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http://purl.uniprot.org/citations/11551227http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11551227http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11551227http://www.w3.org/2000/01/rdf-schema#comment"Syntrophins have been proposed to serve as adapter proteins. Syntrophins are found in the dystrophin glycoprotein complex (DGC); defects in the constituents of this complex are linked to various muscular dystrophies. Blot overlay experiments demonstrate that alpha-dystroglycan, beta-dystroglycan, and syntrophins all bind Grb2, the growth factor receptor bound adapter protein. Mouse alpha1-syntrophin sequences were produced as chimeric fusion proteins in bacteria and found to also bind Grb2 in a Ca2+-independent manner. This binding was localized to the proline rich sequences adjacent to and overlapping with the N-terminal pleckstrin homology domain (PH1). Grb2 bound syntrophin with an apparent KD of 563 +/-15 nM. Grb2-C-SH3 domain bound syntrophin with slightly higher affinity than Grb2-N-SH3 domain. Crk-L, an SH2/SH3 protein of similar domain structure but different specificity, does not bind these syntrophin sequences."xsd:string
http://purl.uniprot.org/citations/11551227http://purl.org/dc/terms/identifier"doi:10.1021/bi010490n"xsd:string
http://purl.uniprot.org/citations/11551227http://purl.org/dc/terms/identifier"doi:10.1021/bi010490n"xsd:string
http://purl.uniprot.org/citations/11551227http://purl.uniprot.org/core/author"Petrucci T.C."xsd:string
http://purl.uniprot.org/citations/11551227http://purl.uniprot.org/core/author"Petrucci T.C."xsd:string
http://purl.uniprot.org/citations/11551227http://purl.uniprot.org/core/author"Jarrett H.W."xsd:string
http://purl.uniprot.org/citations/11551227http://purl.uniprot.org/core/author"Jarrett H.W."xsd:string
http://purl.uniprot.org/citations/11551227http://purl.uniprot.org/core/author"Oak S.A."xsd:string
http://purl.uniprot.org/citations/11551227http://purl.uniprot.org/core/author"Oak S.A."xsd:string
http://purl.uniprot.org/citations/11551227http://purl.uniprot.org/core/author"Russo K."xsd:string
http://purl.uniprot.org/citations/11551227http://purl.uniprot.org/core/author"Russo K."xsd:string
http://purl.uniprot.org/citations/11551227http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11551227http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11551227http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/11551227http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/11551227http://purl.uniprot.org/core/pages"11270-11278"xsd:string
http://purl.uniprot.org/citations/11551227http://purl.uniprot.org/core/pages"11270-11278"xsd:string
http://purl.uniprot.org/citations/11551227http://purl.uniprot.org/core/title"Mouse alpha1-syntrophin binding to Grb2: further evidence of a role for syntrophin in cell signaling."xsd:string
http://purl.uniprot.org/citations/11551227http://purl.uniprot.org/core/title"Mouse alpha1-syntrophin binding to Grb2: further evidence of a role for syntrophin in cell signaling."xsd:string
http://purl.uniprot.org/citations/11551227http://purl.uniprot.org/core/volume"40"xsd:string
http://purl.uniprot.org/citations/11551227http://purl.uniprot.org/core/volume"40"xsd:string
http://purl.uniprot.org/citations/11551227http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11551227
http://purl.uniprot.org/citations/11551227http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11551227