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http://purl.uniprot.org/citations/9373175http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9373175http://www.w3.org/2000/01/rdf-schema#comment"293 cells were transfected with wild-type GSK3beta (WT-GSK3beta) or a mutant in which the PKB phosphorylation site (Ser-9) was altered to Ala (A9-GSK3beta). Upon stimulation with IGF-1 or insulin, WT-GSK3beta was inhibited 75% or 60%, respectively, whereas the activity of the A9-GSK3beta mutant was unaffected. Incubation of WT-GSK3beta with PP2A1 (a Ser/Thr-specific phosphatase) completely reversed the IGF-1- or insulin-induced inhibition. IGF-1 stimulation did not induce any tyrosine dephosphorylation of WT-GSK3beta or A9-GSK3beta. Coexpression of WT-GSK3beta in 293 cells with either PKB alpha (also known as AKT) or PDK1 (the 'upstream' activator of PKB) mimicked the IGF-1- or insulin-induced phosphorylation of Ser-9 and inactivation of GSK3beta."xsd:string
http://purl.uniprot.org/citations/9373175http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(97)01235-0"xsd:string
http://purl.uniprot.org/citations/9373175http://purl.uniprot.org/core/author"Alessi D.R."xsd:string
http://purl.uniprot.org/citations/9373175http://purl.uniprot.org/core/author"Shaw M."xsd:string
http://purl.uniprot.org/citations/9373175http://purl.uniprot.org/core/author"Cohen P."xsd:string
http://purl.uniprot.org/citations/9373175http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9373175http://purl.uniprot.org/core/name"FEBS Lett"xsd:string
http://purl.uniprot.org/citations/9373175http://purl.uniprot.org/core/pages"307-311"xsd:string
http://purl.uniprot.org/citations/9373175http://purl.uniprot.org/core/title"Further evidence that the inhibition of glycogen synthase kinase-3beta by IGF-1 is mediated by PDK1/PKB-induced phosphorylation of Ser-9 and not by dephosphorylation of Tyr-216."xsd:string
http://purl.uniprot.org/citations/9373175http://purl.uniprot.org/core/volume"416"xsd:string
http://purl.uniprot.org/citations/9373175http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9373175
http://purl.uniprot.org/citations/9373175http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9373175
http://purl.uniprot.org/uniprot/P31749#attribution-80B6A043197D546865CFF6EB4979346Ahttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/9373175
http://purl.uniprot.org/uniprot/O15530#attribution-20BAF4424E42942BFFE94D6703727152http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/9373175
http://purl.uniprot.org/uniprot/#_P49841-mappedCitation-9373175http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9373175
http://purl.uniprot.org/uniprot/P49841http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/9373175