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http://purl.uniprot.org/citations/10318824http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10318824http://www.w3.org/2000/01/rdf-schema#comment"To understand the mechanism of how Axin acts as an inhibitory molecule in the Wnt pathway, we generated a series of mutated forms of Axin. From the binding experiments, we defined the domains of Axin that bind glycogen synthase kinase-3beta (GSK-3beta) and beta-catenin. We also examined the ability of each Axin mutant to inhibit lymphoid enhancer factor-1 (Lef-1) reporter activity in a cell line expressing high levels of beta-catenin. Axin mutants that did not bind GSK-3beta or beta-catenin were ineffective in suppressing Lef-1 reporter activity. Binding GSK-3beta and beta-catenin was not sufficient for this inhibitory effect of Axin. Axin mutants with C-terminal truncations lacked the ability to inhibit Lef-1 reporter activity, even though they bound GSK-3beta and beta-catenin. The C-terminal region was required for binding to Axin itself. Substitution of the C-terminal region with an unrelated dimerizing molecule, the retinoid X receptor restored its inhibitory effect on Lef-1-dependent transcription. The oligomerization of Axin through its C terminus is important for its function in regulation of beta-catenin-mediated response."xsd:string
http://purl.uniprot.org/citations/10318824http://purl.org/dc/terms/identifier"doi:10.1074/jbc.274.20.14090"xsd:string
http://purl.uniprot.org/citations/10318824http://purl.uniprot.org/core/author"Sakanaka C."xsd:string
http://purl.uniprot.org/citations/10318824http://purl.uniprot.org/core/author"Williams L.T."xsd:string
http://purl.uniprot.org/citations/10318824http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10318824http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/10318824http://purl.uniprot.org/core/pages"14090-14093"xsd:string
http://purl.uniprot.org/citations/10318824http://purl.uniprot.org/core/title"Functional domains of axin. Importance of the C terminus as an oligomerization domain."xsd:string
http://purl.uniprot.org/citations/10318824http://purl.uniprot.org/core/volume"274"xsd:string
http://purl.uniprot.org/citations/10318824http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10318824
http://purl.uniprot.org/citations/10318824http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10318824
http://purl.uniprot.org/uniprot/O35625#attribution-443867C99F0711548E605574E4B30889http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/10318824
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http://purl.uniprot.org/uniprot/Q02248#attribution-7E83886D1EA9A15F5DE847DD8049CC97http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/10318824
http://purl.uniprot.org/uniprot/Q9WV60#attribution-7E83886D1EA9A15F5DE847DD8049CC97http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/10318824
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http://purl.uniprot.org/uniprot/#_A0A338P6P8-mappedCitation-10318824http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/10318824
http://purl.uniprot.org/uniprot/#_F7CRC6-mappedCitation-10318824http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/10318824
http://purl.uniprot.org/uniprot/#_E9QMJ8-mappedCitation-10318824http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/10318824
http://purl.uniprot.org/uniprot/#_F6XWC2-mappedCitation-10318824http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/10318824
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http://purl.uniprot.org/uniprot/#_F7BAC9-mappedCitation-10318824http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/10318824