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http://purl.uniprot.org/citations/12456653http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12456653http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12456653http://www.w3.org/2000/01/rdf-schema#comment"Assembly of intracellular macromolecular complexes is thought to provide an important mechanism to coordinate the generation of second messengers upon receptor activation. We have previously identified a B cell linker protein, termed BLNK, which serves such a scaffolding function in B cells. We demonstrate here that phosphorylation of five tyrosine residues within human BLNK nucleates distinct signaling effectors following B cell antigen receptor activation. The phosphorylation of multiple tyrosine residues not only amplifies PLCgamma-mediated signaling but also supports 'cis'-mediated interaction between distinct signaling effectors within a large molecular complex. These data demonstrate the importance of coordinate phosphorylation of molecular scaffolds, and provide insights into how assembly of macromolecular complexes is required for normal receptor function."xsd:string
http://purl.uniprot.org/citations/12456653http://purl.org/dc/terms/identifier"doi:10.1093/emboj/cdf658"xsd:string
http://purl.uniprot.org/citations/12456653http://purl.org/dc/terms/identifier"doi:10.1093/emboj/cdf658"xsd:string
http://purl.uniprot.org/citations/12456653http://purl.uniprot.org/core/author"Kurosaki T."xsd:string
http://purl.uniprot.org/citations/12456653http://purl.uniprot.org/core/author"Kurosaki T."xsd:string
http://purl.uniprot.org/citations/12456653http://purl.uniprot.org/core/author"Dalton M."xsd:string
http://purl.uniprot.org/citations/12456653http://purl.uniprot.org/core/author"Dalton M."xsd:string
http://purl.uniprot.org/citations/12456653http://purl.uniprot.org/core/author"Chan A.C."xsd:string
http://purl.uniprot.org/citations/12456653http://purl.uniprot.org/core/author"Chan A.C."xsd:string
http://purl.uniprot.org/citations/12456653http://purl.uniprot.org/core/author"Chiu C.W."xsd:string
http://purl.uniprot.org/citations/12456653http://purl.uniprot.org/core/author"Chiu C.W."xsd:string
http://purl.uniprot.org/citations/12456653http://purl.uniprot.org/core/author"Ishiai M."xsd:string
http://purl.uniprot.org/citations/12456653http://purl.uniprot.org/core/author"Ishiai M."xsd:string
http://purl.uniprot.org/citations/12456653http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12456653http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12456653http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/12456653http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/12456653http://purl.uniprot.org/core/pages"6461-6472"xsd:string
http://purl.uniprot.org/citations/12456653http://purl.uniprot.org/core/pages"6461-6472"xsd:string
http://purl.uniprot.org/citations/12456653http://purl.uniprot.org/core/title"BLNK: molecular scaffolding through 'cis'-mediated organization of signaling proteins."xsd:string
http://purl.uniprot.org/citations/12456653http://purl.uniprot.org/core/title"BLNK: molecular scaffolding through 'cis'-mediated organization of signaling proteins."xsd:string
http://purl.uniprot.org/citations/12456653http://purl.uniprot.org/core/volume"21"xsd:string
http://purl.uniprot.org/citations/12456653http://purl.uniprot.org/core/volume"21"xsd:string