{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,16]],"date-time":"2026-10-16T21:21:12Z","timestamp":1792185672145,"version":"4.4.0"},"reference-count":95,"publisher":"Elsevier","isbn-type":[{"value":"9780443295188","type":"print"}],"license":[{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2024,1,1]],"date-time":"2024-01-01T00:00:00Z","timestamp":1704067200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2024]]},"DOI":"10.1016\/bs.enz.2024.06.006","type":"book-chapter","created":{"date-parts":[[2024,7,5]],"date-time":"2024-07-05T11:27:09Z","timestamp":1720178829000},"page":"143-191","source":"Crossref","is-referenced-by-count":1,"title":["Sulfonamide inhibitors of bacterial carbonic anhydrases"],"prefix":"10.1016","author":[{"given":"Alessio","family":"Nocentini","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"26","key":"10.1016\/bs.enz.2024.06.006_bib1","doi-asserted-by":"crossref","first-page":"15184","DOI":"10.1073\/pnas.96.26.15184","article-title":"Carbonic anhydrase is an ancient enzyme widespread in prokaryotes","volume":"96","author":"Smith","year":"1999","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/bs.enz.2024.06.006_bib2","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1152\/physrev.1967.47.4.595","article-title":"Carbonic anhydrase: chemistry, physiology, and inhibition","volume":"47","author":"Maren","year":"1967","journal-title":"Physiol. Rev."},{"issue":"14","key":"10.1016\/bs.enz.2024.06.006_bib3","doi-asserted-by":"crossref","first-page":"2023","DOI":"10.1042\/BCJ20160115","article-title":"Structure and function of carbonic anhydrases","volume":"473","author":"Supuran","year":"2016","journal-title":"Biochem. J."},{"issue":"1","key":"10.1016\/bs.enz.2024.06.006_bib4","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1186\/s12915-021-01039-8","article-title":"Characterization of a novel type of carbonic anhydrase that acts without metal cofactors","volume":"19","author":"Hirakawa","year":"2021","journal-title":"BMC Biol."},{"key":"10.1016\/bs.enz.2024.06.006_bib5","doi-asserted-by":"crossref","first-page":"4421","DOI":"10.1021\/cr200176r","article-title":"Multiple binding modes of inhibitors to carbonic anhydrases: how to design specific drugs targeting 15 different isoforms?","volume":"112","author":"Alterio","year":"2012","journal-title":"Chem. Rev."},{"key":"10.1016\/bs.enz.2024.06.006_bib6","series-title":"Carbonic Anhydrases","first-page":"151","article-title":"Human carbonic anhydrases: tissue distribution, physiological role, and druggability","author":"Nocentini","year":"2019"},{"key":"10.1016\/bs.enz.2024.06.006_bib7","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1038\/nrd2467","article-title":"Carbonic anhydrases: novel therapeutic applications for inhibitors and activators","volume":"7","author":"Supuran","year":"2008","journal-title":"Nat. Rev. Drug Discov."},{"issue":"10","key":"10.1016\/bs.enz.2024.06.006_bib8","doi-asserted-by":"crossref","first-page":"1233","DOI":"10.1042\/CS20210040","article-title":"Emerging role of carbonic anhydrase inhibitors","volume":"135","author":"Supuran","year":"2021","journal-title":"Clin. Sci."},{"key":"10.1016\/bs.enz.2024.06.006_bib9","doi-asserted-by":"crossref","first-page":"1689","DOI":"10.1517\/14728222.2015.1067685","article-title":"Bacterial, fungal and protozoan carbonic anhydrases as drug targets","volume":"19","author":"Capasso","year":"2015","journal-title":"Expert. Opin. Ther. Targets"},{"issue":"10","key":"10.1016\/bs.enz.2024.06.006_bib10","doi-asserted-by":"crossref","first-page":"897","DOI":"10.1080\/14728222.2023.2263914","article-title":"An overview of novel antimicrobial carbonic anhydrase inhibitors","volume":"27","author":"Supuran","year":"2023","journal-title":"Expert. Opin. Ther. Targets"},{"issue":"19","key":"10.1016\/bs.enz.2024.06.006_bib11","doi-asserted-by":"crossref","first-page":"1619","DOI":"10.4155\/fmc-2021-0207","article-title":"Bacterial carbonic anhydrases: underexploited antibacterial therapeutic targets","volume":"13","author":"Flaherty","year":"2021","journal-title":"Future Med. Chem."},{"issue":"2","key":"10.1016\/bs.enz.2024.06.006_bib12","doi-asserted-by":"crossref","first-page":"325","DOI":"10.3109\/14756366.2014.910202","article-title":"An overview of the alpha-, beta- and gamma-carbonic anhydrases from bacteria: can bacterial carbonic anhydrases shed new light on evolution of bacteria?","volume":"30","author":"Capasso","year":"2015","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"12","key":"10.1016\/bs.enz.2024.06.006_bib13","doi-asserted-by":"crossref","first-page":"963","DOI":"10.1080\/13543776.2020.1811853","article-title":"Antibacterial carbonic anhydrase inhibitors: an update on the recent literature","volume":"30","author":"Supuran","year":"2020","journal-title":"Expert. Opin. Ther. Pat."},{"issue":"1","key":"10.1016\/bs.enz.2024.06.006_bib14","doi-asserted-by":"crossref","first-page":"142","DOI":"10.3390\/antibiotics12010142","article-title":"Carbonic anhydrase inhibitors as novel antibacterials in the era of antibiotic resistance: where are we now?","volume":"12","author":"Nocentini","year":"2023","journal-title":"Antibiotics"},{"key":"10.1016\/bs.enz.2024.06.006_bib15","doi-asserted-by":"crossref","first-page":"345","DOI":"10.3109\/14756366.2015.1122001","article-title":"How many carbonic anhydrase inhibition mechanisms exist?","volume":"31","author":"Supuran","year":"2016","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"11","key":"10.1016\/bs.enz.2024.06.006_bib16","doi-asserted-by":"crossref","first-page":"1175","DOI":"10.1080\/17460441.2019.1651289","article-title":"Advances in the structural annotation of human carbonic anhydrases and impact on future drug discovery","volume":"14","author":"Nocentini","year":"2019","journal-title":"Expert. Opin. Drug Discov."},{"issue":"Pt 6","key":"10.1016\/bs.enz.2024.06.006_bib17","doi-asserted-by":"crossref","first-page":"1150","DOI":"10.1107\/S0907444913007208","article-title":"X-ray structure of the first 'extremo-alpha-carbonic anhydrase', a dimeric enzyme from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1","volume":"69","author":"Di Fiore","year":"2013","journal-title":"Acta Crystallogr. D. Biol. Crystallogr."},{"issue":"9","key":"10.1016\/bs.enz.2024.06.006_bib18","doi-asserted-by":"crossref","first-page":"2002","DOI":"10.1016\/j.bmcl.2015.02.068","article-title":"Crystal structure of the most catalytically effective carbonic anhydrase enzyme known, SazCA from the thermophilic bacterium Sulfurihydrogenibium azorense","volume":"25","author":"De Simone","year":"2015","journal-title":"Bioorg Med. Chem. Lett."},{"issue":"Pt 8","key":"10.1016\/bs.enz.2024.06.006_bib19","doi-asserted-by":"crossref","first-page":"1005","DOI":"10.1107\/S2053230X15010407","article-title":"Structure of alpha-carbonic anhydrase from the human pathogen Helicobacter pylori","volume":"71","author":"Compostella","year":"2015","journal-title":"Acta Crystallogr. Sect. F Struct. Biol. Commun."},{"key":"10.1016\/bs.enz.2024.06.006_bib20","series-title":"Carbonic Anhydrases","first-page":"19","article-title":"\u03b1-Carbonic anhydrases","author":"Di Fiore","year":"2019"},{"issue":"1","key":"10.1016\/bs.enz.2024.06.006_bib21","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1006\/jmbi.1998.2077","article-title":"Crystal structure of carbonic anhydrase from Neisseria gonorrhoeae and its complex with the inhibitor acetazolamide","volume":"283","author":"Huang","year":"1998","journal-title":"J. Mol. Biol."},{"issue":"1","key":"10.1016\/bs.enz.2024.06.006_bib22","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1021\/acsmedchemlett.2c00471","article-title":"Structural characterization of thiadiazolesulfonamide inhibitors bound to Neisseria gonorrhoeae \u03b1-carbonic anhydrase","volume":"14","author":"Marapaka","year":"2022","journal-title":"ACS Med. Chem. Lett."},{"issue":"5","key":"10.1016\/bs.enz.2024.06.006_bib23","article-title":"Structural basis for the inhibition of helicobacter pylori alpha-carbonic anhydrase by sulfonamides","volume":"10","author":"Modak","year":"2015","journal-title":"PLoS One"},{"issue":"24","key":"10.1016\/bs.enz.2024.06.006_bib24","doi-asserted-by":"crossref","first-page":"11098","DOI":"10.1021\/acs.jmedchem.6b01333","article-title":"Structure-activity relationship for sulfonamide inhibition of Helicobacter pylori alpha-carbonic anhydrase","volume":"59","author":"Modak","year":"2016","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.006_bib25","series-title":"Carbonic Anhydrases","first-page":"55","article-title":"\u03b2-Carbonic anhydrases","author":"Murray","year":"2019"},{"issue":"15","key":"10.1016\/bs.enz.2024.06.006_bib26","doi-asserted-by":"crossref","first-page":"4831","DOI":"10.1016\/j.bmc.2015.05.029","article-title":"Structure and inhibition studies of a type II beta-carbonic anhydrase psCA3 from Pseudomonas aeruginosa","volume":"23","author":"Pinard","year":"2015","journal-title":"Bioorg Med. Chem."},{"issue":"19","key":"10.1016\/bs.enz.2024.06.006_bib27","doi-asserted-by":"crossref","first-page":"18782","DOI":"10.1074\/jbc.M414348200","article-title":"Structure and function of carbonic anhydrases from Mycobacterium tuberculosis","volume":"280","author":"Suarez Covarrubias","year":"2005","journal-title":"J. Biol. Chem."},{"issue":"12","key":"10.1016\/bs.enz.2024.06.006_bib28","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0028458","article-title":"Structural studies of \u03b2-carbonic anhydrase from the green alga Coccomyxa: inhibitor complexes with anions and acetazolamide","volume":"6","author":"Huang","year":"2011","journal-title":"PLoS One"},{"issue":"19","key":"10.1016\/bs.enz.2024.06.006_bib29","doi-asserted-by":"crossref","first-page":"2024","DOI":"10.1002\/cmdc.201800375","article-title":"Structural mapping of anion inhibitors to \u03b2-carbonic anhydrase psCA3 from Pseudomonas aeruginosa","volume":"13","author":"Murray","year":"2018","journal-title":"ChemMedChem"},{"key":"10.1016\/bs.enz.2024.06.006_bib30","series-title":"Carbonic Anhydrases","first-page":"79","article-title":"\u03b3-Carbonic anhydrases","author":"Ferraroni","year":"2019"},{"key":"10.1016\/bs.enz.2024.06.006_bib31","doi-asserted-by":"crossref","first-page":"2323","DOI":"10.1002\/j.1460-2075.1996.tb00588.x","article-title":"A left-handed \u03b2-helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila","volume":"15","author":"Kisker","year":"1996","journal-title":"EMBO J."},{"issue":"Pt 8","key":"10.1016\/bs.enz.2024.06.006_bib32","doi-asserted-by":"crossref","first-page":"920","DOI":"10.1107\/S0907444912017210","article-title":"Structures of the \u03b3-class carbonic anhydrase homologue YrdA suggest a possible allosteric switch","volume":"68","author":"Park","year":"2012","journal-title":"Acta Crystallogr. D. Biol. Crystallogr."},{"issue":"1","key":"10.1016\/bs.enz.2024.06.006_bib33","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1080\/14756366.2020.1862102","article-title":"Inhibition of \u03b1-, \u03b2- and \u03b3-carbonic anhydrases from the pathogenic bacterium Vibrio cholerae with aromatic sulphonamides and clinically licenced drugs\u2014a joint docking\/molecular dynamics study","volume":"36","author":"Bonardi","year":"2021","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"6","key":"10.1016\/bs.enz.2024.06.006_bib34","doi-asserted-by":"crossref","first-page":"2117","DOI":"10.1021\/jm0512600","article-title":"Carbonic anhydrase inhibitors: DNA cloning and inhibition studies of the alpha-carbonic anhydrase from Helicobacter pylori, a new target for developing sulfonamide and sulfamate gastric drugs","volume":"49","author":"Nishimori","year":"2006","journal-title":"J. Med. Chem."},{"issue":"13","key":"10.1016\/bs.enz.2024.06.006_bib35","doi-asserted-by":"crossref","first-page":"3585","DOI":"10.1016\/j.bmcl.2007.04.063","article-title":"Carbonic anhydrase inhibitors: the beta-carbonic anhydrase from Helicobacter pylori is a new target for sulfonamide and sulfamate inhibitors","volume":"17","author":"Nishimori","year":"2007","journal-title":"Bioorg Med. Chem. Lett."},{"issue":"8","key":"10.1016\/bs.enz.2024.06.006_bib36","doi-asserted-by":"crossref","first-page":"2226","DOI":"10.1021\/jm9000488","article-title":"Molecular cloning, characterization, and inhibition studies of the Rv1284 beta-carbonic anhydrase from Mycobacterium tuberculosis with sulfonamides and a sulfamate","volume":"52","author":"Minakuchi","year":"2009","journal-title":"J. Med. Chem."},{"issue":"23","key":"10.1016\/bs.enz.2024.06.006_bib37","doi-asserted-by":"crossref","first-page":"6649","DOI":"10.1016\/j.bmcl.2009.10.009","article-title":"Carbonic anhydrase inhibitors. Characterization and inhibition studies of the most active beta-carbonic anhydrase from Mycobacterium tuberculosis, Rv3588c","volume":"19","author":"Carta","year":"2009","journal-title":"Bioorg Med. Chem. Lett."},{"issue":"9","key":"10.1016\/bs.enz.2024.06.006_bib38","doi-asserted-by":"crossref","first-page":"3116","DOI":"10.1021\/jm9003126","article-title":"Carbonic anhydrase inhibitors. Cloning, characterization, and inhibition studies of a new beta-carbonic anhydrase from Mycobacterium tuberculosis","volume":"52","author":"Nishimori","year":"2009","journal-title":"J. Med. Chem."},{"issue":"5","key":"10.1016\/bs.enz.2024.06.006_bib39","doi-asserted-by":"crossref","first-page":"2277","DOI":"10.1021\/jm901855h","article-title":"Cloning, characterization, and inhibition studies of a beta-carbonic anhydrase from Brucella suis","volume":"53","author":"Joseph","year":"2010","journal-title":"J. Med. Chem."},{"issue":"3","key":"10.1016\/bs.enz.2024.06.006_bib40","doi-asserted-by":"crossref","first-page":"1172","DOI":"10.1016\/j.bmc.2010.12.048","article-title":"A new \u03b2-carbonic anhydrase from Brucella suis, its cloning, characterization, and inhibition with sulfonamides and sulfamates, leading to impaired pathogen growth","volume":"19","author":"Joseph","year":"2011","journal-title":"Bioorg Med. Chem."},{"issue":"16","key":"10.1016\/bs.enz.2024.06.006_bib41","doi-asserted-by":"crossref","first-page":"5023","DOI":"10.1016\/j.bmc.2011.06.038","article-title":"Inhibition studies of the \u03b2-carbonic anhydrases from the bacterial pathogen Salmonella enterica serovar Typhimurium with sulfonamides and sulfamates","volume":"19","author":"Nishimori","year":"2011","journal-title":"Bioorg Med. Chem."},{"issue":"23","key":"10.1016\/bs.enz.2024.06.006_bib42","doi-asserted-by":"crossref","first-page":"10742","DOI":"10.1021\/jm301611m","article-title":"DNA cloning, characterization, and inhibition studies of an \u03b1-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae","volume":"55","author":"Del Prete","year":"2012","journal-title":"J. Med. Chem."},{"issue":"5","key":"10.1016\/bs.enz.2024.06.006_bib43","doi-asserted-by":"crossref","first-page":"1115","DOI":"10.1016\/j.bmc.2016.01.037","article-title":"Sulfonamide inhibition studies of the \u03b2-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae","volume":"24","author":"Del Prete","year":"2016","journal-title":"Bioorg Med. Chem."},{"issue":"8","key":"10.1016\/bs.enz.2024.06.006_bib44","doi-asserted-by":"crossref","first-page":"1941","DOI":"10.1016\/j.bmcl.2016.03.014","article-title":"Comparison of the sulfonamide inhibition profiles of the \u03b1-, \u03b2- and \u03b3-carbonic anhydrases from the pathogenic bacterium Vibrio cholerae","volume":"26","author":"Del Prete","year":"2016","journal-title":"Bioorg Med. Chem. Lett."},{"issue":"17","key":"10.1016\/bs.enz.2024.06.006_bib45","doi-asserted-by":"crossref","first-page":"4537","DOI":"10.1016\/j.bmc.2014.07.048","article-title":"Sulfonamide inhibition study of the carbonic anhydrases from the bacterial pathogen Porphyromonas gingivalis: the \u03b2-class (PgiCAb) versus the \u03b3-class (PgiCA) enzymes","volume":"22","author":"Del Prete","year":"2014","journal-title":"Bioorg Med. Chem."},{"issue":"11","key":"10.1016\/bs.enz.2024.06.006_bib46","doi-asserted-by":"crossref","first-page":"2939","DOI":"10.1016\/j.bmc.2014.04.006","article-title":"Sulfonamide inhibition studies of two \u03b2-carbonic anhydrases from the bacterial pathogen Legionella pneumophila","volume":"22","author":"Nishimori","year":"2014","journal-title":"Bioorg Med. Chem."},{"issue":"11","key":"10.1016\/bs.enz.2024.06.006_bib47","doi-asserted-by":"crossref","first-page":"2291","DOI":"10.1016\/j.bmcl.2015.04.037","article-title":"Sulfonamide inhibition study of the \u03b2-class carbonic anhydrase from the caries producing pathogen Streptococcus mutans","volume":"25","author":"Dedeoglu","year":"2015","journal-title":"Bioorg Med. Chem. Lett."},{"issue":"3","key":"10.1016\/bs.enz.2024.06.006_bib48","doi-asserted-by":"crossref","first-page":"421","DOI":"10.3390\/molecules22030421","article-title":"Comparison of the sulfonamide inhibition profiles of the \u03b2- and \u03b3-carbonic anhydrases from the pathogenic bacterium Burkholderia pseudomallei","volume":"22","author":"Vullo","year":"2017","journal-title":"Molecules"},{"issue":"13","key":"10.1016\/bs.enz.2024.06.006_bib49","doi-asserted-by":"crossref","first-page":"3555","DOI":"10.1016\/j.bmc.2017.05.007","article-title":"Sulfonamide inhibition profiles of the \u03b2-carbonic anhydrase from the pathogenic bacterium Francisella tularensis responsible of the febrile illness tularemia","volume":"25","author":"Del Prete","year":"2017","journal-title":"Bioorg Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2024.06.006_bib50","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1080\/14756366.2017.1388233","article-title":"Sulphonamide inhibition studies of the \u03b2-carbonic anhydrase from the bacterial pathogen Clostridium perfringens","volume":"33","author":"Vullo","year":"2018","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"11","key":"10.1016\/bs.enz.2024.06.006_bib51","doi-asserted-by":"crossref","first-page":"4175","DOI":"10.3390\/ijms21114175","article-title":"The effect of substituted benzene-sulfonamides and clinically licensed drugs on the catalytic activity of CynT2, a carbonic anhydrase crucial for Escherichia coli life cycle","volume":"21","author":"Del Prete","year":"2020","journal-title":"Int. J. Mol. Sci."},{"issue":"1","key":"10.1016\/bs.enz.2024.06.006_bib52","doi-asserted-by":"crossref","first-page":"1545","DOI":"10.1080\/14756366.2020.1800670","article-title":"Escherichia coli \u03b3-carbonic anhydrase: characterisation and effects of simple aromatic\/heterocyclic sulphonamide inhibitors","volume":"35","author":"Del Prete","year":"2020","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"22","key":"10.1016\/bs.enz.2024.06.006_bib53","doi-asserted-by":"crossref","first-page":"13827","DOI":"10.3390\/ijms232213827","article-title":"May sulfonamide inhibitors of carbonic anhydrases from Mammaliicoccus sciuri prevent antimicrobial resistance due to gene transfer to other harmful Staphylococci?","volume":"23","author":"De Luca","year":"2022","journal-title":"Int. J. Mol. Sci."},{"issue":"6","key":"10.1016\/bs.enz.2024.06.006_bib54","doi-asserted-by":"crossref","first-page":"1534","DOI":"10.1016\/j.bmc.2012.07.024","article-title":"The alpha-carbonic anhydrase from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1 is highly susceptible to inhibition by sulfonamides","volume":"21","author":"Vullo","year":"2013","journal-title":"Bioorg Med. Chem."},{"issue":"15","key":"10.1016\/bs.enz.2024.06.006_bib55","doi-asserted-by":"crossref","first-page":"4521","DOI":"10.1016\/j.bmc.2013.05.042","article-title":"The extremo-\u03b1-carbonic anhydrase from the thermophilic bacterium Sulfurihydrogenibium azorense is highly inhibited by sulfonamides","volume":"21","author":"Vullo","year":"2013","journal-title":"Bioorg. Med. Chem."},{"issue":"4","key":"10.1016\/bs.enz.2024.06.006_bib56","doi-asserted-by":"crossref","first-page":"1253","DOI":"10.1016\/j.bmcl.2016.01.023","article-title":"Sulfonamide inhibition studies of the \u03b3-carbonic anhydrase from the Antarctic bacterium Colwellia psychrerythraea","volume":"26","author":"Vullo","year":"2016","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"8","key":"10.1016\/bs.enz.2024.06.006_bib57","doi-asserted-by":"crossref","first-page":"1728","DOI":"10.1016\/j.bmc.2015.02.045","article-title":"Sulfonamide inhibition studies of the \u03b3-carbonic anhydrase from the Antarctic cyanobacterium Nostoc commune","volume":"23","author":"Vullo","year":"2015","journal-title":"Bioorg. Med. Chem."},{"issue":"17","key":"10.1016\/bs.enz.2024.06.006_bib58","doi-asserted-by":"crossref","first-page":"3550","DOI":"10.1016\/j.bmcl.2015.06.079","article-title":"Sulfonamide inhibition studies of the \u03b3-carbonic anhydrase from the Antarctic bacterium Pseudoalteromonas haloplanktis","volume":"25","author":"Vullo","year":"2015","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"2","key":"10.1016\/bs.enz.2024.06.006_bib59","doi-asserted-by":"crossref","first-page":"571","DOI":"10.3390\/ijms22020571","article-title":"Effect of sulfonamides and their structurally related derivatives on the activity of \u03b9-carbonic anhydrase from Burkholderia territorii","volume":"22","author":"De Luca","year":"2021","journal-title":"Int. J. Mol. Sci."},{"issue":"13","key":"10.1016\/bs.enz.2024.06.006_bib60","doi-asserted-by":"crossref","first-page":"4063","DOI":"10.1021\/jm9004016","article-title":"Discovery of low nanomolar and subnanomolar inhibitors of the mycobacterial beta-carbonic anhydrases Rv1284 and Rv3273","volume":"52","author":"G\u00fczel","year":"2009","journal-title":"J. Med. Chem."},{"issue":"17","key":"10.1016\/bs.enz.2024.06.006_bib61","doi-asserted-by":"crossref","first-page":"4929","DOI":"10.1016\/j.bmcl.2009.07.088","article-title":"Carbonic anhydrase inhibitors. Inhibition of the Rv1284 and Rv3273 beta-carbonic anhydrases from Mycobacterium tuberculosis with diazenylbenzenesulfonamides","volume":"19","author":"Maresca","year":"2009","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"2","key":"10.1016\/bs.enz.2024.06.006_bib62","doi-asserted-by":"crossref","first-page":"384","DOI":"10.3109\/14756366.2011.645539","article-title":"Dihalogenated sulfanilamides and benzolamides are effective inhibitors of the three \u03b2-class carbonic anhydrases from Mycobacterium tuberculosis","volume":"28","author":"Maresca","year":"2013","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"18","key":"10.1016\/bs.enz.2024.06.006_bib63","doi-asserted-by":"crossref","first-page":"5210","DOI":"10.1016\/j.bmcl.2011.07.045","article-title":"Synthesis of rhodamine B-benzenesulfonamide conjugates and their inhibitory activity against human \u03b1- and bacterial\/fungal \u03b2-carbonic anhydrases","volume":"21","author":"Rami","year":"2011","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"1","key":"10.1016\/bs.enz.2024.06.006_bib64","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1016\/j.bmcl.2010.11.064","article-title":"Inhibition of \u03b2-carbonic anhydrases with ureido-substituted benzenesulfonamides","volume":"21","author":"Pacchiano","year":"2011","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"5","key":"10.1016\/bs.enz.2024.06.006_bib65","doi-asserted-by":"crossref","first-page":"686","DOI":"10.3109\/14756366.2013.842233","article-title":"Sulfonamides incorporating fluorine and 1,3,5-triazine moieties are effective inhibitors of three \u03b2-class carbonic anhydrases from Mycobacterium tuberculosis","volume":"29","author":"Ceruso","year":"2014","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"5","key":"10.1016\/bs.enz.2024.06.006_bib66","doi-asserted-by":"crossref","first-page":"2584","DOI":"10.3390\/ijms25052584","article-title":"Benzothiadiazinone-1,1-dioxide carbonic anhydrase inhibitors suppress the growth of drug-resistant Mycobacterium tuberculosis strains","volume":"25","author":"Bua","year":"2024","journal-title":"Int. J. Mol. Sci."},{"issue":"1","key":"10.1016\/bs.enz.2024.06.006_bib67","doi-asserted-by":"crossref","first-page":"1660","DOI":"10.1080\/14756366.2019.1663416","article-title":"Anti-Helicobacter pylori activity of ethoxzolamide","volume":"34","author":"Modak","year":"2019","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"7","key":"10.1016\/bs.enz.2024.06.006_bib68","doi-asserted-by":"crossref","first-page":"2178","DOI":"10.1016\/j.bmcl.2010.02.042","article-title":"Inhibition studies of a beta-carbonic anhydrase from Brucella suis with a series of water soluble glycosyl sulfanilamides","volume":"20","author":"Vullo","year":"2010","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"6","key":"10.1016\/bs.enz.2024.06.006_bib69","doi-asserted-by":"crossref","first-page":"1010","DOI":"10.3109\/14756366.2014.986119","article-title":"N-glycosyl-N-hydroxysulfamides as potent inhibitors of Brucella suis carbonic anhydrases","volume":"30","author":"Ombouma","year":"2015","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2024.06.006_bib70","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1080\/14756366.2017.1413097","article-title":"Inhibition studies of Brucella suis \u03b2-carbonic anhydrases with a series of 4-substituted pyridine-3-sulphonamides","volume":"33","author":"Monti","year":"2018","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"15","key":"10.1016\/bs.enz.2024.06.006_bib71","doi-asserted-by":"crossref","first-page":"4181","DOI":"10.1016\/j.bmc.2015.06.050","article-title":"Inhibition studies of bacterial, fungal and protozoan \u03b2-class carbonic anhydrases with Schiff bases incorporating sulfonamide moieties","volume":"23","author":"Ceruso","year":"2015","journal-title":"Bioorg. Med. Chem."},{"issue":"21","key":"10.1016\/bs.enz.2024.06.006_bib72","doi-asserted-by":"crossref","first-page":"6794","DOI":"10.1016\/j.bmc.2015.10.006","article-title":"Poly(amidoamine) dendrimers show carbonic anhydrase inhibitory activity against \u03b1-, \u03b2-, \u03b3- and \u03b7-class enzymes","volume":"23","author":"Carta","year":"2015","journal-title":"Bioorg. Med. Chem."},{"issue":"16","key":"10.1016\/bs.enz.2024.06.006_bib73","doi-asserted-by":"crossref","first-page":"4006","DOI":"10.1016\/j.bmcl.2014.06.024","article-title":"Synthesis of sulfonamides with effective inhibitory action against Porphyromonas gingivalis \u03b3-carbonic anhydrase","volume":"24","author":"Ceruso","year":"2014","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"4","key":"10.1016\/bs.enz.2024.06.006_bib74","doi-asserted-by":"crossref","first-page":"592","DOI":"10.3109\/14756366.2014.957202","article-title":"Inhibition studies of quinazoline-sulfonamide derivatives against the \u03b3-CA (PgiCA) from the pathogenic bacterium, Porphyromonas gingivalis","volume":"30","author":"Alafeefy","year":"2015","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"19","key":"10.1016\/bs.enz.2024.06.006_bib75","doi-asserted-by":"crossref","first-page":"5133","DOI":"10.1016\/j.bmc.2014.08.015","article-title":"Quinazoline-sulfonamides with potent inhibitory activity against the \u03b1-carbonic anhydrase from Vibrio cholerae","volume":"22","author":"Alafeefy","year":"2014","journal-title":"Bioorg. Med. Chem."},{"issue":"11","key":"10.1016\/bs.enz.2024.06.006_bib76","doi-asserted-by":"crossref","first-page":"5202","DOI":"10.1128\/IAI.00983-09","article-title":"Bicarbonate induces Vibrio cholerae virulence gene expression by enhancing ToxT activity","volume":"77","author":"Abuaita","year":"2009","journal-title":"Infect. Immun."},{"issue":"8","key":"10.1016\/bs.enz.2024.06.006_bib77","doi-asserted-by":"crossref","first-page":"2524","DOI":"10.1016\/j.bmc.2017.03.017","article-title":"Synthesis and human\/bacterial carbonic anhydrase inhibition with a series of sulfonamides incorporating phthalimido moieties","volume":"25","author":"Mohamed","year":"2017","journal-title":"Bioorg. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2024.06.006_bib78","doi-asserted-by":"crossref","first-page":"1186","DOI":"10.1080\/14756366.2019.1618292","article-title":"Seeking new approach for therapeutic treatment of cholera disease via inhibition of bacterial carbonic anhydrases: experimental and theoretical studies for sixteen benzenesulfonamide derivatives","volume":"34","author":"Gitto","year":"2019","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"11","key":"10.1016\/bs.enz.2024.06.006_bib79","doi-asserted-by":"crossref","first-page":"2294","DOI":"10.1021\/acsmedchemlett.0c00417","article-title":"In silico-guided identification of new potent inhibitors of carbonic anhydrases expressed in Vibrio cholerae","volume":"11","author":"Mancuso","year":"2020","journal-title":"ACS Med. Chem. Lett."},{"issue":"24","key":"10.1016\/bs.enz.2024.06.006_bib80","doi-asserted-by":"crossref","first-page":"3787","DOI":"10.1002\/cmdc.202100510","article-title":"4-Sulfamoylphenylalkylamides as inhibitors of carbonic anhydrases expressed in Vibrio cholerae","volume":"16","author":"Mancuso","year":"2021","journal-title":"ChemMedChem"},{"issue":"1","key":"10.1016\/bs.enz.2024.06.006_bib81","doi-asserted-by":"crossref","DOI":"10.1080\/14756366.2023.2201402","article-title":"Benzenesulfonamide derivatives as Vibrio cholerae carbonic anhydrases inhibitors: a computational-aided insight in the structural rigidity-activity relationships","volume":"38","author":"Fantacuzzi","year":"2023","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.006_bib82","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2021.113444","article-title":"Taurultams incorporating arylsulfonamide: first in vitro inhibition studies of \u03b1-, \u03b2- and \u03b3-class Carbonic Anhydrases from Vibrio cholerae and Burkholderia pseudomallei","volume":"219","author":"Akgul","year":"2021","journal-title":"Eur. J. Med. Chem."},{"issue":"24","key":"10.1016\/bs.enz.2024.06.006_bib83","doi-asserted-by":"crossref","first-page":"2444","DOI":"10.1002\/cmdc.202000680","article-title":"Benzylaminoethylureido-tailed benzenesulfonamides show potent inhibitory activity against bacterial carbonic anhydrases","volume":"15","author":"Ali","year":"2020","journal-title":"ChemMedChem"},{"key":"10.1016\/bs.enz.2024.06.006_bib84","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/j.bioorg.2019.01.065","article-title":"Click-tailed benzenesulfonamides as potent bacterial carbonic anhydrase inhibitors for targeting Mycobacterium tuberculosis and Vibrio cholerae","volume":"86","author":"Bua","year":"2019","journal-title":"Bioorg. Chem."},{"key":"10.1016\/bs.enz.2024.06.006_bib85","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1016\/j.bioorg.2017.09.016","article-title":"Acyl selenoureido benzensulfonamides show potent inhibitory activity against carbonic anhydrases from the pathogenic bacterium Vibrio cholerae","volume":"75","author":"Angeli","year":"2017","journal-title":"Bioorg. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2024.06.006_bib86","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1080\/14756366.2018.1547287","article-title":"Inhibition of bacterial \u03b1-, \u03b2- and \u03b3-class carbonic anhydrases with selenazoles incorporating benzenesulfonamide moieties","volume":"34","author":"Angeli","year":"2019","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"2","key":"10.1016\/bs.enz.2024.06.006_bib87","doi-asserted-by":"crossref","first-page":"598","DOI":"10.3390\/ijms21020598","article-title":"Evaluation of thio- and seleno-acetamides bearing benzenesulfonamide as inhibitor of carbonic anhydrases from different pathogenic bacteria","volume":"21","author":"Angeli","year":"2020","journal-title":"Int. J. Mol. Sci."},{"issue":"11","key":"10.1016\/bs.enz.2024.06.006_bib88","doi-asserted-by":"crossref","first-page":"9610","DOI":"10.3390\/ijms24119610","article-title":"Photoactivatable heptamethine-based carbonic anhydrase inhibitors leading to new anti-antibacterial agents","volume":"24","author":"Carradori","year":"2023","journal-title":"Int. J. Mol. Sci."},{"issue":"7","key":"10.1016\/bs.enz.2024.06.006_bib89","doi-asserted-by":"crossref","first-page":"1969","DOI":"10.1021\/acsinfecdis.1c00055","article-title":"Structure-activity relationship studies of acetazolamide-based carbonic anhydrase inhibitors with activity against Neisseria gonorrhoeae","volume":"7","author":"Ewitt","year":"2021","journal-title":"ACS Infect. Dis."},{"issue":"1","key":"10.1016\/bs.enz.2024.06.006_bib90","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1080\/14756366.2021.1991336","article-title":"Repurposing FDA-approved sulphonamide carbonic anhydrase inhibitors for treatment of Neisseria gonorrhoeae","volume":"37","author":"Abutaleb","year":"2022","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.006_bib91","doi-asserted-by":"crossref","DOI":"10.1016\/j.micpath.2022.105454","article-title":"In vivo efficacy of acetazolamide in a mouse model of Neisseria gonorrhoeae infection","volume":"164","author":"Abutaleb","year":"2022","journal-title":"Microb. Pathog."},{"issue":"17","key":"10.1016\/bs.enz.2024.06.006_bib92","doi-asserted-by":"crossref","first-page":"9540","DOI":"10.1021\/acs.jmedchem.0c00734","article-title":"Optimization of acetazolamide-based scaffold as potent inhibitors of vancomycin-resistant Enterococcus","volume":"63","author":"Kaur","year":"2020","journal-title":"J. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2024.06.006_bib93","doi-asserted-by":"crossref","first-page":"1838","DOI":"10.1080\/14756366.2022.2092729","article-title":"Structure-activity relationship studies for inhibitors for vancomycin-resistant Enterococcus and human carbonic anhydrases","volume":"37","author":"An","year":"2022","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"4","key":"10.1016\/bs.enz.2024.06.006_bib94","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1021\/acsmedchemlett.3c00032","article-title":"Evaluation of 1,3,4-thiadiazole carbonic anhydrase inhibitors for gut decolonization of vancomycin-resistant Enterococci","volume":"14","author":"Abutaleb","year":"2023","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2024.06.006_bib95","doi-asserted-by":"crossref","DOI":"10.1021\/acs.jmedchem.4c00740","article-title":"Development of penicillin-based carbonic anhydrase inhibitors targeting multidrug-resistant Neisseria gonorrhoeae","author":"Bonardi","year":"2024","journal-title":"J. Med. Chem."}],"container-title":["The Enzymes","Bacterial Carbonic Anhydrases"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874604724000234?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874604724000234?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,8,31]],"date-time":"2024-08-31T11:20:44Z","timestamp":1725103244000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1874604724000234"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024]]},"ISBN":["9780443295188"],"references-count":95,"URL":"https:\/\/doi.org\/10.1016\/bs.enz.2024.06.006","relation":{},"ISSN":["1874-6047"],"issn-type":[{"value":"1874-6047","type":"print"}],"subject":[],"published":{"date-parts":[[2024]]}}}