| pubmed-article:11948190 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11948190 | lifeskim:mentions | umls-concept:C0032403 | lld:lifeskim |
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| pubmed-article:11948190 | lifeskim:mentions | umls-concept:C0728940 | lld:lifeskim |
| pubmed-article:11948190 | lifeskim:mentions | umls-concept:C1366475 | lld:lifeskim |
| pubmed-article:11948190 | lifeskim:mentions | umls-concept:C0012899 | lld:lifeskim |
| pubmed-article:11948190 | lifeskim:mentions | umls-concept:C1428200 | lld:lifeskim |
| pubmed-article:11948190 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
| pubmed-article:11948190 | lifeskim:mentions | umls-concept:C0178499 | lld:lifeskim |
| pubmed-article:11948190 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:11948190 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:11948190 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:11948190 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:11948190 | pubmed:issue | 25 | lld:pubmed |
| pubmed-article:11948190 | pubmed:dateCreated | 2002-6-17 | lld:pubmed |
| pubmed-article:11948190 | pubmed:abstractText | The DNA damage dependence of poly(ADP-ribose) polymerase-2 (PARP-2) activity is suggestive of its implication in genome surveillance and protection. Here we show that the PARP-2 gene, mainly expressed in actively dividing tissues follows, but to a smaller extent, that of PARP-1 during mouse development. We found that PARP-2 and PARP-1 homo- and heterodimerize; the interacting interfaces, sites of reciprocal modification, have been mapped. PARP-2 was also found to interact with three other proteins involved in the base excision repair pathway: x-ray cross complementing factor 1 (XRCC1), DNA polymerase beta, and DNA ligase III, already known as partners of PARP-1. XRCC1 negatively regulates PARP-2 activity, as it does for PARP-1, while being a polymer acceptor for both PARP-1 and PARP-2. To gain insight into the physiological role of PARP-2 in response to genotoxic stress, we developed by gene disruption mice deficient in PARP-2. Following treatment by the alkylating agent N-nitroso-N-methylurea (MNU), PARP-2-deficient cells displayed an important delay in DNA strand breaks resealing, similar to that observed in PARP-1 deficient cells, thus confirming that PARP-2 is also an active player in base excision repair despite its low capacity to synthesize ADP-ribose polymers. | lld:pubmed |
| pubmed-article:11948190 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11948190 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11948190 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11948190 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11948190 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:11948190 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:11948190 | pubmed:author | pubmed-author:FraulobValéri... | lld:pubmed |
| pubmed-article:11948190 | pubmed:author | pubmed-author:DolléPascalP | lld:pubmed |
| pubmed-article:11948190 | pubmed:author | pubmed-author:de... | lld:pubmed |
| pubmed-article:11948190 | pubmed:author | pubmed-author:SchreiberValé... | lld:pubmed |
| pubmed-article:11948190 | pubmed:author | pubmed-author:AméJean-Chris... | lld:pubmed |
| pubmed-article:11948190 | pubmed:author | pubmed-author:SchultzInèsI | lld:pubmed |
| pubmed-article:11948190 | pubmed:author | pubmed-author:RinaldiBrunoB | lld:pubmed |
| pubmed-article:11948190 | pubmed:author | pubmed-author:Ménissier-de... | lld:pubmed |
| pubmed-article:11948190 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11948190 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:11948190 | pubmed:volume | 277 | lld:pubmed |
| pubmed-article:11948190 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11948190 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11948190 | pubmed:pagination | 23028-36 | lld:pubmed |
| pubmed-article:11948190 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:11948190 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11948190 | pubmed:articleTitle | Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1. | lld:pubmed |
| pubmed-article:11948190 | pubmed:affiliation | UPR 9003 du Centre National de la Recherche Scientifique, Laboratoire conventionné avec le Commissariat à l'Energie Atomique, Université Louis Pasteur, Ecole Supérieure de Biotechnologie de Strasbourg, Illkirch, France. | lld:pubmed |
| pubmed-article:11948190 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11948190 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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