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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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The role of cell cycle regulation and apoptosis triggering in determining the sensitivity of leukemic cells to topoisomerase I and II inhibitors.

TL;DR: The ability of leukemic cell lines to regulate cell cycle progression and to trigger apoptosis is more indicative of their sensitivity to topoisomerase poisons than cleavable complexes induced by these drugs.
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Induction of topoisomerase I cleavage complexes by 1-beta -D-arabinofuranosylcytosine (ara-C) in vitro and in ara-C-treated cells.

TL;DR: The observed inhibition of religation at the ara-C site suggests the importance of the alignment of the 5'-hydroxyl end for religation with the phosphate group of the top1 phosphotyrosine bond.
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T30177, an oligonucleotide stabilized by an intramolecular guanosine octet, is a potent inhibitor of laboratory strains and clinical isolates of human immunodeficiency virus type 1.

TL;DR: The ability of T 30177 to inhibit both laboratory and clinical isolates of HIV-1 and the experimental data which suggest that T30177 represents a novel class of integrase inhibitors indicate that this compound is a viable candidate for evaluation as a therapeutic agent against HIV- 1 in humans.
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CellMinerCDB for Integrative Cross-Database Genomics and Pharmacogenomics Analyses of Cancer Cell Lines.

TL;DR: The value of CellMinerCDB in selecting drugs with reproducible activity is demonstrated, the dominant role of SLFN11 for drug response is expanded, and novel response determinants and genomic signatures for topoisomerase inhibitors and schweinfurthins are presented.
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Hydrazide-Containing Inhibitors of HIV-1 Integrase†

TL;DR: In this paper, the authors used a three-point pharmacophore search based on its assigned structure N-(2-hydroxybenzoyl)-N-(2hydroxy-3-phenoxypropyl)hydrazine (1) to identify structural leads for the development of new HIV integrase inhibitors which do not rely on potentially cytotoxic catechol substructure.