| pubmed-article:19106109 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19106109 | lifeskim:mentions | umls-concept:C0024337 | lld:lifeskim |
| pubmed-article:19106109 | lifeskim:mentions | umls-concept:C0001038 | lld:lifeskim |
| pubmed-article:19106109 | lifeskim:mentions | umls-concept:C0079419 | lld:lifeskim |
| pubmed-article:19106109 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
| pubmed-article:19106109 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
| pubmed-article:19106109 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:19106109 | pubmed:dateCreated | 2009-2-16 | lld:pubmed |
| pubmed-article:19106109 | pubmed:abstractText | Acetylation of multiple lysine residues in the p53 plays critical roles in the protein stability and transcriptional activity of p53. To better understand how p53 acetylation is regulated, we generated a number of p53 mutants and examined acetylation of each mutant in transfected cells. We found that p53 mutants that are defective in tetramer formation are also defective in C-terminal lysine residue acetylation. Consistently, we found that several cancer-derived p53 mutants that bear mutations in the tetramerization domain cannot form oligomers and are defective in C-terminal lysine acetylation, and these mutants are inactive in p21 transactivation. We demonstrated that the acetyltransferase p300 interacts with and promotes acetylation of wild-type p53 but not with any of the artificially generated or human cancer-derived p53 mutants that are defective in oligomerization. These results, combined with a computer-aided crystal structure analysis, suggest a model in which p53 oligomerization precedes its acetylation by providing docking sites for acetyltransferases. | lld:pubmed |
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| pubmed-article:19106109 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19106109 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19106109 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:19106109 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19106109 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:19106109 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:19106109 | pubmed:author | pubmed-author:KeHengmingH | lld:pubmed |
| pubmed-article:19106109 | pubmed:author | pubmed-author:ItahanaYokoY | lld:pubmed |
| pubmed-article:19106109 | pubmed:author | pubmed-author:ZhangYanpingY | lld:pubmed |
| pubmed-article:19106109 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:19106109 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:19106109 | pubmed:volume | 284 | lld:pubmed |
| pubmed-article:19106109 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19106109 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19106109 | pubmed:pagination | 5158-64 | lld:pubmed |
| pubmed-article:19106109 | pubmed:dateRevised | 2011-4-19 | lld:pubmed |
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| pubmed-article:19106109 | pubmed:meshHeading | pubmed-meshheading:19106109... | lld:pubmed |
| pubmed-article:19106109 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19106109 | pubmed:articleTitle | p53 Oligomerization is essential for its C-terminal lysine acetylation. | lld:pubmed |
| pubmed-article:19106109 | pubmed:affiliation | Department of Radiation Oncology, University of North Carolina, Chapel Hill, North Carolina 27599-7512, USA. | lld:pubmed |
| pubmed-article:19106109 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19106109 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:19106109 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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