C
Casimir Blonski
Researcher at Paul Sabatier University
Publications - 60
Citations - 1114
Casimir Blonski is an academic researcher from Paul Sabatier University. The author has contributed to research in topics: Aldolase A & Fructose-bisphosphate aldolase. The author has an hindex of 19, co-authored 60 publications receiving 1056 citations. Previous affiliations of Casimir Blonski include Vanderbilt University & Centre national de la recherche scientifique.
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Glycolysis as a target for the design of new anti-trypanosome drugs
Christophe L. M. J. Verlinde,Véronique Hannaert,Casimir Blonski,Michèle Willson,Jacques Périé,Linda A. Fothergill-Gilmore,Fred R. Opperdoes,Michael H. Gelb,Wim G. J. Hol,Paul A.M. Michels +9 more
TL;DR: Structural- and catalytic mechanism-based approaches are applied to design compounds that inhibit the glycolytic enzymes of the parasites without affecting the corresponding proteins of the human host.
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Class I aldolases: substrate specificity, mechanism, inhibitors and structural aspects
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Antitrypanosomal alkaloids from Polyalthia suaveolens (Annonaceae): their effects on three selected glycolytic enzymes of Trypanosoma brucei
Igor Ngantchou,Igor Ngantchou,Barthelemy Nyasse,Colette Denier,Casimir Blonski,Véronique Hannaert,Bernd Schneider +6 more
TL;DR: Stem barks of Polyalthia suaveolens were phytochemically studied and yielded a new indolosesquiterpene alkaloid, named polysin, and four hitherto known alkaloids, which exhibited interesting inhibitory effects on selected glycolytic enzymes.
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Spermidinyl-CoA-based HAT inhibitors block DNA repair and provide cancer-specific chemo- and radiosensitization
Keya Bandyopadhyay,Jean-Louis Banères,Aimée Martin,Casimir Blonski,Joseph Parello,Ruth A. Gjerset +5 more
TL;DR: The results demonstrate that Spd-CoA and its truncated version are efficiently and selectively internalized into cancer cells, and suggest that the resulting inhibition of acetylation-dependent DNA repair enhances cellular sensitivity to DNA damage.
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Inhibition of rabbit muscle aldolase by phosphorylated aromatic compounds.
TL;DR: Site-directed mutagenesis of the active-site lysine residues at positions 107, 146 and 229 was found to be consistent with Schiff-base formation between DHBA-P and Lys-146, and this was promoted by Lys-229.