{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,29]],"date-time":"2026-04-29T19:31:13Z","timestamp":1777491073728,"version":"3.51.4"},"reference-count":36,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2019,5,1]],"date-time":"2019-05-01T00:00:00Z","timestamp":1556668800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Bioorganic Chemistry"],"published-print":{"date-parts":[[2019,5]]},"DOI":"10.1016\/j.bioorg.2019.01.065","type":"journal-article","created":{"date-parts":[[2019,1,30]],"date-time":"2019-01-30T06:35:30Z","timestamp":1548830130000},"page":"183-186","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":24,"special_numbering":"C","title":["Click-tailed benzenesulfonamides as potent bacterial carbonic anhydrase inhibitors for targeting Mycobacterium tuberculosis and Vibrio cholerae"],"prefix":"10.1016","volume":"86","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-0107-2682","authenticated-orcid":false,"given":"Silvia","family":"Bua","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sameh M.","family":"Osman","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sonia","family":"Del Prete","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Clemente","family":"Capasso","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Zeid","family":"AlOthman","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3342-702X","authenticated-orcid":false,"given":"Alessio","family":"Nocentini","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Claudiu T.","family":"Supuran","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bioorg.2019.01.065_b0005","doi-asserted-by":"crossref","unstructured":"Eric S. Sulfonamides. Reference Module in Biomedical Sciences, xPharm: The Comprehensive Pharmacology Reference, 2007, pp. 1\u20134.","DOI":"10.1016\/B978-008055232-3.61013-X"},{"key":"10.1016\/j.bioorg.2019.01.065_b0010","doi-asserted-by":"crossref","unstructured":"Greenwood D. Sulfonamides, Antibiotic and chemotherapy. 9th ed., 2010 (Chapter 29).","DOI":"10.1016\/B978-0-7020-4064-1.00029-4"},{"key":"10.1016\/j.bioorg.2019.01.065_b0015","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1517\/13543776.2012.698264","article-title":"Sulfonamides: a patent review (2008\u20132012)","volume":"22","author":"Carta","year":"2012","journal-title":"Expert Opin. Ther. Pat."},{"key":"10.1016\/j.bioorg.2019.01.065_b0020","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."},{"key":"10.1016\/j.bioorg.2019.01.065_b0025","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."},{"key":"10.1016\/j.bioorg.2019.01.065_b0030","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\/j.bioorg.2019.01.065_b0035","doi-asserted-by":"crossref","first-page":"4389","DOI":"10.1016\/j.bmcl.2014.08.015","article-title":"Discovery of a new family of carbonic anhydrases in the malaria pathogen Plasmodium falciparum. The \u03b7-carbonic anhydrases","volume":"18","author":"Del Prete","year":"2014","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.bioorg.2019.01.065_b0040","doi-asserted-by":"crossref","first-page":"9828","DOI":"10.1073\/pnas.1603112113","article-title":"Thylakoid luminal theta-carbonic anhydrase critical for growth and photosynthesis in the marine diatom phaeodactylum tricornutum","volume":"113","author":"Kikutani","year":"2016","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.bioorg.2019.01.065_b0045","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1080\/13543776.2018.1497161","article-title":"Biomedical applications of prokaryotic carbonic anhydrases","volume":"28","author":"Supuran","year":"2018","journal-title":"Expert Opin Ther Pat."},{"key":"10.1016\/j.bioorg.2019.01.065_b0050","doi-asserted-by":"crossref","first-page":"962","DOI":"10.1080\/14756366.2018.1471475","article-title":"Evaluation of sulphonamide derivatives acting as inhibitors of human carbonic anhydrase isoforms I, II and Mycobacterium tuberculosis \u03b2-class enzyme Rv3273","volume":"33","author":"Wani","year":"2018","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/j.bioorg.2019.01.065_b0055","unstructured":"<http:\/\/www.who.int\/en\/news-room\/fact-sheets\/detail\/tuberculosis>."},{"key":"10.1016\/j.bioorg.2019.01.065_b0060","unstructured":"<http:\/\/www.who.int\/gho\/epidemic_diseases\/cholera\/en\/>."},{"key":"10.1016\/j.bioorg.2019.01.065_b0065","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1099\/jmm.0.023051-0","article-title":"Antibiotic resistance mechanisms of Vibrio cholerae","volume":"60","author":"Kitaoka","year":"2011","journal-title":"J. Med. Microbiol."},{"key":"10.1016\/j.bioorg.2019.01.065_b0070","unstructured":"http:\/\/www.who.int\/cholera\/publications\/global-roadmap\/en\/."},{"key":"10.1016\/j.bioorg.2019.01.065_b0075","unstructured":"<https:\/\/www.who.int\/sdg\/targets\/en\/>."},{"key":"10.1016\/j.bioorg.2019.01.065_b0080","doi-asserted-by":"crossref","first-page":"3300","DOI":"10.2174\/138161210793429814","article-title":"The \u03b2-carbonic anhydrases from Mycobacterium tuberculosis as drug targets","volume":"16","author":"Nishimori","year":"2010","journal-title":"Curr. Pharm. Des."},{"key":"10.1016\/j.bioorg.2019.01.065_b0085","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."},{"key":"10.1016\/j.bioorg.2019.01.065_b0090","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."},{"key":"10.1016\/j.bioorg.2019.01.065_b0095","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."},{"key":"10.1016\/j.bioorg.2019.01.065_b0100","doi-asserted-by":"crossref","first-page":"1125","DOI":"10.1080\/14756366.2018.1467901","article-title":"Synthesis of novel benzenesulfamide derivatives with inhibitory activity against human cytosolic carbonic anhydrase I and II and Vibrio cholerae \u03b1- and \u03b2-class enzymes","volume":"33","author":"Bua","year":"2018","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/j.bioorg.2019.01.065_b0105","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3109\/14756360903524304","article-title":"Pharmacological significance of triazole scaffold","volume":"26","author":"Kharb","year":"2011","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/j.bioorg.2019.01.065_b0110","doi-asserted-by":"crossref","first-page":"1195","DOI":"10.1016\/j.bmcl.2007.11.111","article-title":"Synthesis and antibiotic activity of a small molecules library of 1,2,3-triazole derivatives","volume":"18","author":"Aufort","year":"2008","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.bioorg.2019.01.065_b0115","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1016\/j.bioorg.2017.12.003","article-title":"Synthesis, anti-inflammatory, p38\u03b1 MAP kinase inhibitory activities and molecular docking studies of quinoxaline derivatives containing triazole moiety","volume":"76","author":"Tariq","year":"2018","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.bioorg.2019.01.065_b0120","first-page":"22(5)","article-title":"The hypnotic, anxiolytic, and antinociceptive profile of a novel \u03bc-opioid agonist","author":"Montes","year":"2017","journal-title":"Molecules"},{"key":"10.1016\/j.bioorg.2019.01.065_b0125","doi-asserted-by":"crossref","first-page":"465","DOI":"10.2174\/1871520615666150819121106","article-title":"Recent developments on 1,2,4-triazole nucleus in anticancer compounds: a review","volume":"16","author":"Kaur","year":"2016","journal-title":"Anticancer Agents Med. Chem."},{"key":"10.1016\/j.bioorg.2019.01.065_b0130","doi-asserted-by":"crossref","first-page":"1155","DOI":"10.2174\/1570180814666170605120701","article-title":"Design, synthesis and in silico studies of new 5-substituted-2-(2-(5-aryl-1H-1,2,4-triazole-3-ylthio)acetyl) hydrazine carbothioamide\/ carboxamides for anticonvulsant activity","volume":"14","author":"Chelamalla","year":"2017","journal-title":"Lett. Drug. Des. Discov."},{"key":"10.1016\/j.bioorg.2019.01.065_b0135","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1016\/j.ejmech.2013.10.082","article-title":"Rational design and synthesis of novel dibenzo[b, d]furan-1,2,3-triazole conjugates as potent inhibitors of Mycobacterium tuberculosis","volume":"71","author":"Yempala","year":"2014","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.bioorg.2019.01.065_b0140","doi-asserted-by":"crossref","first-page":"10692","DOI":"10.1021\/acs.jmedchem.6b01389","article-title":"Benzenesulfonamides incorporating flexible triazole moieties are highly effective carbonic anhydrase inhibitors: synthesis and kinetic, crystallographic, computational, and intraocular pressure lowering investigations","volume":"59","author":"Nocentini","year":"2016","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bioorg.2019.01.065_b0145","doi-asserted-by":"crossref","first-page":"1314","DOI":"10.1021\/acsmedchemlett.7b00399","article-title":"Discovery of new sulfonamide carbonic anhydrase IX inhibitors incorporating nitrogenous bases","volume":"8","author":"Nocentini","year":"2017","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/j.bioorg.2019.01.065_b0150","doi-asserted-by":"crossref","first-page":"2561","DOI":"10.1016\/S0021-9258(18)62326-9","article-title":"The carbon dioxide hydration activity of carbonic anhydrase","volume":"246","author":"Khalifah","year":"1971","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bioorg.2019.01.065_h0155","doi-asserted-by":"crossref","first-page":"286","DOI":"10.1080\/14756366.2017.1414808","article-title":"Carbonic anhydrases from Trypanosoma cruzi and Leishmania donovani chagasi are inhibited by benzoxaboroles","volume":"33","author":"Nocentini","year":"2018","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/j.bioorg.2019.01.065_h0160","doi-asserted-by":"crossref","first-page":"1260","DOI":"10.1016\/j.bmc.2016.12.040","article-title":"Dithiocarbamates effectively inhibit the \u03b2-carbonic anhydrase from the dandruff-producing fungus Malassezia globosa","volume":"25","author":"Vullo","year":"2017","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.bioorg.2019.01.065_h0165","doi-asserted-by":"crossref","first-page":"5380","DOI":"10.1021\/acs.jmedchem.8b00625","article-title":"Discovery of \u03b2-adrenergic receptors blocker-carbonic anhydrase inhibitor hybrids for multitargeted antiglaucoma therapy","volume":"61","author":"Nocentini","year":"2018","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bioorg.2019.01.065_h0170","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1016\/j.bioorg.2018.01.023","article-title":"Discovery of thiazolin-4-one-based aromatic sulfamates as a new class of carbonic anhydrase isoforms I, II, IV, and IX inhibitors","volume":"77","author":"Nocentini","year":"2018","journal-title":"Bioorganic Chem."},{"key":"10.1016\/j.bioorg.2019.01.065_h0175","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.ejmech.2018.04.016","article-title":"Dual-tail arylsulfone-based benzenesulfonamides differently match the hydrophobic and hydrophilic halves of human carbonic anhydrases active sites: selective inhibitors for the tumor-associated hCA IX isoform","volume":"152","author":"Ibrahim","year":"2018","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.bioorg.2019.01.065_h0180","doi-asserted-by":"crossref","first-page":"1453","DOI":"10.1080\/14756366.2018.1512597","article-title":"Steroids interfere with human carbonic anhydrase activity by using alternative binding mechanisms","volume":"33","author":"Nocentini","year":"2018","journal-title":"J. Enzyme Inhib. Med. Chem."}],"container-title":["Bioorganic Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0045206818314111?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0045206818314111?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2022,9,11]],"date-time":"2022-09-11T03:24:27Z","timestamp":1662866667000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0045206818314111"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,5]]},"references-count":36,"alternative-id":["S0045206818314111"],"URL":"https:\/\/doi.org\/10.1016\/j.bioorg.2019.01.065","relation":{},"ISSN":["0045-2068"],"issn-type":[{"value":"0045-2068","type":"print"}],"subject":[],"published":{"date-parts":[[2019,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Click-tailed benzenesulfonamides as potent bacterial carbonic anhydrase inhibitors for targeting Mycobacterium tuberculosis and Vibrio cholerae","name":"articletitle","label":"Article Title"},{"value":"Bioorganic Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bioorg.2019.01.065","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2019 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}