{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,22]],"date-time":"2026-07-22T16:02:09Z","timestamp":1784736129896,"version":"3.55.0"},"reference-count":73,"publisher":"Elsevier","isbn-type":[{"value":"9780443470868","type":"print"}],"license":[{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"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":[[2026]]},"DOI":"10.1016\/bs.enz.2026.06.002","type":"book-chapter","created":{"date-parts":[[2026,6,22]],"date-time":"2026-06-22T11:34:09Z","timestamp":1782128049000},"page":"271-298","source":"Crossref","is-referenced-by-count":0,"title":["Carbonic anhydrase XIV"],"prefix":"10.1016","author":[{"given":"Giuseppina","family":"De Simone","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vincenzo","family":"Alterio","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/bs.enz.2026.06.002_bib0001","doi-asserted-by":"crossref","first-page":"603","DOI":"10.2174\/138161208783877884","article-title":"Carbonic anhydrases-an overview","volume":"14","author":"Supuran","year":"2008","journal-title":"Curr. Pharm. Des."},{"key":"10.1016\/bs.enz.2026.06.002_bib0002","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/j.resp.2006.03.007","article-title":"The structure and function of carbonic anhydrase isozymes in the respiratory system of vertebrates","volume":"154","author":"Esbaugh","year":"2006","journal-title":"Respir. Physiol. Neurobiol."},{"key":"10.1016\/bs.enz.2026.06.002_bib0003","doi-asserted-by":"crossref","first-page":"769","DOI":"10.1002\/bip.22456","article-title":"The structural comparison between membrane-associated human carbonic anhydrases provides insights into drug design of selective inhibitors","volume":"101","author":"Alterio","year":"2014","journal-title":"Biopolymers"},{"issue":"22","key":"10.1016\/bs.enz.2026.06.002_bib0004","doi-asserted-by":"crossref","first-page":"15701","DOI":"10.1074\/jbc.274.22.15701","article-title":"Isolation and characterization of CA XIV, a novel membrane-bound carbonic anhydrase from mouse kidney","volume":"274","author":"Mori","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/bs.enz.2026.06.002_bib0005","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1006\/geno.1999.5938","article-title":"Human carbonic anhydrase XIV (CA14): cDNA cloning, mRNA expression, and mapping to chromosome 1","volume":"61","author":"Fujikawa-Adachi","year":"1999","journal-title":"Genomics"},{"key":"10.1016\/bs.enz.2026.06.002_bib0006","doi-asserted-by":"crossref","first-page":"893","DOI":"10.2174\/156802607780636672","article-title":"Characterization and inhibition of the recently discovered carbonic anhydrase isoforms CA XIII, XIV and XV","volume":"7","author":"Hilvo","year":"2007","journal-title":"Curr. Top. Med. Chem."},{"key":"10.1016\/bs.enz.2026.06.002_bib0007","doi-asserted-by":"crossref","first-page":"1256","DOI":"10.1152\/ajpregu.00735.2004","article-title":"Expression of membrane-associated carbonic anhydrase isoforms IV, IX, XII, and XIV in the rabbit: induction of CA IV and IX during maturation","volume":"288","author":"Purkerson","year":"2005","journal-title":"Am. J. Physiol. Integr. Comp. Physiol."},{"issue":"12","key":"10.1016\/bs.enz.2026.06.002_bib0008","doi-asserted-by":"crossref","first-page":"1379","DOI":"10.1369\/jhc.6A7003.2006","article-title":"Expression of membrane-bound carbonic anhydrases IV, IX, and XIV in the mouse heart","volume":"54","author":"Scheibe","year":"2006","journal-title":"J. Histochem. Cytochem."},{"key":"10.1016\/bs.enz.2026.06.002_bib0009","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1016\/j.yjmcc.2011.12.008","article-title":"Carbonic anhydrase XIV in the normal and hypertrophic myocardium","volume":"52","author":"Vargas","year":"2012","journal-title":"J. Mol. Cell. Cardiol."},{"key":"10.1016\/bs.enz.2026.06.002_bib0010","doi-asserted-by":"crossref","first-page":"1918","DOI":"10.1073\/pnas.98.4.1918","article-title":"Expression of membrane-associated carbonic anhydrase XIV on neurons and axons in mouse and human brain","volume":"98","author":"Parkkila","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/bs.enz.2026.06.002_bib0011","doi-asserted-by":"crossref","first-page":"7786","DOI":"10.1073\/pnas.89.16.7786","article-title":"pH transients evoked by excitatory synaptic transmission are increased by inhibition of extracellular carbonic anhydrase","volume":"89","author":"Chen","year":"1992","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/bs.enz.2026.06.002_bib0012","doi-asserted-by":"crossref","first-page":"16771","DOI":"10.1073\/pnas.0508449102","article-title":"Carbonic anhydrase IV and XIV knockout mice: roles of the respective carbonic anhydrases in buffering the extracellular space in brain","volume":"102","author":"Shah","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/bs.enz.2026.06.002_bib0013","doi-asserted-by":"crossref","first-page":"2111","DOI":"10.1046\/j.1523-1755.2002.00371.x","article-title":"Carbonic anhydrase XIV: luminal expression suggests key role in renal acidification","volume":"61","author":"Kaunisto","year":"2002","journal-title":"Kidney Int."},{"key":"10.1016\/bs.enz.2026.06.002_bib0014","doi-asserted-by":"crossref","DOI":"10.1186\/1471-230X-2-13","article-title":"The plasma membrane carbonic anhydrase in murine hepatocytes identified as isozyme XIV","volume":"2","author":"Parkkila","year":"2002","journal-title":"BMC Gastroenterol."},{"key":"10.1016\/bs.enz.2026.06.002_bib0015","article-title":"Carbonic anhydrase 14 protects the liver against the cytotoxicity of bile acids in a biliary bicarbonate umbrella-related manner","volume":"301","author":"Qian","year":"2022","journal-title":"Life Sci."},{"key":"10.1016\/bs.enz.2026.06.002_bib0016","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1007\/s00424-021-02659-3","article-title":"Loss of luminal carbonic anhydrase XIV results in decreased biliary bicarbonate output, liver fibrosis, and cholangiocyte proliferation in mice","volume":"474","author":"Zhou","year":"2022","journal-title":"Pflugers. Arch."},{"key":"10.1016\/bs.enz.2026.06.002_bib0017","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1369\/jhc.4A6575.2005","article-title":"Region-and cell-specific differences in the distribution of carbonic anhydrases II, III, XII, and XIV in the adult rat epididymis","volume":"53","author":"Hermo","year":"2005","journal-title":"J. Histochem. Cytochem."},{"key":"10.1016\/bs.enz.2026.06.002_bib0018","doi-asserted-by":"crossref","first-page":"492","DOI":"10.1016\/j.exer.2005.03.010","article-title":"Carbonic anhydrase XIV identified as the membrane CA in mouse retina: strong expression in M\u00fcller cells and the RPE","volume":"81","author":"Ochrietor","year":"2005","journal-title":"Exp. Eye Res."},{"key":"10.1016\/bs.enz.2026.06.002_bib0019","doi-asserted-by":"crossref","first-page":"8030","DOI":"10.1073\/pnas.0503021102","article-title":"Carbonic anhydrase XIV is enriched in specific membrane domains of retinal pigment epithelium, Muller cells, and astrocytes","volume":"102","author":"Nagelhus","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/bs.enz.2026.06.002_bib0020","doi-asserted-by":"crossref","first-page":"8514","DOI":"10.1073\/pnas.0702899104","article-title":"Carbonic anhydrase XIV deficiency produces a functional defect in the retinal light response","volume":"104","author":"Ogilvie","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/bs.enz.2026.06.002_bib0021","doi-asserted-by":"crossref","first-page":"4342","DOI":"10.3390\/ijms23084342","article-title":"Roles of carbonic anhydrases and carbonic anhydrase related proteins in zebrafish","volume":"23","author":"Aspatwar","year":"2022","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/bs.enz.2026.06.002_bib0022","doi-asserted-by":"crossref","first-page":"1327","DOI":"10.1152\/physrev.00018.2021","article-title":"Carbonic anhydrases in metazoan model organisms: molecules, mechanisms, and physiology","volume":"102","author":"Aspatwar","year":"2022","journal-title":"Physiol. Rev."},{"key":"10.1016\/bs.enz.2026.06.002_bib0023","doi-asserted-by":"crossref","DOI":"10.15252\/embr.201948333","article-title":"pH-controlled histone acetylation amplifies melanocyte differentiation downstream of MITF","volume":"21","author":"Raja","year":"2020","journal-title":"EMBO Rep."},{"key":"10.1016\/bs.enz.2026.06.002_bib0024","doi-asserted-by":"crossref","first-page":"13589","DOI":"10.1073\/pnas.93.24.13589","article-title":"Crystal structure of the secretory form of membrane-associated human carbonic anhydrase IV at 2.8-\u00c5\u2009resolution","volume":"93","author":"Stams","year":"1996","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/bs.enz.2026.06.002_bib0025","doi-asserted-by":"crossref","first-page":"16233","DOI":"10.1073\/pnas.0908301106","article-title":"Crystal structure of the catalytic domain of the tumor-associated human carbonic anhydrase IX","volume":"106","author":"Alterio","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/bs.enz.2026.06.002_bib0026","doi-asserted-by":"crossref","first-page":"9545","DOI":"10.1073\/pnas.161301298","article-title":"Crystal structure of the dimeric extracellular domain of human carbonic anhydrase XII, a bitopic membrane protein overexpressed in certain cancer tumor cells","volume":"98","author":"Whittington","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/bs.enz.2026.06.002_bib0027","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1042\/BJ20051102","article-title":"Characterization of CA XV, a new GPI-anchored form of carbonic anhydrase","volume":"392","author":"Hilvo","year":"2005","journal-title":"Biochem. J."},{"key":"10.1016\/bs.enz.2026.06.002_bib0028","doi-asserted-by":"crossref","first-page":"7223","DOI":"10.1074\/jbc.M310809200","article-title":"Expression, assay, and structure of the extracellular domain of murine carbonic anhydrase XIV: implications for selective inhibition of membrane-associated isozymes","volume":"279","author":"Whittington","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/bs.enz.2026.06.002_bib0029","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1006\/jmbi.1999.3488","article-title":"Statistical analysis of amino acid patterns in transmembrane helices: the GxxxG motif occurs frequently and in association with \u03b2-branched residues at neighboring positions","volume":"296","author":"Senes","year":"2000","journal-title":"J. Mol. Biol."},{"key":"10.1016\/bs.enz.2026.06.002_bib0030","doi-asserted-by":"crossref","first-page":"911","DOI":"10.1006\/jmbi.1999.3489","article-title":"The GxxxG motif: a framework for transmembrane helix-helix association","volume":"296","author":"Russ","year":"2000","journal-title":"J. Mol. Biol."},{"key":"10.1016\/bs.enz.2026.06.002_bib0031","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.2026.06.002_bib0032","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1113\/JP283579","article-title":"Mitochondrial carbonic anhydrase VA and VB: properties and roles in health and disease","volume":"601","author":"Aspatwar","year":"2023","journal-title":"J. Physiol."},{"key":"10.1016\/bs.enz.2026.06.002_bib0033","doi-asserted-by":"crossref","first-page":"3828","DOI":"10.1016\/j.bmcl.2005.06.055","article-title":"Carbonic anhydrase inhibitors: inhibition of the transmembrane isozyme XIV with sulfonamides","volume":"15","author":"Nishimori","year":"2005","journal-title":"Bioorganic Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2026.06.002_bib0034","doi-asserted-by":"crossref","first-page":"2719","DOI":"10.1074\/jbc.M308984200","article-title":"Characterization of CA XIII, a novel member of the carbonic anhydrase isozyme family","volume":"279","author":"Lehtonen","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/bs.enz.2026.06.002_bib0035","doi-asserted-by":"crossref","first-page":"6089","DOI":"10.1016\/j.bmc.2005.06.022","article-title":"Carbonic anhydrase inhibitors: inhibition of the human transmembrane isozyme XIV with a library of aromatic\/heterocyclic sulfonamides","volume":"13","author":"\u00d6zensoy","year":"2005","journal-title":"Bioorganic Med. Chem."},{"key":"10.1016\/bs.enz.2026.06.002_bib0036","doi-asserted-by":"crossref","first-page":"3063","DOI":"10.1016\/j.bmcl.2012.03.071","article-title":"Flavones and structurally related 4-chromenones inhibit carbonic anhydrases by a different mechanism of action compared to coumarins","volume":"22","author":"Balboni","year":"2012","journal-title":"Bioorganic Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2026.06.002_bib0037","doi-asserted-by":"crossref","first-page":"1214","DOI":"10.1016\/j.bmc.2008.12.023","article-title":"Carbonic anhydrase inhibitors. Comparison of chlorthalidone, indapamide, trichloromethiazide, and furosemide X-ray crystal structures in adducts with isozyme II, when several water molecules make the difference","volume":"17","author":"Temperini","year":"2009","journal-title":"Bioorganic Med. Chem."},{"key":"10.1016\/bs.enz.2026.06.002_bib0038","doi-asserted-by":"crossref","first-page":"4282","DOI":"10.1016\/j.bmcl.2008.06.105","article-title":"Carbonic anhydrase inhibitors. Interaction of the antitumor sulfamate EMD 486019 with twelve mammalian carbonic anhydrase isoforms: kinetic and X-ray crystallographic studies","volume":"18","author":"Temperini","year":"2008","journal-title":"Bioorganic Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2026.06.002_bib0039","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1080\/17460441.2020.1743676","article-title":"Exploring the multiple binding modes of inhibitors to carbonic anhydrases for novel drug discovery","volume":"15","author":"Supuran","year":"2020","journal-title":"Expert Opin. Drug. Discov."},{"key":"10.1016\/bs.enz.2026.06.002_bib0040","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3390\/ijms22052264","article-title":"Anticonvulsant effects of topiramate and lacosamide on pilocarpine-induced status epilepticus in rats: a role of reactive oxygen species and inflammation","volume":"22","author":"Shishmanova-Doseva","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/bs.enz.2026.06.002_bib0041","doi-asserted-by":"crossref","first-page":"2685","DOI":"10.1016\/j.bmcl.2007.03.008","article-title":"Carbonic anhydrase inhibitors. Inhibition of isoforms I, II, IV, VA, VII, IX, and XIV with sulfonamides incorporating fructopyranose-thioureido tails","volume":"17","author":"Winum","year":"2007","journal-title":"Bioorganic Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2026.06.002_bib0042","doi-asserted-by":"crossref","first-page":"987","DOI":"10.1016\/j.bmcl.2006.11.046","article-title":"Inhibition of membrane-associated carbonic anhydrase isozymes IX, XII and XIV with a library of glycoconjugate benzenesulfonamides","volume":"17","author":"Wilkinson","year":"2007","journal-title":"Bioorganic Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2026.06.002_bib0043","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1021\/acs.chemrev.4c00278","article-title":"Multiple binding modes of inhibitors to human carbonic anhydrases: an update on the design of isoform-specific modulators of activity","volume":"125","author":"D\u2019Ambrosio","year":"2025","journal-title":"Chem. Rev."},{"key":"10.1016\/bs.enz.2026.06.002_bib0044","doi-asserted-by":"crossref","first-page":"3105","DOI":"10.1016\/j.bmc.2011.04.005","article-title":"Sulfonamides incorporating 1,3,5-triazine moieties selectively and potently inhibit carbonic anhydrase transmembrane isoforms IX, XII and XIV over cytosolic isoforms I and II: solution and X-ray crystallographic studies","volume":"19","author":"Carta","year":"2011","journal-title":"Bioorganic Med. Chem."},{"key":"10.1016\/bs.enz.2026.06.002_bib0045","doi-asserted-by":"crossref","first-page":"3891","DOI":"10.1021\/jm300112w","article-title":"Synthesis, structure-activity relationship studies, and X-ray crystallographic analysis of arylsulfonamides as potent carbonic anhydrase inhibitors","volume":"55","author":"Gitto","year":"2012","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.06.002_bib0046","doi-asserted-by":"crossref","first-page":"6929","DOI":"10.1016\/j.bmc.2013.09.031","article-title":"Inhibition of human carbonic anhydrase isoforms I-XIV with sulfonamides incorporating fluorine and 1,3,5-triazine moieties","volume":"21","author":"Ceruso","year":"2013","journal-title":"Bioorganic Med. Chem."},{"key":"10.1016\/bs.enz.2026.06.002_bib0047","doi-asserted-by":"crossref","first-page":"6768","DOI":"10.1016\/j.bmc.2014.10.041","article-title":"Inhibition studies of new ureido-substituted sulfonamides incorporating a GABA moiety against human carbonic anhydrase isoforms I-XIV","volume":"22","author":"Ceruso","year":"2014","journal-title":"Bioorganic Med. Chem."},{"key":"10.1016\/bs.enz.2026.06.002_bib0048","doi-asserted-by":"crossref","first-page":"2396","DOI":"10.1016\/j.ejmech.2010.02.020","article-title":"Carbonic anhydrase inhibitors: synthesis and inhibition of the human cytosolic isozymes I and II and transmembrane isozymes IX, XII (cancer-associated) and XIV with 4-substituted 3-pyridinesulfonamides","volume":"45","author":"Brzozowski","year":"2010","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.06.002_bib0049","doi-asserted-by":"crossref","first-page":"9113","DOI":"10.1016\/j.bmc.2008.09.032","article-title":"Carbonic anhydrase inhibitors: synthesis and inhibition studies against mammalian isoforms I-XV with a series of 2-(hydrazinocarbonyl)-3-substituted-phenyl-1H-indole-5-sulfonamides","volume":"16","author":"G\u00fczel","year":"2008","journal-title":"Bioorganic Med. Chem."},{"key":"10.1016\/bs.enz.2026.06.002_bib0050","doi-asserted-by":"crossref","first-page":"2853","DOI":"10.1016\/j.ejmech.2008.02.018","article-title":"Indanesulfonamides as carbonic anhydrase inhibitors and anticonvulsant agents: structure-activity relationship and pharmacological evaluation","volume":"43","author":"Thiry","year":"2008","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.06.002_bib0051","doi-asserted-by":"crossref","first-page":"8564","DOI":"10.1021\/acs.jmedchem.5b01144","article-title":"Discovery of 1,1\u2019-Biphenyl-4-sulfonamides as a new class of potent and selective carbonic anhydrase XIV inhibitors","volume":"58","author":"La Regina","year":"2015","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.06.002_bib0052","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1007\/s11030-010-9271-4","article-title":"Carbonic anhydrase inhibition with natural products: novel chemotypes and inhibition mechanisms","volume":"15","author":"Supuran","year":"2011","journal-title":"Mol. Divers."},{"key":"10.1016\/bs.enz.2026.06.002_bib0053","doi-asserted-by":"crossref","first-page":"2159","DOI":"10.1016\/j.bmc.2010.01.076","article-title":"Carbonic anhydrase inhibitors. Inhibition of mammalian isoforms I-XIV with a series of natural product polyphenols and phenolic acids","volume":"18","author":"Innocenti","year":"2010","journal-title":"Bioorganic Med. Chem."},{"key":"10.1016\/bs.enz.2026.06.002_bib0054","doi-asserted-by":"crossref","first-page":"7424","DOI":"10.1016\/j.bmc.2008.06.013","article-title":"Carbonic anhydrase inhibitors: inhibition of mammalian isoforms I-XIV with a series of substituted phenols including paracetamol and salicylic acid","volume":"16","author":"Innocenti","year":"2008","journal-title":"Bioorganic Med. Chem."},{"key":"10.1016\/bs.enz.2026.06.002_bib0055","doi-asserted-by":"crossref","first-page":"1489","DOI":"10.1016\/j.bmc.2012.09.002","article-title":"Synthesis of C-cinnamoyl glycosides and their inhibitory activity against mammalian carbonic anhydrases","volume":"21","author":"Riafrecha","year":"2013","journal-title":"Bioorganic Med. Chem."},{"key":"10.1016\/bs.enz.2026.06.002_bib0056","doi-asserted-by":"crossref","first-page":"3790","DOI":"10.1016\/j.bmc.2013.04.041","article-title":"Natural product hybrid and its superacid synthesized analogues: dodoneine and its derivatives show selective inhibition of carbonic anhydrase isoforms I, III, XIII and XIV","volume":"21","author":"Carreyre","year":"2013","journal-title":"Bioorganic Med. Chem."},{"key":"10.1016\/bs.enz.2026.06.002_bib0057","doi-asserted-by":"crossref","first-page":"1564","DOI":"10.1016\/j.bmc.2012.05.019","article-title":"Mono-\/dihydroxybenzoic acid esters and phenol pyridinium derivatives as inhibitors of the mammalian carbonic anhydrase isoforms I, II, VII, IX, XII and XIV","volume":"21","author":"Carta","year":"2013","journal-title":"Bioorganic Med. Chem."},{"key":"10.1016\/bs.enz.2026.06.002_bib0058","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.2026.06.002_bib0059","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.2026.06.002_bib0060","doi-asserted-by":"crossref","first-page":"773","DOI":"10.3109\/14756366.2014.970185","article-title":"7-Amino-3,4-dihydro-1H-quinolin-2-one, a compound similar to the substituted coumarins, inhibits \u03b1-carbonic anhydrases without hydrolysis of the lactam ring","volume":"30","author":"Vullo","year":"2015","journal-title":"J. Enzyme. Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2026.06.002_bib0061","doi-asserted-by":"crossref","first-page":"397","DOI":"10.3109\/14756366.2011.650692","article-title":"Metronidazole-coumarin conjugates and 3-cyano-7-hydroxy-coumarin act as isoform-selective carbonic anhydrase inhibitors","volume":"28","author":"Bonneau","year":"2013","journal-title":"J. Enzyme. Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2026.06.002_bib0062","doi-asserted-by":"crossref","first-page":"2182","DOI":"10.1016\/j.bmcl.2012.01.129","article-title":"New chemotypes acting as isozyme-selective carbonic anhydrase inhibitors with low affinity for the offtarget cytosolic isoform II","volume":"22","author":"Carta","year":"2012","journal-title":"Bioorganic Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2026.06.002_bib0063","doi-asserted-by":"crossref","first-page":"1548","DOI":"10.1016\/j.bmcl.2010.01.081","article-title":"Carbonic anhydrase inhibitors. Inhibition of transmembrane isoforms IX, XII, and XIV with less investigated anions including trithiocarbonate and dithiocarbamate","volume":"20","author":"Innocenti","year":"2010","journal-title":"Bioorganic Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2026.06.002_bib0064","doi-asserted-by":"crossref","first-page":"1532","DOI":"10.1016\/j.bmcl.2006.12.113","article-title":"Carbonic anhydrase inhibitors. Inhibition of transmembrane isozymes XII (cancer-associated) and XIV with anions","volume":"17","author":"Innocenti","year":"2007","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2026.06.002_bib0065","doi-asserted-by":"crossref","first-page":"628","DOI":"10.1016\/j.bmcl.2006.11.027","article-title":"Carbonic anhydrase activators: l-adrenaline plugs the active site entrance of isozyme II, activating better isoforms I, IV, VA, VII, and XIV","volume":"17","author":"Temperini","year":"2007","journal-title":"Bioorganic Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2026.06.002_bib0066","doi-asserted-by":"crossref","first-page":"4107","DOI":"10.1016\/j.bmcl.2007.05.052","article-title":"Carbonic anhydrase activators: activation of the human isoforms VII (cytosolic) and XIV (transmembrane) with amino acids and amines","volume":"17","author":"Vullo","year":"2007","journal-title":"Bioorganic Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2026.06.002_bib0067","doi-asserted-by":"crossref","first-page":"7057","DOI":"10.1002\/chem.200600159","article-title":"Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and crystallographic analysis of their adducts with isoform II: engineering proton-transfer processes within the active site of an enzyme","volume":"12","author":"Temperini","year":"2006","journal-title":"Chemistry"},{"key":"10.1016\/bs.enz.2026.06.002_bib0068","doi-asserted-by":"crossref","first-page":"3019","DOI":"10.1021\/jm0603320","article-title":"Carbonic Anhydrase Activators. Activation of isoforms I, II, IV, VA, VII, and XIV with l- and d-phenylalanine and crystallographic analysis of their adducts with isozyme II: stereospecific recognition within the active site of an enzyme and its consequence","volume":"49","author":"Temperini","year":"2006","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.06.002_bib0069","doi-asserted-by":"crossref","first-page":"8373","DOI":"10.1016\/j.bmc.2008.08.043","article-title":"Carbonic anhydrase activators: kinetic and X-ray crystallographic study for the interaction of d- and l-tryptophan with the mammalian isoforms I-XIV","volume":"16","author":"Temperini","year":"2008","journal-title":"Bioorganic Med. Chem."},{"key":"10.1016\/bs.enz.2026.06.002_bib0070","doi-asserted-by":"crossref","first-page":"1170","DOI":"10.1021\/jm101284a","article-title":"Carbonic anhydrase activators: gold nanoparticles coated with derivatized histamine, histidine, and carnosine show enhanced activatory effects on several mammalian isoforms","volume":"54","author":"Saada","year":"2011","journal-title":"J Med. Chem."},{"key":"10.1016\/bs.enz.2026.06.002_bib0071","doi-asserted-by":"crossref","first-page":"4752","DOI":"10.1016\/j.bmc.2014.07.005","article-title":"Mono- and di-halogenated histamine, histidine and carnosine derivatives are potent carbonic anhydrase I, II, VII, XII and XIV activators","volume":"22","author":"Saada","year":"2014","journal-title":"Bioorganic Med. Chem."},{"key":"10.1016\/bs.enz.2026.06.002_bib0072","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1080\/14756366.2018.1543292","article-title":"(Hetero)aryl substituted thiazol-2,4-yl scaffold as human carbonic anhydrase I, II, VII and XIV activators","volume":"34","author":"Rami","year":"2019","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2026.06.002_bib0073","doi-asserted-by":"crossref","first-page":"7493","DOI":"10.1073\/pnas.0502829102","article-title":"Three-dimensional structure of a halotolerant algal carbonic anhydrase predicts halotolerance of a mammalian homolog","volume":"102","author":"Premkumar","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U.S.A."}],"container-title":["The Enzymes","Vertebrate Carbonic Anhydrases"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874604726000156?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874604726000156?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,7,22]],"date-time":"2026-07-22T15:15:32Z","timestamp":1784733332000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1874604726000156"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026]]},"ISBN":["9780443470868"],"references-count":73,"URL":"https:\/\/doi.org\/10.1016\/bs.enz.2026.06.002","relation":{},"ISSN":["1874-6047"],"issn-type":[{"value":"1874-6047","type":"print"}],"subject":[],"published":{"date-parts":[[2026]]}}}