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Yves Pommier
Researcher at National Institutes of Health
Publications - 847
Citations - 65543
Yves Pommier is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Topoisomerase & DNA. The author has an hindex of 123, co-authored 789 publications receiving 58898 citations. Previous affiliations of Yves Pommier include Purdue University & Kyushu University.
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Effects of DNA intercalating agents on topoisomerase II induced DNA strand cleavage in isolated mammalian cell nuclei.
TL;DR: Because these results were reproduced in experiments using DNA topoisomerase II isolated from L1210 nuclei, it is likely that the intercalator-induced protein-associated DNA breaks detected by alkaline elution in nuclei representDNA topoisomersase II-DNA complexes.
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DNA unwinding and inhibition of mouse leukemia L1210 DNA topoisomerase I by intercalators
TL;DR: The DNA unwinding effects of some 9-aminoacridine derivatives were compared under reaction conditions that could be used to study drug-induced topoisomerase II inhibition and led to the definition of a drug intrinsic unwinding constant (k).
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HIV-1 integrase inhibitors: a decade of research and two drugs in clinical trial.
TL;DR: An update on integrase inhibitors reported in the last two years, including two novel inhibitors in early clinical trials, recently developed hydroxylated aromatics, natural products, peptide, antibody and oligonucleotide inhibitors, and the proposed mechanism of diketo acid inhibition are reviewed.
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Covalent binding of the natural antimicrobial peptide indolicidin to DNA abasic sites
Christophe Marchand,Krzysztof Krajewski,Hsiu-Fang Lee,Smitha Antony,Allison A. Johnson,Ronak Amin,Peter P. Roller,Mamuka Kvaratskhelia,Yves Pommier +8 more
TL;DR: It is found that indolicidin interferes with formation of the catalytic integrase-DNA complex by directly binding DNA and that multiple actions at the level of DNA might be a common property of antimicrobial peptides.
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Design, Synthesis, and Biological Evaluation of Indenoisoquinoline Topoisomerase I Inhibitors Featuring Polyamine Side Chains on the Lactam Nitrogen
TL;DR: One of the monoamine analogues, which features a bis(2-hydroxyethyl)amino group in the side chain, proved to be one of the most cytotoxic indenoisoquinoline synthesized to date, with a GI50 mean-graph midpoint of 0.07 microM in the NIH human cancer cell culture screen, and topoisomerase I inhibitory activity comparable to that of camptothecin.