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- W2003669491 abstract "We examined HMG domain protein recognition of major 1,2-GG intrastrand DNA crosslinks, formed by two bifunctional enantiomeric analogs of antitumor cis-diamminedichloroplatinum(II) (cisplatin), and removal of these crosslinks during in vitro nucleotide excision repair (NER) reactions. Electrophoretic mobility shift assays show that domains A and B of HMGB1 protein bind to (2R,3R)-diaminobutanedichloroplatinum(II)-generated crosslinks with a higher affinity than to those generated by (2S,3S)-diaminobutanedichloroplatinum(II). The crosslinks of both enantiomers are removed by NER with a similar efficiency; however, HMG1B protein significantly inhibits removal of the (2R,3R)-diaminobutaneplatinum(II) adduct, but not that of the (2S,3S) enantiomer. Thus, HMG domain proteins discriminate among different conformations of the 1,2-GG intrastrand crosslinks of the two enantiomeric analogs of cisplatin, which results in different NER of these crosslinks. This observation may provide insight into the mechanisms underlying antitumor activity of cisplatin and its analogs." @default.
- W2003669491 created "2016-06-24" @default.
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- W2003669491 date "2002-05-01" @default.
- W2003669491 modified "2023-10-05" @default.
- W2003669491 title "Recognition of Major DNA Adducts of Enantiomeric Cisplatin Analogs by HMG Box Proteins and Nucleotide Excision Repair of These Adducts" @default.
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- W2003669491 doi "https://doi.org/10.1016/s1074-5521(02)00134-5" @default.
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