| http://purl.uniprot.org/citations/10862053 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10862053 | http://www.w3.org/2000/01/rdf-schema#comment | "Axin is a recently discovered component of a multiprotein complex containing APC, beta-catenin, GSK3, and PP2A, which functions in the degradation of the beta-catenin protein. As part of WNT signal transduction, the function of the Axin complex is inhibited, leading to the accumulation of beta-catenin. The inappropriate stabilization of beta-catenin has been implicated in a range of human tumors. Two oncogenic mechanisms leading to beta-catenin stabilization are the loss of the APC tumor suppressor protein and the mutational activation of beta-catenin, such that the Axin/APC complex can no longer regulate it. Studies in Drosophila and mammalian tissue culture showed loss of Axin function interfered with beta-catenin turnover and activated beta-catenin/TCF-dependent transcription. Based on these observations, Axin was screened for mutations in a range of human tumor cell lines and primary breast tumor samples. We identified two sequence variants causing amino acid substitutions in four colon cancer cell lines, a Ser-to-Leu at residue 215 in LS513 and a Leu-to-Met at residue 396 in HCT-8, HCT-15, and DLD-1. The Axin L396M mutation was selected for further study since it lay within a region that was shown to interact with glycogen synthase kinase-3. Biochemical and functional studies showed that the L396M change interfered with Axin's ability to bind GSK3. Interestingly, this mutation and a neighboring L392M change differentially altered Axin's ability to interfere with two upstream activators of TCF-dependent transcription, Frat1 and Disheveled."xsd:string |
| http://purl.uniprot.org/citations/10862053 | http://purl.org/dc/terms/identifier | "doi:10.1002/1098-2264(200008)28:4<443::aid-gcc10>3.3.co;2-4"xsd:string |
| http://purl.uniprot.org/citations/10862053 | http://purl.uniprot.org/core/author | "Wooster R."xsd:string |
| http://purl.uniprot.org/citations/10862053 | http://purl.uniprot.org/core/author | "Rozycka M."xsd:string |
| http://purl.uniprot.org/citations/10862053 | http://purl.uniprot.org/core/author | "Webster M.T."xsd:string |
| http://purl.uniprot.org/citations/10862053 | http://purl.uniprot.org/core/author | "Davis E."xsd:string |
| http://purl.uniprot.org/citations/10862053 | http://purl.uniprot.org/core/author | "Dale T.C."xsd:string |
| http://purl.uniprot.org/citations/10862053 | http://purl.uniprot.org/core/author | "Young N."xsd:string |
| http://purl.uniprot.org/citations/10862053 | http://purl.uniprot.org/core/author | "Smalley M."xsd:string |
| http://purl.uniprot.org/citations/10862053 | http://purl.uniprot.org/core/author | "Sara E."xsd:string |
| http://purl.uniprot.org/citations/10862053 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10862053 | http://purl.uniprot.org/core/name | "Genes Chromosomes Cancer"xsd:string |
| http://purl.uniprot.org/citations/10862053 | http://purl.uniprot.org/core/pages | "443-453"xsd:string |
| http://purl.uniprot.org/citations/10862053 | http://purl.uniprot.org/core/title | "Sequence variants of the axin gene in breast, colon, and other cancers: an analysis of mutations that interfere with GSK3 binding."xsd:string |
| http://purl.uniprot.org/citations/10862053 | http://purl.uniprot.org/core/volume | "28"xsd:string |
| http://purl.uniprot.org/citations/10862053 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10862053 |
| http://purl.uniprot.org/citations/10862053 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10862053 |
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| http://purl.uniprot.org/uniprot/#_P30153-mappedCitation-10862053 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/10862053 |