A nuclear-magnetic-resonance study of the binding of novel N-hydroxybenzenesulphonamide carbonic anhydrase inhibitors to native and cadmium-111-substituted carbonic anhydrase-Reference-Cited by-同舟云学术

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A nuclear-magnetic-resonance study of the binding of novel N-hydroxybenzenesulphonamide carbonic anhydrase inhibitors to native and cadmium-111-substituted carbonic anhydrase

Published:1985-12 Issue:3 Volume:153 Page:553-558
ISSN:0014-2956
Container-title:European Journal of Biochemistry
language:en
Short-container-title:Eur J Biochem

Author:

BLACKBURN G. Michael,MANN Brain E.,TAYLOR Brain F.,WORRALL Andrew F.

Publisher

Wiley

Subject

Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1985.tb09336.x/fullpdf

Reference22 articles.

1. Carbonic Anhydrase

2. Sulphanilamide as a Specific Inhibitor of Carbonic Anhydrase

3. Inhibition of carbonic anhydrase by sulphonamides

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2. Structure and mechanism of secondary sulfonamide binding to carbonic anhydrases;European Biophysics Journal;2021-07-30

3. Nature of S–N Bonding in Sulfonamides and Related Compounds: Insights into π-Bonding Contributions from Sulfur K-Edge X-ray Absorption Spectroscopy;The Journal of Physical Chemistry A;2021-01-07

4. The pH of HNO donation is modulated by ring substituents in Piloty's acid derivatives: azanone donors at biological pH;Journal of Inorganic Biochemistry;2013-01

5. Nitroxyl (azanone) trapping by metalloporphyrins;Coordination Chemistry Reviews;2011-12

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