Structure and mechanism of secondary sulfonamide binding to carbonic anhydrases-Reference-Cited by-同舟云学术

Structure and mechanism of secondary sulfonamide binding to carbonic anhydrases

Published:2021-07-30 Issue:7 Volume:50 Page:993-1011
ISSN:0175-7571
Container-title:European Biophysics Journal
language:en
Short-container-title:Eur Biophys J

Author:

Baronas Denis,Dudutienė Virginija,Paketurytė Vaida,Kairys Visvaldas,Smirnov Alexey,Juozapaitienė Vaida,Vaškevičius Aivaras,Manakova Elena,Gražulis Saulius,Zubrienė Asta,Matulis Daumantas^ORCID

Funder

Lietuvos Mokslo Taryba

Publisher

Springer Science and Business Media LLC

Subject

General Medicine,Biophysics

Link

https://link.springer.com/content/pdf/10.1007/s00249-021-01561-1.pdf

Reference64 articles.

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2. Alp C, Maresca A, Alp NA, Gültekin MS, Ekinci D, Scozzafava A, Supuran CT (2013) Secondary/tertiary benzenesulfonamides with inhibitory action against the cytosolic human carbonic anhydrase isoforms I and II. J Enzyme Inhib Med Chem 28(2):294–298. https://doi.org/10.3109/14756366.2012.658788

3. Andreini C, Bertini I, Cavallaro G, Holliday GL, Thornton JM (2008) Metal Ions in biological catalysis: from enzyme databases to general principles. J Biol Inorg Chem 13(8):1205–1218. https://doi.org/10.1007/s00775-008-0404-5

4. Baranauskienė L, Matulis D (2019) Catalytic activity and inhibition of human carbonic anhydrases. In: Matulis D (ed) Carbonic anhydrase as drug target: thermodynamics and structure of inhibitor binding. Springer International Publishing, Cham, pp 39–49. https://doi.org/10.1007/978-3-030-12780-0_3

5. Bieliauskas AV, Weerasinghe SVW, Negmeldin AT, Pflum MKH (2016) Structural requirements of histone deacetylase inhibitors: SAHA analogs modified on the hydroxamic acid. Arch Pharm 349(5):373–382. https://doi.org/10.1002/ardp.201500472

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