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http://purl.uniprot.org/citations/17055998http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17055998http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17055998http://www.w3.org/2000/01/rdf-schema#comment"Glycogen synthase plays a key role in regulating glycogen metabolism. In a search for regulators of glycogen synthase, a yeast two-hybrid study was performed. Two glycogen synthase-interacting proteins were identified in human skeletal muscle, glycogenin-1, and nebulin. The interaction with glycogenin was found to be mediated by the region of glycogenin which contains the 33 COOH-terminal amino acid residues. The regions in glycogen synthase containing both NH2- and COOH-terminal phosphorylation sites are not involved in the interaction. The core segment of glycogen synthase from Glu21 to Gly503 does not bind COOH-terminal fragment of glycogenin. However, this region of glycogen synthase binds full-length glycogenin indicating that glycogenin contains at least one additional interacting site for glycogen synthase besides the COOH-terminus. We demonstrate that the COOH-terminal fragment of glycogenin can be used as an effective high affinity reagent for the purification of glycogen synthase from skeletal muscle and liver."xsd:string
http://purl.uniprot.org/citations/17055998http://purl.org/dc/terms/identifier"doi:10.1016/j.abb.2006.09.024"xsd:string
http://purl.uniprot.org/citations/17055998http://purl.org/dc/terms/identifier"doi:10.1016/j.abb.2006.09.024"xsd:string
http://purl.uniprot.org/citations/17055998http://purl.uniprot.org/core/author"Roach P.J."xsd:string
http://purl.uniprot.org/citations/17055998http://purl.uniprot.org/core/author"Roach P.J."xsd:string
http://purl.uniprot.org/citations/17055998http://purl.uniprot.org/core/author"Dietrich A.D."xsd:string
http://purl.uniprot.org/citations/17055998http://purl.uniprot.org/core/author"Dietrich A.D."xsd:string
http://purl.uniprot.org/citations/17055998http://purl.uniprot.org/core/author"Skurat A.V."xsd:string
http://purl.uniprot.org/citations/17055998http://purl.uniprot.org/core/author"Skurat A.V."xsd:string
http://purl.uniprot.org/citations/17055998http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17055998http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17055998http://purl.uniprot.org/core/name"Arch. Biochem. Biophys."xsd:string
http://purl.uniprot.org/citations/17055998http://purl.uniprot.org/core/name"Arch. Biochem. Biophys."xsd:string
http://purl.uniprot.org/citations/17055998http://purl.uniprot.org/core/pages"93-97"xsd:string
http://purl.uniprot.org/citations/17055998http://purl.uniprot.org/core/pages"93-97"xsd:string
http://purl.uniprot.org/citations/17055998http://purl.uniprot.org/core/title"Interaction between glycogenin and glycogen synthase."xsd:string
http://purl.uniprot.org/citations/17055998http://purl.uniprot.org/core/title"Interaction between glycogenin and glycogen synthase."xsd:string
http://purl.uniprot.org/citations/17055998http://purl.uniprot.org/core/volume"456"xsd:string
http://purl.uniprot.org/citations/17055998http://purl.uniprot.org/core/volume"456"xsd:string
http://purl.uniprot.org/citations/17055998http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17055998
http://purl.uniprot.org/citations/17055998http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17055998
http://purl.uniprot.org/citations/17055998http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17055998
http://purl.uniprot.org/citations/17055998http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17055998