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http://purl.uniprot.org/citations/12408825http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12408825http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12408825http://www.w3.org/2000/01/rdf-schema#comment"In the canonical Wnt signaling pathway, beta-catenin activates target genes through its interactions with Tcf/Lef-family transcription factors and additional transcriptional coactivators. The crystal structure of ICAT, an inhibitor of beta-catenin-mediated transcription, bound to the armadillo repeat domain of beta-catenin, has been determined. ICAT contains an N-terminal helilical domain that binds to repeats 11 and 12 of beta-catenin, and an extended C-terminal region that binds to repeats 5-10 in a manner similar to that of Tcfs and other beta-catenin ligands. Full-length ICAT dissociates complexes of beta-catenin, Lef-1, and the transcriptional coactivator p300, whereas the helical domain alone selectively blocks binding to p300. The C-terminal armadillo repeats of beta-catenin may be an attractive target for compounds designed to disrupt aberrant beta-catenin-mediated transcription associated with various cancers."xsd:string
http://purl.uniprot.org/citations/12408825http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(02)00631-7"xsd:string
http://purl.uniprot.org/citations/12408825http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(02)00631-7"xsd:string
http://purl.uniprot.org/citations/12408825http://purl.uniprot.org/core/author"Daniels D.L."xsd:string
http://purl.uniprot.org/citations/12408825http://purl.uniprot.org/core/author"Daniels D.L."xsd:string
http://purl.uniprot.org/citations/12408825http://purl.uniprot.org/core/author"Weis W.I."xsd:string
http://purl.uniprot.org/citations/12408825http://purl.uniprot.org/core/author"Weis W.I."xsd:string
http://purl.uniprot.org/citations/12408825http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12408825http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12408825http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/12408825http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/12408825http://purl.uniprot.org/core/pages"573-584"xsd:string
http://purl.uniprot.org/citations/12408825http://purl.uniprot.org/core/pages"573-584"xsd:string
http://purl.uniprot.org/citations/12408825http://purl.uniprot.org/core/title"ICAT inhibits beta-catenin binding to Tcf/Lef-family transcription factors and the general coactivator p300 using independent structural modules."xsd:string
http://purl.uniprot.org/citations/12408825http://purl.uniprot.org/core/title"ICAT inhibits beta-catenin binding to Tcf/Lef-family transcription factors and the general coactivator p300 using independent structural modules."xsd:string
http://purl.uniprot.org/citations/12408825http://purl.uniprot.org/core/volume"10"xsd:string
http://purl.uniprot.org/citations/12408825http://purl.uniprot.org/core/volume"10"xsd:string
http://purl.uniprot.org/citations/12408825http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12408825
http://purl.uniprot.org/citations/12408825http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12408825
http://purl.uniprot.org/citations/12408825http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12408825
http://purl.uniprot.org/citations/12408825http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12408825
http://purl.uniprot.org/uniprot/Q02248http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/12408825
http://purl.uniprot.org/uniprot/Q9NSA3http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/12408825