Hydroxylamine-O-sulfonamide is a versatile lead compound for the development of carbonic anhydrase inhibitors-Reference-Cited by-同舟云学术

Hydroxylamine-O-sulfonamide is a versatile lead compound for the development of carbonic anhydrase inhibitors

Published:2015 Issue:57 Volume:51 Page:11519-11522
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Di Fiore Anna¹²³,Vergara Alessandro¹²³⁴⁵,Caterino Marco⁴⁵³,Alterio Vincenzo¹²³,Monti Simona M.¹²³,Ombouma Joanna⁶⁷⁸⁹¹⁰,Dumy Pascal⁶⁷⁸⁹¹⁰,Vullo Daniela¹¹¹²¹³¹⁴³,Supuran Claudiu T.¹¹¹²¹³¹⁴³,Winum Jean-Yves⁶⁷⁸⁹¹⁰,De Simone Giuseppina¹²³

Affiliation:

1. Istituto di Biostrutture e Bioimmagini-CNR

2. 80134 Napoli

3. Italy

4. Department of Chemical Sciences

5. Napoli

6. Institut des Biomolécules Max Mousseron (IBMM) UMR 5247 CNRS

7. ENSCM

8. Université de Montpellier

9. Bâtiment de Recherche Max Mousseron

10. Ecole Nationale Supérieure de Chimie de Montpellier

11. Università degli Studi di Firenze

12. Polo Scientifico

13. Laboratorio di Chimica Bioinorganica

14. Florence

Abstract

Hydroxylamine-O-sulfonamide has been investigated as CA inhibitor by means of kinetic and structural studies clarifying its mechanism of action.

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2015/CC/C5CC03711E

Reference28 articles.

1. Multiple Binding Modes of Inhibitors to Carbonic Anhydrases: How to Design Specific Drugs Targeting 15 Different Isoforms?

2. Carbonic anhydrases: novel therapeutic applications for inhibitors and activators

3. The zinc coordination pattern in the η-carbonic anhydrase from Plasmodium falciparum is different from all other carbonic anhydrase genetic families

4. Carbonic anhydrase inhibitors as emerging drugs for the treatment of obesity

5. Recent Advances in Structural Studies of the Carbonic Anhydrase Family: The Crystal Structure of Human CA IX and CA XIII

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