| pubmed-article:12660252 | rdf:type | pubmed:Citation | lld:pubmed |
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| pubmed-article:12660252 | lifeskim:mentions | umls-concept:C1704632 | lld:lifeskim |
| pubmed-article:12660252 | lifeskim:mentions | umls-concept:C0871261 | lld:lifeskim |
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| pubmed-article:12660252 | lifeskim:mentions | umls-concept:C2911692 | lld:lifeskim |
| pubmed-article:12660252 | lifeskim:mentions | umls-concept:C1706817 | lld:lifeskim |
| pubmed-article:12660252 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
| pubmed-article:12660252 | lifeskim:mentions | umls-concept:C0596311 | lld:lifeskim |
| pubmed-article:12660252 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:12660252 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:12660252 | pubmed:issue | 22 | lld:pubmed |
| pubmed-article:12660252 | pubmed:dateCreated | 2003-5-26 | lld:pubmed |
| pubmed-article:12660252 | pubmed:abstractText | DNA double-strand breaks originating from diverse causes in eukaryotic cells are accompanied by the formation of phosphorylated H2AX (gammaH2AX) foci. Here we show that gammaH2AX formation is also a cellular response to topoisomerase I cleavage complexes known to induce DNA double-strand breaks during replication. In HCT116 human carcinoma cells exposed to the topoisomerase I inhibitor camptothecin, the resulting gammaH2AX formation can be prevented with the phosphatidylinositol 3-OH kinase-related kinase inhibitor wortmannin; however, in contrast to ionizing radiation, only camptothecin-induced gammaH2AX formation can be prevented with the DNA replication inhibitor aphidicolin and enhanced with the checkpoint abrogator 7-hydroxystaurosporine. This gammaH2AX formation is suppressed in ATR (ataxia telangiectasia and Rad3-related) deficient cells and markedly decreased in DNA-dependent protein kinase-deficient cells but is not abrogated in ataxia telangiectasia cells, indicating that ATR and DNA-dependent protein kinase are the kinases primarily involved in gammaH2AX formation at the sites of replication-mediated DNA double-strand breaks. Mre11- and Nbs1-deficient cells are still able to form gammaH2AX. However, H2AX-/- mouse embryonic fibroblasts exposed to camptothecin fail to form Mre11, Rad50, and Nbs1 foci and are hypersensitive to camptothecin. These results demonstrate a conserved gammaH2AX response for double-strand breaks induced by replication fork collision. gammaH2AX foci are required for recruiting repair and checkpoint protein complexes to the replication break sites. | lld:pubmed |
| pubmed-article:12660252 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:12660252 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12660252 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12660252 | pubmed:month | May | lld:pubmed |
| pubmed-article:12660252 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:12660252 | pubmed:author | pubmed-author:PommierYvesY | lld:pubmed |
| pubmed-article:12660252 | pubmed:author | pubmed-author:AladjemMirit... | lld:pubmed |
| pubmed-article:12660252 | pubmed:author | pubmed-author:BonnerWilliam... | lld:pubmed |
| pubmed-article:12660252 | pubmed:author | pubmed-author:FurutaTakahis... | lld:pubmed |
| pubmed-article:12660252 | pubmed:author | pubmed-author:RedonChristop... | lld:pubmed |
| pubmed-article:12660252 | pubmed:author | pubmed-author:CelesteArkady... | lld:pubmed |
| pubmed-article:12660252 | pubmed:author | pubmed-author:ChenHua... | lld:pubmed |
| pubmed-article:12660252 | pubmed:author | pubmed-author:SedelnikovaOl... | lld:pubmed |
| pubmed-article:12660252 | pubmed:author | pubmed-author:PilchDuane... | lld:pubmed |
| pubmed-article:12660252 | pubmed:author | pubmed-author:TakemuraHaruy... | lld:pubmed |
| pubmed-article:12660252 | pubmed:author | pubmed-author:NussenzweigAn... | lld:pubmed |
| pubmed-article:12660252 | pubmed:author | pubmed-author:AuneGregory... | lld:pubmed |
| pubmed-article:12660252 | pubmed:author | pubmed-author:RogakouEmmy... | lld:pubmed |
| pubmed-article:12660252 | pubmed:author | pubmed-author:LiaoZhi-YongZ... | lld:pubmed |
| pubmed-article:12660252 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12660252 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:12660252 | pubmed:volume | 278 | lld:pubmed |
| pubmed-article:12660252 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12660252 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12660252 | pubmed:pagination | 20303-12 | lld:pubmed |
| pubmed-article:12660252 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:12660252 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12660252 | pubmed:articleTitle | Phosphorylation of histone H2AX and activation of Mre11, Rad50, and Nbs1 in response to replication-dependent DNA double-strand breaks induced by mammalian DNA topoisomerase I cleavage complexes. | lld:pubmed |
| pubmed-article:12660252 | pubmed:affiliation | Laboratory of Molecular Pharmacology, Center for Cancer Research, NCI, National Institutes of Health, Bethesda, Maryland 20892-4255, USA. | lld:pubmed |
| pubmed-article:12660252 | pubmed:publicationType | Journal Article | lld:pubmed |
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