| pubmed-article:17891139 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17891139 | lifeskim:mentions | umls-concept:C0027950 | lld:lifeskim |
| pubmed-article:17891139 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:17891139 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:17891139 | lifeskim:mentions | umls-concept:C0079419 | lld:lifeskim |
| pubmed-article:17891139 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:17891139 | lifeskim:mentions | umls-concept:C0887840 | lld:lifeskim |
| pubmed-article:17891139 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:17891139 | pubmed:dateCreated | 2007-10-2 | lld:pubmed |
| pubmed-article:17891139 | pubmed:abstractText | Poly(ADP-ribose) polymerase 1 (PARP-1) and p53 are two key proteins in the DNA-damage response. Although PARP-1 is known to poly(ADP-ribosyl)ate p53, the role of this modification remains elusive. Here, we identify the major poly(ADP-ribosyl)ated sites of p53 by PARP-1 and find that PARP-1-mediated poly(ADP-ribosyl)ation blocks the interaction between p53 and the nuclear export receptor Crm1, resulting in nuclear accumulation of p53. These findings molecularly link PARP-1 and p53 in the DNA-damage response, providing the mechanism for how p53 accumulates in the nucleus in response to DNA damage. PARP-1 becomes super-activated by binding to damaged DNA, which in turn poly(ADP-ribosyl)ates p53. The nuclear export machinery is unable to target poly(ADP-ribosyl)ated p53, promoting accumulation of p53 in the nucleus where p53 exerts its transactivational function. | lld:pubmed |
| pubmed-article:17891139 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17891139 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17891139 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17891139 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17891139 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17891139 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17891139 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17891139 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17891139 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17891139 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17891139 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17891139 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17891139 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17891139 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17891139 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17891139 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17891139 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:17891139 | pubmed:issn | 1465-7392 | lld:pubmed |
| pubmed-article:17891139 | pubmed:author | pubmed-author:BoularesA... | lld:pubmed |
| pubmed-article:17891139 | pubmed:author | pubmed-author:HanaiShujiS | lld:pubmed |
| pubmed-article:17891139 | pubmed:author | pubmed-author:MiwaMasanaoM | lld:pubmed |
| pubmed-article:17891139 | pubmed:author | pubmed-author:HanashiroKazu... | lld:pubmed |
| pubmed-article:17891139 | pubmed:author | pubmed-author:FukasawaKenji... | lld:pubmed |
| pubmed-article:17891139 | pubmed:author | pubmed-author:KanaiMasayuki... | lld:pubmed |
| pubmed-article:17891139 | pubmed:author | pubmed-author:KimSong-HeeSH | lld:pubmed |
| pubmed-article:17891139 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17891139 | pubmed:volume | 9 | lld:pubmed |
| pubmed-article:17891139 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17891139 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17891139 | pubmed:pagination | 1175-83 | lld:pubmed |
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| pubmed-article:17891139 | pubmed:meshHeading | pubmed-meshheading:17891139... | lld:pubmed |
| pubmed-article:17891139 | pubmed:meshHeading | pubmed-meshheading:17891139... | lld:pubmed |
| pubmed-article:17891139 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17891139 | pubmed:articleTitle | Inhibition of Crm1-p53 interaction and nuclear export of p53 by poly(ADP-ribosyl)ation. | lld:pubmed |
| pubmed-article:17891139 | pubmed:affiliation | H. Lee Moffitt Cancer Center and Research Institute, Tampa, Florida 33612, USA. | lld:pubmed |
| pubmed-article:17891139 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17891139 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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