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http://purl.uniprot.org/citations/21073888http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21073888http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21073888http://www.w3.org/2000/01/rdf-schema#comment"Insularin (INS) was obtained from Bothrops insularis venom by reversed-phase high-performance liquid chromatography using a C(18) column and characterized as a disintegrin by peptide mass fingerprint and inhibition of ADP-induced platelet aggregation. A cDNA coding for P-II a metalloproteinase/disintegrin was cloned from a cDNA library from B. insularis venom glands. The deduced protein sequence possesses 73 amino acid residues, including the N-terminal, internal peptides of native insularin, the ARGDNP-sequence and 12 cysteines in a conserved alignment. This cDNA fragment was subcloned in the pGEX-4T-1 vector and expressed in a prokaryotic expression system as a fusion protein with glutathione S-transferase (GST-INS). Both native and recombinant insularin inhibited ADP-induced platelet aggregation and endothelial cells (HUVEC) adhesion with similar activities indicating that GST-INS folded correctly and preserved the integrin-binding loop. Insularin may be a tool in studies that involve platelets and endothelial cell adhesion dependent on alphaIIbeta3 and alphavbeta3 integrins."xsd:string
http://purl.uniprot.org/citations/21073888http://purl.org/dc/terms/identifier"doi:10.1016/j.toxicon.2010.10.013"xsd:string
http://purl.uniprot.org/citations/21073888http://purl.org/dc/terms/identifier"doi:10.1016/j.toxicon.2010.10.013"xsd:string
http://purl.uniprot.org/citations/21073888http://purl.uniprot.org/core/author"Ho P.L."xsd:string
http://purl.uniprot.org/citations/21073888http://purl.uniprot.org/core/author"Ho P.L."xsd:string
http://purl.uniprot.org/citations/21073888http://purl.uniprot.org/core/author"Pimenta D.C."xsd:string
http://purl.uniprot.org/citations/21073888http://purl.uniprot.org/core/author"Pimenta D.C."xsd:string
http://purl.uniprot.org/citations/21073888http://purl.uniprot.org/core/author"Della-Casa M.S."xsd:string
http://purl.uniprot.org/citations/21073888http://purl.uniprot.org/core/author"Della-Casa M.S."xsd:string
http://purl.uniprot.org/citations/21073888http://purl.uniprot.org/core/author"Magalhaes G.S."xsd:string
http://purl.uniprot.org/citations/21073888http://purl.uniprot.org/core/author"Magalhaes G.S."xsd:string
http://purl.uniprot.org/citations/21073888http://purl.uniprot.org/core/author"Serrano S.M."xsd:string
http://purl.uniprot.org/citations/21073888http://purl.uniprot.org/core/author"Serrano S.M."xsd:string
http://purl.uniprot.org/citations/21073888http://purl.uniprot.org/core/author"Moura-da-Silva A.M."xsd:string
http://purl.uniprot.org/citations/21073888http://purl.uniprot.org/core/author"Moura-da-Silva A.M."xsd:string
http://purl.uniprot.org/citations/21073888http://purl.uniprot.org/core/author"Junqueira-de-Azevedo I."xsd:string
http://purl.uniprot.org/citations/21073888http://purl.uniprot.org/core/author"Junqueira-de-Azevedo I."xsd:string
http://purl.uniprot.org/citations/21073888http://purl.uniprot.org/core/author"Clissa P.B."xsd:string
http://purl.uniprot.org/citations/21073888http://purl.uniprot.org/core/author"Clissa P.B."xsd:string
http://purl.uniprot.org/citations/21073888http://purl.uniprot.org/core/author"Lopes D.S."xsd:string
http://purl.uniprot.org/citations/21073888http://purl.uniprot.org/core/author"Lopes D.S."xsd:string
http://purl.uniprot.org/citations/21073888http://purl.uniprot.org/core/author"Butera D."xsd:string
http://purl.uniprot.org/citations/21073888http://purl.uniprot.org/core/author"Butera D."xsd:string