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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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Chemical Trapping of Ternary Complexes of Human Immunodeficiency Virus Type 1 Integrase, Divalent Metal, and DNA Substrates Containing an Abasic Site: IMPLICATIONS FOR THE ROLE OF LYSINE 136 IN DNA BINDING

TL;DR: Both the N- and C-terminal domains of integrase contributed to efficient DNA binding, and mutation of Lys-136 significantly reduced Schiff base formation, implicating this residue in viral DNA binding.
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Increased negative supercoiling of mtDNA in TOP1mt knockout mice and presence of topoisomerases IIα and IIβ in vertebrate mitochondria

TL;DR: It is demonstrated that mitochondrial DNA displays increased negative supercoiling in TOP1mt knockout cells and murine tissues, and the presence of Top2α-DNA complexes in the mtDNA D-loop region, at the sites where both ends of 7S DNA are positioned, suggests a structural role for Top2 in addition to its classical topoisomerase activities.
Journal Article

Apoptosis of human leukemic HL-60 cells induced to differentiate by phorbol ester treatment.

TL;DR: Internucleosomal DNA fragmentation was also identified in HL-60 cells induced to differentiate by sodium butyrate and dimethylsulfoxide treatment, suggesting that apoptosis could be the common mode of death of terminally differentiated HL- 60 cells.
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Benzo[a]pyrene diol epoxide adducts in DNA are potent suppressors of a normal topoisomerase I cleavage site and powerful inducers of other topoisomerase I cleavages

TL;DR: It is reported here that DNA adducts formed from benzo[a]pyrene bay-region diol epoxides can markedly affect top1 activity, and the trans opened adduct from the highly carcinogenic (+)-diol epoxide is the most active in inducing top1 cleavage independently of camptothecin, demonstrating that minor groove alkylation can efficiently poison top1.