



@article {2859,
	title = {Expression of ST3GAL4 Leads to SLex Expression and Induces c-Met Activation and an Invasive Phenotype in Gastric Carcinoma Cells},
	journal = {PLoS ONE},
	volume = {8},
	year = {2013},
	note = {Cited By (since 1996):1Export Date: 12 December 2013Source: ScopusArt. No.: e66737},
	month = {2013///},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-84879165131\&partnerID=40\&md5=58617c0600b708de7a68556b87336112},
	author = {Gomes, C. and Os{\'o}rio, H. and Pinto, M.T. and Campos, D. and Oliveira, M.J. and Reis, C.A.}
}
@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.}
}
