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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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Evaluation of current methods used to analyze the expression profiles of ATP-binding cassette transporters yields an improved drug-discovery database

TL;DR: A previously established database that allows the identification of lead compounds in the early stages of drug discovery that are not ATP-binding cassette (ABC) transporter substrates is used and two platforms are found to be superior methods for the analysis of expression profiles of highly homologous gene superfamilies.
Journal Article

Effects of Dimethyl Sulfoxide and Thiourea upon Intercalator-induced DNA Single-Strand Breaks in Mouse Leukemia (L1210) Cells

TL;DR: Experiments using nucleoid sedimentation to assess the DNA linking number and domain size from cells treated with Me2SO and thiourea indicated that these chemicals alter chromatin structure in a fashion which may account for effects on intercalator-induced DNA scission.
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Alcohol-, diol-, and carbohydrate-substituted indenoisoquinolines as topoisomerase I inhibitors: investigating the relationships involving stereochemistry, hydrogen bonding, and biological activity.

TL;DR: Investigation of how similar functionalities could be "translated" to the indenoisoquinoline system and how stereochemistry and hydrogen bonding affect biological activity found a stereochemical dependence was also observed for carbohydrate-derived indenoiseoquinolines.
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Activation of Aminoflavone (NSC 686288) by a Sulfotransferase Is Required for the Antiproliferative Effect of the Drug and for Induction of Histone γ-H2AX

TL;DR: The results reported here suggest using SULT1A1 and gamma-H2AX as biomarkers for prediction of AF activity during patient selection and monitoring of clinical trials and suggest that both N-sulfoxy-groups can be further converted to nitrenium ions that form adducts with DNA and proteins.