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http://purl.uniprot.org/citations/7538118http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7538118http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7538118http://www.w3.org/2000/01/rdf-schema#comment"Syk is a cytoplasmic protein-tyrosine kinase containing two amino-terminal Src homology 2 domains that is activated following ligation of the B cell antigen receptor. Syk activation in B cells correlates with Syk tyrosine phosphorylation as well as with Syk SH2-mediated association with the tyrosine-phosphorylated Ig alpha and Ig beta B cell antigen receptor subunits. Tyrosine-phosphorylated peptide 20-mers representing Ig alpha and Ig beta immunoreceptor tyrosine activation motifs were synthesized and found to stimulate the specific activity of Syk by as much as 10-fold in vitro. Maximal phosphopeptide-induced Syk activation required both Syk SH2 domains and phosphorylation of both tyrosine residues present in the immunoreceptor tyrosine activation motif. The biochemical mechanism responsible for the phosphopeptide-induced Syk enzyme activation appears to be a function of Syk autophosphorylation. Our observations suggest the association of Syk tandem SH2 domains with the tyrosine-phosphorylated Ig alpha and/or Ig beta immunoreceptor tyrosine activation motifs in B cells stimulates Syk autophosphorylation leading to Syk enzyme activation."xsd:string
http://purl.uniprot.org/citations/7538118http://purl.org/dc/terms/identifier"doi:10.1074/jbc.270.19.11590"xsd:string
http://purl.uniprot.org/citations/7538118http://purl.org/dc/terms/identifier"doi:10.1074/jbc.270.19.11590"xsd:string
http://purl.uniprot.org/citations/7538118http://purl.uniprot.org/core/author"Bolen J.B."xsd:string
http://purl.uniprot.org/citations/7538118http://purl.uniprot.org/core/author"Bolen J.B."xsd:string
http://purl.uniprot.org/citations/7538118http://purl.uniprot.org/core/author"Burkhardt A.L."xsd:string
http://purl.uniprot.org/citations/7538118http://purl.uniprot.org/core/author"Burkhardt A.L."xsd:string
http://purl.uniprot.org/citations/7538118http://purl.uniprot.org/core/author"Rowley R.B."xsd:string
http://purl.uniprot.org/citations/7538118http://purl.uniprot.org/core/author"Rowley R.B."xsd:string
http://purl.uniprot.org/citations/7538118http://purl.uniprot.org/core/author"Chao H.-G."xsd:string
http://purl.uniprot.org/citations/7538118http://purl.uniprot.org/core/author"Chao H.-G."xsd:string
http://purl.uniprot.org/citations/7538118http://purl.uniprot.org/core/author"Matsueda G.R."xsd:string
http://purl.uniprot.org/citations/7538118http://purl.uniprot.org/core/author"Matsueda G.R."xsd:string
http://purl.uniprot.org/citations/7538118http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7538118http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7538118http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/7538118http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/7538118http://purl.uniprot.org/core/pages"11590-11594"xsd:string
http://purl.uniprot.org/citations/7538118http://purl.uniprot.org/core/pages"11590-11594"xsd:string
http://purl.uniprot.org/citations/7538118http://purl.uniprot.org/core/title"Syk protein-tyrosine kinase is regulated by tyrosine-phosphorylated Ig alpha/Ig beta immunoreceptor tyrosine activation motif binding and autophosphorylation."xsd:string
http://purl.uniprot.org/citations/7538118http://purl.uniprot.org/core/title"Syk protein-tyrosine kinase is regulated by tyrosine-phosphorylated Ig alpha/Ig beta immunoreceptor tyrosine activation motif binding and autophosphorylation."xsd:string
http://purl.uniprot.org/citations/7538118http://purl.uniprot.org/core/volume"270"xsd:string
http://purl.uniprot.org/citations/7538118http://purl.uniprot.org/core/volume"270"xsd:string