Yves Pommier

TL;DR: DNA topoisomerases I and II (Top1 and Top2) are established molecular targets of anticancer drugs and eukaryotic Top1 enzymes belong to the broader family of site-specific tyrosine recombinases of prokaryotes and yeast.

TL;DR: This review will focus on programmed cell death (apoptosis) and on survival pathways (Bcl-2, Apaf-1, AKT, NF-κB) involved in multidrug resistance, and introduce the ‘permissive apoptosis-resistance’ model for the selection ofMultidrug-resistant cells.

TL;DR: The present review describes the topoisomerase I catalytic mechanisms with particular emphasis on the cleavage complex that represents the enzyme's catalytic intermediate and the site of action for camptothecins.

TL;DR: It is shown that staurosporine can rapidly trigger both the morphological changes and intranucleosomal DNA fragmentation typical of apoptosis, and results obtained in a cell-free assay suggest that cytoplasmic proteins directly modulated by stauosporine may be involved in a ubiquitous signal for the induction of DNA fragmentation and apoptosis.

TL;DR: Stereochemistry and the positions of substituents were found to be crucial for the presence or absence of effects on topoisomerase I, indicating that the compounds interact with an asymmetrical receptor site on the enzyme or enzyme-DNA complex.