed ID: 16028235Language of Original Document: EnglishCorrespondence Address: Barrias, C.C.; Instituto de Engenharia Biom{\'e}dica (INEB), Laborat{\'o}rio de Biomateriais, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: ccbarrias@ineb.up.ptChemicals/CAS: alginic acid, 28961-37-7, 29894-36-8, 9005-32-7, 9005-38-3; calcium alginate, 9005-35-0; glucosylceramidase, 37228-64-1; iodine 125, 14158-31-7, 22822-81-7; Alginates; alginic acid, 9005-32-7; Drug Carriers; Enzymes, Immobilized; Glucosylceramidase, EC 3.2.1.45; Glucuronic Acid, 576-37-4; Hexuronic AcidsManufacturers: GenzymeReferences: Grabowski, G.A., Leslie, N., Wenstrup, R., Enzyme therapy for Gaucher disease: The first 5 years (1998) Blood Rev, 12, pp. 115-133;Zhao, H., Grabowski, G.A., Gaucher disease: Perspectives on a prototype lysosomal disease (2002) Cell Mol Life Sci, 59, pp. 694-707; 
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},
	month = {2005///},
	pages = {545 - 552},
	abstract = {Gaucher disease (GD) is caused by the decreased activity and/or stability of the lysosomal enzyme glucocerebrosidase (GCR). The available treatment consists in the intravenous administration of exogenous GCR, and is effective in reverting most of the symptoms. However, in terms of bone pathology, which is among the most disabling manifestations, a slow and incomplete response is observed, indicating that adjuvant therapies are necessary to consistently restore GCR activity in bone and accelerate regeneration. In this study, calcium alginate microspheres were analyzed as a vehicle for localized GCR delivery to bone. Results demonstrated that the entrapped enzyme retained full activity and exhibited a broader pH-dependent activity profile, compared to that of free-GCR, with improved stability at physiological pH. GCR release profile was established, and it was demonstrated that GCR could be released in a sustained manner. The biological behavior of the system was evaluated by analyzing the uptake of released GCR by GCR-deficient cells from GD patients, using different techniques: GCR activity measurements, radiolabeling, and cellulose acetate electrophoresis. Results demonstrated that GCR was internalized by cells significantly enhancing the residual enzymatic activity. To achieve an activity reconstitution level comparable to that obtained using free-GCR, only half of the dose was required with entrapped-GCR. {\textcopyright} 2005 Wiley Periodicals, Inc.},
	keywords = {Alginates, alginic acid, article, Bone, bone disease, Bone Regeneration, Calcium alginate, Calcium Compounds, catalysis, Cell culture, Cells, Cultured, controlled study, Drug Carriers, drug delivery system, enzyme activity, enzyme assay, enzyme replacement, Enzymes, Enzymes, Immobilized, fibroblast culture, Fibroblasts, Gaucher disease, Gaucher disease (GD), Glucocerebrosidase (GCR), Glucosylceramidase, Glucuronic Acid, Hexuronic Acids, human, human cell, Humans, iodine 125, Localized delivery, lysosome enzyme, lysosome storage disease, microsphere, Microspheres, Pathology, pH effects, physiology, recombinant enzyme, Therapeutic enzyme},
	isbn = {00219304 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-24044465170\&partnerID=40\&md5=bbcee8568e0c0223975853a8177439c8},
	author = {Barrias, C.C. and Lamghari, M. and Granja, P.L. and S{\'a} Miranda, M.C. and Barbosa, M.A.}
}
@article {2438,
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	year = {2005},
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},
	month = {2005///},
	pages = {1575 - 1593},
	abstract = {In the present work, the surface of chitosan membranes was modified using a phosphorylation method carried out at room temperature. Phosphorylation may be of particular interest in materials for orthopaedic applications, due to the cation-exchange properties of phosphate functionalities. Phosphate groups chelate calcium ions, thus inducing the deposition of an apatite-like layer known to improve the osteoconduction of polymer-based implants. Additionally, the negatively charged phosphate functionalities, together with the positively charged amine groups from chitosan, are expected to provide chitosan with an amphoteric character, which may be useful as a combinatorial therapeutic strategy, by simultaneously allowing the immobilization of signalling molecules like growth factors. Phosphorylation was carried out at room temperature using the H                        3 PO
                        4/Et
                        3 PO
                        4/P
                        2O
                        5/butanol method. Surface characterization was performed by XPS, ATR-FT-IR, and SEM. Cross-sections were analyzed by SEM fitted with EDS. The phosphate content increased with the reaction time, as shown by XPS and ATR-FT-IR, a P/N atomic ratio of 0.73 being obtained after 48 h of treatment. High-resolution XPS spectra regarding C
                        1s, O
                        1s, N
                        1s and P
                        2p are discussed. The introduction of a neutralization step led to a reduction of P content, which pointed out to the presence of phosphates ionically bound to protonated amines, in addition to phosphate esters. EDS analysis of cross-sections revealed a gradual P reduction up to 50\% towards the inner part of the membrane. {\textcopyright} VSP 2005.
},
	keywords = {Acetylation, amine, animal, Animals, Apatite, article, bone conduction, butanol, calcium ion, cation exchange, cephalopod, chelate, Chemical modification, chemistry, Chitin, chitosan, comparative study, controlled study, Decapodiformes, Fourier transform infrared spectroscopy, Fourier transform infrared spectroscopy (FT-IR), Growth factor, immobilization, Implants (surgical), infrared spectroscopy, isolation and purification, Microscopy, Electron, Scanning, molecular weight, organophosphate, phosphate, Phosphate groups, Phosphates, Phosphorylation, Phosphorylation method, Plastics applications, priority journal, reflectometry, room temperature, Scanning electron microscopy, SEM-EDS, signal transduction, spectrometry, Spectrometry, X-Ray Emission, Spectroscopy, Fourier Transform Infrared, Surface chemical reaction, Surface Properties, surface property, temperature, time, Time Factors, viscosity, X ray photoelectron spectroscopy, X-rayphotoelectron spectroscopy (XPS)},
	isbn = {09205063 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-33644875542\&partnerID=40\&md5=cb42a0fba6d2000d93b90af9724a5bc1},
	author = {Amaral, I.F. and Granja, P.L. and Barbosa, M.A.}
}
@book {2426,
	title = {Effect of calcium phosphate addition to alginate microspheres: modulation of enzyme release kinetics and improvement of cell adhesion},
	series = {Key Engineering MaterialsKey Eng Mat},
	volume = {284-286},
	year = {2005},
	note = {Cited By (since 1996): 4Export Date: 21 November 2012Source: ScopusCODEN: KEMAELanguage of Original Document: EnglishCorrespondence Address: Barrias, C.C.; INEB - Institute de Engenharia Biom{\'e}dica, Laborat{\'o}rio de Biomaterials, R. Campo Alegre 823, 4150-180 Porto, Portugal; email: ccbarrias@ineb.up.ptReferences: Graopwski, G.A., Leslie, N., Wenstrup, R., (1998) Blood Rev, 12, p. 115;Rowley, J.A., Madlambayan, G., Mooney, D.J., (1999) Biomaterials, 20, p. 45; 
Dalby, M.J., Di Silvio, L., Harper, E.J., Bonfield, W., (2002) Biomaterials, 23, p. 569
},
	month = {2005///},
	pages = {689 - 692},
	abstract = {In this study, the addition of calcium phosphate powders to an alginate matrix was evaluated as a strategy to modulate enzyme release-kinetics from alginate microspheres and, simultaneously, to improve cell adhesion to the polymer. Pre-adsorption of the enzyme to the ceramic powders resulted in a more adequate release pattern. The ratio of ceramic-to-polymer had a pronounced effect on osteoblast adhesion to microspheres. Cells were only able to spread on microspheres with the highest percentage of ceramic (0.4 w/w using a 1.5\% w/v alginate solution).},
	keywords = {Alginate, Bioceramics, calcium phosphate, Calcium titanium phosphate, cell adhesion, Enzyme kinetics, Enzyme release, hydroxyapatite, Microspheres, Osteoblasts},
	isbn = {10139826 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-20744433251\&partnerID=40\&md5=30ce8fc67d1e3e37074cc056f650b798},
	author = {Barrias, C.C. and Ribeiro, C.C. and Rodrigues, D. and Miranda, M.C.S. and Barbosa, M.A.}
}
@article {2441,
	title = {Improving the adhesion of poly(ethylene terephthalate) fibers to poly(hydroxyethyl methacrylate) hydrogels by ozone treatment: Surface characterization and pull-out tests},
	journal = {PolymerPolymer},
	volume = {46},
	year = {2005},
	note = {Cited By (since 1996): 6Export Date: 21 November 2012Source: ScopusCODEN: POLMAdoi: 10.1016/j.polymer.2005.08.033Language of Original Document: EnglishCorrespondence Address: Ferreira, L.; Instituto de Engenharia Biom{\'e}dica, Laborat{\'o}rio de Biomateriais, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: lino@mit.eduReferences: Hart, B.L., Deyo, R.A., Cherkin, D.C., (1995) Spine, 20, pp. 11-19;Bao, Q.-B., McCullen, G.M., Higham, P.A., Dumbleton, J.H., Yuan, H.A., (1996) Biomaterials, 17, pp. 1157-1167; 
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},
	month = {2005///},
	pages = {9840 - 9850},
	abstract = {This work reports a methodology to improve the adhesion between poly(ethylene terephthalate) (PET) fibers and poly(hydroxyethyl methacrylate) (pHEMA) hydrogels by treating PET with ozone. The surface chemistry of PET was examined by water contact angle measurements, X-ray photoelectron spectroscopy (XPS), infrared reflection absorption spectroscopy (IRAS) and attenuated total reflectance infrared spectroscopy (ATR-IR) yielding information about the chemical functionalities at depths upon 0.6 μm. Ozone treatment introduces several polar groups in the surface of PET through oxidation and chain scission resulting in increased wettability. These groups include mostly carboxylic and anhydride groups and in small extent hydroxyl groups. Atomic force microscopy (AFM) analysis shows that the surface of ozone-treated PET films is fully covered with spherical particles that are removed after washing the film with water. During the washing step carboxylic functionalities were removed preferentially, as demonstrated by XPS and IR analysis. According to pull-out tests, PET monofilaments and bundles treated by ozone had a higher adhesion to pHEMA hydrogels than untreated ones. The apparent interfacial shear strength is 65\% higher on pHEMA hydrogel containing an ozonated than an untreated PET monofilament. In addition, the force to pull-out an ozone-treated PET bundle from pHEMA hydrogel is ca. 81\% higher than the one observed for the untreated bundle. {\textcopyright} 2005 Elsevier Ltd. All rights reserved.},
	keywords = {Adhesion, Atomic force microscopy, Contact angle, hydrogel, Hydrogels, infrared spectroscopy, Oxidation, Ozone, ozone treatment, Ozone treatments, Poly(ethylene terephthalate), polyethylene terephthalate fiber, Polyethylene terephthalates, Polymethyl methacrylates, pull-out, Pull-out tests, Surface characterization, Surface chemistry, surface property, X ray photoelectron spectroscopy},
	isbn = {00323861 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-26844540116\&partnerID=40\&md5=bebe6186e9e73c41648eedee7d5c0f61},
	author = {Ferreira, L. and Evangelista, M.B. and Martins, M.C.L. and Granja, P.L. and Esteves, J.L. and Barbosa, M.A.}
}
@article {2450,
	title = {In vitro degradation behavior of a novel bioresorbable composite material based on PLA and a soluble CaP glass},
	journal = {Acta BiomaterialiaActa Biomater.},
	volume = {1},
	year = {2005},
	note = {Cited By (since 1996): 24Export Date: 21 November 2012Source: Scopusdoi: 10.1016/j.actbio.2005.03.004PubMed ID: 16701822Language of Original Document: EnglishCorrespondence Address: Ginebra, M.P.; Reference Centre for Bioengineering of Catalonia (CREBEC), Department of Materials Science, Universitat Polit{\`e}cnica de Catalunya, Av. Diagonal 647, 08028 Barcelona, Spain; email: maria.pau.ginebra@upc.esChemicals/CAS: calcium phosphate, 10103-46-5, 13767-12-9, 14358-97-5, 7758-87-4; polylactic acid, 26100-51-6; Bone Substitutes; calcium phosphate, 10103-46-5; Calcium Phosphates; Lactic Acid, 50-21-5; poly(lactic acid), 26100-51-6; PolymersManufacturers: Purac, NetherlandsReferences: Rokkanen, P., Bioabsorbable fixation in orthopaedic surgery and traumatology (2000) Biomaterials, 21, pp. 2607-2613;Middleton, J.C., Tipton, A.J., Synthetic biodegradable polymers as orthopedic devices (2000) Biomaterials, 21 (23), pp. 2335-2346; 
Adriano, K.P., Daniels, A.U., Smutz, W.P., Wyatt, R.W.B., Heller, J., Preliminary biocompatibility screening of several biodegradable phosphate fiber reinforced polymers (1993) J Appl Biomater, 4, pp. 1-12; 
Nazhat, S.N., Kellomaki, M., Tormala, P., Tanner, K.E., Bonfield, W., Dynamic mechanical characterization of biodegradable composites of hydroxyapatite and polylactides (2001) J Biomed Mater Res, 58 (4), pp. 335-343; 
Dupraz, A.M.P., de Wijn, J.R., v.d. Meer, S.A.T., de Groot, K., Characterization of silane-treated hydroxyapatite powders for use as filler in biodegradable composites (1996) J Biomed Mater Res, 30, pp. 231-238; 
Kasuga, T., Maeda, H., Kato, K., Nogami, M., Hata, K.-I., Ueda, M., Preparation of poly (lactic acid) composites containing calcium carbonate (vaterite) (2003) Biomaterials, 24, pp. 3247-3253; 
Ylinen, P., Suuronen, R., Taurio, R., Tormala, P., Rokkanen, P., Use of hydroxylapatite/polymer-composite in facial bone augmentation. An experimental study (2002) Int J Oral Maxillofac Surg, 31 (4), pp. 405-409; 
Lu, H.H., El-Amin, S., Scott, K., Laurencin, C., Three-dimensional, bioactive, biodegradable, polymer-bioactive glass composite scaffolds with improved mechanical properties support collagen synthesis and mineralization of human osteoblast-like cells in vitro (2003) J Biomed Mater Res, 64 A, pp. 465-474; 
Navarro, M., Ginebra, M.P., Planell, J.A., Zeppetelli, S., Ambrosio, L., Development and cell response of a new biodegradable composite scaffold for guided bone regeneration (2004) J Mater Sci-Mater Med, 15 (4), pp. 419-422; 
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Navarro, M., Ginebra, M.P., Clement, J., Martinez, S., Avila, G., Planell, J.A., Physicochemical degradation of titania-stabilized soluble phosphate glasses for medical applications (2003) J Am Ceram Soc, 86 (8), pp. 1345-1352; 
Navarro, M., Ginebra, M.P., Planell, J.A., Cellular response to calcium phosphate glasses with controlled solubility (2003) J Biomed Mater Res Part A, 67 A (3), pp. 1009-1015; 
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},
	month = {2005///},
	pages = {411 - 419},
	abstract = {Poly(α-hydroxy acids), and in particular polylactic acid (PLA), are nowadays amongst the most used bioabsorbable materials. However, this polymer may not meet some application requirements due to inadequate mechanical properties and or its degradation characteristics. A possible strategy to tackle this problem is the incorporation of an inorganic phase into the polymeric matrix. In this work a new fully biodegradable composite material made with PLA and calcium phosphate soluble glass particles has been developed. The behaviour of the PLA/ glass composite has been analysed during its degradation in simulated physiological conditions by means of weight loss, molecular weight and thermal properties analysis and electron microscopy observation. The results showed that the incorporation of phosphate glass particles into the polymer significantly accelerated the degradation of the PLA and induced the formation of calcium phosphate precipitates at the composite surface. {\textcopyright} 2005 Acta Materialia Inc. Published by Elsevier Ltd. All rights reserved.},
	keywords = {Absorbable Implants, Absorption, article, biodegradability, Biodegradable composite, Biomimetic materials, Body fluids, Bone Regeneration, Bone Substitutes, calcium phosphate, Calcium phosphates, composite material, Degradation, electron microscopy, glass, In vitro degradation, in vitro study, Lactic Acid, materials testing, molecular weight, observation, Phosphate glass, polylactic acid, Polymers, precipitation, priority journal, reaction analysis, simulation, Solubility, Surface Properties, surface property, temperature, weight reduction},
	isbn = {17427061 (ISSN)},
	author = {Navarro, M. and Ginebra, M.P. and Planell, J.A. and Barrias, C.C. and Barbosa, M.A.}
}
@article {2455,
	title = {Inflammatory cell recruitment and adhesion to methyl-terminated self-assembled monolayers: Effect of implantation time},
	journal = {Microscopy Research and TechniqueMicrosc. Res. Tech.},
	volume = {66},
	year = {2005},
	note = {Cited By (since 1996): 4Export Date: 21 November 2012Source: ScopusCODEN: MRTEEdoi: 10.1002/jemt.20141PubMed ID: 15816035Language of Original Document: EnglishCorrespondence Address: Barbosa, J.N.; INEB, Inst. de Engenharia Biom{\'e}dica, Laborat{\'o}rio de Biomateriais, Rua do Campo Alegre 823, 4150-180 Porto, Portugal; email: judite@ibmc.up.ptChemicals/CAS: gold, 7440-57-5; thiol derivative, 13940-21-1; Coated Materials, Biocompatible; Gold, 7440-57-5References: Anderson, J.M., Biological responses to materials (2001) Annu Rev Mater Res, 31, pp. 81-110;Babensee, J.E., Anderson, J.M., Mclntire, L.V., Mikos, A.G., Host response to tissue engineered devices (1998) Adv Drug Deliv Rev, 33, pp. 111-139; 
Barbosa, J.N., Barbosa, M.A., {\'A}guas, A.P., Inflammatory responses and cell adhesion to self-assembled monolayers of alkanethiolates on gold (2004) Biomaterials, 25, pp. 2557-2563; 
Castro, A.G., Esaguy, N., Macedo, P.M., {\'A}guas, A.P., Silva, M.T., Live but not heat-killed mycobacteria cause rapid chemotaxis of large numbers of eosinophils in vivo and are ingested by the attracted granulocytes (1991) Infect Immun, 59, pp. 3009-3014; 
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Hu, W., Eaton, J.W., Tang, L., Molecular basis of biomaterial-mediated foreign body reactions (2001) Blood, 98, pp. 1231-1238; 
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},
	month = {2005///},
	pages = {37 - 42},
	abstract = {The contribution of methyl groups in implant-triggered inflammation was investigated in vivo using self-assembled monolayers (SAMs) of alkanethiols on gold. The CH                        3-coated implants were inserted in an air-pouch cavity induced in BALB/c mice. The in situ inflammatory response was monitored 24, 48, and 72 hours later. Inflammatory cells recovered from the air pouches were counted and observed by light microscopy. The cellularity of the implant surfaces was defined by scanning electron microscopy (SEM). In comparison with gold implants, the CH
                        3-coated SAMs recruited a significantly higher number of inflammatory cells. Polymorphonuclear leukocytes (PMN) were more numerous than mononuclear cells (Mo) in the exudates recovered from the air pouches with CH
                        3-coated SAMs. The opposite PMN/Mo proportion was observed in air pouches of the two control groups (mice receiving gold implants or sham-operated animals). A low density of adherent cells was seen on CH 
                        3-coated implants, with no significant quantitative differences during the time course of the study. In contrast, the gold-coated surfaces were covered with numerous cells during all of the 3 days of the inflammation. In conclusion, implants with CH
                        3 surfaces are likely to induce PMN-dominated local acute inflammation but these surfaces are not associated with a significant adherence of leukocytes to the implant. {\textcopyright} 2005 Wiley-Liss, Inc.
},
	keywords = {Air-pouch model, animal experiment, animal model, Animalia, Animals, article, biomaterial, cell adhesion, Cell Count, cell density, cell surface, Cell-surface interactions, Coated Materials, Biocompatible, Contact angle, controlled study, gold, implantation, Implants, Experimental, Inflammation, inflammatory cell, Inflammatory responses, leukocyte adherence, Leukocytes, male, materials testing, methyl group, Mice, Microscopy, Electron, Scanning, mononuclear cell, mouse, neutrophil, nonhuman, priority journal, Scanning electron microscopy, Self-assembled monolayers, Surface Properties, thiol derivative, Time Factors},
	isbn = {1059910X (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-17144372986\&partnerID=40\&md5=1d2d00c4efe22d960872f5e785c7d4c7},
	author = {Barbosa, J.N. and Barbosa, M.A. and {\'A}guas, A.P.}
}
@article {2452,
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	year = {2005},
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},
	month = {2005///},
	pages = {31 - 39},
	abstract = {The proliferation of cultured human bone marrow stromal cells (HBMSC) on regenerated cellulose hydrogels was assessed. Regenerated cellulose hydrogels showed good rates of HBMSC proliferation, the cells exhibiting a flattened morphology, and after 22 days in culture, the cells had homogeneously colonized the surface of the materials. Moreover, since the early days in culture, between the surface of the materials and attached cells a continuous granulated hydroxyapatite layer was formed. It has been previously demonstrated in vitro, but without cells, that these materials did not mineralize. Hence, it seems that HBMSC promoted the mineralization of the surface.},
	keywords = {article, bone marrow cell, Bone Marrow Cells, bone mineralization, Calcification, Physiologic, Calcium phosphates, Cell culture, cell proliferation, cell regeneration, Cells, Cultured, Cellulose, hematopoietic stem cell, human, Human bone marrow stromal cells, human cell, Humans, hydrogel, Hydrogels, hydroxyapatite, in vitro study, mineralization, Regenerated cellulose hydrogels, Regeneration, Spectroscopy, Fourier Transform Infrared, stroma cell, Stromal Cells, Time series analysis},
	isbn = {14732262 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-28444434484\&partnerID=40\&md5=336e1872af4f9b4274cda0b46e091486},
	author = {Granja, P.L. and De J{\'e}so, B. and Bareille, R. and Rouais, F. and Baquey, C. and Barbosa, M.A.}
}
@article {2454,
	title = {Polysaccharides as scaffolds for bone regeneration},
	journal = {ITBM-RBMITBM-RBM},
	volume = {26},
	year = {2005},
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},
	month = {2005///},
	pages = {212 - 217},
	abstract = {This review is concerned with the use of polysaccharides for bone regeneration. Cellulose, alginate and chitosan have been chosen as examples of the formidable potential of this class of materials. Many others could be cited but our experience and research interests dictated the choice. As in many areas of research we know how they started but we cannot see how and if they will end. Modification of cellulose was our entrance to the world of polysaccharides and a lot of what we know we owe to Charles Baquey, to whom we would like to express our immense gratitude. This chapter is dedicated to him, for his cooperation, unlimited enthusiasm and friendship. {\textcopyright} 2005 Elsevier SAS. All rights reserved.},
	keywords = {Alginate, alginic acid, Amino Acid Sequence, arginylglycylaspartic acid, biomaterial, biotechnology, bone cell, bone prosthesis, Bone Regeneration, Cellulose, chitosan, enzyme degradation, polysaccharide, Polysaccharides, review, Tissue engineering},
	isbn = {12979562 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-20744434609\&partnerID=40\&md5=43d83907f18b3e44035dfe14ff13a24f},
	author = {Barbosa, M.A. and Granja, P.L. and Barrias, C.C. and Amaral, I.F.}
}
@article {2460,
	title = {Proliferation, activity, and osteogenic differentiation of bone marrow stromal cells cultured on calcium titanium phosphate microspheres},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {72},
	year = {2005},
	note = {Cited By (since 1996): 34Export Date: 21 November 2012Source: ScopusCODEN: JBMRCdoi: 10.1002/jbm.a.30217PubMed ID: 15543603Language of Original Document: EnglishCorrespondence Address: Barrias, C.C.; INEB, Instituto de Engenharia Biomedica, Laboratorio de Biomateriais, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: ccbarrias@ineb.up.ptChemicals/CAS: alkaline phosphatase, 9001-78-9; calcium phosphate, 10103-46-5, 13767-12-9, 14358-97-5, 7758-87-4; osteocalcin, 136461-80-8; titanium, 7440-32-6; Alkaline Phosphatase, EC 3.1.3.1; Calcium, 7440-70-2; Osteocalcin, 104982-03-8; titanium phosphate, 17017-57-1; Titanium, 7440-32-6References: Senuma, Y., Franceschin, S., Hilborn, J.G., Tissieres, P., Bisson, I., Frey, P., Bioresorbable microspheres by spinning disk atomization as injectable cell carrier: From preparation to in vitro evaluation (2000) Biomaterials, 21 (11), pp. 1135-1144;Hsu, F.Y., Chueh, S.C., Wang, Y.J., Microspheres of hydroxyapatite/ reconstituted collagen as supports for osteoblast cell growth (1999) Biomaterials, 20 (20), pp. 1931-1936; 
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Barrias, C.C., Ribeiro, C.C., Barbosa, M.A., Adhesion and proliferation of human osteoblastic cells seeded on injectable hydroxyapatite microspheres (2004) Key Eng Mater, 254-256, pp. 877-880; 
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Ribeiro, C.C., Barrias, C.C., Barbosa, M.A., (2004) Preparation and Characterisation of Calcium-phosphate Microspheres for Biomedical Applications, , Submitted for publication; 
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},
	month = {2005///},
	pages = {57 - 66},
	abstract = {In this study, the behavior of bone marrow stromal cells cultured on calcium titanium phosphate (CTP) microspheres was analyzed. Cell adhesion and proliferation were estimated by the neutral red assay and by total DNA quantification. Morphology and deposition of extracellular matrix were assessed by confocal laser scanning microscopy and/or scanning electron microscopy. The expression of the osteoblastic phenotype was evaluated by monitoring alkaline phosphatase activity and osteocalcin secretion. Results revealed that cells were able to attach and spread on the surface of CTP microspheres, and gradually grow into nearly confluent monolayers. Moreover, cells were able to bridge adjacent microspheres forming microsphere-cell clusters. Cells produced an abundant amount of fibrillar extracellular matrix that covered the substrate surface. Alkaline phosphatase activity peaked around days 7-14 and then decreased until day 21. Cells secreted osteocalcin, with higher levels being detected at day 14 than at day 21. Taken together, these results suggest that CTP microspheres are appropriate scaffolds for the growth and differentiation of cells along the osteoblastic lineage. {\textcopyright} 2004 Wiley Periodicals, Inc.},
	keywords = {alkaline phosphatase, animal cell, Animals, article, Bioassay, Bone, bone marrow cell, Bone Marrow Cells, bone marrow stromal cell, Bone marrow stromal cells, Calcium, Calcium Compounds, calcium phosphate, Calcium titanium phosphate, cell adhesion, Cell culture, cell differentiation, cell growth, cell lineage, cell proliferation, cell structure, Confluent monolayers, confocal laser microscopy, Confocal laser scanning microscopy, controlled study, Deposition, DNA determination, enzyme activity, Enzyme kinetics, extracellular matrix, Microscopy, Electron, microsphere, Microspheres, nonhuman, osteoblast, osteocalcin, Osteogenesis, Osteogenic differentiation, phenotype, protein expression, protein secretion, rat, Rats, Scanning electron microscopy, Stromal Cells, surface property, Tissue culture, Tissue engineering, Titanium, unclassified drug},
	isbn = {00219304 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-10444223137\&partnerID=40\&md5=ab1b84ba6dd86274c0102567dffe1418},
	author = {Barrias, C.C. and Ribeiro, C.C. and Lamghari, M. and S{\'a} Miranda, C. and Barbosa, M.A.}
}
@article {2444,
	title = {Rat bone marrow stromal cell osteogenic differentiation and fibronectin adsorption on chitosan membranes: The effect of the degree of acetylation},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {75},
	year = {2005},
	note = {Cited By (since 1996): 25Export Date: 21 November 2012Source: ScopusCODEN: JBMRCdoi: 10.1002/jbm.a.30436PubMed ID: 16092111Language of Original Document: EnglishCorrespondence Address: Amaral, I.F.; INEB-Instituto de Engenharia Biom{\'e}dica, Laborat{\'o}rio de Biomateriais, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: iamaral@ineb.up.ptChemicals/CAS: chitosan, 9012-76-4; fibronectin, 86088-83-7; polystyrene, 9003-53-6; Chitosan, 9012-76-4; Coated Materials, Biocompatible; FibronectinsReferences: VandeVord, P.J., Matthew, H.W.T., DeSilva, S.P., Mayton, L., Wu, B., Wooley, P.H., Evaluation of the biocompatibility of a chitosan scaffold in mice (2002) J Biomed Mater Res, 59 (3), pp. 585-590;Muzzarelli, R.A.A., Human enzymatic activities related to the therapeutic administration of chitin derivatives (1997) Cell Mol Life Sci, (53), pp. 131-140; 
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Stephansson, S.N., Byers, B.A., Garcia, A.J., Enhanced expression of the osteoblastic phenotype on substrates that modulate fibronectin conformation and integrin receptor binding (2002) Biomaterials, 23 (12), pp. 2527-2534
},
	month = {2005///},
	pages = {387 - 397},
	abstract = {Cell adhesion, migration, and proliferation of a few anchorage-dependent cells cultured on chitosan (Ch) matrices are influenced by the degree of N-acetylation (DA) of Ch. In the present work, we examined the influence of the DA on the attachment, spreading, proliferation, and osteogenic differentiation of rat bone marrow stromal cells (rBM-SCs). Ch membranes were characterized in terms of surface morphology, roughness, and wettability, and in terms of adsorption of an adhesive protein, fibronectin (Fn). Chs with DAs in the range of 4 to 49\% were used. Among the Ch samples, the DA of 4\% led to the highest Fn surface concentration, both from single protein solution and from diluted serum. Furthermore, the levels of Fn adsorbed from serum found for this DA were threefold higher than for the tissue culture polystyrene control, indicating that in the presence of competitive proteins Ch is more specific toward Fn adsorption than tissue culture polystyrene. rBMSCs cultured on Ch carrying a DA of 4\% were able to spread, proliferate, and differentiate, reaching a higher level of osteogenic differentiation than on the control, despite the lower cell attachment observed for all Ch samples. Because the Ch sample with a DA of 4\% showed the highest Fn adsorption from serum, we suggest that cell adhesion, spreading, and osteogenic differentiation of rBMSCs on Ch may be mediated by the adsorbed layer of Fn. {\textcopyright} 2005 Wiley Periodicals, Inc.},
	keywords = {Acetylation, Adhesion, Adsorption, animal cell, Animals, article, artificial membrane, binding affinity, binding competition, Bone, bone development, bone marrow cell, Bone Marrow Cells, Bone marrow stomal cells, Bone marrow stromal cells, cell adhesion, cell anchorage, Cell culture, cell differentiation, Cell membranes, cell migration, cell proliferation, Cell Shape, cell spreading, chitosan, Coated Materials, Biocompatible, controlled study, cytoskeleton, Degree of acetylation, Fibronectin, Fibronectins, male, materials testing, morphology, nonhuman, polystyrene, Proteins, rat, Rats, Rats, Wistar, roughness, stroma cell, Stromal Cells, Surface Properties, surface property, Tissue culture, wettability},
	isbn = {00219304 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-26844551535\&partnerID=40\&md5=fa91e3e29d946053ae7bb231b6a2640e},
	author = {Amaral, I.F. and Lamghari, M. and Sousa, S.R. and Sampaio, P. and Barbosa, M.A.}
}
@article {2443,
	title = {Recombinant glucocerebrosidase uptake by Gaucher disease human osteoblast culture model},
	journal = {Blood Cells, Molecules, and DiseasesBlood Cells Mol. Dis.},
	volume = {35},
	year = {2005},
	note = {Cited By (since 1996): 3Export Date: 21 November 2012Source: ScopusCODEN: BCMDFdoi: 10.1016/j.bcmd.2005.07.009PubMed ID: 16125984Language of Original Document: EnglishCorrespondence Address: Lamghari, M.; INEB-Instituto de Engenharia Biom{\'e}dica, Laborat{\'o}rio de Biomateriais, R. Campo Alegre 823, 4150-180 Porto, Portugal; email: lamghari@ineb.up.ptChemicals/CAS: conduritol b epoxide, 6090-95-5; imiglucerase, 154248-97-2; iodine 125, 14158-31-7, 22822-81-7; conduritol epoxide, 6090-95-5; Glucosylceramidase, EC 3.2.1.45; Inositol, 6917-35-7; Recombinant ProteinsTradenames: cerezyme, GenzymeManufacturers: GenzymeReferences: Beutler, E., Grabowski, G., Gaucher disease (1995) The Metabolic and Molecular Bases of Inherited Disease, 2, pp. 2641-2661. , C.R. Scriber A.L. Beaudet W.S. Sly 7th ed. McGraw-Hill New York, NY;Beutler, E., Enzyme replacement in Gaucher disease (2004) PLoS Med., 1 (2), p. 21; 
Elstein, D., Itzchaki, M., Mankin, H., Skeletal involvement in Gaucher{\textquoteright}s disease (1997) Balli{\`e}re{\textquoteright}s Clin. Haematol., 10 (4), pp. 793-815; 
Wenstrup, R.J., Roca-Espiau, M., Weinreb, N.J., Bembi, B., Skeletal aspects of Gaucher disease: A review (2002) Br. J. Radiol., 75 (1 SUPPL.), pp. 2-A12; 
Barranger, J.A., O{\textquoteright}Rourke, E., Lessons learned from the development of enzyme therapy for Gaucher disease (2001) J. Inherited Metab. Dis., 24 (2 SUPPL.), pp. 89-96; 
Zimran, A., Elstein, D., Levy-Lahad, E., Zevin, S., Hadas-Halpern, I., Bar-Ziv, Y., Foldes, J., Abrahamov, A., Replacement therapy with imiglucerase for type 1 Gaucher{\textquoteright}s disease (1995) Lancet, 345 (8963), pp. 1479-1480; 
Barton, N.W., Brady, R.O., Dambrosia, J.M., Di Bisceglie, A.M., Doppelt, S.H., Hill, S.C., Mankin, H.J., Argoff, C.E., Replacement therapy for inherited enzyme deficiency-macrophage-targeted glucocerebrosidase for Gaucher{\textquoteright}s disease (1991) N. Engl. J. Med., 324 (21), pp. 1464-1470; 
Barton, N.W., Furbish, F.S., Murray, G.J., Garfield, M., Brady, R.O., Therapeutic response to intravenous infusions of glucocerebrosidase in a patient with Gaucher disease (1990) Proc. Natl. Acad. Sci. U. S. A., 87 (5), pp. 1913-1916; 
Friedman, B., Vaddi, K., Preston, C., Mahon, E., Cataldo, J.R., McPherson, J.M., A comparison of the pharmacological properties of carbohydrate remodeled recombinant and placental-derived beta-glucocerebrosidase: Implications for clinical efficacy in treatment of Gaucher disease (1999) Blood, 93, pp. 2807-2816; 
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(1993) Iodine-125, a Guide to Radioiodination, p. 64. , Amersham Life Science; 
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S{\'a} Miranda, M.C., Aerts, J.M., Pinto, R., Fontes, A., Lacerda, L.W., Van Weely, S., Barranger, J., Tager, J.M., Activity of glucocerebrosidase in extracts of different cell types from type 1 Gaucher disease patients (1990) Clin. Genet., 38, pp. 218-227; 
Barrias, C.C., Lamghari, M., Granja, P.L., S{\'a} Miranda, C., Barbosa, M.A., Biological evaluation of calcium alginate microspheres as a vehicle for the localised delivery of a therapeutic enzyme (2005) J. Biomed. Mater. Res.; 
Barrias, C.C., Ribeiro, C.C., Lamghari, M., S{\'a} Miranda, C., Barbosa, M.A., Proliferation, activity, and osteogenic differentiation of bone marrow stromal cells cultured on calcium titanium phosphate microspheres (2005) J. Biomed. Mater. Res., 72 A (1), pp. 57-66; 
Ribeiro, C.C., Barrias, C.C., Barbosa, M.A., Calcium phosphate-alginate microspheres as enzyme delivery matrices (2004) Biomaterials, 25 (18), pp. 4363-4373; 
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Pelled, D., Shogomori, H., Futerman, A.H., The increased sensitivity of neurons with elevated glucocerebroside to neurotoxic agents can be reversed by imiglucerase (2000) J. Inherited Metab. Dis., 23 (2), pp. 175-184; 
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Engelholm, L.H., Nielsen, B.S., Netzel-Arnett, S., Solberg, H., Chen, X.D., Lopez Garcia, J.M., Lopez-Otin, C., Bugge, T.H., The urokinase plasminogen activator receptor-associated protein/endo180 is coexpressed with its interaction partners urokinase plasminogen activator receptor and matrix metalloprotease-13 during osteogenesis (2001) Lab. Invest., 81, pp. 1403-1414; 
Bailey, L., Wienke, D., Howard, M., Knauper, V., Isacke, C.M., Murphy, G., Investigation of the role of Endo180/urokinase-type plasminogen activator receptor-associated protein as a collagenase 3 (matrix metalloproteinase 13) receptor (2002) Biochem. J., 1 (363 PART 1), pp. 67-72
},
	month = {2005///},
	pages = {348 - 354},
	abstract = {Bone lesions are a major cause of morbidity in Gaucher disease (GD) type I. Enzyme replacement therapy (ERT) has been successful in treating many symptoms of type I GD but skeletal response lags behind. Local exogenous glucocerebrosidase supplementation in bone lesions via a drug delivery system may overcome this limitation. Although local enzyme supplementation aims to target lipid-engorged macrophages (Gaucher Cells) in bone compartment, enzyme uptake by osteoblasts is not excluded. To investigate the ability of human osteoblasts to internalize recombinant glucocerebrosidase (rGCR), we have used an artificial GD human osteoblasts cell culture system. MG63 human osteoblasts were treated with conduritol B epoxide (CBE) to induce complete and prolonged inhibition of endogenous glucocerebrosidase activity of cells. rGCR uptake by glucocerebrosidase-inactivated osteoblasts was examined using                        125I-radiolabelling, Western blot analysis and measurement of glucocerebrosidase activity. Analysis of radiolabeled enzyme uptake by CBE treated osteoblasts showed 67.9\% of internalized protein in cell extract. Enzyme internalization was also observed by Western blot analysis where the amount of mature form of glucocerebrosidase protein recognized by the glucocerebrosidase antibody was increased following the administrations of rGCR. Moreover, enzymatic activity measurement showed 23.9\% of glucocerebrosidase activity of control cells. The rGCR internalization by MG63 osteoblast seems to be partially mediated by mannose receptors. These data provide evidence that MG63 human osteoblasts are able to internalize rGCR. {\textcopyright} 2005 Elsevier Inc. All rights reserved.
},
	keywords = {article, Cell culture, cell extract, Cells, Cultured, conduritol b epoxide, controlled study, drug activity, drug uptake, enzyme activity, enzyme antibody, Enzyme inhibition, Enzyme uptake, epoxide, Gaucher disease, Glucocerebrosidase, Glucosylceramidase, human, human cell, Humans, imiglucerase, Inositol, internalization, iodine 125, isotope labeling, mannose receptor, osteoblast, Osteoblasts, priority journal, Recombinant Proteins, unclassified drug, Western blotting},
	isbn = {10799796 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-27744461413\&partnerID=40\&md5=575b4d8cc3f6e5b8e846cf6de71852b3},
	author = {Lamghari, M. and Barrias, C.C. and S{\'a} Miranda, C. and Barbosa, M.A.}
}
@article {2431,
	title = {TiO                    2 type influences fibronectin adsorption
},
	journal = {Journal of Materials Science: Materials in MedicineJ. Mater. Sci. Mater. Med.},
	volume = {16},
	year = {2005},
	note = {Cited By (since 1996): 28Export Date: 21 November 2012Source: ScopusCODEN: JSMMEdoi: 10.1007/s10856-005-4725-4Language of Original Document: EnglishCorrespondence Address: Sousa, S.R.; INEB, Instituto de Engenharia Biom{\'e}dica, Lab. Biomateriais, R. do Campo Alegre, 823, 4150-180 Porto, Portugal; email: ssousa@ibmc.up.ptChemicals/CAS: fibronectin, 86088-83-7; titanium dioxide, 1317-70-0, 1317-80-2, 13463-67-7, 51745-87-0; titanium, 7440-32-6; hydrogen peroxide, 7722-84-1; iodine 125, 14158-31-7, 22822-81-7; Fibronectins; Solutions; titanium dioxide, 13463-67-7; Titanium, 7440-32-6References: Horbett, T.A., (1994) Colloids and Surfaces B: Biointerfaces, 2, p. 225;Amaral, I.F., Lamghari, M., Sousa, S.R., Sampaio, P., Barbosa, M.A., (2005) J Biomed Mater Res., 75 A, p. 387; 
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},
	month = {2005///},
	pages = {1173 - 1178},
	abstract = {Human fibronectin (FN) plays a key role in the biointegration of implants as the success depends on adsorption of proteins like FN [1]. Indeed FN can be an intermediary between the biomaterial surface and cells. The adsorption of human fibronectin (FN) on commercially pure titanium with a titanium oxide layer formed in a H                        2O
                        2 solution (TiO
                        2 cp) and TiO
                        2 sputtered on Si (TiO
                        2 sp) was studied. Adsorption isotherms and the work of adhesion were assessed by wettability studies, X-ray photoelectron spectroscopy (XPS), and by radiolabelling of FN with 
                        125I, 
                        125I-FN. Exchangeability of bound FN by free FN, was also evaluated by the radiolabelling technique. Contact angle determinations have shown that FN displays higher affinity for the TiO
                        2 cp surface than for the TiO
                        2 sp. As expected from the surface free energy values, the work of adhesion of FN is higher for the TiO
                        2 cp substrate, the more hydrophilic one, and lower for the TiO
                        2 sp substrate, the more hydrophobic one. The adsorption isotherms were evaluated by two different techniques: radiolabelling of FN (
                        125I-FN) and XPS. TiO
                        2 cp adsorbs more FN than the TiO
                        2 sp surfaces as shown by the radiolabelling data. FN molecules are also more strongly attached to the former surface as indicated by the work of adhesion and by the exchangeability studies. Results using 
                        125I-FN also suggests that FN adsorbs as a multilayer for FN concentrations in solution higher than 100 μg/mL. {\textcopyright} 2005 Springer Science + Business Media, Inc.
},
	keywords = {Adsorption, adsorption kinetics, article, binding affinity, Biointegration, Biomaterials, Cells, chemistry, conference paper, Contact angles, Fibronectin, Fibronectins, human, Human fibronectin (FN), Humans, hydrogen peroxide, hydrophilicity, hydrophobicity, Implants (surgical), iodine 125, isotherm, Isotherms, isotope labeling, physical chemistry, priority journal, protein binding, Proteins, Radiolabelling, solution and solubility, Solutions, surface property, Titanium, Titanium dioxide, wettability, X ray photoelectron spectroscopy},
	isbn = {09574530 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-29144439699\&partnerID=40\&md5=f98f8448d034d8f8627d752516e3afbd},
	author = {Sousa, S.R. and Moradas-Ferreira, P. and Barbosa, M.A.}
}
@article {2484,
	title = {Biocompatibility of chemoenzymatically derived dextran-acrylate hydrogels},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {68},
	year = {2004},
	note = {Cited By (since 1996): 21Export Date: 21 November 2012Source: ScopusCODEN: JBMRCPubMed ID: 14762939Language of Original Document: EnglishCorrespondence Address: Dordick, J.S.; Department of Chemical Engineering, Rensselaer Polytechnic Institute, Troy, NY 12180, United States; email: dordick@rpi.eduChemicals/CAS: acrylic acid, 10344-93-1, 79-10-7; dextran, 87915-38-6, 9014-78-2; Acrylates; Biocompatible Materials; Dextrans, 9004-54-0; Enzymes; HydrogelsReferences: Ferreira, L., Gil, M.H., Dordick, J.S., Enzymatic synthesis of dextran-containing hydrogels (2002) Biomaterials, 23, pp. 3957-3967;Peppas, N.A., Bures, P., Leobandung, W., Ichikawa, H., Hydrogels in pharmaceutical formulations (2000) Eur J Pharm Biopharm, 50, pp. 27-46; 
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},
	month = {2004///},
	pages = {584 - 596},
	abstract = {The biocompatibility of chemoenzymatically generated dextran-acrylate hydrogels has been evaluated in vitro, using human foreskin fibroblasts, and in vivo, by subcutaneous and intramuscular implantation in Wistar rats for up to 40 days. In vitro tests show that hydrogel extracts only minimally reduced (<10\%) the mitochondrial metabolic activity of fibroblasts. Direct contact of the hydrogels with cells induced a cellular proliferation inhibition index (CPII) of 50-80\%, compared with a control, whereas through indirect contact, the CPII values were <16\%, suggesting that the high CPII values achieved in the direct assay test were likely due to mechanical stress or limitations in oxygen diffusion. Hence, the hydrogels were noncytotoxic. Moreover, cell-material interaction studies show that these hydrogels were nonadhesive. Finally, histologic evaluation of tissue response to subcutaneous and intramuscular implants showed acceptable levels of biocompatibility, as characterized by a normal cellular response and the absence of necrosis of the surrounding tissues of the implant. In the first 10 days, the foreign-body reaction in the intramuscular implantation was more severe than in subcutaneous implantation, becoming identical after 30 days. In both cases, dextran hydrogels did not show signs of degradation 6 weeks postimplantation and were surrounded by a thin fibrous capsule and some macrophages and giant cells. This response is typical with a number of nondegradable biocompatible materials. These results indicate that dextran hydrogels are biocompatible, and may have suitable applications as implantable long-term peptide/protein delivery systems or scaffolds for tissue engineering. {\textcopyright} 2004 Wiley Periodicals, Inc.},
	keywords = {Acrylates, acrylic acid, animal experiment, animal model, animal tissue, Animals, article, Biocatalytic polyester, Biocompatibility, Biocompatible Materials, Biodegradation, Environmental, Biodiversity, Biomaterials, cell adhesion, Cell Division, cell interaction, cell proliferation, Cells, Cultured, Coenzymes, controlled study, Cytotoxicity, dextran, dextran acrylate, dextran acrylate hydrogel, dextran hydrogel, Dextrans, drug delivery system, Enzymes, fibroblast, Fibroblasts, Fibrous capsules, foreign body reaction, Foreign-Body Reaction, giant cell, human, human cell, Humans, hydrogel, Hydrogels, implantation, Implants (surgical), Implants, Experimental, in vitro study, in vivo study, macrophage, male, materials testing, mechanical stress, Mechanical stresses, metabolism, Mitochondria, mitochondrial respiration, nonhuman, oxygen diffusion, prepuce, rat, Rats, Rats, Wistar, Tissue, Tissue engineering, unclassified drug},
	isbn = {00219304 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-1342280525\&partnerID=40\&md5=fe5529e53db4261e72bde7a75e2cf2cc},
	author = {Ferreira, L. and Rafael, A. and Lamghari, M. and Barbosa, M.A. and Gil, M.H. and Cabrita, A.M.S. and Dordick, J.S.}
}
@article {2474,
	title = {Calcium phosphate-alginate microspheres as enzyme delivery matrices},
	journal = {BiomaterialsBiomaterials},
	volume = {25},
	year = {2004},
	note = {Cited By (since 1996): 92Export Date: 21 November 2012Source: ScopusCODEN: BIMADdoi: 10.1016/j.biomaterials.2003.11.028PubMed ID: 15046927Language of Original Document: EnglishCorrespondence Address: Ribeiro, C.C.; Laborat{\'o}rio de Biomateriais, INEB, Inst. de Engenharia Biom{\'e}dica, Rua do Campo Alegre 823, Porto 4150-180, Portugal; email: cribeiro@ineb.up.ptChemicals/CAS: Alginates; alginic acid, 9005-32-7; calcium phosphate, 10103-46-5; Calcium Phosphates; Drug Carriers; Enzymes, Immobilized; Glucosylceramidase, EC 3.2.1.45; Glucuronic Acid, 576-37-4; Hexuronic Acids; PowdersReferences: Griffith, L.G., Naughton, G., Tissue engineering: Current challenges and expanding opportunities (2002) Science, 295, pp. 1009-1014;Hench, L.L., Polak, J.M., Third-generation biomedical materials (2002) Science, 295, pp. 1014-1017; 
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},
	month = {2004///},
	pages = {4363 - 4373},
	abstract = {The present study concerns the preparation and initial characterisation of novel calcium titanium phosphate-alginate (CTP-alginate) and hydroxyapatite-alginate (HAp-alginate) microspheres, which are intended to be used as enzyme delivery matrices and bone regeneration templates. Microspheres were prepared using different concentrations of polymer solution (1\% and 3\%w/v) and different ceramic-to-polymer solution ratios (0.1, 0.2 and 0.4w/w). Ceramic powders were characterised using X-ray diffraction, laser granulometry, Brunauer, Emmel and Teller (BET) method for the determination of surface area, zeta potential and Fourier transform infrared spectroscopy (FT-IR). Alginate was characterised using high performance size exclusion chromatography. The methodology followed in this investigation enabled the preparation of homogeneous microspheres with a uniform size. Studies on the immobilisation and release of the therapeutic enzyme glucocerebrosidase, employed in the treatment of Gaucher disease, were also performed. The enzyme was incorporated into the ceramic-alginate matrix before gel formation in two different ways: pre-adsorbed onto the ceramic particles or dispersed in the polymeric matrix. The two strategies resulted in distinct release profiles. Slow release was obtained after adsorption of the enzyme to the ceramic powders, prior to preparation of the microspheres. An initial fast release was achieved when the enzyme and the ceramic particles were dispersed in the alginate solution before producing the microspheres. The latter profile is very similar to that of alginate microspheres. The different patterns of enzyme release increase the range of possible applications of the system investigated in this work. {\textcopyright} 2003 Elsevier Ltd. All rights reserved.},
	keywords = {Absorption, Adsorption, Alginate, Alginates, article, Biomaterials, Bone, Calcium Compounds, Calcium phosphates, Calcium titanium phosphate, calcium titanium phosphate alginate, ceramics, Drug Carriers, Drug Delivery Systems, Enzyme delivery, Enzyme-delivery, Enzymes, Enzymes, Immobilized, Fourier transform infrared spectroscopy, Glucosylceramidase, Glucuronic Acid, Hexuronic Acids, High performance liquid chromatography, hydroxyapatite, hydroxyapatite alginate, laser, methodology, microsphere, Microspheres, Molecular Conformation, Particle Size, Powders, priority journal, surface property, unclassified drug, X ray diffraction},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-1642331315\&partnerID=40\&md5=217590793385cbaff039a6b260d3d85c},
	author = {Ribeiro, C.C. and Barrias, C.C. and Barbosa, M.A.}
}
@article {2467,
	title = {Electrochemical behaviour of titanium coated stainless steel by r.f. sputtering in synthetic sweat solutions for electrode applications},
	journal = {Corrosion ScienceCorros. Sci.},
	volume = {46},
	year = {2004},
	note = {Cited By (since 1996): 13Export Date: 21 November 2012Source: ScopusCODEN: CRRSAdoi: 10.1016/j.corsci.2004.04.006Language of Original Document: EnglishCorrespondence Address: Fonseca, C.; Inst. de Engenharia Biom{\'e}dica, Laboratorio de Biomateriais, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: cfonseca@fe.up.ptReferences: Cooper, R., Osselton, J.W., Shaw, J.C., (1980) EEG Technology, pp. 20-28. , Butterworths and Co. Ltd;Femandez, M., Pallas-Aieny, R., (2000) Biomed. Iustrum. Technol., pp. 125-130. , March/April; 
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},
	month = {2004///},
	pages = {3005 - 3018},
	abstract = {The r.f. sputtering technique was used to deposit titanium thin films on stainless steel substrates, aiming at the application of the coated samples as skin contact materials for "dry" active electrodes. In this work the electrochemical behaviour of the coated samples was investigated in synthetic sweat solutions and their performance was compared with that of uncoated stainless steel and bulk titanium. The characterisation of the samples was carried out by electrochemical techniques and scanning electron microscopy. The coated samples displayed corrosion resistance values in synthetic sweat solutions much higher than stainless steel samples and of the same order of the values measured for bulk titanium in the same conditions. {\textcopyright} 2004 Elsevier Ltd. All rights reserved.},
	keywords = {A. Sputtered films, A. Stainless steel, A. Titanium, B. EIS, coating, Corrosion resistance, Electrochemical corrosion, Electrochemical techniques, electrochemistry, electrode, Electrodes, Protective coatings, Scanning electron microscopy, Sputtering, Stainless steel, Synthetic sweat solutions, Thin films, Titanium},
	isbn = {0010938X (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-4644222640\&partnerID=40\&md5=7a4d452b2c52c155967ea2edb0cabb58},
	author = {Fonseca, C. and Vaz, F. and Barbosa, M.A.}
}
@article {2482,
	title = {Fabrication of alternating polycation and albumin multilayer coating onto stainless steel by electrostatic layer-by-layer adsorption},
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	year = {2004},
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},
	month = {2004///},
	pages = {185 - 190},
	abstract = {Multilayer films consisting of polyethylenimine (PEI) and albumin were successfully prepared on biomedical 316L stainless steel surface via electrostatic self-assembly of the PEI and albumin. The process of electrostatic self-assembly of PEI/albumin was monitored by                        125I radiolabeling, electrochemical impedance spectroscopy (EIS) and atomic force microscopy (AFM). The EIS data revealed that the multilayer coating was stable in Tris-HCl (pH 7.35) buffer solution for 21 days. 
                        125I radiolabeling experiments indicated that less than 10\% albumin was eluted by PBS in 45 days. Static platelet adhesion experiments indicated that the PEI/albumin deposited on stainless steel could resist platelet adhesion effectively. Such an easy processing and shape-independent method may have good potential for surface modification of cardiovascular devices. {\textcopyright} 2004 Elsevier B.V. All rights reserved.
},
	keywords = {Adhesion, Adsorption, Albumin, Albumins, article, Atomic force microscopy, Cardiovascular devices, Chemical modification, Coatings, Electric Impedance, Electric Potential, Electrochemical impedance spectroscopy, electrochemistry, Electrons, Electrostatics, film coating, iodine 125, isotope labeling, Layer-by-layer, Lipid Bilayers, Microscopy, Atomic Force, Multilayers, Nonthrombogenic, pH effects, Platelet Adhesiveness, Polyamines, polycation, Polycations, Polyethyleneimine, priority journal, Proteins, Self assembly, Spectroscopy, Spectrum Analysis, Stainless steel, Surface modification, Surface Properties, surface property, Surface treatment, thrombocyte adhesion},
	isbn = {09277765 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-1642271404\&partnerID=40\&md5=29885596e6efdc7afcc5b2fdd57317be},
	author = {Ji, J. and Tan, Q. and Fan, D.-Z. and Sun, F.-Y. and Barbosa, M.A. and Shen, J.}
}
@article {2500,
	title = {Fabrication of alternating polycation and albumin multilayer coating by electrostatic layer-by-layer adsorption},
	journal = {Journal of Materials ScienceJ Mater Sci},
	volume = {39},
	year = {2004},
	note = {Cited By (since 1996): 1Export Date: 21 November 2012Source: ScopusCODEN: JMTSAdoi: 10.1023/B:JMSC.0000008087.71937.71Language of Original Document: EnglishCorrespondence Address: Ji, J.; Department of Polymer Science, Zhejiang University, Hangzhou 310027, China; email: jianji@mail.hz.zj.cnReferences: Bertrand, P., Jonas, A., Laschewsky, A., (2000) Macr. Rap. Comm., 21, p. 319;Ulman, A., (1996) Chem. Rev., 96, p. 1533; 
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},
	month = {2004///},
	pages = {349 - 351},
	abstract = {The construction of albumin multilayers via the electrostatic self-assembly (ESA) method was explored. Based on the results, it was possible to develop a fast, easy processing and shape-independent method for nonthrombogenic coating.},
	keywords = {Adhesion, Adsorption, Albumin, Biocompatibility, Biological materials, Biopolymers, Blood, Charge transfer, Chemical bonds, Covalent binding, Desorption, Electron transfer, Electron transfer resistance, Electrostatic layer by layer adsorption, Electrostatics, Multilayers, polycation, Positive ions, Spectroscopic analysis, Static platelet adhesion},
	isbn = {00222461 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0842312335\&partnerID=40\&md5=90716a579ba430045f75ca682551d418},
	author = {Ji, J. and Tan, Q. and Fan, D.-Z. and Sun, Y.-F. and Barbosa, M.A. and Shen, J.}
}
@article {2472,
	title = {Human serum albumin adsorption on TiO                    2 from single protein solutions and from plasma
},
	journal = {LangmuirLangmuir},
	volume = {20},
	year = {2004},
	note = {Cited By (since 1996): 58Export Date: 21 November 2012Source: ScopusCODEN: LANGDdoi: 10.1021/la049158dPubMed ID: 15491210Language of Original Document: EnglishCorrespondence Address: Sousa, S.R.; Inst. de Engenharia Biom{\'e}dica, Laborat{\'o}rio Biomateriais, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: ssousa@ibmc.up.ptChemicals/CAS: serum albumin, 9048-46-8; titanium dioxide, 1317-70-0, 1317-80-2, 13463-67-7, 51745-87-0; titanium, 7440-32-6; Serum Albumin; Solutions; titanium dioxide, 13463-67-7; Titanium, 7440-32-6References: Nakabayashi, N., Iwasaki, Y., (2000) European White Book on Fundamental Research in Materials Science, pp. pp70-71. , R{\"u}hle, M., Dosch, H., Mittemeijer, E. J.Van de Voorde, M. H., Eds.; Max Plank Institut fur Metallforschung: Stuttgart, Germany;Windler, M., Klabunde, R., (2001) Titanium in Medicine; Material Science, Surface Science, Engineering, Biological Responses and Medical Applications, pp. 703-746. , Brunette, D. M., Tengvall, P., Textor, M., Thomsen, P., Eds.; Springer-Verlag: Berlin, Germany; 
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},
	month = {2004///},
	pages = {9745 - 9754},
	abstract = {In the present work, the adsorption of human serum albumin (HSA) on commercially pure titanium with a titanium oxide layer formed in a H                        2O
                        2 solution (TiO
                        2 cp) and on TiO
                        2 sputtered on Si (TiO
                        2 sp) was analyzed. Adsorption isotherms, kinetic studies, and work of adhesion determinations were carried out. HSA exchangeability was also evaluated. Surface characterization was performed by atomic force microscopy (AFM), X-ray photoelectron spectroscopy (XPS), and wettability studies. The two TiO
                        2 surfaces have very distinct roughnesses, the TiO
                        2 sp having a mean R
                        a value 14 times smaller than the one of TiO
                        2 cp. XPS analysis revealed consistent peaks representative of TiO
                        2 on sputtered samples as well as on Ti cp substrate after 48 h of H
                        2O
                        2 immersion. Nitrogen was observed as soon as protein was present, while sulfur, present in disulfide bonds in HSA, was observed for concentrations of protein higher than 0.30 mg/mL. The work of adhesion was determined from contact angle measurements. As expected from the surface free energy values, the work of adhesion of HSA solution is higher for the TiO
                        2 cp substrate, the more hydrophilic one, and lower for the TiO
                        2 sp substrate, the more hydrophobic one. The work of adhesion between plasma and the substrates assumed even higher values for the TiO
                        2 cp surface, indicating a greater interaction between the surface and the complex protein solutions. Adsorption studies by radiolabeling of albumin (
                        125I-HSA) suggest that rapid HSA adsorption takes place on both surfaces, reaching a maximum value after ~60 min of incubation. For the higher HSA concentrations in solution, a multilayer coverage was observed on both substrates. After the adsorption step from single HSA solutions, the exchangeability of adsorbed HSA molecules by HSA in solution was evaluated. The HSA molecules adsorbed on TiO
                        2 sp seem to be more easily exchanged by HSA itself than those adsorbed on TiO
                        2 cp after 24 h. In contrast, after 72 h, nearly all the adsorbed albumin molecules effectively exchange with other albumin molecules.
},
	keywords = {Adsorption, article, Atomic force microscopy, Blood, chemistry, human, Human serum albumin (HSA), Humans, hydrophobicity, Multilayers, plasma, Plasmas, Plastic surgery, Proteins, Radiolabeling, Serum Albumin, solution and solubility, Solutions, Substrates, Surface characterization, Surface Properties, surface property, Titanium, Titanium dioxide, X ray photoelectron spectroscopy},
	isbn = {07437463 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-8344221996\&partnerID=40\&md5=60496aebf9155224cadbbb1456ff8a25},
	author = {Sousa, S.R. and Moradas-Ferreira, P. and Saramago, B. and Viseu Melo, L. and Barbosa, M.A.}
}
@article {2473,
	title = {Protein electrostatic self-assembly on poly(DL-lactide) scaffold to promote osteoblast growth},
	journal = {Journal of Biomedical Materials Research - Part B Applied BiomaterialsJ. Biomed. Mater. Res. Part B Appl. Biomater.},
	volume = {71},
	year = {2004},
	note = {Cited By (since 1996): 14Export Date: 21 November 2012Source: ScopusCODEN: JBMRGdoi: 10.1002/jbm.b.30080PubMed ID: 15368240Language of Original Document: EnglishCorrespondence Address: Ji, J.; Dept. of Poly. Sci. and Engineering, Zhejiang University, Hangzhou 310027, China; email: jianji@mail.hz.zj.cnChemicals/CAS: DNA, 9007-49-2; gelatin, 9000-70-8; polyethyleneimine, 74913-72-7; polylactide, 26680-10-4; DNA, 9007-49-2; Gelatin, 9000-70-8; poly(lactide), 26969-66-4; PolyestersReferences: Anselme, K., Osteoblast adhesion on biomaterials (2000) Biomaterials, 21, pp. 667-681;Kim, B.S., Mooney, D.J., Development of biocompatible synthetic extracellular matrices for tissue engineering (1998) Trend Biotechnol, 16, pp. 224-230; 
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},
	month = {2004///},
	pages = {159 - 165},
	abstract = {The development of protein coating on 3D biodegradable scaffold based on electrostatic self-assembly (ESA) to promote osteoblast growth is reported. Poly (ethylenimine) (PEI) was employed to obtain a stable positively charged surface on poly(DL-lactide) (PDL-LA) substrate. An extracellular-matrix (ECM)-like biomacromolecule, gelatin, was chosen as the polyelectrolyte to deposit on the activated PDL-LA substrate via ESA technique. Osteoblast (MC3T3) was then cultured on unmodified and gelatin-modified PDL-LA scaffolds. Osteoblast testing regarding total intracellular protein content, total DNA content, cell activity, and cell morphology on the ECM-like multilayer-modified PDL-LA scaffold showed that osteoblast growth was promoted. It will be easy to replace the gelatin with osteoinductive proteins or other polyelectrolytes to promote specific osteoblast functions. In comparison with conventional coating methods, polyelectrolyte multilayers are easy and stable to prepare. They may be a good choice for the surface modification of complex biomedical devices, especially for the 3D tissue-engineering scaffold. These very flexible systems allow broad medical applications for drug delivery and tissue engineering. {\textcopyright} 2004 Wiley Periodicals, Inc.},
	keywords = {3T3 Cells, Absorbable Implants, Activation analysis, animal cell, Animals, article, Biodegradation, Biomedical engineering, cell activity, cell adhesion, Cell Division, cell growth, cell level, cell protein, cell structure, cell surface, Cell-material interactions, Cells, Coating techniques, DNA, DNA content, Drug products, Electrostatics, ethylene derivative, extracellular matrix, gelatin, Gelation, Growth (materials), Kinetics, macromolecule, materials testing, Mice, Microscopy, Confocal, mouse, nonhuman, osteoblast, Osteoblast growth, Osteoblast testing, Osteoblasts, polyelectrolyte, Polyelectrolytes, Polyesters, Polyethyleneimine, polylactide, polymer, protein assembly, Proteins, Surface modification, Tissue, Tissue engineering},
	isbn = {00219304 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-4644230505\&partnerID=40\&md5=2c6499a5f15b19dfab9731021aa4639b},
	author = {Zhu, H. and Ji, J. and Barbosa, M.A. and Shen, J.}
}
@article {2516,
	title = {Adhesion of human leukocytes to biomaterials: An in vitro study using alkanethiolate monolayers with different chemically functionalized surfaces},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {65},
	year = {2003},
	note = {Cited By (since 1996): 24Export Date: 21 November 2012Source: ScopusCODEN: JBMRCLanguage of Original Document: EnglishCorrespondence Address: Barbosa, J.N.; INEB-Inst. de Engenharia Biomedica, Laborat{\'o}rio de Biomateriais, Rua do Campo Alegre 823, 4150-180 Porto, Portugal; email: judite@ibmc.up.ptChemicals/CAS: gold, 7440-57-5; hydroxide, 14280-30-9; methane, 74-82-8; phorbol 12 acetate 13 myristate, 31365-46-5; phytohemagglutinin, 9008-97-3; phorbol 13 acetate 12 myristate, 16561-29-8; Biocompatible Materials; Gold, 7440-57-5; Phytohemagglutinins; Tetradecanoylphorbol Acetate, 16561-29-8References: Jones, D.A., Smith, C.W., McIntire, L.V., Leucocyte adhesion under flow conditions: Principles importante in tissue engineering (1996) Biomaterials, 17, pp. 337-347;Marchant, R.E., Cell adhesion and interactions with biomaterials (1984) J Adhes, 20, pp. 211-225; 
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},
	month = {2003///},
	pages = {429 - 434},
	abstract = {The adhesion of human leukocytes to self-assembled monolayers of well-defined surface chemistry was investigated in vitro. Polymorphonuclear (PMN) and mononuclear leukocytes were isolated from human blood by centrifugation techniques. The effect on adhesion of cell activation produced by pre-incubation of leukocytes with phytohemagglutinin (PHA) and phorbol 12-myristate 13-acetate (PMA) was also studied. Gold substrates were modified by treatment with alkanethiols with three different terminal chemical groups: COOH, OH, and CH                        3. After incubation with the two subpopulations of leukocytes, the monolayers were washed, treated with fixative, stained with a Giemsa method, and observed by light microscopy to quantify the number of attached leukocytes. Comparative quantification of the density of leukocyte adhesion to the three types of self-assembled monolayers was determined. The hydrophobic surface expressing CH
                        3 was found to be the one that induced the highest adhesion density of leukocytes, both of PMN and mononuclear cells. In vitro activation of both mononuclear and PMN leukocytes further increased cell adhesion to the chemically defined monolayers that were used. This enhancement was higher for PHA-activated than for PMA-stimulated mononuclear cells, whereas PMA treatment of neutrophils resulted in a higher rate of adhesion of these cells than PHA stimulation. {\textcopyright} 2003 Wiley Periodicals, Inc.
},
	keywords = {alkane derivative, article, Biocompatible Materials, biomaterial, Biomaterials, Blood, carboxyl group, cell adhesion, cell interaction, cell isolation, cell subpopulation, cell surface, Cell-surface interactions, Cells, Centrifugation, controlled study, drug effect, Giemsa stain, gold, human, human cell, Humans, hydrophobicity, hydroxide, in vitro study, Incubation, lectin, Lectins, leukocyte, Leukocyte activation, leukocyte adherence, Leukocyte adhesion, Leukocytes, Leukocytes, Mononuclear, materials testing, methane, microscopy, Monolayers, mononuclear cell, neutrophil, Neutrophils, Optical microscopy, phorbol 12 acetate 13 myristate, phorbol 13 acetate 12 myristate, physiology, phytohemagglutinin, Phytohemagglutinins, polymorphonuclear cell, Self-assembled monolayers, Surface Properties, surface property, Tetradecanoylphorbol Acetate, thiolacid},
	isbn = {00219304 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0042970748\&partnerID=40\&md5=87f1101c5250d34ddc259f7f43f37e16},
	author = {Barbosa, J.N. and Barbosa, M.A. and {\'A}gua, A.P.}
}
@article {2512,
	title = {Albumin adsorption on alkanethiols self-assembled monolayers on gold electrodes studied by chronopotentiometry},
	journal = {BiomaterialsBiomaterials},
	volume = {24},
	year = {2003},
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},
	month = {2003///},
	pages = {3697 - 3706},
	abstract = {Chronopotentiometry was used to study the adsorption of human serum albumin (HSA) to self-assembled monolayers with the following terminal functional groups: CH                        3, COOH and OH. Surfaces were characterized by X-ray photoelectron spectroscopy, water contact angle measurements and cyclic voltammetry. HSA coverage of the different SAMs was investigated by chronopotentiometry and the total amount of adsorbed protein was determined using radiolabelled albumin. Both techniques have demonstrated that HSA adsorption to the different SAM-modified electrodes increases in the following order: OH\&lt;COOH\&lt;CH
                        3-terminated SAMs. A good correlation between coverage and total amount of HSA adsorbed was observed for long adsorption times (900s). {\textcopyright} 2003 Elsevier Science Ltd. All rights reserved.
},
	keywords = {Adsorption, Albumin, Albumin adsorption, Albumins, alkane, Alkanes, article, Biocompatible Materials, biomaterial, Biomaterials, carboxyl group, Chemical modification, Chronopotentiometry, Contact angle, correlation analysis, cyclic potentiometry, Cyclic voltammetry, electrochemistry, electrode, Electron Probe Microanalysis, Functional groups, gold, Humans, hydroxyl group, isotope labeling, methyl group, Monolayers, potentiometry, priority journal, protein analysis, Self assembly, Self-assembled monolayers, Serum Albumin, Sulfhydryl Compounds, Surface modification, Surface Properties, surface property, temperature, thiol derivative, Time Factors, Water, X ray photoelectron spectroscopy},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0038802804\&partnerID=40\&md5=d9b75bc199d3c909e08c53f4de329ce5},
	author = {Martins, M.C.L. and Fonseca, C. and Barbosa, M.A. and Ratner, B.D.}
}
@article {2509,
	title = {Albumin adsorption on Cibacron Blue F3G-A immobilized onto oligo(ethylene glycol)-terminated self-assembled monolayers},
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	volume = {14},
	year = {2003},
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},
	month = {2003///},
	pages = {945 - 954},
	abstract = {Self-assembled monolayers can be tailored with specific ligands to a certain protein and at the same time prevent the non-specific adsorption of other proteins. Cibacron Blue F3G-A (CB-thiol) was successfully immobilized onto tetra(ethylene glycol)-terminated alkanethiol (CB-thiol). The affinity of human serum albumin (HSA) to immobilized Cibacron Blue F3G-A was studied using mixed thiolate self-assembled monolayers on gold with different n-alkyl chain lengths and functional terminal groups (CH                        3-; OH- and tetra(ethylene glycol)). Surfaces were characterized using X-ray photoelectron spectroscopy and water contact angle measurements. Albumin adsorption and exchangeability of the adsorbed albumin molecules with other albumin molecules in solution were evaluated using 
                        125I-radiolabeled HSA. Competitive adsorption between albumin and fibrinogen to the different self-assembled monolayers (SAMs) was also investigated. Results showed that the incorporation of CB-thiol on the monolayers does not increase the HSA adsorption and reversibility on the SAMs. However, although specific adsorption of HSA to the immobilized Cibacron Blue F3G-A was not demonstrated, the presence of CB-thiol decreases the affinity of fibrinogen to the OH-terminated SAMs. {\textcopyright} 2003 Kluwer Academic Publishers.
},
	keywords = {Adsorption, Albumin, aqueous solution, article, Cell immobilization, cibacron blue f3ga, Contact angle, controlled study, Drug products, Ethylene Glycol, fibrinogen, functional group, Glycols, gold, human, human serum albumin, iodine 125, isotope labeling, ligand, macrogol, molecule, priority journal, protein assembly, protein binding, protein immobilization, protein structure, Proteins, radioassay, Self assembly, surface property, synthesis, tetra(ethylene glycol) undecanethiol, thiol, thiol derivative, unclassified drug, Water, X ray photoelectron spectroscopy},
	isbn = {09574530 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0344629191\&partnerID=40\&md5=6ebb3020ea2ade3febc3906ce0672cc1},
	author = {Martins, Ma.C.L. and Naeemi, E. and Ratner, B.D. and Barbosa, M.A.}
}
@article {2515,
	title = {Albumin and fibrinogen adsorption on Cibacron blue F3G-A immobilised onto PU-PHEMA (polyurethane-poly (hydroxyethylmethacrylate)) surfaces},
	journal = {Journal of Biomaterials Science, Polymer EditionJ. Biomater. Sci. Polym. Ed.},
	volume = {14},
	year = {2003},
	note = {Cited By (since 1996): 16Export Date: 21 November 2012Source: ScopusCODEN: JBSEEdoi: 10.1163/156856203766652057PubMed ID: 12807146Language of Original Document: EnglishCorrespondence Address: Martins, M.C.L.; Inst. de Engenharia Biomedica, Laborat{\'o}rio de Biomateriais, Rua do Campo Alegre 823, 4150-180 Porto, Portugal; email: cmartins@ibmc.up.ptChemicals/CAS: cibacron blue f3ga, 12236-82-7, 53127-08-5; dextran, 87915-38-6, 9014-78-2; fibrinogen, 9001-32-5; polymacon, 25053-81-0, 25249-16-5, 98932-78-6; polyurethan, 61789-63-7; Albumins; Biocompatible Materials; Cibacron Blue F 3GA, 12236-82-7; Fibrinogen, 9001-32-5; Membranes, Artificial; Polyhydroxyethyl Methacrylate, 25249-16-5; TriazinesReferences: Ratner, B.D., Hoffman, A.S., Schoen, F.J., Lemons, J.L., (1996) Biomaterials Science - an Introduction to Materials in Medicine, , (Eds), Academic Press, San Diego, CA;Greco, R.S., (1994) Implantation Biology, the Host Response and Biomedical Devices, , (Ed.), CRC Press, Ann Arbour, MI; 
Sapatnekar, S., Anderson, J.M., (1999) Handbook of Biomaterials Evaluation. Scientific, Technical and Clinical Testing of Implant Materials, p. 353. , A. F. von Recum (Ed.), Taylor \& Francis, Philadelphia, PA; 
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},
	month = {2003///},
	pages = {439 - 455},
	abstract = {In the present work, it is intended to study the effect of Cibacron blue F3G-A (CB) immobilised onto PU-PHEMA (polyurethane-poly(hydroxyethylmethacrylate)) surfaces on protein adsorption and bacterial adhesion. CB immobilisation was carried out by covalent binding between its triazine ring and the hydroxyl groups of the polymer. Characterisation of the films was carried out by attenuated total reflection Fourier transform infrared spectroscopy (ATR-FT-IR), contact angle measurements, X-ray photoelectron spectroscopy (XPS) and scanning electron microscopy (SEM). CB efficiency was evaluated using radiolabelled albumin and fibrinogen from pure solutions, mixtures of both and plasma. Bacterial adhesion tests before and after albumin pre-coating were also performed. The presence of CB increases albumin and fibrinogen adsorption to PU-PHEMA surfaces. The incorporation of CB onto the PU-PHEMA surface also increases bacterial adhesion. Although albumin pre-coating decreases bacterial adhesion onto PU (67\% decrease) and PU-PHEMA-CB (80\%), bacterial adhesion is always lower on PU and PU-PHEMA surfaces than on PU-PHEMA-CB. These results demonstrate that, in contrast to what has been described for CB bound to dextran, CB immobilisation on PU-PHEMA surfaces presents low selectivity to albumin and increased bacterial adhesion relatively to PU and PU-PHEMA surfaces.},
	keywords = {Adsorption, Albumin, Albumins, article, Bacterial adhesion, bacterium adherence, Biocompatible Materials, Chemical structure, Cibacron blue, cibacron blue f3ga, Contact angle, controlled study, covalent bond, dextran, fibrinogen, hydroxyl group, immobilization, infrared spectroscopy, isotope labeling, Membranes, Artificial, Microscopy, Electron, Scanning, nonhuman, PHEMA, Polyhydroxyethyl Methacrylate, polymacon, polyurethan, priority journal, Protein adsorption, Scanning electron microscopy, Spectroscopy, Fourier Transform Infrared, Staphylococcus epidermidis, Surface Properties, triazine derivative, Triazines, X ray photoelectron spectroscopy, XPS},
	isbn = {09205063 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0038316702\&partnerID=40\&md5=6f911799b67ba3289c643eb874879e1f},
	author = {Martins, M.C.L. and Wang, D. and Ji, J. and Feng, L. and Barbosa, M.A.}
}
@article {2517,
	title = {Albumin and fibrinogen adsorption on PU-PHEMA surfaces},
	journal = {BiomaterialsBiomaterials},
	volume = {24},
	year = {2003},
	note = {Cited By (since 1996): 41Export Date: 21 November 2012Source: ScopusCODEN: BIMADdoi: 10.1016/S0142-9612(03)00002-4PubMed ID: 12628827Language of Original Document: EnglishCorrespondence Address: Martins, M.C.L.; Laborat{\'o}rio de Biomateriais, Inst. de Engenharia Biom{\'e}dica, Rua do Campo Algre 823, Porto 4150-180, Portugal; email: cmartins@ibmc.up.ptChemicals/CAS: acrylic acid ethyl ester, 140-88-5; fibrinogen, 9001-32-5; poly(2 hydroxyethyl acrylate), 26022-14-0; polyetherurethan, 76600-67-4; polymacon, 25053-81-0, 25249-16-5, 98932-78-6; protein, 67254-75-5; Albumins; Biocompatible Materials; Fibrinogen, 9001-32-5; poly(2-hydroxyethyl acrylate), 26022-14-0; Polyhydroxyethyl Methacrylate, 25249-16-5; Water, 7732-18-5References: Ratner, B.D., Hoffman, A.S., Schoen, F.J., Lemons, J.L., (1996) Biomaterials science - An introduction to materials in medicine, , CA, USA, San Diego: Academic Press;Greco, R.S., (1994) Implantation biology, the host response and biomedical devices, , Ann Arbour, USA: CRC Press; 
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},
	month = {2003///},
	pages = {2067 - 2076},
	abstract = {Materials that adsorb specific proteins may find a variety of applications in the biomedical field. The aim of this study was the preparation of a hydrophilic surface, with low protein adsorption, to be used in the future as a support for the immobilisation of several species, e.g. Cibacron Blue F3G-A, which has been described to induce specific albumin adsorption. Poly(hydroxyethylmethacrylate) (PHEMA) and poly(hydroxyethylacrylate) (PHEA) were chosen as the hydrophilic surface because they can be easily polymerised and possess hydroxyl groups that can be used for the immobilisation of different compounds. Thin films of PHEMA and PHEA were successfully graft polymerised onto the surface of a commercial poly(etherurethane) (PU) using ceric ion as initiator. Grafting polymerisations were followed by mass gain and attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR). Since stability tests demonstrated that only PU-PHEMA was stable in alkaline solutions, a necessary condition to future immobilisations, the investigation was focused on the coating of PU with PHEMA. PU-PHEMA films were characterised in detail using several techniques as mass gain, ATR-FTIR, contact angle measurements, X-ray photoelectron spectroscopy (XPS) and scanning electron microscopy (SEM). Protein adsorption was evaluated using radiolabelled albumin and fibrinogen from pure solutions and from mixtures of both proteins. PU surfaces modified with PHEMA have demonstrated low protein adsorption, showing their potential use as substrates. This opens the possibly of exploring the advantages of selective adsorption by appropriate immobilisation of specific molecules. {\textcopyright} 2003 Elsevier Science Ltd. All rights reserved.},
	keywords = {acrylic acid ethyl ester, Adsorption, Albumin, Albumins, article, ATR-FTIR, Biocompatible Materials, Chemical modification, Dose-Response Relationship, Drug, fibrinogen, film, Fourier transform infrared spectroscopy, Graft polymerisation, Humans, Hydrogen-Ion Concentration, Hydrophilic surfaces, hydrophilicity, hydroxyl group, infrared spectroscopy, isotope labeling, Microscopy, Electron, Scanning, molecular stability, Pellethane, PHEMA, poly(2 hydroxyethyl acrylate), polyetherurethan, Polyhydroxyethyl Methacrylate, polymacon, Polymerization, priority journal, protein, Protein adsorption, Proteins, Scanning electron microscopy, Spectrometry, X-Ray Emission, Spectroscopy, Fourier Transform Infrared, surface property, Thin films, unclassified drug, Water, X ray photoelectron spectroscopy},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0037400503\&partnerID=40\&md5=dc989d7fe65e35d20f250cf3e7c245f9},
	author = {Martins, M.C.L. and Wang, D. and Ji, J. and Feng, L. and Barbosa, M.A.}
}
@article {2508,
	title = {Constructing thromboresistant surface on biomedical stainless steel via layer-by-layer deposition anticoagulant},
	journal = {BiomaterialsBiomaterials},
	volume = {24},
	year = {2003},
	note = {Cited By (since 1996): 67Export Date: 21 November 2012Source: ScopusCODEN: BIMADdoi: 10.1016/S0142-9612(03)00363-6PubMed ID: 12951013Language of Original Document: EnglishCorrespondence Address: Ji, J.; Department of Polymer Science, Zhejiang University, Hangzhou 310027, China; email: jianji@mail.hz.zj.cnChemicals/CAS: heparin, 37187-54-5, 8057-48-5, 8065-01-8, 9005-48-5; polyethyleneimine, 74913-72-7; stainless steel, 12597-68-1; trometamol, 1185-53-1, 77-86-1; Anticoagulants; Coated Materials, Biocompatible; Heparin, 9005-49-6; Polyethyleneimine, 9002-98-6; Stainless Steel, 12597-68-1Manufacturers: AldrichReferences: Bertrand, P., Jonas, A., Laschewsky, A., Legras, R., Ultrathin polymer coating by complexation of polyelectrolytes at interfaces: Suitable materials, structure and properties (2000) Macromol Rapid Commun, 21, pp. 319-348;Ulman, A., Formation and structure of self-assembled monolayers (1996) Chem Rev, 96, pp. 1533-1554; 
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},
	month = {2003///},
	pages = {4699 - 4705},
	abstract = {Multilayer films consisting of polyethylenimine (PEI) and heparin were successfully prepared on biomedical 316L stainless steel surface via electrostatic self-assembly (ESA) of the PEI and heparin. The process of ESA of PEI/heparin was monitored by static contact angle, electrochemical impedance spectroscopy (EIS), reflection adsorption spectroscopy and X-ray photoelectron spectroscopy data. The contact angle and EIS data revealed that the multilayer coating was stable in Tris-HCl (pH 7.35) buffer solution for 21 days. The static platelet adhesion and static clotting time experiments indicated that the PEI/heparin-deposited stainless steel could resist the platelet adhesion and prolong the static clotting time effectively. Such an easy processing and shape-independent method may have good potential for surface modification of cardiovascular devices. {\textcopyright} 2003 Elsevier Ltd. All rights reserved.},
	keywords = {316L stainless steel, Adhesion, Adsorption, anticoagulant agent, Anticoagulants, aqueous solution, article, Biocompatibility, biomaterial, Biomaterials, blood clotting time, Blood Platelets, Blood-compatibility, buffer, Coated Materials, Biocompatible, coating, Coatings, Contact angle, controlled study, Deposition, device, electricity, Electrochemical impedance spectroscopy, electrochemistry, Electrostatics, heparin, human, human cell, Humans, implant, Layer-by-layer, material coating, materials testing, Multilayers, Organic polymers, pH, Platelet Adhesiveness, Polyethyleneimine, priority journal, reflection adsorption spectroscopy, Self assembly, Spectroscopy, Stainless steel, Surface Properties, surface property, Surfaces, thrombocyte adhesion, Thromboresistant surfaces, trometamol, X ray photoelectron spectroscopy},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0041386468\&partnerID=40\&md5=a68c77a7525bca1760cc298a394c713f},
	author = {Tan, Q. and Ji, J. and Barbosa, M.A. and Fonseca, C. and Shen, J.}
}
@article {2510,
	title = {Protein adsorption on mixtures of hydroxyl- and methyl-terminated alkanethiols self-assembled monolayers},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {67},
	year = {2003},
	note = {Cited By (since 1996): 63Export Date: 21 November 2012Source: ScopusCODEN: JBMRCPubMed ID: 14517873Language of Original Document: EnglishCorrespondence Address: Martins, M.C.L.; INEB-Inst. de Engenharia Biomedica, Laborat{\'o}rio de Biomateriais, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: cmartins@ibmc.up.ptChemicals/CAS: human serum albumin, 9048-49-1; thiol derivative, 13940-21-1; Biocompatible Materials; Gold, 7440-57-5; Proteins; Sulfhydryl CompoundsReferences: Ratner, B.D., Hoffman, A.S., Schoen, F.J., Lemons, J.L., (1996) Biomaterials Science - An Introduction to Materials in Medicine, , San Diego, CA: Academic;Kottke-Marchant, K., Anderson, J.M., Umemura, Y., Marchant, R.E., Effect of albumin coating on the in vitro blood compatibility of Dacron arterial prostheses (1989) Biomaterials, 10, pp. 147-155; 
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},
	month = {2003///},
	pages = {158 - 171},
	abstract = {The effect of surface composition and wettability on the adsorption of human serum albumin (HSA) was studied. Self-assembled monolayers (SAMs) containing mixtures of longer chain methyl- and shorter chain hydroxyl-terminated alkanethiols on gold were used to produce a range of surfaces with different wettabilities and exposed functional groups. Different SAMs were characterized by X-ray photoelectron spectroscopy, water contact angles, and Fourier transform infrared reflection absorption spectroscopy (IRAS). HSA adsorption onto the different SAMs was evaluated by contact angle measurements (wetting tension determinations), radiolabeling of proteins, and IRAS. Concerning HSA adsorption, all the techniques demonstrated higher HSA adsorption on more hydrophobic surfaces. The wetting tension measurements and IRAS suggested a gradual decrease of the HSA adsorption with increases of surface hydrophilicity. Radiolabeled albumin measurements also demonstrated a significant decrease of HSA adsorption on the pure hydroxyl-terminated SAMs. However, no significant differences were detected between mixed and pure methyl-terminated SAMs. Studies of HSA exchangeability with human fibrinogen have suggested that an ideal percentage of hydroxyl groups on the surface may increase albumin affinity without fibrinogen adsorption. {\textcopyright} 2003 Wiley Periodicals, Inc.},
	keywords = {Absorption spectroscopy, Adsorption, article, Biocompatible Materials, Contact angle, Contact angles, fourier transform infrared reflection absorption spectroscopy, Fourier transform infrared spectroscopy, Functional groups, gold, human serum albumin, hydrophilicity, hydrophobicity, IRAS, isotope labeling, measurement, Mixtures, monolayer culture, Monolayers, Protein adsorption, Proteins, Self-assembled monolayers, Spectrum Analysis, Sulfhydryl Compounds, surface property, tension, thiol derivative, Time Factors, wettability, X ray photoelectron spectroscopy, XPS},
	isbn = {00219304 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0344306504\&partnerID=40\&md5=cc1823cda1406a9f9572da09315251f7},
	author = {Martins, M.C.L. and Ratner, B.D. and Barbosa, M.A.}
}
@article {2520,
	title = {Surface engineering of poly(DL-lactide) via electrostatic self-assembly of extracellular matrix-like molecules},
	journal = {BiomacromoleculesBiomacromolecules},
	volume = {4},
	year = {2003},
	note = {Cited By (since 1996): 48Export Date: 21 November 2012Source: ScopusCODEN: BOMAFdoi: 10.1021/bm025773pPubMed ID: 12625735Language of Original Document: EnglishCorrespondence Address: Ji, J.; Department of Polymer Science/Eng., Zhejing University, Hangzhou 310027, China; email: jianji@mail.hz.zj.cnChemicals/CAS: gelatin, 9000-70-8; polyethyleneimine, 74913-72-7; polylactide, 26680-10-4; poly(lactide), 26969-66-4; PolyestersTradenames: AXIOVERT 200, Zeiss; ESCA LAB 200A, VG; Radiance 2100, Biorad; Shimadzu UV-1201, Shimadzu; SPA 400, Seiko; Vectro 22, BrukerManufacturers: Biorad; Bruker; Seiko; Shimadzu; VG; ZeissReferences: Sittinger, M., Perka, C., Schutz, O., Haupl, T., Burmester, G.R.Z., (1999) Rheumatol., 58, pp. 130-135;Kim, B.S., Mooney, D.J., (1998) Trends Biotechnol., 16, p. 224; 
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},
	month = {2003///},
	pages = {378 - 386},
	abstract = {We report the development of new biomacromolecule coatings on biodegradable biomaterials based on electrostatic assembly of extracellular matrix-like molecules. Poly(ethylene imine) (PEI) was employed to engineer poly(DL-lactide) (PDL-LA) substrate to obtain a stable positively charged surface. An extracellular matrix- (ECM-) like biomacromolecule, gelatin, was selected as the polyelectrolyte to deposit on the activated PDL-LA substrate via the electrostatic assemble technique. The extracellular matrix-like multilayer on the PDL-LA substrate was investigated by attenuated total reflection (ATR-FTIR), X-ray photoelectron spectrscopy (XPS), contact angle, and atomic force microscopy (AFM). The gradual buildup of the protein layer was investigated by UV-vis spectra, and it was further given a quantitative analysis of the protein layer on the PDL-LA substrate via the radioiodination technique. The stability of the protein layer under aqueous condition was also tested by the radiolabeling method. Chondrocyte was selected as the model system for testing the cell behavior and morphology on modified PDL-LA substrates. The chondrocyte test about cell attachment, proliferation, cell activity and cell morphology by SEM, and confocal laser scanning microscopy (CLSM) investigation on extracellular matrix-like multilayer modified PDL-LA substrate was shown to promote chondrocyte attachment and growth. Comparing conventional coating methods, polyelectrolyte multiplayers are easy and stable to prepare. It may be a good choice for the modification of 3-D scaffolds used in tissue engineering. These very flexible systems allow broad medical applications for drug delivery and tissue engineering.},
	keywords = {animal cell, Animalia, Animals, article, Atomic force microscopy, biodegradability, biomaterial, cartilage cell, cell activity, cell adhesion, cell function, cell growth, cell proliferation, cell structure, Cells, Cultured, Chondrocytes, confocal laser microscopy, controlled study, Electron Probe Microanalysis, Electrostatics, extracellular matrix, Fourier transform infrared spectroscopy, gelatin, macromolecule, Macromolecules, Microscopy, Atomic Force, nonhuman, polyelectrolyte, Polyesters, Polyethyleneimine, Polyethylenes, polylactide, priority journal, protein analysis, protein stability, quantitative analysis, Rabbits, radioiodination, Scanning electron microscopy, Self assembly, Spectrophotometry, Ultraviolet, Spectroscopy, Fourier Transform Infrared, Surface charge, Surface engineering, Surface Properties, Tissue engineering, Ultraviolet spectroscopy, X ray photoelectron spectroscopy},
	isbn = {15257797 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0038071804\&partnerID=40\&md5=dc56622e3535f161005efe1ae86f4d23},
	author = {Zhu, H. and Ji, J. and Tan, Q. and Barbosa, M.A. and Shen, J.}
}
@article {2533,
	title = {Cellulose phosphates as biomaterials. In vivo biocompatibility studies},
	journal = {BiomaterialsBiomaterials},
	volume = {23},
	year = {2002},
	note = {Cited By (since 1996): 45Export Date: 21 November 2012Source: ScopusCODEN: BIMADdoi: 10.1016/S0142-9612(01)00152-1PubMed ID: 11791931Language of Original Document: EnglishCorrespondence Address: Granja, P.L.; Laborat{\'o}rio de Biomateriais, INEB-Inst. de Engenliaria Biomedica, Rua do Campo Alegre, 823-4150-180 Porto, Portugal; email: pgranja@ibmc.up.ptChemicals/CAS: Biocompatible Materials; Calcium Radioisotopes; Calcium, 7440-70-2; Cellulose, 9004-34-6; phosphocellulose, 9015-14-9References: Jochanan, H., Boss, M.D., Osseointegration (1999) J Long-Term Eff Med Impl, 9, pp. 1-10;Albrektsson, T., Hard tissue response (1998) Handbook of biomaterial properties, pp. 500-512. , Black J, Hastings G, editors. London, UK: Chapman \& Hall; 
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},
	month = {2002///},
	pages = {971 - 980},
	abstract = {Femoral implantation of regenerated cellulose hydrogels revealed their biocompatibility, but a complete osseointegration could not be observed. Phosphorylation was therefore envisaged as the means to enhance cellulose bioactivity. In vitro studies showed that regenerated cellulose hydrogels promote bone cells attachment and proliferation but do not mineralize in acellular simulated physiological conditions. On the contrary, phosphorylated cellulose has shown an opposite behavior, by inducing the formation of a calcium phosphate layer in simulated physiological conditions, but behaving as a poor substrate for bone cells attachment and proliferation. In order to investigate the in vivo behavior of these materials, and assess the influence of mineralization induction ability vs. bone cells compatibility, unmodified and phosphorylated cellulose hydrogels were implanted in rabbits for a maximum period of 6 months and bone regeneration was investigated. Despite the difficulties arising from the retraction of cellulose hydrogels upon dehydration during the preparation of retrieved implants, histological observations showed no inflammatory response after implantation, with bone intra-spongious regeneration of cells and the integration of the unmodified as well as the phosphorylated cellulose implants. After a maximum implantation period of 6 months, histological observations, histomorphometry and the measurement of the amount of                        45Ca incorporated in the surrounding tissue indicated a slightly better osseointegration of phosphorylated cellulose, although no significant differences between the two materials were found. {\textcopyright} 2001 Elsevier Science Ltd. All rights reserved.
},
	keywords = {animal experiment, Animal implantation, animal tissue, Animalia, Animals, article, Biocompatibility, Biocompatible Materials, biomaterial, Biomaterials, Bone, bone cell, bone mineralization, Bone Regeneration, Calcium, calcium 45, Calcium Compounds, calcium phosphate, Calcium Radioisotopes, cell adhesion, cell proliferation, Cells, Cellulose, Cellulose phosphate, Chemical modification, controlled study, Dehydration, histology, hydrogel, Hydrogels, implant, in vivo study, Inflammation, materials testing, Microscopy, Electron, Scanning, morphometrics, nonhuman, Oryctolagus cuniculus, Osseointegration, Phosphates, Phosphorylation, priority journal, Prostheses and Implants, rabbit, Rabbits, Regenerated cellulose hydrogels},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0037082737\&partnerID=40\&md5=faae93af84ab2762579f90bd2d64eefa},
	author = {Fricain, J.C. and Granja, P.L. and Barbosa, M.A. and De J{\'e}so, B. and Barthe, N. and Baquey, C.}
}
@article {2529,
	title = {A novel urethane containing copolymer as a surface modification additive for blood contact materials},
	journal = {Journal of Materials Science: Materials in MedicineJ. Mater. Sci. Mater. Med.},
	volume = {13},
	year = {2002},
	note = {Cited By (since 1996): 6Export Date: 21 November 2012Source: ScopusCODEN: JSMMEdoi: 10.1023/A:1015789726455Language of Original Document: EnglishCorrespondence Address: Ji, J.; Department of Polymer Science, Zhejiang University, HangZhou 310027, China; email: jianji@mail.hz.zj.cnReferences: Elbert, D., Hubbell, J., (1996) Annu. Rev. Mater., p. 365;Munro, M., Quattrone, A., Ellsworth, S., Kulkarni, P., Eberhart, R., (1981) Trans. Am. Soc. Artif. Intern. Organs., p. 499; 
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},
	month = {2002///},
	pages = {677 - 684},
	abstract = {Surface modification to develop a biomolecules-presenting surface is of interest, both from a scientific and an industrial point of view. In this research, a penta-block-coupling polymer of warfarin-PEO-MDI-PEO-warfarin was specially designed as the surface modifying additive (SMA). The warfarin-modified polyurethane surfaces were then prepared by dip-coating method. Attenuated total reflection fourier transform infra-red (ATR-FTIR) spectra revealed that the urethane segments in the SMA could penetrate into the hard block of segmented polyurethane (SPU) via intermolecular hydrogen bonds. The X-ray photoelectron spectroscopy (XPS) results indicated that the intermolecular hydrogen bonds were strong enough to form stable warfarin-PEO composite surfaces in an aqueous environment. Fibrinogen and albumin adsorption onto unmodified and SMA-modified SPU was investigated by the                        125l-labeled method. The surface for attracting and reversibly binding albumin, which was proved to suppress the platelet adhesion and prolong the clotting time, has been developed by the simple coating of the novel SMA in SPU. {\textcopyright} 2002 Kluwer Academic Publishers.
},
	keywords = {Adhesion, Adsorption, Albumin, article, Attenuation, biomaterial, Block copolymers, Blood, blood clotting time, Chemical modification, Coatings, copolymer, fibrinogen, Fourier transform infrared spectroscopy, human, human cell, hydrogen bond, Hydrogen bonds, infrared spectroscopy, iodine 125, material coating, Polyurethanes, priority journal, Surface modifying additives (SMA), surface property, Surface treatment, synthesis, thrombocyte adhesion, urethan, warfarin, X ray photoelectron spectroscopy},
	isbn = {09574530 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0036308146\&partnerID=40\&md5=4767c8a335b26ea0390bc42ddbbaf6b1},
	author = {Ji, J. and Barbosa, M.A. and Feng, L. and Shen, J.}
}
@article {2530,
	title = {Preparation of albumin preferential surfaces on poly(vinyl chloride) membranes via surface self-segregation},
	journal = {Journal of Biomedical Materials ResearchJ. Biomed. Mater. Res.},
	volume = {61},
	year = {2002},
	note = {Cited By (since 1996): 3Export Date: 21 November 2012Source: ScopusCODEN: JBMRBdoi: 10.1002/jbm.10187Language of Original Document: EnglishCorrespondence Address: Ji, J.; Department of Polymer Science, Zhejiang University, HangZhou, 310027, China; email: jianji@mail.hz.zj.cnChemicals/CAS: Membranes, Artificial; Polyethylene Glycols; Polyvinyl Chloride, 9002-86-2; Serum Albumin; Stearates; stearyl poly(ethylene oxide)References: Blass, C.R., Jones, C., Courtney, J.M., Biomaterials for blood tubing: The application of plasticised poly(vinyl chloride) (1992) Int J Artif Organs, 15 (4), pp. 200-203;Brash, J.L., (1983) Biocompatible polymer, metals and composites, p. 35. , Szycher M, editor. London, UK: Technomic Pub. Co; 
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},
	month = {2002///},
	pages = {252 - 259},
	abstract = {Poly(vinyl chlorides)-graft-[w-stearyl-poly(ethylene oxide)] (PVC-g-SPEO), which has a poly(vinyl chloride) (PVC) backbone, poly(ethylene oxide) (PEO) side chain, and stearyl end groups, has been synthesized. Self-organizing blends of the amphiphilic comb polymer in poly-(vinyl chlorides) have been examined as a means to create albumin preferential surfaces on polymer films. X-ray photoelectron spectroscopy (XPS) analysis indicates substantial surface segregation of the PVC-g-SPEO. A surface concentration of 59.9 EO wt \% is achieved by the solution casting and heat treatment of a film with a bulk concentration of only 3.78 EO wt \%. In the aqueous environment, the surface rearrangement of PVC-g-SPEO/PVC blend film is limited and presents a high interfacial energy and high depolar component of interfacial energy due to the "tail-like" SPEO side chain. Protein adsorption tests confirm that PVC-g-SPEO/PVC blend films absorb high levels of albumin and dramatically resist fibrinogen adsorption. Surfaces to attract and reversibly bind albumin, which might diminish the occurrence of thrombosis, inflammation, and infection, are developed by self-organizing blends of the amphiphilic comb polymer in poly(vinyl chlorides). {\textcopyright} 2002 Wiley Periodicals, Inc.},
	keywords = {Adsorption, Albumin, Amphiphilic copolymer, amphophile, aqueous solution, article, artificial membrane, Biocompatible Materials, cell separation, cell surface, chemical binding, combinatorial chemistry, concentration response, conference paper, dimerization, energy resource, film, human, Humans, infection, Inflammation, Inflammations, macrogol, macrogol derivative, membrane structure, Membranes, Artificial, metabolism, Plastic films, Polyethylene Glycols, polymer, Polymeric membranes, Polyvinyl Chloride, Polyvinyl chlorides, polyvinylchloride, protein binding, Serum Albumin, Stearates, stearic acid derivative, stearyl poly(ethylene oxide), Surface modification, Surface Properties, surface property, Surface segregation, Synthesis (chemical), thrombosis, X ray analysis, X ray photoelectron spectroscopy},
	isbn = {00219304 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0036268941\&partnerID=40\&md5=fbe73c0e87ccb8188bce7a8565a7d39a},
	author = {Ji, A. and Feng, L. and Shen, J. and Barbosa, M.A.}
}
@article {2550,
	title = {Affinity of hydroxyapatite to metal cations - a study on the composition and structure of phosphates formed in the presence of titanium and aluminum},
	journal = {Key Engineering MaterialsKey Eng Mat},
	volume = {192-195},
	year = {2001},
	note = {Conference code: 57760Export Date: 21 November 2012Source: ScopusCODEN: KEMAELanguage of Original Document: EnglishCorrespondence Address: Ribeiro, C.C.; INEB, Porto, PortugalReferences: Andress, D.L., Maloney, N.A., Endres, D.B., Sherrard, D.J., (1986) J. Bone Mineral Res., 1, p. 391;Posner, A.S., Blumenthal, N.C., Boskey, A.L., (1986) Kidney Int., 29, p. 17; 
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},
	month = {2001///},
	pages = {55 - 58},
	publisher = {Trans Tech Publ},
	address = {Bologna, Italy},
	abstract = {The purpose of this study was to contribute to the understanding of the effect of titanium, aluminium and titanium/aluminium on the Hap structure and to investigate if a synergistic effect between the two cations exists. The effect of the metal ion concentration was studied. The solids were analysed by X-ray diffraction, Fourier transform infrared spectroscopy, FT-Raman spectroscopy and energy dispersive X-ray analysis.},
	keywords = {Aluminum, Energy dispersive spectroscopy, Fourier transform infrared spectroscopy, Hap structure, hydroxyapatite, Positive ions, Raman spectroscopy, Structure (composition), Synergistic effect, Titanium, X ray diffraction analysis},
	isbn = {10139826 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0035147724\&partnerID=40\&md5=519703da8430f82ae6ea9c07670463e7},
	author = {Ribeiro, C.C. and Barbosa, M.A.}
}
@article {2536,
	title = {Cellulose phosphates as biomaterials. I. Synthesis and characterization of highly phosphorylated cellulose gels},
	journal = {Journal of Applied Polymer ScienceJ. Appl. Polym. Sci.},
	volume = {82},
	year = {2001},
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},
	month = {2001///},
	pages = {3341 - 3353},
	abstract = {The present study concerns the investigation of a material expected to be biocompatible and able to promote bone regeneration. For this purpose, cellulose was chemically modified by phosphorylation. Once implanted, phosphorylated cellulose could promote the formation of calcium phosphates, thus having closer resemblance to bone functionality. In a previous investigation, the obtention and the preliminary characterization of cellulose phosphate gels were reported. In the present study, the synthesis by the H                        3PO
                        4/P
                        2O
                        5/Et
                        3PO 
                        4/hexanol method was optimized in terms of reaction parameters. The structure of materials was investigated by FTIR, Raman, and solid-state 
                        31P- and 
                        13C-NMR spectroscopic studies, and X-ray diffraction. Water swelling and stability to sterilization by gamma-radiation were also assessed. It was demonstrated that the present method allows highly phosphorylated cellulose derivatives to be obtained. Cellulose triphosphates gels are described here for the first time. Products obtained were poorly crystallized monoesters, apparently not significantly affected by gamma sterilization and showed a high water swelling capability. Chemical bonding was confirmed by FTIR, Raman, and both 
                        31P- and 
                        13C-NMR spectroscopies. It was also shown that the H
                        3PO
                        4/P
                        2O
                        5/Et
                        3PO 
                        4/hexanol method provides a versatile and interesting alternative route to some of the more widely used techniques for the phosphorylation of cellulose. {\textcopyright} 2001 John Wiley \&amp; Sons, Inc. J. Appl. Polym. Sci.
},
	keywords = {13C-NMR, 2O, 3PO, 4/hexanol method, 4/P, 5/Et, Biomaterials, Cellulose derivatives, Cellulose gels, Cellulose triphosphates, Chemical bonds, Fourier transform infrared spectroscopy, Gels, H, medical textile, Nuclear magnetic resonance spectroscopy, Phosphorylation, Raman scattering, Sterilizers, Synthesis (chemical), X ray diffraction analysis},
	isbn = {00218995 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0035923986\&partnerID=40\&md5=7a58f84a4d86e26d35d7d90d44aecb63},
	author = {Granja, P.L. and Pouysgu, L. and Ptraud, M. and De Jso, B. and Baquey, C. and Barbosa, M.A.}
}
@article {2537,
	title = {Cellulose phosphates as biomaterials. II. Surface chemical modification of regenerated cellulose hydrogels},
	journal = {Journal of Applied Polymer ScienceJ. Appl. Polym. Sci.},
	volume = {82},
	year = {2001},
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},
	month = {2001///},
	pages = {3354 - 3365},
	abstract = {Cellulose regenerated by the viscose process was previously investigated as an implantable material in orthopedic surgery. It was envisaged to take advantage not only of its good matching with mechanical properties of bone but also of its hydroexpansivity, therefore allowing a satisfactory fixation to hard tissue. Both the osteoconduction and the lack of ostcoinduction of this material were demonstrated. Grafting of phosphate groups was then envisaged as the means to render cellulose more suitable for orthopedic applications by enhancing its bioactivity. In the present work, the previously optimized phosphorylation reaction was successfully adapted to the surface modification of regenerated cellulose. Modified materials were characterized by XPS, FTIR, and                        31P MAS NMR spectroscopic studies, and contact angle measurements, revealing the chemical bond between phosphate groups and cellulose, as well as the hydrophilic nature of phosphorylated materials, which increases with increasing phosphate contents. Water swelling and resistance to gamma sterilization were assessed as well, showing that phosphorylated materials swell considerably in water and were not affected when sterilization was carried out under a nitrogen atmosphere. The increase in surface roughness attributed to chemical modification was demonstrated through laser rugosimetry measurements. {\textcopyright} 2001 John Wiley \&amp; Sons, Inc. J. Appl. Polym. Sci.
},
	keywords = {2O, 3PO, 4/hexanol method, 4/P, 5/Et, Biomaterials, Cellulose derivatives, Cellulose phosphates, Chemical bonds, Chemical modification, Energy dispersive spectroscopy, Fourier transform infrared spectroscopy, H, Hydrogels, Phosphorylation, Regenerated cellulose hydrogels, Sterilization (cleaning), Surface modification, Surface roughness, X ray photoelectron spectroscopy},
	isbn = {00218995 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0035923980\&partnerID=40\&md5=5663bc99f91ce47534779e826f87ed97},
	author = {Granja, P.L. and Pouysgu, L. and Ptraud, M. and De Jso, B. and Baquey, C. and Barbosa, M.A.}
}
@article {2546,
	title = {Corrosion behaviour of titanium in biofluids containing H                    2O
                    2 studied by electrochemical impedance spectroscopy
},
	journal = {Corrosion ScienceCorros Sci},
	volume = {43},
	year = {2001},
	note = {Cited By (since 1996): 73Export Date: 21 November 2012Source: ScopusCODEN: CRRSAdoi: 10.1016/S0010-938X(00)00107-4Language of Original Document: EnglishCorrespondence Address: Fonseca, C.; Inst de Engenharia Biomedica, Porto, PortugalReferences: Hugot-Le-Goff, A., (1986) Thin Solid Films, 142, p. 193;Pascal, P., (1963) Nouveau Trait{\'e} de Chimie Min{\'e}rale, 14. , Masson \& Cie, Paris; 
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},
	month = {2001///},
	pages = {547 - 559},
	publisher = {Elsevier Science Ltd},
	abstract = {This work aims at studying the electrochemical behaviour of titanium in the presence of an artificial biofluid containing H                        2O
                        2, mimicing the situation, where the metal is implanted in the human body and hydrogen peroxide is generated by an inflammatory reaction. A phosphate buffered saline (PBS) solution and two PBS/H
                        2O
                        2 solutions containing 50 and 150 mM of H
                        2O
                        2 were used to simulate the body fluids. The behaviour of the metal was monitored as a function of time by electrochemical impedance spectroscopy (EIS) for three weeks. After one week, the PBS/H
                        2O
                        2 solutions were replaced by fresh PBS solutions in order to simulate the end of the inflammatory process and recovery of the system. All the experiments were carried out at a constant temperature of 37 {\textdegree}C. From the simulation of the experimental EIS spectra, it was concluded that the corrosion resistance of titanium is strongly affected by the presence of H
                        2O
                        2 and when the peroxide is removed, the metal displays a sharp resistance increase. Furthermore, the oxides formed in H
                        2O
                        2 are rougher and display higher ionic conductivities than the oxides formed in the absence of peroxide. The study was complemented with potentiostatic experiments and scanning electron microscopy observation of the metal surfaces.
},
	keywords = {Biomaterials, Body fluids, Corrosion resistance, Electrochemical corrosion, electrochemical process, hydrogen peroxide, impedance technique, Implants (surgical), Phosphate buffered saline, Solutions, Spectroscopy, Titanium},
	isbn = {0010938X (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0035275589\&partnerID=40\&md5=ef23abf56839789d71056a03bc1523e3},
	author = {Fonseca, C. and Barbosa, M.A.}
}
@article {2539,
	title = {Mineralization of regenerated cellulose hydrogels},
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	volume = {12},
	year = {2001},
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},
	month = {2001///},
	pages = {785 - 791},
	abstract = {Due to their high water swelling, regenerated cellulose hydrogels and sponges were pre-incubated in a Ca-containing solution, and their mineralization was investigated. Results obtained demonstrate that a simple pre-incubation treatment in a Ca containing solution can induce mineralization in materials with limited or no tendency to mineralize. The minerals formed had an apatitic carbonated and poorly crystalline structure, resembling carbonated hydroxyapatite found in bone mineral. The apatitic layer formed showed a relatively accelerated growth using this technique, exhibiting nodules in their macroscopic structure, which seem to indicate lateral growth. The porous structure of regenerated cellulose sponges was also homogeneously mineralized using this technique. {\textcopyright} 2001 Kluwer Academic Publishers.},
	keywords = {Apatite, article, Bone, bone mineral, Calcification (biochemistry), Calcium, Carbon, Cellulose, crystal, hydrogel, Hydrogels, hydroxyapatite, Incubation, infrared spectroscopy, mineralization, porosity, priority journal, Scanning electron microscopy, surface property, Swelling, Water},
	isbn = {09574530 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0034771780\&partnerID=40\&md5=58fcd227f17f7da6e5e0af69c7351f0a},
	author = {Granja, P.L. and Ribeiro, C.C. and De J{\'e}so, B. and Baquey, C. and Barbosa, M.A.}
}
@article {2538,
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	year = {2001},
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Walton, D.G., Mayes, A.M., Entropically driven segregation in blend of branched and liner polymers (1996) Phys Rev E, 54 (3), pp. 2811-2815
},
	month = {2001///},
	pages = {3015 - 3023},
	abstract = {An ideal surface for many biomedical applications would resist non-specific protein adsorption while at the same time triggering a specific biological pathway. Based on the approach of selectively binding albumin to free fatty acids, stearyl groups were immobilized onto poly(styrene) backbone via poly(ethylene oxide) side chains. X-ray photoelectron spectroscopy (XPS) analysis indicates substantial surface enrichment of the stearyl poly(ethylene oxide) (SPEO). In an aqueous environment, the surface rearrangement is limited, as proved by dynamic contact angle tests. The comb-like copolymer presents a special hydrophobic surface with high SPEO surface density, which may be due to the {\textquoteright}tail like{\textquoteright} SPEO architecture at the copolymer/water interface. Protein adsorption tests confirm that the comb-like surfaces adsorb high levels of albumin and resist fibrinogen adsorption very significantly. The surfaces prepared in this research attract and reversibly bind albumin due to the synergistic action of the PEO chains and the stearyl end groups. Copyright {\textcopyright} 2001 Elsevier Science Ltd.},
	keywords = {Adsorption, Albumin, Amphiphilic copolymer, article, Biocompatible Materials, Biomedical engineering, Catalyst selectivity, Cell immobilization, Contact angle, copolymer, Copolymers, density, Electron Probe Microanalysis, fibrinogen, Grafting (chemical), Humans, hydrophobicity, Ligands, macrogol, macrogol derivative, materials testing, Polyethylene Glycols, Polystyrenes, priority journal, Protein adsorption, protein binding, Proteins, roentgen spectroscopy, Serum Albumin, Stearates, Stearyl end groups, Surface Properties, surface property, Ultraviolet spectroscopy, X ray photoelectron spectroscopy},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0035889824\&partnerID=40\&md5=9e163aafab1e37712839a8c35e902110},
	author = {Ji, J. and Feng, L. and Barbosa, M.A.}
}
@article {2565,
	title = {Brazing parameters determine the degradation and mechanical behaviour of alumina/titanium brazed joints},
	journal = {Journal of Materials ScienceJ Mater Sci},
	volume = {35},
	year = {2000},
	note = {Cited By (since 1996): 16Export Date: 21 November 2012Source: ScopusCODEN: JMTSAdoi: 10.1023/A:1004776117823Language of Original Document: EnglishCorrespondence Address: Paiva, O.C.; Inst de Engenharia Biomedica, Porto, PortugalReferences: Samandi, M., Gudze, M., Evans, P., Nucl, (1997) Instr. and Meth. in Phys. Res. B, 127-128, p. 669;Paiva, O.C., Barbosa, M.A., (1997) J. Mater. Sci., 32, p. 653; 
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},
	month = {2000///},
	pages = {1165 - 1175},
	publisher = {Kluwer Academic Publishers},
	abstract = {The main aims of the present study are simultaneously to relate tho brazing parameters with the correspondent interfacial microstructure, the resultant mechanical properties and the electrochemical degradation behaviour of commercially pure titanium/alumina brazed joints. A filler metal on the Ag-26.5Cu-3Ti system has been used. Three different brazing temperatures (850, 900 and 950 {\textdegree}C) and three holding times (0.3, 1.2, 2.4 ks) were tested, in order to understand the influence of each combination of brazing temperature holding times, over the final microstructure and properties of the joints. The mechanical properties of the M/C joints were assessed on the basis of bond strength tests carried out using a shear solicitation scheme. The fracture surfaces were studied morphologically and structurally using scanning electron microscopy (SEM), energy dispersive spectroscopy (EDS) and X-ray diffraction analysis (XRD). The degradation behaviour of the M/C joints was assessed by means of electrochemical techniques. It was found that a brazing temperature of 850 {\textdegree}C and a holding time of 2.4 ks, produces the best results in terms of bond strength, 130{\textpm}16 MPa. The mechanical properties obtained could be explained on the basis of the different compounds identified on the fracture surfaces by XRD. On the other hand, a brazing temperature of 950 {\textdegree}C produces the best results in terms of corrosion rates (lower corrosion current), 3.44{\textpm}0.73 μA cm},
	keywords = {Alumina, Aluminum copper titanide, Brazing filler metals, Ceramic matrix composites, Degradation, Energy dispersive spectroscopy, fracture, Joints (structural components), Scanning electron microscopy, Silver alloys, Titanium, X ray diffraction analysis},
	isbn = {00222461 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0033881734\&partnerID=40\&md5=058678288fbb7c85032cae1530352c40},
	author = {Paiva, O.C. and Barbosa, M.A.}
}
@article {2559,
	title = {Self-assembly and surface structure of an amphiphilic graft copolymer, polystyrene-graft-ω-stearyl-poly(ethylene oxide)},
	journal = {Journal of Colloid and Interface ScienceJ. Colloid Interface Sci.},
	volume = {224},
	year = {2000},
	note = {Cited By (since 1996): 12Export Date: 21 November 2012Source: ScopusCODEN: JCISAdoi: 10.1006/jcis.2000.6729Language of Original Document: EnglishCorrespondence Address: Ji, J.; Instituto de Engenharia Biomedica, Laboratorio de Biomateriais, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: jian@ibmc.up.ptChemicals/CAS: macrogol, 25322-68-3; polystyrene, 9003-53-6; stearic acid, 57-11-4, 646-29-7References: Brash, J.L., (1983) Biocompatible Polymer, Metals and Composites, p. 35. , M. Szycher. Lancaster: Technomic;Gombotz, W.R., Guanghui, W., Horbett, T.A., Hoffman, A.S., (1991) J. Biomed. Mater. Res., 25, p. 1547; 
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},
	month = {2000///},
	pages = {255 - 260},
	abstract = {Surface properties of the polystyrene-graft-ω-stearyl-poly(ethylene oxide) (PS-g-SPEO) have been characterized by X-ray photoelectron spectroscopy (XPS), differential scanning calorimetry (DSC), contact angle, and spin probe techniques. The XPS results indicate that the surface and bulk composition of the PS-g-SPEO copolymers differ remarkably from each other. The stearyl and EO components enrich at the copolymer/air interfaces due to the self-assembly of the stearyl groups. At the PS-g-SPEO-72.6 surface (the x in PS-g-SPEO-x indicates the bulk density of the SPEO in wt\%), the self- assembly of the hydrophobic stearyl groups is strong enough to form a stable liquid crystalline phase as indicated by DSC. At polymer/water interfaces, PS-g-SPEO-72.6 presents a hydrophilic surface with low PEO mobility, whereas PS-g-SPEO-50.6 and PS-g-SPEO-31.0 present the hydrophobic surface with high PEO mobility. The two different types of the surfaces, with different characters in surface energy, surface mobility of PEO, and surface architecture of SPEO, will be quite valuable as models for detecting the synergistic action of the PEO chains and the stearyl groups (specific ligand for albumin binding) in protein solutions. (C) 2000 Academic Press.},
	keywords = {Amphiphilic copolymer, article, biomaterial, copolymer, crystal, differential scanning calorimetry, electron microscopy, electron spin resonance, hydrophobicity, macrogol, polystyrene, priority journal, protein assembly, protein binding, protein structure, Self-assembly, stearic acid, Surface structure, X ray analysis},
	isbn = {00219797 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0034655268\&partnerID=40\&md5=1628a0cfec8d5ced3e11c87d74ceae44},
	author = {Ji, J. and Feng, L. and Qiu, Y. and Yu, X. and Barbosa, M.A.}
}
@article {2582,
	title = {In vitro testing of surface-modified biomaterials},
	journal = {Journal of Materials Science: Materials in MedicineJ. Mater. Sci. Mater. Med.},
	volume = {9},
	year = {1998},
	note = {Cited By (since 1996): 16Export Date: 21 November 2012Source: ScopusCODEN: JSMMEdoi: 10.1023/A:1008896106994Language of Original Document: EnglishCorrespondence Address: Leitao, E.; INEB-Instituto Engenharia Biomedica, FEUP-Faculdade de Engenharia, Universidade do Porto, Praca Coronel Pacheco 1, 4050 Porto, Portugal; email: eleitao@fsl.ho.man.ac.ukChemicals/CAS: calcium, 7440-70-2; carbon, 7440-44-0; nitrogen, 7727-37-9; stainless steel, 12597-68-1Tradenames: 316 L, aubert and duval; Thermanox; Ti-5Al-2.5Fe, deutsch titan; Ti-6Al-4V, deutsch titanManufacturers: aubert and duval; deutsch titanReferences: Kirkpatrick, C.J., Mittermayer, C., (1990) J. Mater. Sci. Mater. Med., 1, p. 9;Van Loon, J., (1995), PhD thesis, University of Leiden, The NetherlandsLi, P., De Groot, K., (1991) J. Mater. Sci. Mater. Med., 2, p. 125; 
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},
	month = {1998///},
	pages = {543 - 548},
	publisher = {Kluwer Academic Publishers},
	abstract = {The influence of surface modification treatments such as ion implantation and sputter coating on an in vitro rat bone-marrow cell culture was studied by scanning electron microscopy and X-ray microanalysis. 316 L stainless steel, Ti-6Al-4V and Ti-5Al-2.5Fe were nitrogen ion-implanted with three fluences: 10                        15, 10
                        16 and 10
                        17 ion cm
},
	keywords = {animal cell, animal tissue, article, biomaterial, Biomaterials, bone marrow culture, Calcium, Carbon, Cell culture, cell suspension, collagen fiber, extracellular matrix, implantation, in vitro study, In vitro testing, Ion implantation, male, materials testing, mineralization, morphology, nitrogen, nonhuman, priority journal, rat, Scanning electron microscopy, Sputtering, Stainless steel, Titanium alloys, Titanium aluminum iron alloy, Titanium aluminum vanadium alloy, X ray analysis, X ray microanalysis},
	isbn = {09574530 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0032170120\&partnerID=40\&md5=c39e91f7fc339fc95c225903e26f0ba5},
	author = {Leit{\~a}o, E. and Barbosa, M.A. and De Groot, K.}
}
@article {2605,
	title = {Apatite deposition on titanium surfaces - The role of albumin adsorption},
	journal = {BiomaterialsBIOMATERIALS},
	volume = {18},
	year = {1997},
	note = {Cited By (since 1996): 72Export Date: 21 November 2012Source: ScopusCODEN: BIMADdoi: 10.1016/S0142-9612(97)00031-8PubMed ID: 9212191Language of Original Document: EnglishCorrespondence Address: Serro, A.P.; Centro de Quimica Estrutural, Complexo I, Instituto Superior Tecnico, Av. Rovisco Pais, 1096 Lisboa Codex, PortugalChemicals/CAS: alpha-tricalcium phosphate; Apatites; calcium phosphate, 10103-46-5; Calcium Phosphates; dicalcium phosphate anhydrous, 7757-93-9; Hanks Balanced Salt Solution; Isotonic Solutions; monocalcium phosphate; Serum Albumin, Bovine; tetracalcium phosphate; Titanium, 7440-32-6References: Sundgren, J.-E., Bodo, P., Lundstrom, I., Auger electron spectroscopic studies of the interface between human tissue and implants of titanium and stainless steel (1986) J. Colloid Interface Sci., 10, pp. 9-20;Hanawa, T., Ota, M., Characterization of surface film formed on titanium in electrolyte using XPS (1992) Appl. Surface Sci., 55, pp. 269-276; 
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},
	month = {1997///},
	pages = {963 - 968},
	publisher = {Elsevier Science Ltd},
	abstract = {Titanium implant surfaces are known to spontaneously nucleate apatite layers when in contact with simulated body fluids. However, adsorption of proteins may influence the process of apatite layer formation. In this study the role of bovine serum albumin (BSA) adsorption in the process of apatite deposition on titanium substrates is investigated. Deposition of calcium phosphate was induced by immersing titanium substrates in a Hank{\textquoteright}s balanced salt solution (HBSS) for times ranging from 1 to 23 days. The resulting substrates were studied by scanning electron microscopy (SEM), energy dispersive spectroscopy (EDS), X-ray photoelectron spectroscopy (XPS), wettability measurements and electrochemical impedance determinations. All these methods indicate the presence of a calcium phosphate layer. The same procedure was repeated substituting HBSS with a solution of BSA in HBSS. Although SEM, EDS and electrochemical impedance spectra do not reveal the presence of an apatite layer, XPS analysis strongly indicates that the inhibition of apatite formation by BSA is only partial. The competition between BSA adsorption and apatite deposition seems to lead to a mixed film where the protein co-exists with calcium phosphate. Wettability studies suggest that this surface film is heterogeneous and porous, similar to the thicker films formed in albumin-free HBSS.Titanium implant surfaces are known to spontaneously nucleate apatite layers when in contact with simulated body fluids. However, adsorption of proteins may influence the process of apatite layer formation. In this study the role of bovine serum albumin (BSA) adsorption in the process of apatite deposition on titanium substrates is investigated. Deposition of calcium phosphate was induced by immersing titanium substrates in a Hank{\textquoteright}s balanced salt solution (HBSS) for times ranging from 1 to 23 days. The resulting substrates were studied by scanning electron microscopy (SEM), energy dispersive spectroscopy (EDS), X-ray photoelectron spectroscopy (XPS), wettability measurements and electrochemical impedance determinations. All these methods indicate the presence of a calcium phosphate layer. The same procedure was repeated substituting HBSS with a solution of BSA in HBSS. Although SEM, EDS and electrochemical impedance spectra do not reveal the presence of an apatite layer, XPS analysis strongly indicates that the inhibition of apatite formation by BSA is only partial. The competition between BSA adsorption and apatite deposition seems to lead to a mixed film where the protein co-exists with calcium phosphate. Wettability studies suggest that this surface film is heterogeneous and porous, similar to the thicker films formed in albumin-free HBSS.
},
	keywords = {Adsorption, Albumin, Albumin adsorption, Animals, Apatite, Apatite deposition, Apatites, article, Binding Sites, Bovinae, bovine serum albumin, Calcium Compounds, calcium phosphate, Calcium phosphates, Cattle, Deposition, Electric Impedance, Electrochemical impedance, Energy dispersive spectroscopy, impedance, implant, Isotonic Solutions, Microscopy, Electron, Scanning, priority journal, Prostheses and Implants, Proteins, Scanning electron microscopy, Serum Albumin, Bovine, Spectrometry, X-Ray Emission, Substrates, Surface Properties, surface property, Surfaces, Tissue Preservation, Titanium, wettability, X ray photoelectron spectroscopy},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0031193883\&partnerID=40\&md5=b9eea9b29c987a3c928f576d0b9cdb67},
	author = {Serro, A.P. and Fernandes, A.C. and Saramago, B. and Lima, J. and Barbosa, M.A.}
}
@article {2597,
	title = {Dissolution and deposition processes at metal/apatite interfaces},
	journal = {Anales de Quimica},
	volume = {93},
	year = {1997},
	note = {Export Date: 21 November 2012Source: ScopusLanguage of Original Document: EnglishCorrespondence Address: Barbosa, M.A.; INEB-Instituto de Engenharia Biom{\'e}dica, FEUP Faculdade de Engenharia da, Universidade do Porto Pra{\c c}a do Coronel Pacheco I, 4050 Porto, Portugal; email: barbosa@garfield.fe.up.ptReferences: Silva, R.A., Barbosa, M.A., Costa, A.S., Ribeiro, J.A.C., Esiudo analftico de implantes e pr{\^o}teses ortop{\'e}dicas (1985) Proceedings of Materials 85., p. 5. , Sociedade Portuguesa de Materials;Ma, Q.Y., Tra{\^\i}na, S.J., Logan, T.J., Ryan, J.A., Effects of aqueous Al, Cd. Cu. Fe(II). Ni. and Zn on Pb immobilization by hydroxyapatite (1994) Environ Sei Technol, 28, pp. 1219-1228; 
Oonishi, H., Noda, T., Ito, S., Kohda, A., Ishimaru, H., Yamamoto, M., Tsuji, Y., Effect of hydroxyapatite coating on bone growth into porous titanium alloy implants under loaded conditions (1994) J Appl Biom, 5, pp. 23-37; 
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},
	month = {1997///},
	pages = {S56 - S63},
	abstract = {The coating of implant surfaces with an apatite layer has become one of the most widely used methods to improve bonding to bone. The metal/apatite interface is, however, a region of chemical and mechanical weaknesses, which led some Authors to cast doubts on the long-term integrity of apatite coated implants. These concerns arc essentially related to coatings obtained by conventional plasma-spraying techniques. Recently, there have been attempts to produce coatings with better properties, particularly by acting at the surface preparation stages and by using alternative methods of deposition. Apatite deposition in a liquid phase is one of the new routes being explored. This paper attempts to focus on the main chemical processes involved in the stability of the metal/apatite interface, in order to establish the basic principles for further technological developments. {\textcopyright} Springer-Verlag Ib{\'e}rica 1997.},
	isbn = {11302283 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-33749286735\&partnerID=40\&md5=7cb4c9ae42f83fcd01fc4d918709d99f},
	author = {Barbosa, M.A.}
}
@article {2611,
	title = {Electrochemical and surface modifications on N                    +-ion implanted Ti-5Al-2.5Fe immersed in HBSS
},
	journal = {Corrosion ScienceCorros. Sci.},
	volume = {39},
	year = {1997},
	note = {Cited By (since 1996): 21Export Date: 21 November 2012Source: ScopusCODEN: CRRSALanguage of Original Document: EnglishCorrespondence Address: Leit{\~a}o, E.; INEB - Inst. de Engenharia Biomedica, Pra{\c c}a do Coronel Pacheco, 1, 4050, Porto, PortugalReferences: Tengvall, P., Lundstr{\"o}m, I., (1992) Clinical Mater., 9, pp. 115-134;Seah, K.H.W., Chen, X., (1993) Corros. Sci., 34 (11), pp. 1841-1851; 
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},
	month = {1997///},
	pages = {377 - 383},
	abstract = {The electrochemical behaviour of nitrogen ion-implanted Ti-5Al-2.5Fe was studied in HBSS-Hank{\textquoteright}s balanced salt solution, by open-circuit potential vs time and cyclic polarization techniques. Three fluences (10                        15, 10
                        16 and 10
                        17 ions/cm
                        2) were used. All ion-implanted surfaces showed higher corrosion resistance than the non-implanted ones. The corrosion potential of the ion-implanted samples was more noble and their passivation current was lower than the non-implanted ones. X-ray photo-electron spectroscopy showed that the immersion of Ti-5Al-2.5Fe in HBSS produces a Ca- and P-rich surface layer. {\textcopyright} 1997 Elsevier Science Ltd. All rights reserved.
},
	keywords = {A. titanium alloys, B. EIS, B. XPS, C. passive films, Corrosion resistance, Cyclic polarization technique, Hank{\textquoteright}s balanced salt solution (HBSS), Ion implantation, nitrogen, Open circuit potential technique, Passivation, Passive films, Surface treatment, Titanium alloys, X ray photoelectron spectroscopy},
	isbn = {0010938X (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0031079659\&partnerID=40\&md5=25add0bc42e8e86ba9168bc4700a1124},
	author = {Leit{\~a}o, E. and Silva, R.A. and Barbosa, M.A.}
}
@article {2606,
	title = {Electrochemical and surface modifications on N                    +-ion-implanted 316L stainless steel
},
	journal = {Journal of Materials Science: Materials in MedicineJ. MATER. SCI. MATER. MED.},
	volume = {8},
	year = {1997},
	note = {Cited By (since 1996): 32Export Date: 21 November 2012Source: ScopusCODEN: JSMMEdoi: 10.1023/A:1018532900458Language of Original Document: EnglishCorrespondence Address: Leitao, E.; Instituto de Engenharia Biomedica, Praca do Coronel Pacheco 1, 4050 Porto, PortugalReferences: Seah, K.H.W., Chen, X., (1993) Corros. Sci., 34, pp. 1841-1851;Fraker, A.C., Ruff, A.W., Sung, P., Van Orden, A.C., Speck, K.M., (1983) Titanium Alloys in Surgical Implants, pp. 206-219. , ASTM STP 796, edited by H. A. Luckey and F. Kublei Jr; 
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},
	month = {1997///},
	pages = {365 - 368},
	publisher = {Chapman \& Hall Ltd},
	abstract = {The effect of nitrogen-ion implantation on the electrochemical behaviour of 316L stainless steel in a simulated physiological solution (HBSS-Hank{\textquoteright}s Balanced Salt Solution) was studied by open-circuit potential versus time and cyclic polarization techniques, with the aim of characterizing the surfaces and choosing the best nitrogen-ion fluence. Three fluences (10                        15, 10
                        16 and 10
                        17 ions/cm
                        2) were used. The 10
                        16 ions/cm
                        2 N
                        + fluence improves the corrosion resistance of the 316L stainless steel.
The effect of nitrogen-ion implantation on the electrochemical behaviour of 316L stainless steel in a simulated physiological solution (HBSS-Hank{\textquoteright}s Balanced Salt Solution) was studied by open-circuit potential versus time and cyclic polarization techniques, with the aim of characterizing the surfaces and choosing the best nitrogen-ion fluence. Three fluences (10
                        15, 10
                        16 and 10
                        17 ions/cm
                        2) were used. The 10
                        16 ions/cm
                        2 N
                        + fluence improves the corrosion resistance of the 316L stainless steel.
},
	keywords = {article, balanced salt solution, Composition effects, Corrosion, Corrosion resistance, Cyclic polarization technique, Electrochemical corrosion, electrochemistry, implantation, Ion implantation, limb prosthesis, nitrogen, Polarization, priority journal, prosthesis failure, Simulated physiological solutions, Solutions, Stainless steel, Stainless steel 316L, Surface Properties, Surface treatment, time},
	isbn = {09574530 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0031172794\&partnerID=40\&md5=9e1c626433826a9739f6a007e215a88f},
	author = {Leit{\~a}o, E. and Silva, R.A. and Barbosa, M.A.}
}
@article {2610,
	title = {Electrochemical impedance spectroscopy of nitrogen- and carbon-sputter coated 316 L stainless steel},
	journal = {Corrosion ScienceCorros. Sci.},
	volume = {39},
	year = {1997},
	note = {Cited By (since 1996): 9Export Date: 21 November 2012Source: ScopusCODEN: CRRSALanguage of Original Document: EnglishCorrespondence Address: Leit{\~a}o, E.; INEB - Inst. de Engenharia Biomedica, Pra{\c c}a do Coronel Pacheco, 1, 4050, Porto, PortugalReferences: Gristina, A.G., Naylor, P., Myrvik, Q., (1988) Medical Progress Through Technology, 14, pp. 205-224;Gomi, K., Davies, J.E., (1993) J. Biomedical Mater. Res., 27, pp. 429-431; 
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R{\"o}stlund, T., Thomsen, P., Bjursten, L.M., Ericson, L.E., (1990) J. Biomedical Mater. Res., 24, pp. 847-860; 
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Leit{\~a}o, E., S{\'a}, C., Silva, R.A., Barbosa, M.A., Ali, H., (1995) Corros. Sci., 37, pp. 1861-1866; 
Garrido, A., Leit{\~a}o, E., (1992) IMPFRA-electrochemical Impedance Software, , internal publication; 
(1993) Project BRITE/EURAM n{\textdegree}0477 Internal Report; 
Barbosa, M.A., (1991) Bioceramics, 4, pp. 325-333. , Edited by W. Bonfield, G.W. Hastings and K.E. Tanner; 
Sousa, S.R., Barbosa, M.A., (1993) Clinical Materials, 14, pp. 287-294
},
	month = {1997///},
	pages = {333 - 338},
	abstract = {The effect of nitrogen and carbon sputter coatings on the electrochemical behaviour of 316 L stainless steel in a simulated physiological solution (Hank{\textquoteright}s Balanced Salt Solution) was studied by electrochemical impedance spectroscopy with the aim of characterizing the surfaces and choosing the best coating. Coatings with different thicknesses and structures were tested. The results showed that thicker sputter coatings produce surfaces with higher charge transfer resistance and lower interface capacities. This indicates that these materials probably owe their high corrosion resistance to the formation of more protective films. {\textcopyright} 1997 Elsevier Science Ltd. All rights reserved.},
	keywords = {A. Stainless steel, B. EIS, C. passive films, Carbon, Charge transfer, Coatings, Composition effects, Corrosion resistance, electrochemistry, Films, Hank{\textquoteright}s balanced salt solution, nitrogen, Passive films, Protective coatings, sodium chloride, Spectroscopy, Sputter deposition, Stainless steel, Surface phenomena},
	isbn = {0010938X (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0031080418\&partnerID=40\&md5=8768ca67f5fad93ace86c90323473352},
	author = {Leit{\~a}o, E. and Silva, R.A. and Barbosa, M.A.}
}
@article {2603,
	title = {Influence of substrate material and surface finishing on the morphology of the calcium-phosphate coating},
	journal = {Journal of Biomedical Materials ResearchJ. BIOMED. MATER. RES.},
	volume = {36},
	year = {1997},
	note = {Cited By (since 1996): 11Export Date: 21 November 2012Source: ScopusCODEN: JBMRBdoi: 10.1002/(SICI)1097-4636(199707)36:1<85::AID-JBM10>3.0.CO;2-IPubMed ID: 9212392Language of Original Document: EnglishCorrespondence Address: Leitao, E.; INEB, FEUP, Praca do Coronel Pacheco 1, 4050 Porto, PortugalChemicals/CAS: Alloys; alpha-tricalcium phosphate; Aluminum, 7429-90-5; Biocompatible Materials; calcium phosphate, 10103-46-5; Calcium Phosphates; dicalcium phosphate anhydrous, 7757-93-9; Hanks Balanced Salt Solution; Iron, 7439-89-6; Isotonic Solutions; monocalcium phosphate; Stainless Steel, 12597-68-1; tetracalcium phosphate; titanium alloy (TiAl6V4), 12743-70-3; Titanium, 7440-32-6References: Fujishiro, Y., Sato, T., Okuwaki, A., Coating of hydroxyapatite on metal plates using thermal dissociation of calcium-EDTA chelate in phosphate solutions under hydrothermal conditions (1995) Mater. Sci. Mater. Med., 6, pp. 172-176;Shirkhanzadeh, M., Calcium phosphate coatings prepared by electrocrystallization from aqueous electrolytes (1995) J. Mater, Sci. Mater. Med., 6, pp. 90-93; 
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},
	month = {1997///},
	pages = {85 - 90},
	publisher = {John Wiley \& Sons Inc},
	abstract = {The formation of an apatite-like layer was achieved by immersing Ti- 6A1-4V, Ti-A1-2.5Fe, and 316 L stainless-steel substrata in Hank{\textquoteright}s balanced salt solution (HBSS). The layer was characterized by surface analysis techniques, namely, X-ray microanalysis and X-ray diffraction, and the morphology was observed by scanning electron microscopy and atomic force microscopy. The concentrations of Ca and P were monitored as a function of time. The morphology of the precipitate layer seems to be dependent both on the type of metal substrate and its surface finish. Polished Ti-6A1-4V and Ti-A1-2.5Fe surfaces exhibit a plate precipitate morphology, whereas rougher surfaces show scattered crystal-like precipitation. The results suggest that the layer produced by immersion of polished titanium alloys in HBSS is constituted by an amorphous apatite.The formation of an apatite-like layer was achieved by immersing Ti-6Al-4V, Ti-Al-2.5Fe, and 316 L stainless-steel substrata in Hank{\textquoteright}s balanced salt solution (HBSS). The layer was characterized by surface analysis techniques, namely, X-ray microanalysis and X-ray diffraction, and the morphology was observed by scanning electron microscopy and atomic force microscopy. The concentrations of Ca and P were monitored as a function of time. The morphology of the precipitate layer seems to be dependent both on the type of metal substrate and its surface finish. Polished Ti-6Al-4V and Ti-Al-2.5Fe surfaces exhibit a plate precipitate morphology, whereas rougher surfaces show scattered crystal-like precipitation. The results suggest that the layer produced by immersion of polished titanium alloys in HBSS is constituted by an amorphous apatite.
},
	keywords = {Alloys, Aluminum, Aluminum alloys, article, Biocompatibility, Biocompatible Materials, biomaterial, Calcium Compounds, calcium phosphate, Calcium phosphate coatings, Calcium phosphates, Coatings, Finishing, Humans, hydroxyapatite, Implants (surgical), Iron, Isotonic Solutions, materials testing, metal implantation, Microscopy, Electron, Scanning, morphology, Phosphates, Stainless steel, Surface Properties, surface property, Surface testing, Surface treatment, Time Factors, Titanium, Titanium alloys, X ray diffraction, X ray diffraction analysis},
	isbn = {00219304 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0031195147\&partnerID=40\&md5=07a9f4ca9de83fbb3c66a25cfea71228},
	author = {Leit{\~a}o, E. and Barbosa, M.A. and De Groot, K.}
}
@article {2612,
	title = {Investigation of the dissolution of the bioceramic hydroxyapatite in the presence of titanium ions using ToF-SIMS and XPS},
	journal = {BiomaterialsBIOMATERIALS},
	volume = {18},
	year = {1997},
	note = {Cited By (since 1996): 28Export Date: 21 November 2012Source: ScopusCODEN: BIMADdoi: 10.1016/S0142-9612(96)00134-2PubMed ID: 9068892Language of Original Document: EnglishCorrespondence Address: Davies, M.C.; Lab. Biophysics and Surface Analysis, Department Pharmaceutical Sciences, University of Nottingham, Nottingham NG7 2RD, United KingdomChemicals/CAS: Biocompatible Materials; Cations; Ceramics; Durapatite, 1306-06-5; Titanium, 7440-32-6References: Hench, L.L., Wilson, J., Bioceramics (1991) MRS Bull, p. 62. , September;Katz, J.L., Harper, R.A., (1990) Concise Encyclopedia of Medical and Dental Materials, p. 87. , ed. D. F. Williams, Pergamon Press, Oxford; 
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De Groot, K., (1981) Biocompatibility of Clinical Implant Materials. Vol. I, 1, p. 199. , ed. D. F. Williams, CRC Press, Boca Raton; 
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Jarcho, M., Calcium phosphate ceramics as hard tissue prosthetics (1981) Clin Orthop Rel Res, 157, p. 259; 
De Groot, K., Geesink, R., Klein, C.P.A.T., Serekian, P., Plasma sprayed coatings of hydroxylapatite (1987) J Biomed Mater Res, 21, p. 1375; 
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Geesink, R.G.T., De Groot, K.A., Klein, C.P.A.T., Chemical implant fixation using hydroxylapatite coatings: The development of a human total hip prosthesis for chemical fixation to bone using hydroxylapatite coatings on titanium substrates (1987) Clin Orthop Rel Res, 225, p. 147; 
Cook, S.D., Thomas, K.A., Kay, J.F., Jarcho, M., Hydroxyapatite coated titanium for orthopaedic implant applications (1988) Clin Orthop Rel Res, 232, p. 225; 
Van Blitterswijk, C.A., Grote, J.J., Kuijpers, Blok-Van Hoek, C.J.G., Daems, W.T., Bioreactions at the tissue/hydroxyapatite interface (1985) Biomaterials, 6, p. 243; 
De Lange, G.L.A., Donath, K., Interface between bone tissue and implants of solid hydroxyapatite-coated titanium implants (1989) Biomaterials, 10, p. 121; 
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Driessens, F.C.M., (1983) Bioceramics of Calcium Phosphate, p. 1. , ed. K. de Groot, CRC Press, Boca Raton; 
Van Raemdonck, W., Ducheyne, P., DeMeester, P., (1984) Metal and Ceramic Biomaterials Vol. II, Strength and Surface, 2, p. 143. , eds P. Ducheyne and G. W. Hastings, CRC Press, Boca Raton; 
Lee, D.R., (1988) Dissolution Characterisation of Commercially Available Hydroxylapatite Particulate, , MSc thesis, University of Alabama at Birmingham; 
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Briggs, D., Ratner, B.D., A semi-quantitative SIMS analysis of the surfaces of random ethyl methacrylate:-Hydroxyethylmethacrylate copolymer films (1988) Polym Comm, 29, p. 6; 
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Briggs, D., Analysis of polymer surfaces by SIMS. VII. Homopolymer and copolymer nylons (1987) Org Mass Spectrom, 22, p. 91
},
	month = {1997///},
	pages = {311 - 316},
	publisher = {Elsevier Science Ltd},
	abstract = {Time-of-flight secondary ion mass spectrometry (ToF-SIMS) and X-ray photoelectron spectroscopy (XPS) analyses have been used to investigate the dissolution of hydroxyapatite in the presence of titanium chloride suggesting the substitution of titanium ions for calcium in the hydroxyapatite structure. The surface analytical data suggest that titanium was incorporated within the solid phase as titanium phosphate. Comparison of relative ion intensities in the ToF-SIMS spectra reveals changes in the composition of the surface chemistry of hydroxyapatite. These relative ion intensities show that the maximum surface uptake of titanium occurred at a solution concentration of 500 ppm titanium chloride for a time of incubation of 30 min. These data correlate with that obtained using XPS highlighting the semi-quantitative information which ToF-SIMS can provide.Time-of-flight secondary ion mass spectrometry (ToF-SIMS) and X-ray photoelectron spectroscopy (XPS) analyses have been used to investigate the dissolution of hydroxyapatite in the presence of titanium chloride suggesting the substitution of titanium ions for calcium in the hydroxyapatite structure. The surface analytical data suggest that titanium was incorporated within the solid phase as titanium phosphate. Comparison of relative ion intensities in the ToF-SIMS spectra reveals changes in the composition of the surface chemistry of hydroxyapatite. These relative ion intensities show that the maximum surface uptake of titanium occurred at a solution concentration of 500 ppm titanium chloride for a time of incubation of 30 min. These data correlate with that obtained using XPS highlighting the semi-quantitative information which ToF-SIMS can provide.
},
	keywords = {article, Bioceramic hydroxyapatite, Biocompatible Materials, biomaterial, Biomaterials, Cations, ceramic prosthesis, ceramics, Composition, Dissolution, Durapatite, hydroxyapatite, information processing, mass spectrometry, Phosphates, priority journal, Radiography, Secondary ion mass spectrometry, Spectrometry, Mass, Secondary Ion, Spectrometry, X-Ray Emission, Spectrophotometry, Substitution reactions, Surface chemistry, surface property, Surface structure, Time of flight secondary ion mass spectrometry, Time-of-flight secondary ion mass spectrometry, Titanium, Titanium chloride, X ray photoelectron spectroscopy, X-ray photoelectron spectroscopy},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0031080821\&partnerID=40\&md5=9581c063071547190645f666a211bddb},
	author = {Leadley, S.R. and Davies, M.C. and Ribeiro, C.C. and Barbosa, M.A. and Paul, A.J. and Watts, J.F.}
}
@article {2598,
	title = {Production, bonding strength and electrochemical behaviour of commercially pure Ti/Al                    2O
                    3 brazed joints
},
	journal = {Journal of Materials ScienceJ Mater Sci},
	volume = {32},
	year = {1997},
	note = {Cited By (since 1996): 8Export Date: 21 November 2012Source: ScopusCODEN: JMTSALanguage of Original Document: EnglishCorrespondence Address: Paiva, O.C.; INEB-Inst. de Engenharia Biomedica, Pra{\c c}a do Coronel Pacheco 1, 4050 Porto, PortugalReferences: Paiva, O.C., Barbosa, M.A., (1995) Advances in Materials Science and Implant Orthopaedic Surgery, p. 275. , edited by R. Kossowsky and N. Kossowsky NATO ASI Series, Dordercht, The Netherlands;Hongqi, H., Zhihao, J., Xiaotian, W., (1994) J. Mater. Sci., 29, p. 5041; 
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},
	month = {1997///},
	pages = {653 - 659},
	abstract = {The brazing of commercially pure titanium to Al                        2O
                        3 has been studied. Two different brazing alloys within the Ag-Cu-Ti system and pure silver were selected as bonding agents. Titanium hydride (TiH
                        2) additions were also tested, with the aim of improving the wetting of the ceramic surface by the melted brazing alloy. The mechanical and electrochemical behaviour of the produced joints was assessed, and related to chemical and morphological features resulting from an analysis by scanning electron microscopy and energy dispersive spectroscopy. It was possible to produce joints presenting high integrity, good strength and high resistance to corrosion. The best results were obtained when using an Ag-26Cu-3Ti brazing alloy. The addition of TiH
                        2 increased the mechanical properties, leading to a maximum bonding strength of 80 {\textpm} 8 MPa, as determined in three-point bending tests. In most of the cases, for a maximum deflection of 5 mm, there was only a partial detachment of the ceramic/metal joints. The lowest values for the corrosion rates (i
                        corr = 1.38 μA cm
},
	keywords = {Agents, Aluminum compounds, Aluminum trioxide, Bond strength (materials), Bonding, Brazed joints, Brazing, Brazing alloys, Corrosion resistance, Energy dispersive spectroscopy, Interfaces (materials), Joints (structural components), Scanning electron microscopy, Silver alloys, Strength of materials, Titanium, Titanium compounds, Titanium hydride},
	isbn = {00222461 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0031075923\&partnerID=40\&md5=e1879111241c72f3096a0a8277f73c50},
	author = {Paiva, O.C. and Barbosa, M.A.}
}
@article {2604,
	title = {XPS characterization of surface films formed on surface-modified implant materials after cell culture},
	journal = {Journal of Materials Science: Materials in MedicineJ. MATER. SCI. MATER. MED.},
	volume = {8},
	year = {1997},
	note = {Cited By (since 1996): 7Export Date: 21 November 2012Source: ScopusCODEN: JSMMEdoi: 10.1023/A:1018505621839Language of Original Document: EnglishCorrespondence Address: Leitao, E.; INEB-Instituto Engenharia Biomedica, FEUP-Faculdade de Engenharia, Universidade do Porto, Praca Coronel Pacheco 7, 4050 Porto, PortugalReferences: Schmidt, H., Exner, H.E., R{\"u}ck, D.M., Angert, N., Fink, U., Advances in material science and implant orthopaedic surgery (1995) NATO-ASI Series E: Applied Science, 24, pp. 207-221. , edited by R. Kossowsky and N. Kossowsky;Leit{\~a}o, E., S{\'a}, C., Silva, R.A., Barbosa, M.A., Ali, H., (1995) Corros. Sci., 37, p. 1861; 
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},
	month = {1997///},
	pages = {423 - 426},
	publisher = {Chapman \& Hall Ltd},
	abstract = {Nitrogen ion-implanted Ti-6AI-4V, Ti-5AI-2.5Fe and 316 L stainless steel and nitrogen or carbon sputter-coated samples were inoculated with rat bone marrow. The interface between the cell layer and the substrata was studied by X-ray photo-electron spectrometry and observed by scanning electron microscopy (SEM). Ca and P were detected on all materials after in vitro cell culture. Titanium appears to be present mainly in the form of TiO                        2.
Nitrogen ion-implanted Ti-6Al-4V, Ti-5Al-2.5Fe and 316 L stainless steel and nitrogen or carbon sputter-coated samples were inoculated with rat bone marrow. The interface between the cell layer and the substrata was studied by X-ray photo-electron spectrometry and observed by scanning electron microscopy (SEM). Ca and P were detected on all materials after in vitro cell culture. Titanium appears to be present mainly in the form of TiO
                        2.
},
	keywords = {Animal cell culture, Animalia, article, Bone, bone marrow, Calcium, Carbon, Cell culture, implant, Implants (surgical), Interfaces (materials), Ion implantation, nitrogen, phosphorus, priority journal, Scanning electron microscopy, Stainless steel, Surface films, surface property, Surface treatment, Titanium alloys, Titanium dioxide, X ray spectrometry},
	isbn = {09574530 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0031194230\&partnerID=40\&md5=38633ecb076a75d73f9fb1bfc40bc0cf},
	author = {Leit{\~a}o, E. and Barbosa, M.A. and De Groot, K.}
}
@article {2625,
	title = {Effect of hydroxyapatite thickness on metal ion release from Ti6Al4V substrates},
	journal = {BiomaterialsBIOMATERIALS},
	volume = {17},
	year = {1996},
	note = {Cited By (since 1996): 62Export Date: 21 November 2012Source: ScopusCODEN: BIMADdoi: 10.1016/0142-9612(96)89655-4PubMed ID: 8938233Language of Original Document: EnglishCorrespondence Address: Sousa, S.R.; INEB, Praca do Coronel Pacheco 1, 4050 Porto, PortugalChemicals/CAS: Alloys; Biocompatible Materials; Durapatite, 1306-06-5; titanium alloy (TiAl6V4), 12743-70-3; Titanium, 7440-32-6References: Barbosa, M.A., Electrochemical impedance studies on calcium phosphate-metal interfaces (1991) Bioceramics, 4, pp. 325-333. , Bonfield W, Hastings GW, Tanner KE, eds. London: Butterworth-Heinemann;Sousa, S.R., Barbosa, M.A., Electrochemistry of AISI 316L stainless steel in calcium phosphate and protein solutions (1991) J Mater Sci: Mater Med, 2, pp. 19-26; 
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Li, P., De Groot, K., Calcium phosphate formation within sol-gel prepared titania in vitro and in vivo (1993) J Biomed Mater Res, 27, pp. 1495-1500; 
Li, P., Kangasniemi, I., De Groot, K., Bonelike hydroxyapatitc induction by a gel-derived titania and a titanium substrate (1994) J Am Ceram Soc, 77, pp. 1307-1312; 
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Weng, J., Liu, X., Zhang, X., Li, X., Thermal decomposition of hydroxyapatite structure induced by titanium and its dioxide (1994) J Mater Sci Lett, 13, pp. 159-161; 
Castro Ribeiro, C., Barbosa, M.A., Influence of metal ions on the dissolution behaviour of hydroxyapatite (1991) Bioceramics, 4, pp. 145-153. , Bonfield W, Hastings GW, Tanner KE, eds. Butterworth-Heinemann; 
ASTM G61-86, standard test method for: Conducting cyclic potentiodynamic polarization measurements for localized corrosion susceptibility of iron, nickel, or cobalt based alloys (1989) Annual Book of ASTM Standards, pp. 345-361. , 03.02. Philadelphia, PA: American Society for Testing and Materials; 
ASTM G 31-72 e1, standard practice for: Laboratory immersion corrosion testing of metals (1989) Annual Book of ASTM Standards, pp. 176-186. , 03.02. Philadelphia, PA: American Society for Testing and Materials; 
Barbosa, M.A., Surface layers and the reactivity of metallic implants (1992) Biomaterials - Hard Tissue Repair and Replacement, pp. 257-283. , Muster D et al. ed. Amsterdam: Elsevier Science Publishers BV; 
Rivero, D.P., Fox, J., Skipor, A.K., Urban, R.M., Galante, J.O., Calcium phosphate-coated porous titanium implants for enhanced skeletal fixation (1988) J Biomed Mater Res, 22, pp. 191-201; 
Oonishi, H., Yamamoto, M., Ishimaru, H., The effect of hydroxyapatite coating on bone growth into porous titanium alloy implants (1989) J Bone Joint Surg, 71 B, pp. 213-216; 
Bourne, R.B., Rorabeck, C.H., Burkar, B., Kirk, P.G., Ingrowth surfaces - Plasma spray coating to titanium alloy hip replacements (1994) Clin Orthop Rel Res, 298, pp. 37-46; 
Oonishi, H., Noda, T., Ito, S., Effect of hydroxyapatite coatings on bone growth into porous titanium alloy implants under loaded conditions (1994) J Appl Biomater, 5, pp. 23-37; 
Moroni, A., Caja, V.L., Egger, E.L., Trinchese, L., Chao, E.Y.S., Histomorphometry of hydroxyapatite coated and uncoated porous titanium bone implants (1994) Biomaterials, 15, pp. 926-930; 
Bloebaum, R.D., DuPont, J.A., Osteolysis from a press-fit hydroxyapatite-coated implant (1993) J Arthroplasty, 8, pp. 195-202; 
Bloebaum, R.D., Beeks, D., Dorr, L.D., Savory, C.G., DuPont, J.A., Hofmann, A.A., Complications with hydroxyapatite particulate separation in total hip arthroplasty (1994) Clin Orthop, 298, pp. 19-26; 
Klein, C.P.A.T., Patka, P., Wolke, J.G.C., De Blieck-Hogervorst, J.M.A., De Groot, K., Long-term in vivo study of plasma-sprayed coatings on titanium alloys of tetracalcium phosphate, hydroxyapatite and α-tricalcium phosphate (1994) Biomaterials, 15, pp. 146-160; 
Reis, R.L., Monteiro, F.J., Hastings, G.W., Stability of hydroxyapatite plasma-sprayed coated Ti-6Al-4V under cyclic bending in simulated physiological solutions (1994) J Mater Sci: Mater Med, 5, pp. 457-462; 
Wang, B.C., Lee, T.M., Chang, E., Yang, C.Y., The shear strength and the failure mode of plasma-sprayed hydroxyapatite coating to bone: The effect of coating thickness (1993) J Biomed Mater Res, 27, pp. 1315-1327; 
Tranquilli Leali, P., Merolli, A., Palmacci, O., Gabbi, C., Cacchiolo, A., Gonizzi, G., Evaluation of different preparations of plasma-spray hydroxyapatite coating on titanium alloy and duplex stainless steel in the rabbit (1994) J Mater Sci: Mater Med, 5, pp. 345-349
},
	month = {1996///},
	pages = {397 - 404},
	publisher = {Elsevier Science Ltd},
	abstract = {The electrochemical dissolution behaviour of Ti6Al4V alloy coated with hydroxyapatite (HA) by plasma spraying was studied in Hank{\textquoteright}s balanced salt solution (HBSS) and compared with that of polished and grit-blasted passivated surfaces. Two different nominal thicknesses of HA (50 and 200 μm) were used. Taking a polished passivated surface as reference, grit blasting of the substrate increased the electrical charge used in the oxidation of Ti6Al4V alloy at constant potential, as a result of increased surface area. However, only HA coatings with a thickness of 200 μm were capable of reducing the charge to values lower than those measured for polished surfaces. Electrochemical impedance spectroscopy has also shown that only 200 μm thick coatings are effective in reducing the oxidation rate of the substrate. Furthermore, in potentiostatic experiments the 50 μm thick coating detached from the substrate, which did not occur with the 200 μm thick coating. However, after 6 months immersion in HBSS, detachment occurred in some regions of both coatings. No titanium, aluminium or vanadium were detected in solution by electrothermal atomic absorption spectroscopy. These data indicate that HA is an effective barrier to metal ion release, even for the thinner coatings, due to formation of metal phosphates or to incorporation of metal ions in the HA structure.The electrochemical dissolution behaviour of Ti6Al4V alloy coated with hydroxyapatite (HA) by plasma spraying was studied in Hank{\textquoteright}s balanced salt solution (HBSS) and compared with that of polished and grit-blasted passivated surfaces. Two different nominal thicknesses of HA (50 and 200 μm) were used. Taking a polished passivated surface as reference, grit blasting of the substrate increased the electrical charge used in the oxidation of Ti6Al4V alloy at constant potential, as a result of increased surface area. However, only HA coatings with a thickness of 200 μm were capable of reducing the charge to values lower than those measured for polished surfaces. Electrochemical impedance spectroscopy has also shown that only 200 μm thick coatings are effective in reducing the oxidation rate of the substrate. Furthermore, in potentiostatic experiments the 50 μm thick coating detached from the substrate, which did not occur with the 200 μm thick coating. However, after 6 months immersion in HBSS, detachment occurred in some regions of both coatings. No titanium, aluminium or vanadium were detected in solution by electrothermal atomic absorption spectroscopy. These data indicate that HA is an effective barrier to metal ion release, even for the thinner coatings, due to formation of metal phosphates or to incorporation of metal ions in the HA structure.
},
	keywords = {Absorption spectroscopy, Alloys, Aluminum, article, Atomic spectroscopy, balanced salt solution, Bioactive coatings, Biocompatible Materials, Biomaterials, Calcium Compounds, Dissolution, Durapatite, Electric charge, Electrochemical dissolution, Electrochemical impedance spectroscopy, electrochemistry, Electrothermal atomic absorption spectroscopy, Hank balanced salt solution, hydroxyapatite, Ion release, Ions, metal ion, Metal ion release, Metal phosphates, Microscopy, Electron, Scanning, Oxidation, Plasma spraying, potentiometry, priority journal, Spectrophotometry, Atomic, Spectroscopy, Substrates, thickness, Thickness effect, Time Factors, Titanium, Titanium alloys, vanadium},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0030087995\&partnerID=40\&md5=ec5e4bddc601b37b0dbe58029dd679d4},
	author = {Sousa, S.R. and Barbosa, M.A.}
}
@article {2628,
	title = {Implant recovery and tissue reaction in growing pigs following implantation of packaging materials for injectable electronic identification and monitoring devices},
	journal = {Preventive Veterinary MedicinePrev. Vet. Med.},
	volume = {25},
	year = {1996},
	note = {Cited By (since 1996): 5Export Date: 21 November 2012Source: ScopusCODEN: PVMEELanguage of Original Document: EnglishCorrespondence Address: Janssens, S.; Lab. for Agric. Buildings Research, K.U. Leuven, K. Mercierlaan 92, B-3001 Heverlee, BelgiumReferences: Agresti, A., (1990) Categorical Data Analysis, , John Wiley, New York, 558 pp;Report from the working group on transponders (1990) CBSG News, 1 (3), p. 13; 
Davis, S.D., Gibbons, D.F., Martin, R.L., Levitt, S.R., Smith, J., Harrington, R.V., Biocompatibility of ceramic implants in soft tissue (1972) J. Biomed. Mater. Res., 6, pp. 425-449; 
Dorn, H.J., Vorstellung des EURO I.D. Systems zur kennzeichnung von tieren mit mikrochips in transpondern (1987) Tierarztl. Umschau, 12, pp. 978-981; 
Fallon, R.J., Rogers, P.A.M., Use and recovery of implantable electronic transponders in beef cattle (1991) Automatic Electronic Identification Systems for Farm Animals, pp. 61-67. , E. Lambooij (Editor), Commission European Community, Luxembourg; 
Konermann, H., Identification of horses by implantation of microchips (1991) Automatic Electronic Identification Systems for Farm Animals, pp. 37-43. , E. Lambooij (Editor), Commission European Community, Luxembourg; 
Lambooij, E., Injectable electronic identification systems: Some veterinary aspects (1991) Automatic Electronic Identification Systems for Farm Animals, pp. 21-27. , E. Lambooij (Editor), Commission European Community, Luxembourg; 
Lambooij, E., Merks, J.W.M., De techniek en plaats van injectie van elektronische levensnummers in varkens (1989) IVO-Rapp., B-335. , IVO-DLO, Zeist, The Netherlands, 12 pp; 
Lambooij, E., De Groot, P.H.S., Molenbeek, R.F., Gruys, E., Subcutaneous tissue reaction to polyethylene terephtalate-covered electronic identification transponders in pigs (1992) Vet. Q., 14 (4), pp. 145-147; 
Interim report following six month checks (1991) Livestock Identification Trial, , MLC, Milton Keynes, UK, 14 pp; 
Petersen, B., Kunneken, J., Norpoth, A., BIPS: An information and preventive system for pig breeding farms (1989) Pigs News Inf., 10 (4), pp. 473-476; 
Rao, G.N., Edmondson, J., Tissue reaction to an implantable identification device in mice (1990) Toxicol. Pathol., 18 (3), pp. 412-416; 
(1989) SAS/STAT User{\textquoteright}s Guide, Version 6, 4th Edn., 1. , SAS Institute Inc., Cary, NC, 943 pp; 
Williams, D.F., The response of the body environment to implants (1973) Implants in Surgery, pp. 203-297. , D.F. Williams (Editor), Saunders, London; 
Williams, D.F., Titanium and titanium alloys (1981) Biocompatibility of Clinical Implant Materials, 1, pp. 188-200. , D.F. Williams (Editor), CRC Press, Boca Raton, FL
},
	month = {1996///},
	pages = {249 - 258},
	abstract = {Different materials were used as cylindrical housings (40 mm {\texttimes} 5 mm) for implantable electronic identification and monitoring tags in livestock. A total of 299 pigs received an implant in the right ear base. Wound healing was complete after 6 weeks in all animals, whereas tissue reaction at the site of the transponder started from the first week with highest levels between 6 and 9 weeks. About 10\% of pigs showed visible swelling of the tissue surrounding the implant. Severeness of tissue reaction ante-mortem influenced the recovery rate of implants. Histological sections obtained from the pigs at slaughter show signs of an inflammatory response in most of the pigs which was associated with the implantation duration/body weight effect. Overall recovery of implants was 90\%. The unfavourable inflammation and recovery results might be attributed to a sub-optimal injection procedure.},
	keywords = {implant, Implant recovery, Pig, tissue reaction},
	isbn = {01675877 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0038873896\&partnerID=40\&md5=5fb7280a2742ab9dfe152ec1045acb44},
	author = {Janssens, S. and Rocha, L.A. and Bosschaerts, L. and Barbosa, M.A. and Puers, R. and Vill{\'e}, H. and Geers, R.}
}
@article {2630,
	title = {The effect of hydroxyapatite thickness on metal ion release from stainless steel substrates},
	journal = {Journal of Materials Science: Materials in MedicineJ. MATER. SCI. MATER. MED.},
	volume = {6},
	year = {1995},
	note = {Cited By (since 1996): 18Export Date: 21 November 2012Source: ScopusCODEN: JSMMEdoi: 10.1007/BF00134324Language of Original Document: EnglishCorrespondence Address: Sousa, S.R.; INEB, Instituto Engenharia Biomedica, Praca do Coronel Pacheco, 1, 4050 Porto, Portugal},
	month = {1995///},
	pages = {818 - 823},
	publisher = {Chapman \& Hall Ltd},
	abstract = {The corrosion behaviour of 350 stainless steel coated with hydroxyapatite, HA, by plasma spraying was studied in Hank{\textquoteright}s Balanced Salt Solution, HBSS, and compared with that of polished passivated surfaces. Two different nominal thicknesses, 50 μm and 200 μm, corresponding to what one might consider a thin and a thick coating, respectively, were used. Only HA coatings with a thickness of 200 μm were capable of reducing the electrical charge consumed at constant potential to values lower than those measured for polished surfaces. However, no HA detachment occurred for both thicknesses, as opposed to what has been found in a previous work with Ti6A14V alloy coated with 50 μm HA. No iron, chromium or nickel were detected in solution by Atomic Absorption Spectroscopy with electrothermal atomization (ET-AAS). These elements were also absent from the bulk of the HA coating, both after a 6 month immersion period and electrochemical accelerated tests. The data indicate that in spite of the relatively low corrosion resistance of stainless steel as compared to that of titanium alloys, a thin (50 μm) HA coating prevents the release of metal ions, while remaining adherent to the substrate.The corrosion behaviour of 350 stainless steel coated with hydroxyapatite, HA, by plasma spraying was studied in Hank{\textquoteright}s Balanced Salt Solution, HBSS, and compared with that of polished passivated surfaces. Two different nominal thicknesses, 50 μm and 200 μm, corresponding to what one might consider a thin and a thick coating, respectively, were used. Only HA coatings with a thickness of 200 μm were capable of reducing the electrical charge consumed at constant potential to values lower than those measured for polished surfaces. However, no HA detachment occurred for both thicknesses, as opposed to what has been found in a previous work [1] with Ti6Al4V alloy coated with 50 μm HA. No iron, chromium or nickel were detected in solution by Atomic Absorption Spectroscopy with electrothermal atomization (ET-AAS). These elements were also absent from the bulk of the HA coating, both after a 6 month immersion period and electrochemical accelerated tests. The data indicate that in spite of the relatively low corrosion resistance of stainless steel as compared to that of titanium alloys, a thin (50 μm) HA coating prevents the release of metal ions, while remaining adherent to the substrate.
},
	keywords = {Absorption spectroscopy, atomic absorption spectrometry, Atomic absorption spectroscopy, Atomic spectroscopy, balanced salt solution, Calcium Compounds, Chromium, comparative study, conference paper, Corrosion, Corrosion behaviour, Electric charge, electrochemistry, Hank balanced salt solution, hydroxyapatite, immersion, Inorganic coatings, Ions, Iron, metal ion, Metal ion release, Nickel, Plasma spraying, priority journal, Stainless steel, Stainless steel substrates, Substrates, thickness, Thickness effect, Titanium, Titanium alloys},
	isbn = {09574530 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0029616612\&partnerID=40\&md5=d2be2280e7407eb6232225ae459f896f},
	author = {Sousa, S.R. and Barbosa, M.A.}
}
@article {2632,
	title = {Electrochemical and surface modifications on N                    +-ion implanted Ti-6A1-4V immersed in HBSS
},
	journal = {Corrosion ScienceCorros. Sci.},
	volume = {37},
	year = {1995},
	note = {Cited By (since 1996): 37Export Date: 21 November 2012Source: ScopusCODEN: CRRSALanguage of Original Document: EnglishCorrespondence Address: Leit{\~a}o, E.; INEB-Instituto de Engenharia Biom{\'e}dica, Praca do Coronel Pacheco, 1, 4050 Porto, Portugal},
	month = {1995///},
	pages = {1861 - 1866},
	abstract = {The effect of nitrogen-ion implantation on the electrochemical behaviour of Ti-6Al-4V in a simulated physiological solution (HBSS-Hank{\textquoteright}s balanced salt solution) was studied by open-circuit potential versus time and cyclic polarization techniques, with the aim of characterizing better the surface prior to biological testing and to choose the most appropriate nitrogen-ion fluence. Three fluences (10                        15, 10
                        16 and 10
                        17 ions/cm
                        2) were used. The 10
                        16 ions/cm
                        2 N
                        + fluence produced the lowest corrosion rate under passive conditions. The highest fluence originated a large increase in the corrosion rate and inhibited the formation of a calcium- and phosphate-rich layer on the electrode surface. {\textcopyright} 1995.
},
	keywords = {Biological testing, Characterization, Corrosion, Corrosion rate, Cyclic polarization technique, Electrochemical behaviour, electrochemistry, Hank balanced salt solution, Ion implantation, materials testing, Nitrogen ion implanted titanium aluminum vanadium alloy, Nitrogen-ion fluence, Open circuit potential, Passivation, Polarization, Simulated physiological solution, Solutions, Surface modification, Surface treatment, Titanium alloys},
	isbn = {0010938X (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0029403524\&partnerID=40\&md5=4726589b20b429b97686cee3106fed88},
	author = {Leit{\~a}o, E. and Sa, C. and Silva, R.A. and Barbosa, M.A. and Ali, H.}
}
@article {2631,
	title = {In vitro calcification of orthopaedic implant materials},
	journal = {Journal of Materials Science: Materials in MedicineJ. MATER. SCI. MATER. MED.},
	volume = {6},
	year = {1995},
	note = {Cited By (since 1996): 23Export Date: 21 November 2012Source: ScopusCODEN: JSMMEdoi: 10.1007/BF00134330Language of Original Document: EnglishCorrespondence Address: Leitao, E.; Instituto de Engenharia Biomedica, Faculdade de Engenharia, Universidade do Porto, Praca Coronel Pacheco 1, 4050 Porto, Portugal},
	month = {1995///},
	pages = {849 - 852},
	publisher = {Chapman \& Hall Ltd},
	abstract = {The formation of an apatite-like layer is achieved by immersing Ti6A14V and TiA12.5Fe substrata in Hank{\textquoteright}s Balanced Salt Solution (HBSS). The layer was characterized by several techniques, namely X-ray microanalysis, X-ray diffraction and X-ray photoelectron spectroscopy. The results suggest that the layer produced by immersion in HBSS is in the form of an amorphous apatite. The pH and the concentrations of calcium and phosphate were monitored as a function of time. In vitro tests with rat bone marrow were performed in order to mimic the bone/biomaterial interface. They were performed on both immersed and non-immersed samples. The in vitro bone marrow results suggest that the apatite-like layer formed may improve the bone bonding characteristics of the studied titanium alloys.The formation of an apatite-like layer is achieved by immersing Ti6Al4V and TiAl2.5Fe substrata in Hank{\textquoteright}s Balanced Salt Solution (HBSS). The layer was characterized by several techniques, namely X-ray microanalysis, X-ray diffraction and X-ray photoelectron spectroscopy. The results suggest that the layer produced by immersion in HBSS is in the form of an amorphous apatite. The pH and the concentrations of calcium and phosphate were monitored as a function of time. In vitro tests with rat bone marrow were performed in order to mimic the bone/biomaterial interface. They were performed on both immersed and non-immersed samples. The in vitro bone marrow results suggest that the apatite-like layer formed may improve the bone bonding characteristics of the studied titanium alloys.
},
	keywords = {Amorphous apatite, Amorphous materials, animal cell, Apatite, balanced salt solution, Bone, bone marrow, Calcification, Calcification (biochemistry), Calcium, calcium phosphate, conference paper, Hank balanced salt solution, immersion, implantation, Implants (surgical), metal implantation, Microanalysis, nonhuman, orthopedics, pH, phosphate, Phosphates, priority journal, rat, Spectroscopy, surface property, time, Titanium, Titanium alloys, X ray analysis, X ray diffraction, X ray photoelectron spectroscopy},
	isbn = {09574530 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0029558709\&partnerID=40\&md5=8ba348deca0317db2d0a3521d82f02e0},
	author = {Leitao, E. and Barbosa, M.A. and De Groot, K.}
}
@article {2629,
	title = {Modifications in the molecular structure of hydroxyapatite induced by titanium ions},
	journal = {Journal of Materials Science: Materials in MedicineJ. MATER. SCI. MATER. MED.},
	volume = {6},
	year = {1995},
	note = {Cited By (since 1996): 22Export Date: 21 November 2012Source: ScopusCODEN: JSMMEdoi: 10.1007/BF00134326Language of Original Document: EnglishCorrespondence Address: Ribeiro, C.C.; Instituto de Engenharia Biomedica, Praca do Coronel Pacheco, 1, 4050 Porto, Portugal},
	month = {1995///},
	pages = {829 - 834},
	publisher = {Chapman \& Hall Ltd},
	abstract = {The purpose of this study was to contribute to the understanding of the effect of titanium ions released from a metallic substrate on the molecular structure of hydroxyapatite. The effects of pH, time of incubation and concentration of titanium ions were investigated. The solids were analysed by X-ray diffraction, Fourier transform infrared spectroscopy, Fourier transform Raman spectroscopy, energy dispersive X-ray analysis and thermogravimetric analysis. The results clearly indicate the presence of a titanium phosphate, Ti(HPO                        4)
                        2{\textperiodcentered}nH
                        2O (n = 1-3), which probably has a double layered structure. The formation of this compound is dependent on the titanium concentration and its crystallinity increases with the time of incubation.
The purpose of this study was to contribute to the understanding of the effect of titanium ions released from a metallic substrate on the molecular structure of hydroxyapatite. The effects of pH, time of incubation and concentration of titanium ions were investigated. The solids were analysed by X-ray diffraction, Fourier transform infrared spectroscopy, Fourier transform Raman spectroscopy, energy dispersive X-ray analysis and thermogravimetric analysis. The results clearly indicate the presence of a titanium phosphate, Ti(HPO
                        4)
                        2{\textperiodcentered}nH
                        2O (n = 1-3), which probably has a double layered structure. The formation of this compound is dependent on the titanium concentration and its crystallinity increases with the time of incubation.
},
	keywords = {Calcium Compounds, Chemical structure, Coatings, conference paper, Crystallinity, Crystallization, Dissolution, Energy dispersive x ray analysis, Fourier transform infrared spectroscopy, Fourier transform Raman spectroscopy, hydroxyapatite, Implants (surgical), incubation time, infrared spectroscopy, Ions, metal ion, Molecular Structure, pH, pH effects, phosphate, Phosphates, priority journal, Raman spectrometry, Raman spectroscopy, Thermogravimetric analysis, thermogravimetry, time, Titanium, Titanium compounds, X ray analysis, X ray diffraction},
	isbn = {09574530 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0029583899\&partnerID=40\&md5=724de7ed1c6fddd7a7e258cd19ba3710},
	author = {Ribeiro, C.C. and Barbosa, M.A. and Machado, A.A.S.C. and Tudor, A. and Davies, M.C.}
}
