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http://purl.uniprot.org/citations/7593198http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7593198http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7593198http://www.w3.org/2000/01/rdf-schema#comment"The adhesive and signaling functions of integrins are regulated through their cytoplasmic domains. We identified a novel 111 residue polypeptide, designated beta 3-endonexin, that interacted with the cytoplasmic tail of the beta 3 integrin subunit in a yeast two-hybrid system. This interaction is structurally specific, since it was reduced by 64% by a point mutation in the beta 3 cytoplasmic tail (S752-->P) that disrupts integrin signaling. Moreover, this interaction is integrin subunit specific since it was not observed with the cytoplasmic tails of the alpha IIb, beta 1, or beta 2 subunits. beta 3-Endonexin fusion proteins bound selectively to detergent-solubilized beta 3 from platelets and human umbilical vein endothelial cells, and beta 3-endonexin mRNA and protein were detected in platelets and other tissues. A related mRNA encoded a larger polypeptide that failed to bind to beta integrin tails. The apparent specificity of beta 3-endonexin for the beta 3 integrin subunit suggests potential mechanisms for selective modulation of integrin functions."xsd:string
http://purl.uniprot.org/citations/7593198http://purl.org/dc/terms/identifier"doi:10.1083/jcb.131.3.807"xsd:string
http://purl.uniprot.org/citations/7593198http://purl.org/dc/terms/identifier"doi:10.1083/jcb.131.3.807"xsd:string
http://purl.uniprot.org/citations/7593198http://purl.uniprot.org/core/author"Babior B.M."xsd:string
http://purl.uniprot.org/citations/7593198http://purl.uniprot.org/core/author"Babior B.M."xsd:string
http://purl.uniprot.org/citations/7593198http://purl.uniprot.org/core/author"Ginsberg M.H."xsd:string
http://purl.uniprot.org/citations/7593198http://purl.uniprot.org/core/author"Ginsberg M.H."xsd:string
http://purl.uniprot.org/citations/7593198http://purl.uniprot.org/core/author"Williams M.J."xsd:string
http://purl.uniprot.org/citations/7593198http://purl.uniprot.org/core/author"Williams M.J."xsd:string
http://purl.uniprot.org/citations/7593198http://purl.uniprot.org/core/author"O'Toole T.E."xsd:string
http://purl.uniprot.org/citations/7593198http://purl.uniprot.org/core/author"O'Toole T.E."xsd:string
http://purl.uniprot.org/citations/7593198http://purl.uniprot.org/core/author"Eigenthaler M.J."xsd:string
http://purl.uniprot.org/citations/7593198http://purl.uniprot.org/core/author"Eigenthaler M.J."xsd:string
http://purl.uniprot.org/citations/7593198http://purl.uniprot.org/core/author"Shattil S.J."xsd:string
http://purl.uniprot.org/citations/7593198http://purl.uniprot.org/core/author"Shattil S.J."xsd:string
http://purl.uniprot.org/citations/7593198http://purl.uniprot.org/core/author"Thon V."xsd:string
http://purl.uniprot.org/citations/7593198http://purl.uniprot.org/core/author"Thon V."xsd:string
http://purl.uniprot.org/citations/7593198http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7593198http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7593198http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/7593198http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/7593198http://purl.uniprot.org/core/pages"807-816"xsd:string
http://purl.uniprot.org/citations/7593198http://purl.uniprot.org/core/pages"807-816"xsd:string