http://purl.uniprot.org/citations/12408824 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/12408824 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/12408824 | http://www.w3.org/2000/01/rdf-schema#comment | "Beta-catenin is a multifunctional protein involved in both cell adhesion and transcriptional activation. Transcription mediated by the beta-catenin/Tcf complex is involved in embryological development and is upregulated in various cancers. We have determined the crystal structure at 2.5 A resolution of a complex between beta-catenin and ICAT, a protein that prevents the interaction between beta-catenin and Tcf/Lef family transcription factors. ICAT contains a 3-helix bundle that binds armadillo repeats 10-12 and a C-terminal tail that, similar to Tcf and E-cadherin, binds in the groove formed by armadillo repeats 5-9 of beta-catenin. We show that ICAT selectively inhibits beta-catenin/Tcf binding in vivo, without disrupting beta-catenin/cadherin interactions. Thus, it should be possible to design cancer therapeutics that inhibit beta-catenin-mediated transcriptional activation without interfering with cell adhesion."xsd:string |
http://purl.uniprot.org/citations/12408824 | http://purl.org/dc/terms/identifier | "doi:10.1016/s1097-2765(02)00637-8"xsd:string |
http://purl.uniprot.org/citations/12408824 | http://purl.org/dc/terms/identifier | "doi:10.1016/s1097-2765(02)00637-8"xsd:string |
http://purl.uniprot.org/citations/12408824 | http://purl.uniprot.org/core/author | "Xu W."xsd:string |
http://purl.uniprot.org/citations/12408824 | http://purl.uniprot.org/core/author | "Xu W."xsd:string |
http://purl.uniprot.org/citations/12408824 | http://purl.uniprot.org/core/author | "Kimelman D."xsd:string |
http://purl.uniprot.org/citations/12408824 | http://purl.uniprot.org/core/author | "Kimelman D."xsd:string |
http://purl.uniprot.org/citations/12408824 | http://purl.uniprot.org/core/author | "Clements W.K."xsd:string |
http://purl.uniprot.org/citations/12408824 | http://purl.uniprot.org/core/author | "Clements W.K."xsd:string |
http://purl.uniprot.org/citations/12408824 | http://purl.uniprot.org/core/author | "Graham T.A."xsd:string |
http://purl.uniprot.org/citations/12408824 | http://purl.uniprot.org/core/author | "Graham T.A."xsd:string |
http://purl.uniprot.org/citations/12408824 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
http://purl.uniprot.org/citations/12408824 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
http://purl.uniprot.org/citations/12408824 | http://purl.uniprot.org/core/name | "Mol. Cell"xsd:string |
http://purl.uniprot.org/citations/12408824 | http://purl.uniprot.org/core/name | "Mol. Cell"xsd:string |
http://purl.uniprot.org/citations/12408824 | http://purl.uniprot.org/core/pages | "563-571"xsd:string |
http://purl.uniprot.org/citations/12408824 | http://purl.uniprot.org/core/pages | "563-571"xsd:string |
http://purl.uniprot.org/citations/12408824 | http://purl.uniprot.org/core/title | "The crystal structure of the beta-catenin/ICAT complex reveals the inhibitory mechanism of ICAT."xsd:string |
http://purl.uniprot.org/citations/12408824 | http://purl.uniprot.org/core/title | "The crystal structure of the beta-catenin/ICAT complex reveals the inhibitory mechanism of ICAT."xsd:string |
http://purl.uniprot.org/citations/12408824 | http://purl.uniprot.org/core/volume | "10"xsd:string |
http://purl.uniprot.org/citations/12408824 | http://purl.uniprot.org/core/volume | "10"xsd:string |
http://purl.uniprot.org/citations/12408824 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12408824 |
http://purl.uniprot.org/citations/12408824 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12408824 |