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http://purl.uniprot.org/citations/10811618http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10811618http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10811618http://www.w3.org/2000/01/rdf-schema#comment"Axin and the adenomatous polyposis coli (APC) tumor suppressor protein are components of the Wnt/Wingless growth factor signaling pathway. In the absence of Wnt signal, Axin and APC regulate cytoplasmic levels of the proto-oncogene beta-catenin through the formation of a large complex containing these three proteins, glycogen synthase kinase 3beta (GSK3beta) and several other proteins. Both Axin and APC are known to be critical for beta-catenin regulation, and truncations in APC that eliminate the Axin-binding site result in human cancers. A protease-resistant domain of Axin that contains the APC-binding site is a member of the regulators of G-protein signaling (RGS) superfamily. The crystal structures of this domain alone and in complex with an Axin-binding sequence from APC reveal that the Axin-APC interaction occurs at a conserved groove on a face of the protein that is distinct from the G-protein interface of classical RGS proteins. The molecular interactions observed in the Axin-APC complex provide a rationale for the evolutionary conservation seen in both proteins."xsd:string
http://purl.uniprot.org/citations/10811618http://purl.org/dc/terms/identifier"doi:10.1093/emboj/19.10.2270"xsd:string
http://purl.uniprot.org/citations/10811618http://purl.org/dc/terms/identifier"doi:10.1093/emboj/19.10.2270"xsd:string
http://purl.uniprot.org/citations/10811618http://purl.uniprot.org/core/author"Weis W.I."xsd:string
http://purl.uniprot.org/citations/10811618http://purl.uniprot.org/core/author"Weis W.I."xsd:string
http://purl.uniprot.org/citations/10811618http://purl.uniprot.org/core/author"Polakis P."xsd:string
http://purl.uniprot.org/citations/10811618http://purl.uniprot.org/core/author"Polakis P."xsd:string
http://purl.uniprot.org/citations/10811618http://purl.uniprot.org/core/author"Spink K.E."xsd:string
http://purl.uniprot.org/citations/10811618http://purl.uniprot.org/core/author"Spink K.E."xsd:string
http://purl.uniprot.org/citations/10811618http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10811618http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10811618http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/10811618http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/10811618http://purl.uniprot.org/core/pages"2270-2279"xsd:string
http://purl.uniprot.org/citations/10811618http://purl.uniprot.org/core/pages"2270-2279"xsd:string
http://purl.uniprot.org/citations/10811618http://purl.uniprot.org/core/title"Structural basis of the axin-adenomatous polyposis coli interaction."xsd:string
http://purl.uniprot.org/citations/10811618http://purl.uniprot.org/core/title"Structural basis of the axin-adenomatous polyposis coli interaction."xsd:string
http://purl.uniprot.org/citations/10811618http://purl.uniprot.org/core/volume"19"xsd:string
http://purl.uniprot.org/citations/10811618http://purl.uniprot.org/core/volume"19"xsd:string
http://purl.uniprot.org/citations/10811618http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10811618
http://purl.uniprot.org/citations/10811618http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10811618
http://purl.uniprot.org/citations/10811618http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10811618
http://purl.uniprot.org/citations/10811618http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10811618