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http://purl.uniprot.org/citations/9729467http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9729467http://www.w3.org/2000/01/rdf-schema#comment"The docking protein p130(cas) (Crk-associated substrate) forms a stable complex with the adaptor protein CrkII in a tyrosine-phosphorylation-dependent manner. Insulin-induced tyrosine phosphorylation of insulin receptor substrates results in the redistribution of CrkII between p130(cas) and insulin receptor substrate-1. A decrease in the association between CrkII and p130(cas) in response to insulin stimulation was detected in CHO cells stably expressing insulin receptor or insulin receptor substrate-1, and in L6 rat myoblasts. Along with the decrease in the association of CrkII with p130(cas), the amount of tyrosine-phosphorylated insulin receptor substrate-1 co-precipitated with CrkII increased in all cell types studied. The insulin-induced decrease in the CrkII-p130(cas) association was further confirmed by Far Western Blot analysis with the Src homology 2 (SH2) domain of CrkII. Insulin regulates the association of CrkII with p130(cas) by tyrosine dephosphorylation of p130(cas) and co-ordinated tyrosine phosphorylation of insulin receptor substrate-1. Tyrosine-phosphorylated insulin receptor substrate-1 serves as a docking protein for multiple adaptor proteins and competes with p130(cas) for CrkII."xsd:string
http://purl.uniprot.org/citations/9729467http://purl.org/dc/terms/identifier"doi:10.1042/bj3340595"xsd:string
http://purl.uniprot.org/citations/9729467http://purl.uniprot.org/core/author"Sorokin A."xsd:string
http://purl.uniprot.org/citations/9729467http://purl.uniprot.org/core/author"Reed E."xsd:string
http://purl.uniprot.org/citations/9729467http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9729467http://purl.uniprot.org/core/name"Biochem J"xsd:string
http://purl.uniprot.org/citations/9729467http://purl.uniprot.org/core/pages"595-600"xsd:string
http://purl.uniprot.org/citations/9729467http://purl.uniprot.org/core/title"Insulin stimulates the tyrosine dephosphorylation of docking protein p130cas (Crk-associated substrate), promoting the switch of the adaptor protein crk from p130cas to newly phosphorylated insulin receptor substrate-1."xsd:string
http://purl.uniprot.org/citations/9729467http://purl.uniprot.org/core/volume"334"xsd:string
http://purl.uniprot.org/citations/9729467http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9729467
http://purl.uniprot.org/citations/9729467http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9729467
http://purl.uniprot.org/uniprot/Q64010#attribution-28FF2A55DFF4861CDD562DDA27C0F3B8http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/9729467
http://purl.uniprot.org/uniprot/#_F7D232-mappedCitation-9729467http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9729467
http://purl.uniprot.org/uniprot/#_P35569-mappedCitation-9729467http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9729467
http://purl.uniprot.org/uniprot/#_Q3TXP6-mappedCitation-9729467http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9729467
http://purl.uniprot.org/uniprot/#_Q8BPE7-mappedCitation-9729467http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9729467
http://purl.uniprot.org/uniprot/#_Q5ND50-mappedCitation-9729467http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9729467
http://purl.uniprot.org/uniprot/#_Q5ND51-mappedCitation-9729467http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9729467
http://purl.uniprot.org/uniprot/#_P81122-mappedCitation-9729467http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9729467
http://purl.uniprot.org/uniprot/#_Q3TJB5-mappedCitation-9729467http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9729467
http://purl.uniprot.org/uniprot/#_Q3TJP4-mappedCitation-9729467http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9729467
http://purl.uniprot.org/uniprot/#_Q3TQV3-mappedCitation-9729467http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9729467
http://purl.uniprot.org/uniprot/#_Q3TIT7-mappedCitation-9729467http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9729467
http://purl.uniprot.org/uniprot/#_Q3TLY3-mappedCitation-9729467http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9729467