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http://purl.uniprot.org/citations/2420005http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2420005http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2420005http://www.w3.org/2000/01/rdf-schema#comment"The Rous sarcoma virus oncogene product, pp60v-src, transforms cultured fibroblasts but its corresponding proto-oncogene product, pp60c-src, does not. Both proteins are known to be protein-tyrosine kinases. Published results suggest that the kinase activity of pp60c-src is inhibited relative to that of pp60v-src, due perhaps to phosphorylation of a tyrosine in pp60c-src that is not phosphorylated in pp60v-src. In this study, it was observed that the tyrosine phosphorylated in pp60c-src is Tyr527, six residues from the COOH-terminus of the protein. The region of pp60c-src from residue 515 to the COOH-terminus, including Tyr527, has been replaced with a different sequence in pp60v-src. Thus, the increase in transforming ability and kinase activity that occurred in the genesis of pp60v-src may have resulted from the loss of a tyrosine involved in negative regulation."xsd:string
http://purl.uniprot.org/citations/2420005http://purl.org/dc/terms/identifier"doi:10.1126/science.2420005"xsd:string
http://purl.uniprot.org/citations/2420005http://purl.org/dc/terms/identifier"doi:10.1126/science.2420005"xsd:string
http://purl.uniprot.org/citations/2420005http://purl.uniprot.org/core/author"Hunter T."xsd:string
http://purl.uniprot.org/citations/2420005http://purl.uniprot.org/core/author"Hunter T."xsd:string
http://purl.uniprot.org/citations/2420005http://purl.uniprot.org/core/author"Cooper J.A."xsd:string
http://purl.uniprot.org/citations/2420005http://purl.uniprot.org/core/author"Cooper J.A."xsd:string
http://purl.uniprot.org/citations/2420005http://purl.uniprot.org/core/author"Gould K.L."xsd:string
http://purl.uniprot.org/citations/2420005http://purl.uniprot.org/core/author"Gould K.L."xsd:string
http://purl.uniprot.org/citations/2420005http://purl.uniprot.org/core/author"Cartwright C.A."xsd:string
http://purl.uniprot.org/citations/2420005http://purl.uniprot.org/core/author"Cartwright C.A."xsd:string
http://purl.uniprot.org/citations/2420005http://purl.uniprot.org/core/date"1986"xsd:gYear
http://purl.uniprot.org/citations/2420005http://purl.uniprot.org/core/date"1986"xsd:gYear
http://purl.uniprot.org/citations/2420005http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/2420005http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/2420005http://purl.uniprot.org/core/pages"1431-1434"xsd:string
http://purl.uniprot.org/citations/2420005http://purl.uniprot.org/core/pages"1431-1434"xsd:string
http://purl.uniprot.org/citations/2420005http://purl.uniprot.org/core/title"Tyr527 is phosphorylated in pp60c-src: implications for regulation."xsd:string
http://purl.uniprot.org/citations/2420005http://purl.uniprot.org/core/title"Tyr527 is phosphorylated in pp60c-src: implications for regulation."xsd:string
http://purl.uniprot.org/citations/2420005http://purl.uniprot.org/core/volume"231"xsd:string
http://purl.uniprot.org/citations/2420005http://purl.uniprot.org/core/volume"231"xsd:string
http://purl.uniprot.org/citations/2420005http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2420005
http://purl.uniprot.org/citations/2420005http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2420005