Jean-Yves Winum
0000-0003-3197-3414
Université de Montpellier
154 papers found
Refreshing results…
Carbonic anhydrase activators: Activation of human isozymes I, II and IX with phenylsulfonylhydrazido L-histidine derivatives
Preface
Carbonic Anhydrase Inhibitor Coated Gold Nanoparticles Selectively Inhibit the Tumor-Associated Isoform IX over the Cytosolic Isozymes I and II
Carbonic anhydrase inhibitors: 2-Substituted-1,3,4-thiadiazole-5-sulfamides act as powerful and selective inhibitors of the mitochondrial isozymes VA and VB over the cytosolic and membrane-associated carbonic anhydrases I, II and IV
Carbonic Anhydrase Inhibitors: Design of Membrane-Impermeant Copper(II) Complexes of DTPA-, DOTA-, and TETA-Tailed Sulfonamides Targeting the Tumor-Associated Transmembrane Isoform IX
Carbonic anhydrase inhibitors: Design of spin-labeled sulfonamides incorporating TEMPO moieties as probes for cytosolic or transmembrane isozymes
Design of Zinc Binding Functions for Carbonic Anhydrase Inhibitors
Carbonic anhydrase IX : a new druggable target for the design of antitumor agents
Targeting bacterial metalloenzymes : a new strategy for the development of anti-infective agents.
Carbonic anhydrase inhibitors. Copper(II) complexes of polyamino-polycarboxylamido aromatic/heterocyclic sulfonamides are very potent inhibitors of the tumor associated isoforms IX and XII.
Carbonic anhydrase IX inhibitors: fluorescent sulfonamides as therapeutic and diagnostic agents: Supuran CT; Scozzafava A: WO2006137092
Carbonic anhydrase inhibitors: Selective inhibition of the extracellular, tumor-associated isoforms IX and XII over isozymes I and II with glycosyl-thioureido-sulfonamides
Targeting of the Brucella suis Virulence Factor Histidinol Dehydrogenase by Histidinol Analogues Results in Inhibition of Intramacrophagic Multiplication of the Pathogen
Brucella suis histidinol dehydrogenase: Synthesis and inhibition studies of a series of substituted benzylic ketones derived from histidine
Synthesis of Substituted N-aryl-N-Sulfamoyloxazolidin-2-ones with Potential Antibacterial Activity
Carbonic Anhydrase Inhibitors. The X-ray crystal structure of the adduct of N-hydroxysulfamide with isozyme II explains why this new zinc binding function is effective in the design of potent inhibitors
Carbonic Anhydrase Inhibitors. Inhibition of isoforms I, II, IV, VA, VII, IX and XIV with sulfonamides incorporating fructopyranose-thioureido tails
Carbonic anhydrase inhibitors: Binding of an antiglaucoma glycosyl-sulfanilamide derivative to human isoform II and its consequences for the drug design of enzyme inhibitors incorporating sugar moieties
Metal binding functions in the design of carbonic anhydrase inhibitors
Carbonic Anhydrase Inhibitors: Clash with Ala65 as a Means for Designing Inhibitors with Low Affinity for the Ubiquitous Isozyme II, Exemplified by the Crystal Structure of the Topiramate Sulfamide Analogue †
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