pubmed-article:8538647 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8538647 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
pubmed-article:8538647 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
pubmed-article:8538647 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:8538647 | lifeskim:mentions | umls-concept:C0032405 | lld:lifeskim |
pubmed-article:8538647 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
pubmed-article:8538647 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:8538647 | pubmed:dateCreated | 1996-2-7 | lld:pubmed |
pubmed-article:8538647 | pubmed:abstractText | SKI-1 is a 1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU)-resistant glioma cell line and SK-MG-1 is a BCNU-sensitive glioma cell line. Both cell lines do not express O6-methylguanine-DNA methyl transferase (MGMT) and exhibit comparable levels of 3-methyladenine DNA glycosylase. In order to detect DNA binding proteins involved in alternative DNA repair mechanisms of BCNU damage, we performed Southwestern analysis using a DNA probe damaged with BCNU and nuclear protein extracts from SKI-1 and SK-MG-1 cell lines. Both cell lines express a protein of M(r) 116,000 that is able to bind to BCNU-damaged DNA with higher specificity than to undamaged DNA. This protein was identified as poly(ADP-ribose) polymerase (PARP). Using glioma extracts depleted of PARP or using antibody to block the DNA binding domain of PARP no other protein binding to BCNU-treated probe was observed. Addition of methoxyamine, an inhibitor of DNA strand breaks, led to a significant reduction of PARP binding to BCNU-treated DNA. BCNU treatment of both glioma cell lines led to reduced nicotinamide adenine dinucleotide levels, indicating activation of PARP. Thus, the recognition and binding of PARP to BCNU-induced DNA nicks with concomitant PARP activation may be important processes that are involved in the initial stage of DNA repair of BCNU lesions in glial cells. | lld:pubmed |
pubmed-article:8538647 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8538647 | pubmed:language | eng | lld:pubmed |
pubmed-article:8538647 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8538647 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8538647 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8538647 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8538647 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8538647 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8538647 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8538647 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8538647 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8538647 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8538647 | pubmed:month | Jan | lld:pubmed |
pubmed-article:8538647 | pubmed:issn | 0027-5107 | lld:pubmed |
pubmed-article:8538647 | pubmed:author | pubmed-author:PoirierG GGG | lld:pubmed |
pubmed-article:8538647 | pubmed:author | pubmed-author:PanasciL CLC | lld:pubmed |
pubmed-article:8538647 | pubmed:author | pubmed-author:BergerN ANA | lld:pubmed |
pubmed-article:8538647 | pubmed:author | pubmed-author:MalapetsaAA | lld:pubmed |
pubmed-article:8538647 | pubmed:author | pubmed-author:NoëA JAJ | lld:pubmed |
pubmed-article:8538647 | pubmed:author | pubmed-author:DesnoyersSS | lld:pubmed |
pubmed-article:8538647 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8538647 | pubmed:day | 2 | lld:pubmed |
pubmed-article:8538647 | pubmed:volume | 362 | lld:pubmed |
pubmed-article:8538647 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8538647 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8538647 | pubmed:pagination | 41-50 | lld:pubmed |
pubmed-article:8538647 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:8538647 | pubmed:year | 1996 | lld:pubmed |
pubmed-article:8538647 | pubmed:articleTitle | Identification of a 116 kDa protein able to bind 1,3-bis(2-chloroethyl)-1-nitrosourea-damaged DNA as poly(ADP-ribose) polymerase. | lld:pubmed |
pubmed-article:8538647 | pubmed:affiliation | Lady Davis Institute for Medical Research, Sir Mortimer B. Davis-Jewish General Hospital, Montreal, Québec, Canada. | lld:pubmed |
pubmed-article:8538647 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8538647 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8538647 | lld:pubmed |