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 - Archive ouverte HAL
Article Dans Une Revue Bioorganic and Medicinal Chemistry Letters Année : 2007

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

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Chimie organique

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https://hal.science/hal-00273205

Soumis le : lundi 14 avril 2008-16:43:44

Dernière modification le : vendredi 20 décembre 2024-11:38:17

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hal-00273205 , version 1 (14-04-2008)

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Claudia Temperini, Jean-Yves Winum, Jean-Louis Montero, Andrea Scozzafava, Claudiu T. Supuran. 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. Bioorganic and Medicinal Chemistry Letters, 2007, 17, pp.2795-2801. ⟨10.1016/j.bmcl.2007.02.068⟩. ⟨hal-00273205⟩

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