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http://purl.uniprot.org/citations/11368322http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11368322http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11368322http://www.w3.org/2000/01/rdf-schema#comment"The alpha2beta1 integrin is a major collagen receptor that plays an essential role in the adhesion of normal and tumor cells to the extracellular matrix. Here we describe the isolation of a novel metalloproteinase/disintegrin, which is a potent inhibitor of the collagen binding to alpha2beta1 integrin. This 55-kDa protein (alternagin) and its disintegrin domain (alternagin-C) were isolated from Bothrops alternatus snake venom. Amino acid sequencing of alternagin-C revealed the disintegrin structure. Alternagin and alternagin-C inhibit collagen I-mediated adhesion of K562-alpha2beta1-transfected cells. The IC50 was 134 and 100 nM for alternagin and alternagin-C, respectively. Neither protein interfered with the adhesion of cells expressing alphaIIbeta3, alpha1beta1, alpha5beta1, alpha4beta1 alphavbeta3, and alpha9beta1 integrins to other ligands such as fibrinogen, fibronectin, and collagen IV. Alternagin and alternagin-C also mediated the adhesion of the K562-alpha2beta1-transfected cells. Our results show that the disintegrin-like domain of alternagin is responsible for its ability to inhibit collagen binding to alpha2beta1 integrin."xsd:string
http://purl.uniprot.org/citations/11368322http://purl.org/dc/terms/identifier"doi:10.1006/abbi.2000.2120"xsd:string
http://purl.uniprot.org/citations/11368322http://purl.org/dc/terms/identifier"doi:10.1006/abbi.2000.2120"xsd:string
http://purl.uniprot.org/citations/11368322http://purl.uniprot.org/core/author"Zingali R.B."xsd:string
http://purl.uniprot.org/citations/11368322http://purl.uniprot.org/core/author"Zingali R.B."xsd:string
http://purl.uniprot.org/citations/11368322http://purl.uniprot.org/core/author"Oliva M.L.V."xsd:string
http://purl.uniprot.org/citations/11368322http://purl.uniprot.org/core/author"Oliva M.L.V."xsd:string
http://purl.uniprot.org/citations/11368322http://purl.uniprot.org/core/author"Niewiarowski S."xsd:string
http://purl.uniprot.org/citations/11368322http://purl.uniprot.org/core/author"Niewiarowski S."xsd:string
http://purl.uniprot.org/citations/11368322http://purl.uniprot.org/core/author"Selistre-de-Araujo H.S."xsd:string
http://purl.uniprot.org/citations/11368322http://purl.uniprot.org/core/author"Selistre-de-Araujo H.S."xsd:string
http://purl.uniprot.org/citations/11368322http://purl.uniprot.org/core/author"Souza D.H.F."xsd:string
http://purl.uniprot.org/citations/11368322http://purl.uniprot.org/core/author"Souza D.H.F."xsd:string
http://purl.uniprot.org/citations/11368322http://purl.uniprot.org/core/author"Faria J.P."xsd:string
http://purl.uniprot.org/citations/11368322http://purl.uniprot.org/core/author"Faria J.P."xsd:string
http://purl.uniprot.org/citations/11368322http://purl.uniprot.org/core/author"Ferreira L.L."xsd:string
http://purl.uniprot.org/citations/11368322http://purl.uniprot.org/core/author"Ferreira L.L."xsd:string
http://purl.uniprot.org/citations/11368322http://purl.uniprot.org/core/author"Iemma M.R.C."xsd:string
http://purl.uniprot.org/citations/11368322http://purl.uniprot.org/core/author"Iemma M.R.C."xsd:string
http://purl.uniprot.org/citations/11368322http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/11368322http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/11368322http://purl.uniprot.org/core/name"Arch. Biochem. Biophys."xsd:string
http://purl.uniprot.org/citations/11368322http://purl.uniprot.org/core/name"Arch. Biochem. Biophys."xsd:string