{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,3,27]],"date-time":"2025-03-27T18:05:30Z","timestamp":1743098730639,"version":"3.40.3"},"reference-count":74,"publisher":"Elsevier","isbn-type":[{"type":"print","value":"9780443295188"}],"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.2024.06.007","type":"book-chapter","created":{"date-parts":[[2024,7,20]],"date-time":"2024-07-20T20:08:36Z","timestamp":1721506116000},"page":"193-212","source":"Crossref","is-referenced-by-count":0,"title":["Non-sulfonamide bacterial CA inhibitors"],"prefix":"10.1016","author":[{"given":"Fabrizio","family":"Carta","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/bs.enz.2024.06.007_bib1","doi-asserted-by":"crossref","first-page":"1619","DOI":"10.4155\/fmc-2021-0207","article-title":"Bacterial carbonic anhydrases: underexploited antibacterial therapeutic targets","volume":"19","author":"Flaherty","year":"2021","journal-title":"Future Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib2","first-page":"1","article-title":"Biomedical applications of prokaryotic carbonic anhydrases: an update","author":"Capasso","year":"2024","journal-title":"Expert. Opin. Ther. Pat."},{"issue":"12","key":"10.1016\/bs.enz.2024.06.007_bib3","first-page":"963","article-title":"Antibacterial carbonic anhydrase inhibitors: an update on the recent literature","author":"Capasso","year":"2020","journal-title":"Expert. Opin. Ther. Pat."},{"issue":"11","key":"10.1016\/bs.enz.2024.06.007_bib4","doi-asserted-by":"crossref","first-page":"2911","DOI":"10.3390\/molecules23112911","article-title":"Carbonic anhydrase inhibitors as novel drugs against mycobacterial \u03b2-carbonic anhydrases: an update on in vitro and in vivo studies","author":"Aspatwar","year":"2018","journal-title":"Molecules"},{"key":"10.1016\/bs.enz.2024.06.007_bib5","doi-asserted-by":"crossref","first-page":"4681","DOI":"10.1016\/j.bmcl.2012.05.083","article-title":"Ureido-substituted sulfamates show potent carbonic anhydrase IX inhibitory and antiproliferative activities against breast cancer cell lines","volume":"14","author":"Winum","year":"2012","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2024.06.007_bib6","first-page":"1","article-title":"Carbonic anhydrase and bacterial metabolism: a chance for antibacterial drug discovery","author":"Capasso","year":"2024","journal-title":"Expert. Opin. Ther. Pat."},{"issue":"1","key":"10.1016\/bs.enz.2024.06.007_bib7","doi-asserted-by":"crossref","first-page":"2092","DOI":"10.1080\/14756366.2022.2101644","article-title":"The gram-negative bacterium Escherichia coli as a model for testing the effect of carbonic anhydrase inhibition on bacterial growth","author":"De Luca","year":"2022","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"3","key":"10.1016\/bs.enz.2024.06.007_bib8","doi-asserted-by":"crossref","first-page":"549","DOI":"10.3390\/ma14030549","article-title":"The role of metal ions in biology, biochemistry and medicine","author":"Moustakas","year":"2021","journal-title":"Mater. (Basel)"},{"issue":"1","key":"10.1016\/bs.enz.2024.06.007_bib9","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1080\/14756366.2021.1882453","article-title":"Reconsidering anion inhibitors in the general context of drug design studies of modulators of activity of the classical enzyme carbonic anhydrase","author":"Nocentini","year":"2021","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib10","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/j.jinorgbio.2011.11.017","article-title":"(In)organic anions as carbonic anhydrase inhibitors","volume":"111","author":"De Simone","year":"2012","journal-title":"J. Inorg. Biochem."},{"key":"10.1016\/bs.enz.2024.06.007_bib11","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/S0006-3061(00)80283-5","article-title":"Binding affinity of bicarboxylate ions for cobalt (II) bovine carbonic anhydrase","volume":"9","author":"Bertini","year":"1978","journal-title":"Bioinorg. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib12","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1016\/0005-2744(76)90076-0","article-title":"Interaction of cobalt-bovine carbonic anhydrase with the acetate ion","volume":"452","author":"Bertini","year":"1976","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/bs.enz.2024.06.007_bib13","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1111\/j.1432-1033.1992.tb17225.x","article-title":"The interaction of acetate and formate with cobalt carbonic anhydrase. An NMR study","volume":"208","author":"Bertini","year":"1992","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/bs.enz.2024.06.007_bib14","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1016\/0014-5793(78)81115-6","article-title":"A 31 P NMR study of phosphate in presence of cobalt(II)- and copper(II)- substituted bovine carbonic anhydrase B","volume":"93","author":"Bertini","year":"1978","journal-title":"FEBS Lett."},{"key":"10.1016\/bs.enz.2024.06.007_bib15","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1016\/S0021-9258(19)44331-7","article-title":"Electron spin resonance of 63Cu and 65Cu carbonic anhydrases. Resolution of nitrogen ligand superhyperfine structure","volume":"248","author":"Taylor","year":"1973","journal-title":"J. Biol. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib16","doi-asserted-by":"crossref","first-page":"1088","DOI":"10.1080\/14756366.2021.1931863","article-title":"An anion and small molecule inhibition study of the \u03b2-carbonic anhydrase from Staphylococcus aureus","volume":"1","author":"Urbanski","year":"2021","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib17","doi-asserted-by":"crossref","first-page":"1061","DOI":"10.1080\/14756366.2021.1929202","article-title":"Anion inhibition studies of the \u03b1-carbonic anhydrases from Neisseria gonorrhoeae","volume":"1","author":"Nocentini","year":"2021","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib18","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1080\/14756366.2020.1867122","article-title":"Anion inhibition studies of the Zn(II)-bound \u03b9-carbonic anhydrase from the Gram-negative bacterium Burkholderia territorii","volume":"1","author":"Petreni","year":"2021","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib19","doi-asserted-by":"crossref","first-page":"2564","DOI":"10.3390\/molecules25112564","article-title":"Anion inhibition studies of the beta-carbonic anhydrase from Escherichia coli","volume":"11","author":"Del Prete","year":"2020","journal-title":"Molecules"},{"key":"10.1016\/bs.enz.2024.06.007_bib20","doi-asserted-by":"crossref","first-page":"835","DOI":"10.1016\/j.bmc.2016.01.005","article-title":"Cloning, characterization and anion inhibition studies of a \u03b3-carbonic anhydrase from the Antarctic bacterium Colwellia psychrerythraea","volume":"4","author":"De Luca","year":"2016","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib21","first-page":"2449","article-title":"Crystal structure and kinetic studies of a tetrameric type II \u03b2-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae","volume":"Pt 12","author":"Ferraroni","year":"2015","journal-title":"Acta"},{"key":"10.1016\/bs.enz.2024.06.007_bib22","doi-asserted-by":"crossref","first-page":"2995","DOI":"10.1016\/j.bmc.2015.05.007","article-title":"Cloning, characterization and anion inhibition study of a \u03b2-class carbonic anhydrase from the caries producing pathogen Streptococcus mutans","volume":"13","author":"Dedeoglu","year":"2015","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib23","doi-asserted-by":"crossref","first-page":"1127","DOI":"10.1016\/j.bmcl.2013.12.124","article-title":"Anion inhibition studies of two new \u03b2-carbonic anhydrases from the bacterial pathogen Legionella pneumophila","volume":"4","author":"Nishimori","year":"2014","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2024.06.007_bib24","doi-asserted-by":"crossref","first-page":"6706","DOI":"10.1016\/j.bmcl.2013.10.037","article-title":"Anion inhibition studies of a \u03b2-carbonic anhydrase from Clostridium perfringens","volume":"24","author":"Vullo","year":"2013","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2024.06.007_bib25","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1016\/0014-5793(93)81565-H","article-title":"The structure of human carbonic anhydrase II in complex with bromide and azide","volume":"322","author":"J\u00f6nsson","year":"1993","journal-title":"FEBS Lett."},{"key":"10.1016\/bs.enz.2024.06.007_bib26","doi-asserted-by":"crossref","first-page":"867","DOI":"10.1111\/j.1432-1033.1992.tb17490.x","article-title":"Crystallographic studies of the binding of protonated and unprotonated inhibitors to carbonic anhydrase using hydrogen sulphide and nitrate anions","volume":"3","author":"Mangani","year":"1992","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/bs.enz.2024.06.007_bib27","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1111\/j.1432-1033.1993.tb17788.x","article-title":"Crystallographic studies of azide binding to human carbonic anhydrase II","volume":"1","author":"Nair","year":"1993","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/bs.enz.2024.06.007_bib28","doi-asserted-by":"crossref","first-page":"10609","DOI":"10.1073\/pnas.0904184106","article-title":"Structural study of X-ray induced activation of carbonic anhydrase","volume":"106","author":"Sj\u00f6blom","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/bs.enz.2024.06.007_bib29","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1002\/prot.340040406","article-title":"Refined structure of human carbonic anhydrase II at 2.0 A resolution","volume":"4","author":"Eriksson","year":"1988","journal-title":"Proteins"},{"key":"10.1016\/bs.enz.2024.06.007_bib30","doi-asserted-by":"crossref","first-page":"12391","DOI":"10.1021\/bi000937c","article-title":"Mechanism of cyanamide hydration catalyzed by carbonic anhydrase II suggested by cryogenic X-ray diffraction","volume":"40","author":"Guerri","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/bs.enz.2024.06.007_bib31","doi-asserted-by":"crossref","first-page":"1868","DOI":"10.1039\/c2cc16395k","article-title":"Dithiocarbamates: a new class of carbonic anhydrase inhibitors. Crystallographic and kinetic investigations","volume":"13","author":"Carta","year":"2012","journal-title":"Chem. Commun. (Camb.)"},{"key":"10.1016\/bs.enz.2024.06.007_bib32","doi-asserted-by":"crossref","first-page":"5857","DOI":"10.1021\/acs.jmedchem.6b00462","article-title":"Monothiocarbamates strongly inhibit carbonic anhydrases in vitro and possess intraocular pressure lowering activity in an animal model of glaucoma","volume":"12","author":"Vullo","year":"2016","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib33","doi-asserted-by":"crossref","first-page":"474","DOI":"10.1016\/j.bmcl.2009.11.124","article-title":"Carbonic anhydrase inhibitors. X-ray crystal studies of the carbonic anhydrase II\u2013trithiocarbonate adduct\u2014an inhibitor mimicking the sulfonamide and urea binding to the enzyme","volume":"2","author":"Temperini","year":"2010","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2024.06.007_bib34","doi-asserted-by":"crossref","first-page":"407","DOI":"10.3109\/14756366.2011.641015","article-title":"Dithiocarbamates strongly inhibit the \u03b2-class carbonic anhydrases from Mycobacterium tuberculosis","volume":"2","author":"Maresca","year":"2013","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib35","doi-asserted-by":"crossref","first-page":"832","DOI":"10.1080\/14756366.2017.1332056","article-title":"\u03b2-CA-specific inhibitor dithiocarbamate Fc14-584B: a novel antimycobacterial agent with potential to treat drug-resistant tuberculosis","volume":"1","author":"Aspatwar","year":"2017","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib36","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1080\/14756366.2019.1683007","article-title":"In vitro inhibition of Mycobacterium tuberculosis \u03b2-carbonic anhydrase 3 with Mono- and dithiocarbamates and evaluation of their toxicity using zebrafish developing embryos","volume":"1","author":"Aspatwar","year":"2020","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib37","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1080\/14756366.2021.1988945","article-title":"Dithiocarbamates effectively inhibit the \u03b1-carbonic anhydrase from Neisseria gonorrhoeae","volume":"1","author":"Giovannuzzi","year":"2022","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib38","doi-asserted-by":"crossref","first-page":"2284119","DOI":"10.1080\/14756366.2023.2284119","article-title":"Inhibition of pathogenic bacterial carbonic anhydrases by monothiocarbamates","volume":"1","author":"Giovannuzzi","year":"2023","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib39","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1038\/s41573-020-00114-z","article-title":"Natural products in drug discovery: advances and opportunities","volume":"20","author":"Atanasov","year":"2021","journal-title":"Nat. Rev. Drug. Discov."},{"key":"10.1016\/bs.enz.2024.06.007_bib40","doi-asserted-by":"crossref","first-page":"250","DOI":"10.3390\/molecules23020250","article-title":"Coumarin: a natural, privileged and versatile scaffold for bioactive compounds","volume":"23","author":"Stefanachi","year":"2018","journal-title":"Molecules"},{"key":"10.1016\/bs.enz.2024.06.007_bib41","doi-asserted-by":"crossref","first-page":"1462","DOI":"10.1080\/14756366.2020.1788009","article-title":"Coumarin carbonic anhydrase inhibitors from natural sources","volume":"35","author":"Supuran","year":"2020","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib42","doi-asserted-by":"crossref","first-page":"3057","DOI":"10.1021\/ja809683v","article-title":"Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new class of suicide inhibitors","volume":"131","author":"Maresca","year":"2009","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/bs.enz.2024.06.007_bib43","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1021\/jm901287j","article-title":"Deciphering the mechanism of carbonic anhydrase inhibition with coumarins and thiocoumarins","volume":"53","author":"Maresca","year":"2010","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib44","doi-asserted-by":"crossref","first-page":"1539","DOI":"10.1016\/j.bmc.2012.07.021","article-title":"Natural product coumarins that inhibit human carbonic anhydrases","volume":"21","author":"Davis","year":"2013","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib45","doi-asserted-by":"crossref","first-page":"721","DOI":"10.3390\/md20110721","article-title":"Carbonic anhydrase inhibitors from marine natural products","volume":"20","author":"Supuran","year":"2022","journal-title":"Mar. Drugs"},{"key":"10.1016\/bs.enz.2024.06.007_bib46","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1021\/ml500470b","article-title":"\u03b1-Carbonic anhydrases possess thioesterase activity","volume":"3","author":"Tanc","year":"2015","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2024.06.007_bib47","doi-asserted-by":"crossref","first-page":"462","DOI":"10.1021\/acs.jmedchem.5b01720","article-title":"Thioxocoumarins show an alternative carbonic anhydrase inhibition mechanism compared to coumarins","volume":"1","author":"Ferraroni","year":"2016","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib48","doi-asserted-by":"crossref","first-page":"6208","DOI":"10.1016\/j.bmcl.2010.08.110","article-title":"Paraoxon, 4-nitrophenyl phosphate and acetate are substrates of \u03b1- but not of \u03b2-, \u03b3- and \u03b6-carbonic anhydrases","volume":"20","author":"Innocenti","year":"2010","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2024.06.007_bib49","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1080\/14756366.2021.2012174","article-title":"Coumarins effectively inhibit bacterial \u03b1-carbonic anhydrases","volume":"37","author":"Giovannuzzi","year":"2022","journal-title":"J. Enz. Inh. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib50","doi-asserted-by":"crossref","first-page":"1462","DOI":"10.1080\/14756366.2020.1788009","article-title":"Coumarin carbonic anhydrase inhibitors from natural sources","volume":"1","author":"Supuran","year":"2020","journal-title":"J. Enz. Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib51","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1021\/jm301625s","volume":"1","author":"Tars","year":"2013","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib52","doi-asserted-by":"crossref","first-page":"3975","DOI":"10.1021\/acs.jmedchem.5b00523","article-title":"6-Substituted sulfocoumarins are selective carbonic anhdydrase IX and XII inhibitors with significant cytotoxicity against colorectal cancer cells","volume":"9","author":"Grandane","year":"2015","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib53","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1080\/14756366.2022.2143496","article-title":"3H-1,2-Benzoxaphosphepine 2-oxides as selective inhibitors of carbonic anhydrase IX and XII","volume":"1","author":"Pustenko","year":"2023","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib54","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2022.105751","article-title":"Benzoselenoates: a novel class of carbonic anhydrase inhibitors","volume":"122","author":"Tanini","year":"2022","journal-title":"Bioorg Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib55","article-title":"Selenocarbamates as a prodrug-based approach to carbonic anhydrase inhibition","volume":"11","author":"Angeli","year":"2022","journal-title":"ChemMedChem"},{"key":"10.1016\/bs.enz.2024.06.007_bib56","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1016\/j.bioorg.2019.01.069","article-title":"Discovery of new organoselenium compounds as antileishmanial agents","volume":"86","author":"Al-Tamimi","year":"2019","journal-title":"Bioorg. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib57","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2021.113793","article-title":"Chalcogenides-incorporating carbonic anhydrase inhibitors concomitantly reverted oxaliplatin-induced neuropathy and enhanced antiproliferative action","volume":"225","author":"Tanini","year":"2021","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib58","doi-asserted-by":"crossref","first-page":"1558","DOI":"10.1080\/14786419.2021.1880406","article-title":"Phenols from Origanum dictamnus L. and Thymus vulgaris L. and their activity against Malassezia globosa carbonic anhydrase","volume":"6","author":"Paloukopoulou","year":"2022","journal-title":"Nat. Prod. Res."},{"key":"10.1016\/bs.enz.2024.06.007_bib59","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":"8","author":"Alterio","year":"2012","journal-title":"Chem. Rev."},{"key":"10.1016\/bs.enz.2024.06.007_bib60","doi-asserted-by":"crossref","first-page":"1649","DOI":"10.3390\/molecules21121649","article-title":"Phenols and polyphenols as carbonic anhydrase inhibitors","volume":"12","author":"Karioti","year":"2016","journal-title":"Molecules"},{"key":"10.1016\/bs.enz.2024.06.007_bib61","doi-asserted-by":"crossref","first-page":"7219","DOI":"10.1016\/j.bmc.2015.10.018","article-title":"New natural product carbonic anhydrase inhibitors incorporating phenol moieties","volume":"22","author":"Karioti","year":"2015","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib62","doi-asserted-by":"crossref","first-page":"816","DOI":"10.1002\/cmdc.201800015","article-title":"Natural polyphenols selectively inhibit beta-carbonic anhydrase from the dandruff-producing fungus Malassezia globosa: Activity and modeling studies","volume":"8","author":"Nocentini","year":"2018","journal-title":"ChemMedChem"},{"key":"10.1016\/bs.enz.2024.06.007_bib63","doi-asserted-by":"crossref","first-page":"11583","DOI":"10.3390\/ijms222111583","article-title":"Selective inhibition of Helicobacter pylori carbonic anhydrases by Carvacrol and Thymol could impair biofilm production and the release of outer membrane vesicles","volume":"21","author":"Grande","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/bs.enz.2024.06.007_bib64","doi-asserted-by":"crossref","first-page":"4455","DOI":"10.3390\/ijms24054455","article-title":"Antimicrobial and antibiofilm activities of carvacrol, amoxicillin and salicylhydroxamic acid alone and in combination vs. Helicobacter pylori: towards a new multi-targeted therapy","volume":"5","author":"Puca","year":"2023","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/bs.enz.2024.06.007_bib65","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1080\/14756366.2018.1539716","article-title":"Identification and characterization of the \u03b1-CA in the outer membrane vesicles produced by Helicobacter pylori","volume":"1","author":"Ronci","year":"2019","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib66","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2019.111811","article-title":"Direct and straightforward access to substituted alkyl selenols as novel carbonic anhydrase inhibitors","volume":"185","author":"Tanini","year":"2020","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib67","doi-asserted-by":"crossref","first-page":"8297","DOI":"10.1039\/D0CC02857F","article-title":"2-Mercaptobenzoxazoles: a class of carbonic anhydrase inhibitors with a novel binding mode to the enzyme active site","volume":"59","author":"Bozdag","year":"2020","journal-title":"Chem. Commun. (Camb.)"},{"key":"10.1016\/bs.enz.2024.06.007_bib68","doi-asserted-by":"crossref","first-page":"13033","DOI":"10.1039\/D0CC05172A","article-title":"Catechols: a new class of carbonic anhydrase inhibitors","volume":"85","author":"D\u2019Ambrosio","year":"2020","journal-title":"Chem. Commun. (Camb.)"},{"key":"10.1016\/bs.enz.2024.06.007_bib69","doi-asserted-by":"crossref","first-page":"986","DOI":"10.1080\/14756366.2022.2055009","article-title":"Biological investigation of N-methyl thiosemicarbazones as antimicrobial agents and bacterial carbonic anhydrases inhibitors","volume":"1","author":"D\u2019Agostino","year":"2022","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib70","doi-asserted-by":"crossref","first-page":"2241","DOI":"10.1016\/S0968-0896(03)00112-3","article-title":"Hydroxyurea is a carbonicanhydrase inhibitor","volume":"11","author":"Scozzafava","year":"2003","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib71","doi-asserted-by":"crossref","first-page":"4316","DOI":"10.1016\/j.bmcl.2006.05.068","article-title":"N-hydroxyurea\u2014a versatile zinc binding function in thedesign of metalloenzyme inhibitors","volume":"16","author":"Temperini","year":"2006","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2024.06.007_bib72","doi-asserted-by":"crossref","first-page":"1194","DOI":"10.1080\/14756366.2018.1490733","article-title":"Inhibition of \u03b1-, \u03b2-, \u03b3-, and \u03b4-carbonic anhydrases from bacteria and diatoms with N\u2019-aryl-N-hydroxy-ureas","volume":"1","author":"Berrino","year":"2018","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2024.06.007_bib73","doi-asserted-by":"crossref","first-page":"1904","DOI":"10.1002\/cmdc.201600180","article-title":"Discovery of new potential anti-infective compounds based on carbonic anhydrase inhibitors by rational target-focused repurposing approaches","volume":"17","author":"Annunziato","year":"2016","journal-title":"ChemMedChem"},{"key":"10.1016\/bs.enz.2024.06.007_bib74","unstructured":"https:\/\/www.who.int\/health-topics\/antimicrobial-resistance (Last access 10\/06\/2024)."}],"container-title":["The Enzymes","Bacterial Carbonic Anhydrases"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874604724000246?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874604724000246?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,8,31]],"date-time":"2024-08-31T11:21:04Z","timestamp":1725103264000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1874604724000246"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024]]},"ISBN":["9780443295188"],"references-count":74,"URL":"https:\/\/doi.org\/10.1016\/bs.enz.2024.06.007","relation":{},"ISSN":["1874-6047"],"issn-type":[{"type":"print","value":"1874-6047"}],"subject":[],"published":{"date-parts":[[2024]]}}}