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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
1993-4-15
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pubmed:abstractText |
Rejoining of DNA single-strand breaks generated by treatment of plasmids with gamma-rays, neocarzinostatin, or bleomycin was catalyzed inefficiently by human cell extracts. The reaction was strongly promoted by the addition of NAD+, which was employed for rapid and transient synthesis of poly(ADP-ribose). The DNA rejoining reaction was accompanied by DNA repair replication, apparently due to replacement of damaged residues at termini. Selective depletion of poly(ADP-ribose) polymerase from cell extracts improved the repair of DNA exposed to a variety of DNA-damaging agents by removing the NAD+ dependence of the repair reaction. NAD(+)-promoted DNA repair by soluble cell extracts also occurred with alkylated DNA as substrate and was suppressed by 3-aminobenzamide. A similar stimulatory effect by NAD+ was observed for repair of ultraviolet-irradiated DNA, and this could be ascribed to the presence of pyrimidine hydrates as minor radiation-induced DNA lesions. No effect was observed on the sealing of gamma-irradiated DNA by supplementation of cell extracts with purified mammalian DNA ligase I or DNA ligase II. The results indicate that poly(ADP-ribose) polymerase interferes with base excision-repair processes because bound enzyme molecules block DNA strand interruptions. Release of bound poly-(ADP-ribose) polymerase following automodification, or physical removal of the protein from reaction mixtures, facilitates DNA repair.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenine Phosphoribosyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/Bleomycin,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/NAD,
http://linkedlifedata.com/resource/pubmed/chemical/Poly Adenosine Diphosphate Ribose,
http://linkedlifedata.com/resource/pubmed/chemical/Zinostatin
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
268
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5480-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7680646-Adenine Phosphoribosyltransferase,
pubmed-meshheading:7680646-Alkylation,
pubmed-meshheading:7680646-Bleomycin,
pubmed-meshheading:7680646-Cell-Free System,
pubmed-meshheading:7680646-Cells, Cultured,
pubmed-meshheading:7680646-DNA,
pubmed-meshheading:7680646-DNA Damage,
pubmed-meshheading:7680646-DNA Ligases,
pubmed-meshheading:7680646-DNA Repair,
pubmed-meshheading:7680646-HeLa Cells,
pubmed-meshheading:7680646-Humans,
pubmed-meshheading:7680646-Kinetics,
pubmed-meshheading:7680646-Lymphocytes,
pubmed-meshheading:7680646-NAD,
pubmed-meshheading:7680646-Poly Adenosine Diphosphate Ribose,
pubmed-meshheading:7680646-Ultraviolet Rays,
pubmed-meshheading:7680646-Zinostatin
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pubmed:year |
1993
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pubmed:articleTitle |
NAD(+)-dependent repair of damaged DNA by human cell extracts.
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pubmed:affiliation |
Imperial Cancer Research Fund, Clare Hall Laboratories, South Mimms, Hertfordshire, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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