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http://purl.uniprot.org/citations/17870073http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17870073http://www.w3.org/2000/01/rdf-schema#comment"The inhibition of hepatic glycogen-associated protein phosphatase-1 (PP1-G(L)) by glycogen phosphorylase a prevents the dephosphorylation and activation of glycogen synthase, suppressing glycogen synthesis when glycogenolysis is activated. Here, we show that a peptide ((280)LGPYY(284)) comprising the last five amino acids of G(L) retains high-affinity interaction with phosphorylase a and that the two tyrosines play crucial roles. Tyr284 deletion abolishes binding of phosphorylase a to G(L) and replacement by phenylalanine is insufficient to restore high-affinity binding. We show that a phosphorylase inhibitor blocks the interaction of phosphorylase a with the G(L) C-terminus, suggesting that the latter interaction could be targeted to develop an anti-diabetic drug."xsd:string
http://purl.uniprot.org/citations/17870073http://purl.org/dc/terms/identifier"doi:10.1016/j.febslet.2007.08.073"xsd:string
http://purl.uniprot.org/citations/17870073http://purl.uniprot.org/core/author"Munro S."xsd:string
http://purl.uniprot.org/citations/17870073http://purl.uniprot.org/core/author"Hallyburton I."xsd:string
http://purl.uniprot.org/citations/17870073http://purl.uniprot.org/core/author"Kelsall I.R."xsd:string
http://purl.uniprot.org/citations/17870073http://purl.uniprot.org/core/author"Cohen P.T."xsd:string
http://purl.uniprot.org/citations/17870073http://purl.uniprot.org/core/author"Treadway J.L."xsd:string
http://purl.uniprot.org/citations/17870073http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17870073http://purl.uniprot.org/core/name"FEBS Lett"xsd:string
http://purl.uniprot.org/citations/17870073http://purl.uniprot.org/core/pages"4749-4753"xsd:string
http://purl.uniprot.org/citations/17870073http://purl.uniprot.org/core/title"The hepatic PP1 glycogen-targeting subunit interaction with phosphorylase a can be blocked by C-terminal tyrosine deletion or an indole drug."xsd:string
http://purl.uniprot.org/citations/17870073http://purl.uniprot.org/core/volume"581"xsd:string
http://purl.uniprot.org/citations/17870073http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17870073
http://purl.uniprot.org/citations/17870073http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17870073
http://purl.uniprot.org/uniprot/#_P00489-mappedCitation-17870073http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17870073
http://purl.uniprot.org/uniprot/#_Q00756-mappedCitation-17870073http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17870073
http://purl.uniprot.org/uniprot/P00489http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17870073
http://purl.uniprot.org/uniprot/Q00756http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17870073