pubmed-article:21445056 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:21445056 | lifeskim:mentions | umls-concept:C0079427 | lld:lifeskim |
pubmed-article:21445056 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
pubmed-article:21445056 | lifeskim:mentions | umls-concept:C0079419 | lld:lifeskim |
pubmed-article:21445056 | lifeskim:mentions | umls-concept:C0260037 | lld:lifeskim |
pubmed-article:21445056 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
pubmed-article:21445056 | lifeskim:mentions | umls-concept:C1517378 | lld:lifeskim |
pubmed-article:21445056 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:21445056 | pubmed:dateCreated | 2011-4-19 | lld:pubmed |
pubmed-article:21445056 | pubmed:abstractText | Many p53 missense mutations possess dominant-negative activity and oncogenic gain of function. We report that for structurally destabilized p53 mutants, these effects result from mutant-induced coaggregation of wild-type p53 and its paralogs p63 and p73, thereby also inducing a heat-shock response. Aggregation of mutant p53 resulted from self-assembly of a conserved aggregation-nucleating sequence within the hydrophobic core of the DNA-binding domain, which becomes exposed after mutation. Suppressing the aggregation propensity of this sequence by mutagenesis abrogated gain of function and restored activity of wild-type p53 and its paralogs. In the p53 germline mutation database, tumors carrying aggregation-prone p53 mutations have a significantly lower frequency of wild-type allele loss as compared to tumors harboring nonaggregating mutations, suggesting a difference in clonal selection of aggregating mutants. Overall, our study reveals a novel disease mechanism for mutant p53 gain of function and suggests that, at least in some respects, cancer could be considered an aggregation-associated disease. | lld:pubmed |
pubmed-article:21445056 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21445056 | pubmed:language | eng | lld:pubmed |
pubmed-article:21445056 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21445056 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:21445056 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21445056 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21445056 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21445056 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21445056 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21445056 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21445056 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21445056 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21445056 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:21445056 | pubmed:month | May | lld:pubmed |
pubmed-article:21445056 | pubmed:issn | 1552-4469 | lld:pubmed |
pubmed-article:21445056 | pubmed:author | pubmed-author:MarineJean-Ch... | lld:pubmed |
pubmed-article:21445056 | pubmed:author | pubmed-author:RozenskiJefJ | lld:pubmed |
pubmed-article:21445056 | pubmed:author | pubmed-author:RousseauFrede... | lld:pubmed |
pubmed-article:21445056 | pubmed:author | pubmed-author:MEOLL | lld:pubmed |
pubmed-article:21445056 | pubmed:author | pubmed-author:SuhYoung-AhYA | lld:pubmed |
pubmed-article:21445056 | pubmed:author | pubmed-author:LambrechtsDie... | lld:pubmed |
pubmed-article:21445056 | pubmed:author | pubmed-author:De... | lld:pubmed |
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pubmed-article:21445056 | pubmed:author | pubmed-author:SchymkowitzJo... | lld:pubmed |
pubmed-article:21445056 | pubmed:author | pubmed-author:ReumersJokeJ | lld:pubmed |
pubmed-article:21445056 | pubmed:author | pubmed-author:CouceiroJosé... | lld:pubmed |
pubmed-article:21445056 | pubmed:author | pubmed-author:CornelisAnnA | lld:pubmed |
pubmed-article:21445056 | pubmed:author | pubmed-author:GallardoRodri... | lld:pubmed |
pubmed-article:21445056 | pubmed:author | pubmed-author:ZwolinskaAlek... | lld:pubmed |
pubmed-article:21445056 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:21445056 | pubmed:volume | 7 | lld:pubmed |
pubmed-article:21445056 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:21445056 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:21445056 | pubmed:pagination | 285-95 | lld:pubmed |
pubmed-article:21445056 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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pubmed-article:21445056 | pubmed:year | 2011 | lld:pubmed |
pubmed-article:21445056 | pubmed:articleTitle | Gain of function of mutant p53 by coaggregation with multiple tumor suppressors. | lld:pubmed |
pubmed-article:21445056 | pubmed:affiliation | Switch Laboratory, Flanders Institute for Biotechnology, Vrije Universiteit Brussel, Brussels, Belgium. | lld:pubmed |
pubmed-article:21445056 | pubmed:publicationType | Journal Article | lld:pubmed |
entrez-gene:7157 | entrezgene:pubmed | pubmed-article:21445056 | lld:entrezgene |
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