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http://purl.uniprot.org/citations/7516330http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7516330http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7516330http://www.w3.org/2000/01/rdf-schema#comment"Binding of fibroblast growth factor (FGF) to the fibroblast growth factor receptor leads to autophosphorylation of the receptor on several tyrosine residues. Wild-type FGF receptor 1 (flg) and a mutated receptor (Y766F), in which an autophosphorylation site (Tyr-766) was mutated to phenylalanine, were expressed in rat myoblasts and in hematopoietic Ba/F3 cells. It was found that the point mutation at Tyr-766 resulted in a decrease in FGF receptor internalization, as well as a reduction in both ligand-induced FGF receptor down-regulation and degradation. It has been shown previously that phosphorylation of Tyr-766 is essential for interaction with phospholipase C gamma and that the Y766F FGF receptor mutant is unable to stimulate phosphatidylinositol hydrolysis and Ca2+ release from internal stores. The results presented in this report indicate that Tyr-766 is also essential for cellular trafficking of FGF receptor."xsd:string
http://purl.uniprot.org/citations/7516330http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(17)32519-x"xsd:string
http://purl.uniprot.org/citations/7516330http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(17)32519-x"xsd:string
http://purl.uniprot.org/citations/7516330http://purl.uniprot.org/core/author"Huang J."xsd:string
http://purl.uniprot.org/citations/7516330http://purl.uniprot.org/core/author"Huang J."xsd:string
http://purl.uniprot.org/citations/7516330http://purl.uniprot.org/core/author"Sorokin A."xsd:string
http://purl.uniprot.org/citations/7516330http://purl.uniprot.org/core/author"Sorokin A."xsd:string
http://purl.uniprot.org/citations/7516330http://purl.uniprot.org/core/author"Schlessinger J."xsd:string
http://purl.uniprot.org/citations/7516330http://purl.uniprot.org/core/author"Schlessinger J."xsd:string
http://purl.uniprot.org/citations/7516330http://purl.uniprot.org/core/author"Mohammadi M."xsd:string
http://purl.uniprot.org/citations/7516330http://purl.uniprot.org/core/author"Mohammadi M."xsd:string
http://purl.uniprot.org/citations/7516330http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/7516330http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/7516330http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/7516330http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/7516330http://purl.uniprot.org/core/pages"17056-17061"xsd:string
http://purl.uniprot.org/citations/7516330http://purl.uniprot.org/core/pages"17056-17061"xsd:string
http://purl.uniprot.org/citations/7516330http://purl.uniprot.org/core/title"Internalization of fibroblast growth factor receptor is inhibited by a point mutation at tyrosine 766."xsd:string
http://purl.uniprot.org/citations/7516330http://purl.uniprot.org/core/title"Internalization of fibroblast growth factor receptor is inhibited by a point mutation at tyrosine 766."xsd:string
http://purl.uniprot.org/citations/7516330http://purl.uniprot.org/core/volume"269"xsd:string
http://purl.uniprot.org/citations/7516330http://purl.uniprot.org/core/volume"269"xsd:string
http://purl.uniprot.org/citations/7516330http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7516330
http://purl.uniprot.org/citations/7516330http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7516330