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http://purl.uniprot.org/citations/2550144http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2550144http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2550144http://www.w3.org/2000/01/rdf-schema#comment"We have identified two platelet-derived growth factor (PDGF)-dependent autophosphorylation sites in the beta subunit of the human PDGF receptor (PDGF-R). The major site of phosphorylation (Tyr-857) corresponds to the major autophosphorylation site in many other tyrosine kinases. Tyr-751, which lies within the kinase insert region, is a second in vivo site and the major in vitro site. Immunoprecipitates of wild-type PDGF-Rs prepared from PDGF-treated cells contained a phosphatidylinositol (PI) 3 kinase activity and three specific polypeptides as well as the PDGF-R. Mutation of Tyr-751 to Phe or Gly, or mutation of the catalytic domain to abolish kinase activity, blocked association of the PDGF-R with the PI kinase and the three proteins. These results suggest that autophosphorylation in the kinase insert region triggers the binding of the activated PDGF-R to specific cellular proteins, including a PI kinase whose activity is known to be stimulated by PDGF. Thus autophosphorylation may play a novel role in signal transduction via the PDGF-R."xsd:string
http://purl.uniprot.org/citations/2550144http://purl.org/dc/terms/identifier"doi:10.1016/0092-8674(89)90510-2"xsd:string
http://purl.uniprot.org/citations/2550144http://purl.org/dc/terms/identifier"doi:10.1016/0092-8674(89)90510-2"xsd:string
http://purl.uniprot.org/citations/2550144http://purl.uniprot.org/core/author"Cooper J.A."xsd:string
http://purl.uniprot.org/citations/2550144http://purl.uniprot.org/core/author"Cooper J.A."xsd:string
http://purl.uniprot.org/citations/2550144http://purl.uniprot.org/core/author"Kazlauskas A."xsd:string
http://purl.uniprot.org/citations/2550144http://purl.uniprot.org/core/author"Kazlauskas A."xsd:string
http://purl.uniprot.org/citations/2550144http://purl.uniprot.org/core/date"1989"xsd:gYear
http://purl.uniprot.org/citations/2550144http://purl.uniprot.org/core/date"1989"xsd:gYear
http://purl.uniprot.org/citations/2550144http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/2550144http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/2550144http://purl.uniprot.org/core/pages"1121-1133"xsd:string
http://purl.uniprot.org/citations/2550144http://purl.uniprot.org/core/pages"1121-1133"xsd:string
http://purl.uniprot.org/citations/2550144http://purl.uniprot.org/core/title"Autophosphorylation of the PDGF receptor in the kinase insert region regulates interactions with cell proteins."xsd:string
http://purl.uniprot.org/citations/2550144http://purl.uniprot.org/core/title"Autophosphorylation of the PDGF receptor in the kinase insert region regulates interactions with cell proteins."xsd:string
http://purl.uniprot.org/citations/2550144http://purl.uniprot.org/core/volume"58"xsd:string
http://purl.uniprot.org/citations/2550144http://purl.uniprot.org/core/volume"58"xsd:string
http://purl.uniprot.org/citations/2550144http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2550144
http://purl.uniprot.org/citations/2550144http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2550144
http://purl.uniprot.org/citations/2550144http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/2550144
http://purl.uniprot.org/citations/2550144http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/2550144
http://purl.uniprot.org/uniprot/P09619http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/2550144
http://purl.uniprot.org/uniprot/P09619#attribution-D7107EE65CA389B2B946C31C5265ADDFhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/2550144