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http://purl.uniprot.org/citations/16507368http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16507368http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16507368http://www.w3.org/2000/01/rdf-schema#comment"Tyrosine phosphorylation of cellular proteins induced by extracellular cues serves as a critical mediator in the control of a great variety of cellular processes. Here, we describe an integrated experimental approach including rapid quench methodology and ESI-LC-MS/MS as well as time-resolved ESI-MS to demonstrate that tyrosine autophosphorylation of the catalytic tyrosine kinase domain of FGF-receptor-1 (FGFR1) is mediated by a sequential and precisely ordered reaction. We also demonstrate that the rate of catalysis of two FGFR substrates is enhanced by 50-to 100-fold after autophosphorylation of Y653 in the activation loop, whereas autophosphorylation of the second site in the activation loop (Y654) results in 500-to 1,000-fold increase in the rate of substrate phosphorylation. We propose that FGFR1 is activated by a two-step mechanism mediated by strictly ordered and regulated autophosphorylation, suggesting that distinct phosphorylation states may provide both temporal and spatial resolution to receptor signaling."xsd:string
http://purl.uniprot.org/citations/16507368http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2006.01.022"xsd:string
http://purl.uniprot.org/citations/16507368http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2006.01.022"xsd:string
http://purl.uniprot.org/citations/16507368http://purl.uniprot.org/core/author"Anderson K.S."xsd:string
http://purl.uniprot.org/citations/16507368http://purl.uniprot.org/core/author"Anderson K.S."xsd:string
http://purl.uniprot.org/citations/16507368http://purl.uniprot.org/core/author"Furdui C.M."xsd:string
http://purl.uniprot.org/citations/16507368http://purl.uniprot.org/core/author"Furdui C.M."xsd:string
http://purl.uniprot.org/citations/16507368http://purl.uniprot.org/core/author"Schlessinger J."xsd:string
http://purl.uniprot.org/citations/16507368http://purl.uniprot.org/core/author"Schlessinger J."xsd:string
http://purl.uniprot.org/citations/16507368http://purl.uniprot.org/core/author"Lew E.D."xsd:string
http://purl.uniprot.org/citations/16507368http://purl.uniprot.org/core/author"Lew E.D."xsd:string
http://purl.uniprot.org/citations/16507368http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16507368http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16507368http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/16507368http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/16507368http://purl.uniprot.org/core/pages"711-717"xsd:string
http://purl.uniprot.org/citations/16507368http://purl.uniprot.org/core/pages"711-717"xsd:string
http://purl.uniprot.org/citations/16507368http://purl.uniprot.org/core/title"Autophosphorylation of FGFR1 kinase is mediated by a sequential and precisely ordered reaction."xsd:string
http://purl.uniprot.org/citations/16507368http://purl.uniprot.org/core/title"Autophosphorylation of FGFR1 kinase is mediated by a sequential and precisely ordered reaction."xsd:string
http://purl.uniprot.org/citations/16507368http://purl.uniprot.org/core/volume"21"xsd:string
http://purl.uniprot.org/citations/16507368http://purl.uniprot.org/core/volume"21"xsd:string
http://purl.uniprot.org/citations/16507368http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16507368
http://purl.uniprot.org/citations/16507368http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16507368