{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T00:48:19Z","timestamp":1790038099991,"version":"4.0.1"},"reference-count":270,"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.2026.03.003","type":"book-chapter","created":{"date-parts":[[2026,3,30]],"date-time":"2026-03-30T11:23:11Z","timestamp":1774869791000},"page":"299-342","source":"Crossref","is-referenced-by-count":1,"title":["Challenges and opportunities for developing selective carbonic anhydrase inhibitors and activators for vertebrate isoforms"],"prefix":"10.1016","author":[{"given":"Claudiu T.","family":"Supuran","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"3","key":"10.1016\/bs.enz.2026.03.003_bib0001","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.2026.03.003_bib0002","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."},{"key":"10.1016\/bs.enz.2026.03.003_bib0003","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\/bs.enz.2026.03.003_bib0004","doi-asserted-by":"crossref","first-page":"689","DOI":"10.3109\/14756366.2015.1059333","article-title":"A magnificent enzyme superfamily: carbonic anhydrases, their purification and characterization","volume":"31","author":"Ozensoy Guler","year":"2016","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0005","doi-asserted-by":"crossref","DOI":"10.1016\/j.bmcl.2023.129411","article-title":"A simple yet multifaceted 90 years old, evergreen enzyme: carbonic anhydrase, its inhibition and activation","volume":"93","author":"Supuran","year":"2023","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2026.03.003_bib0006","doi-asserted-by":"crossref","DOI":"10.3389\/fmolb.2023.1326633","article-title":"Carbonic anhydrase versatility: from pH regulation to CO2 sensing and metabolism","volume":"10","author":"Supuran","year":"2023","journal-title":"Front. Mol. Biosci."},{"issue":"2","key":"10.1016\/bs.enz.2026.03.003_bib0007","doi-asserted-by":"crossref","first-page":"25","DOI":"10.3390\/metabo8020025","article-title":"Carbonic anhydrases and metabolism","volume":"8","author":"Supuran","year":"2018","journal-title":"Metabolites"},{"key":"10.1016\/bs.enz.2026.03.003_bib0008","doi-asserted-by":"crossref","first-page":"E4724","DOI":"10.3390\/ijms20194724","article-title":"A new kid on the block? Carbonic anhydrases as possible new targets in Alzheimer\u2019s disease","volume":"20","author":"Provensi","year":"2019","journal-title":"Int. J. Mol. Sci."},{"issue":"10","key":"10.1016\/bs.enz.2026.03.003_bib0009","doi-asserted-by":"crossref","first-page":"412","DOI":"10.3390\/metabo10100412","article-title":"Carbonic anhydrase inhibitors targeting metabolism and tumor microenvironment","volume":"10","author":"Angeli","year":"2020","journal-title":"Metabolites"},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0010","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","volume":"36","author":"Nocentini","year":"2021","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0011","series-title":"Metalloenzymes\u2014From Bench to Bedside","first-page":"139","article-title":"Carbonic anhydrases","author":"Supuran","year":"2024"},{"key":"10.1016\/bs.enz.2026.03.003_bib0012","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/bs.enz.2024.05.004","article-title":"Overview on bacterial carbonic anhydrase genetic families","volume":"55","author":"Capasso","year":"2024","journal-title":"Enzymes"},{"issue":"9","key":"10.1016\/bs.enz.2026.03.003_bib0013","doi-asserted-by":"crossref","first-page":"901","DOI":"10.2174\/156802607780636753","article-title":"Inhibition of the archaeal beta-class (Cab) and gamma-class (Cam) carbonic anhydrases","volume":"7","author":"Zimmerman","year":"2007","journal-title":"Curr. Top. Med. Chem."},{"issue":"6","key":"10.1016\/bs.enz.2026.03.003_bib0014","doi-asserted-by":"crossref","first-page":"906","DOI":"10.3109\/14756366.2013.868599","article-title":"Biochemical characterization of the \u03b4-carbonic anhydrase from the marine diatom Thalassiosira weissflogii, TweCA","volume":"29","author":"Del Prete","year":"2014","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"Pt 7","key":"10.1016\/bs.enz.2026.03.003_bib0015","doi-asserted-by":"crossref","first-page":"676","DOI":"10.1107\/S2059798320007202","article-title":"Structural and biochemical characterization of novel carbonic anhydrases from phaeodactylum tricornutum","volume":"76","author":"Jin","year":"2020","journal-title":"Acta Crystallogr. D Struct. Biol."},{"key":"10.1016\/bs.enz.2026.03.003_bib0016","first-page":"1","article-title":"Overview on fungal and protozoan carbonic anhydrases","volume":"57","author":"Supuran","year":"2025","journal-title":"Enzymes"},{"key":"10.1016\/bs.enz.2026.03.003_bib0017","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/bs.enz.2025.05.002","article-title":"Plasmodium falciparum \u03b7-carbonic anhydrase","volume":"57","author":"Supuran","year":"2025","journal-title":"Enzymes"},{"key":"10.1016\/bs.enz.2026.03.003_bib0018","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/bs.enz.2024.05.003","article-title":"Bacterial \u03b9-CAs","volume":"55","author":"Capasso","year":"2024","journal-title":"Enzymes"},{"issue":"8","key":"10.1016\/bs.enz.2026.03.003_bib0019","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."},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0020","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."},{"issue":"9","key":"10.1016\/bs.enz.2026.03.003_bib0021","doi-asserted-by":"crossref","first-page":"836","DOI":"10.1016\/j.tips.2025.07.002","article-title":"Human carbonic anhydrase modulators: the past, present, and future","volume":"46","author":"Giovannuzzi","year":"2025","journal-title":"Trends Pharmacol. Sci."},{"key":"10.1016\/bs.enz.2026.03.003_bib0022","doi-asserted-by":"crossref","DOI":"10.1124\/pharmrev.124.001125","article-title":"Multi- and polypharmacology of carbonic anhydrase inhibitors","volume":"77","author":"Supuran","year":"2025","journal-title":"Pharmacol. Rev."},{"key":"10.1016\/bs.enz.2026.03.003_bib0023","doi-asserted-by":"crossref","first-page":"1889","DOI":"10.1021\/acsmedchemlett.5c00443","article-title":"Human carbonic anhydrase inhibitors","volume":"16","author":"Supuran","year":"2025","journal-title":"ACS Med. Chem. Lett."},{"issue":"5","key":"10.1016\/bs.enz.2026.03.003_bib0024","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1080\/14656566.2025.2474574","article-title":"Polypharmacology of carbonic anhydrase inhibitors and activators","volume":"26","author":"Bonardi","year":"2025","journal-title":"Expert Opin. Pharmacother."},{"key":"10.1016\/bs.enz.2026.03.003_bib0025","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":"2","key":"10.1016\/bs.enz.2026.03.003_bib0026","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.2026.03.003_bib0027","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1186\/1471-2199-11-25","article-title":"Phylogeny and expression of carbonic anhydrase-related proteins","volume":"11","author":"Aspatwar","year":"2010","journal-title":"BMC Mol. Biol."},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0028","doi-asserted-by":"crossref","first-page":"584","DOI":"10.1186\/s12885-018-4493-4","article-title":"Carbonic anhydrase related protein expression in astrocytomas and oligodendroglial tumors","volume":"18","author":"Karjalainen","year":"2018","journal-title":"BMC Cancer"},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0029","doi-asserted-by":"crossref","first-page":"719","DOI":"10.1080\/14756366.2021.1891051","article-title":"Activation of carbonic anhydrase isoforms involved in modulation of emotional memory and cognitive disorders with histamine agonists, antagonists and derivatives","volume":"36","author":"Provensi","year":"2021","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"27","key":"10.1016\/bs.enz.2026.03.003_bib0030","doi-asserted-by":"crossref","first-page":"16000","DOI":"10.1073\/pnas.1910690117","article-title":"The role of carbonic anhydrases in extinction of contextual fear memory","volume":"117","author":"Schmidt","year":"2020","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/bs.enz.2026.03.003_bib0031","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1007\/0-306-47384-4_24","article-title":"Dorzolamide, a 40-year wait. From an oral to a topical carbonic anhydrase inhibitor for the treatment of glaucoma","volume":"11","author":"Ponticello","year":"1998","journal-title":"Pharm. Biotechnol."},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0032","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1016\/S1350-9462(99)00006-3","article-title":"Pharmacological and ocular hypotensive properties of topical carbonic anhydrase inhibitors","volume":"19","author":"Sugrue","year":"2000","journal-title":"Prog. Retin. Eye Res."},{"issue":"10","key":"10.1016\/bs.enz.2026.03.003_bib0033","doi-asserted-by":"crossref","first-page":"1209","DOI":"10.1080\/17460441.2021.1922384","article-title":"Advances in the discovery of novel agents for the treatment of glaucoma","volume":"16","author":"Mincione","year":"2021","journal-title":"Expert Opin. Drug. Discov."},{"issue":"7","key":"10.1016\/bs.enz.2026.03.003_bib0034","doi-asserted-by":"crossref","first-page":"662","DOI":"10.1021\/acsmedchemlett.6b00176","article-title":"Phenotypic assessment and the discovery of topiramate","volume":"7","author":"Maryanoff","year":"2016","journal-title":"ACS Med. Chem. Lett."},{"issue":"Suppl 1","key":"10.1016\/bs.enz.2026.03.003_bib0035","doi-asserted-by":"crossref","first-page":"S5","DOI":"10.1016\/j.seizure.2004.04.016","article-title":"Zonisamide: chemistry, mechanism of action, and pharmacokinetics","volume":"13","author":"Leppik","year":"2004","journal-title":"Seizure"},{"issue":"3","key":"10.1016\/bs.enz.2026.03.003_bib0036","doi-asserted-by":"crossref","first-page":"550","DOI":"10.1021\/jm030912m","article-title":"Unexpected nanomolar inhibition of carbonic anhydrase by COX-2-selective celecoxib: new pharmacological opportunities due to related binding site recognition","volume":"47","author":"Weber","year":"2004","journal-title":"J. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0037","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.bbrc.2016.07.114","article-title":"Structural insight into the inhibition of carbonic anhydrase by the COX-2-selective inhibitor polmacoxib (CG100649)","volume":"478","author":"Kim","year":"2016","journal-title":"Biochem. Biophys Res. Commun."},{"issue":"8","key":"10.1016\/bs.enz.2026.03.003_bib0038","doi-asserted-by":"crossref","first-page":"2669","DOI":"10.1016\/j.bmcl.2008.03.023","article-title":"Carbonic anhydrase inhibitors: the X-ray crystal structure of ethoxzolamide complexed to human isoform II reveals the importance of thr200 and gln92 for obtaining tight-binding inhibitors","volume":"18","author":"Di Fiore","year":"2008","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"14","key":"10.1016\/bs.enz.2026.03.003_bib0039","doi-asserted-by":"crossref","first-page":"2499","DOI":"10.1039\/b800767e","article-title":"Carbonic anhydrase inhibitors. Sulfonamide diuretics revisited\u2014old leads for new applications?","volume":"6","author":"Temperini","year":"2008","journal-title":"Org. Biomol. Chem."},{"issue":"5","key":"10.1016\/bs.enz.2026.03.003_bib0040","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1016\/S0960-894X(03)00029-5","article-title":"Carbonic anhydrase inhibitors: SAR and X-ray crystallographic study for the interaction of sugar sulfamates\/sulfamides with isozymes I, II and IV","volume":"13","author":"Casini","year":"2003","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"9","key":"10.1016\/bs.enz.2026.03.003_bib0041","doi-asserted-by":"crossref","first-page":"2315","DOI":"10.1016\/j.bmcl.2005.03.032","article-title":"Carbonic anhydrase inhibitors. Zonisamide is an effective inhibitor of the cytosolic isozyme II and mitochondrial isozyme V: solution and X-ray crystallographic studies","volume":"15","author":"De Simone","year":"2005","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"17","key":"10.1016\/bs.enz.2026.03.003_bib0042","doi-asserted-by":"crossref","first-page":"4866","DOI":"10.1016\/j.bmcl.2007.06.044","article-title":"Carbonic anhydrase inhibitors. Interaction of the antiepileptic drug sulthiame with twelve mammalian isoforms: kinetic and X-ray crystallographic studies","volume":"17","author":"Temperini","year":"2007","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"22","key":"10.1016\/bs.enz.2026.03.003_bib0043","doi-asserted-by":"crossref","first-page":"7210","DOI":"10.1016\/j.bmc.2013.08.033","article-title":"Structural study of interaction between brinzolamide and dorzolamide inhibition of human carbonic anhydrases","volume":"21","author":"Pinard","year":"2013","journal-title":"Bioorg. Med. Chem."},{"issue":"6","key":"10.1016\/bs.enz.2026.03.003_bib0044","doi-asserted-by":"crossref","first-page":"759","DOI":"10.3109\/14756366.2012.672983","article-title":"Structure-based drug discovery of carbonic anhydrase inhibitors","volume":"27","author":"Supuran","year":"2012","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"7","key":"10.1016\/bs.enz.2026.03.003_bib0045","doi-asserted-by":"crossref","first-page":"793","DOI":"10.1517\/17460441.2013.795145","article-title":"Exploiting the hydrophobic and hydrophilic binding sites for designing carbonic anhydrase inhibitors","volume":"8","author":"De Simone","year":"2013","journal-title":"Expert. Opin. Drug. Discov."},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0046","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1080\/17460441.2017.1253677","article-title":"Advances in structure-based drug discovery of carbonic anhydrase inhibitors","volume":"12","author":"Supuran","year":"2017","journal-title":"Expert. Opin. Drug. Discov."},{"issue":"11","key":"10.1016\/bs.enz.2026.03.003_bib0047","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":"6","key":"10.1016\/bs.enz.2026.03.003_bib0048","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."},{"issue":"12","key":"10.1016\/bs.enz.2026.03.003_bib0049","doi-asserted-by":"crossref","first-page":"963","DOI":"10.1080\/13543784.2018.1548608","article-title":"Carbonic anhydrase inhibitors as emerging agents for the treatment and imaging of hypoxic tumors","volume":"27","author":"Supuran","year":"2018","journal-title":"Expert. Opin. Investig. Drugs."},{"issue":"12","key":"10.1016\/bs.enz.2026.03.003_bib0050","doi-asserted-by":"crossref","first-page":"1197","DOI":"10.1080\/13543784.2021.2014813","article-title":"Carbonic anhydrase inhibitors: an update on experimental agents for the treatment and imaging of hypoxic tumors","volume":"30","author":"Supuran","year":"2021","journal-title":"Expert. Opin. Investig. Drugs."},{"key":"10.1016\/bs.enz.2026.03.003_bib0051","doi-asserted-by":"crossref","first-page":"1163","DOI":"10.1042\/bj0341163","article-title":"Carbonic anhydrase. Purification and nature of the enzyme","volume":"34","author":"Keilin","year":"1940","journal-title":"Biochem. J."},{"key":"10.1016\/bs.enz.2026.03.003_bib0052","series-title":"Carbonic Anhydrase\u2014Its Inhibitors and Activators","first-page":"67","article-title":"Development of sulfonamide carbonic anhydrase inhibitors (CAIs)","author":"Supuran","year":"2004"},{"issue":"10","key":"10.1016\/bs.enz.2026.03.003_bib0053","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. (Lond)"},{"key":"10.1016\/bs.enz.2026.03.003_bib0054","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1080\/14756366.2018.1428572","article-title":"Carbon- versus sulphur-based zinc binding groups for carbonic anhydrase inhibitors?","volume":"33","author":"Supuran","year":"2018","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0055","doi-asserted-by":"crossref","first-page":"4893","DOI":"10.1021\/ja01167a012","article-title":"Heterocyclic sulfonamides as carbonic anhydrase inhibitors","volume":"72","author":"Miller","year":"1950","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/bs.enz.2026.03.003_bib0056","doi-asserted-by":"crossref","first-page":"4890","DOI":"10.1021\/ja01167a011","article-title":"The preparation of heterocyclic sulfonamides","volume":"72","author":"Roblin","year":"1950","journal-title":"J. Am. Chem. Soc."},{"issue":"8","key":"10.1016\/bs.enz.2026.03.003_bib0057","doi-asserted-by":"crossref","first-page":"959","DOI":"10.1021\/jm00140a009","article-title":"Cerebrovasodilatation through selective inhibition of the enzyme carbonic anhydrase. 3. 5-(Arylthio)-, 5-(arylsulfinyl)-, and 5-(arylsulfonyl)thiophene-2-sulfonamides","volume":"24","author":"Barnish","year":"1981","journal-title":"J. Med. Chem."},{"issue":"6","key":"10.1016\/bs.enz.2026.03.003_bib0058","doi-asserted-by":"crossref","first-page":"1805","DOI":"10.1021\/jm00110a008","article-title":"New isomeric classes of topically active ocular hypotensive carbonic anhydrase inhibitors: 5-substituted thieno[2,3-b]thiophene-2-sulfonamides and 5-substituted thieno[3,2-b]thiophene-2-sulfonamides","volume":"34","author":"Prugh","year":"1991","journal-title":"J. Med. Chem."},{"issue":"16","key":"10.1016\/bs.enz.2026.03.003_bib0059","doi-asserted-by":"crossref","first-page":"3027","DOI":"10.1021\/jm00094a016","article-title":"Thieno[2,3-b]furan-2-sulfonamides as topical carbonic anhydrase inhibitors","volume":"35","author":"Hartman","year":"1992","journal-title":"J. Med. Chem."},{"issue":"7","key":"10.1016\/bs.enz.2026.03.003_bib0060","doi-asserted-by":"crossref","first-page":"716","DOI":"10.1002\/jps.2600810726","article-title":"Carbonic anhydrase inhibitors. V: pyrylium salts in the synthesis of isozyme-specific inhibitors","volume":"81","author":"Supuran","year":"1992","journal-title":"J. Pharm. Sci."},{"issue":"7","key":"10.1016\/bs.enz.2026.03.003_bib0061","doi-asserted-by":"crossref","first-page":"3220","DOI":"10.3390\/molecules28073220","article-title":"Five-membered heterocyclic sulfonamides as carbonic anhydrase inhibitors","volume":"28","author":"Angeli","year":"2023","journal-title":"Molecules"},{"issue":"14","key":"10.1016\/bs.enz.2026.03.003_bib0062","doi-asserted-by":"crossref","first-page":"2641","DOI":"10.1021\/jm9900523","article-title":"Carbonic anhydrase inhibitors. Synthesis of water-soluble, topically effective, intraocular pressure-lowering aromatic\/heterocyclic sulfonamides containing cationic or anionic moieties: is the tail more important than the ring?","volume":"42","author":"Scozzafava","year":"1999","journal-title":"J. Med. Chem."},{"issue":"4","key":"10.1016\/bs.enz.2026.03.003_bib0063","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1016\/S0928-0987(99)00022-6","article-title":"Carbonic anhydrase inhibitors. Part 71. Synthesis and ocular pharmacology of a new class of water-soluble, topically effective intraocular pressure lowering sulfonamides incorporating picolinoyl moieties","volume":"8","author":"Supuran","year":"1999","journal-title":"Eur. J. Pharm. Sci."},{"key":"10.1016\/bs.enz.2026.03.003_bib0064","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2022.105920","article-title":"A decade of tail-approach based design of selective as well as potent tumor associated carbonic anhydrase inhibitors","volume":"126","author":"Kumar","year":"2022","journal-title":"Bioorg. Chem."},{"issue":"7","key":"10.1016\/bs.enz.2026.03.003_bib0065","doi-asserted-by":"crossref","first-page":"1937","DOI":"10.1016\/j.bmcl.2005.01.086","article-title":"Carbonic anhydrase inhibitors: X-ray crystal structure of a benzenesulfonamide strong CA II and CA IX inhibitor bearing a pentafluorophenylaminothioureido tail in complex with isozyme II","volume":"15","author":"Di Fiore","year":"2005","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"18","key":"10.1016\/bs.enz.2026.03.003_bib0066","doi-asserted-by":"crossref","first-page":"5721","DOI":"10.1021\/jm050333c","article-title":"Carbonic anhydrase inhibitors: stacking with Phe131 determines active site binding region of inhibitors as exemplified by the X-ray crystal structure of a membrane-impermeant antitumor sulfonamide complexed with isozyme II","volume":"48","author":"Menchise","year":"2005","journal-title":"J. Med. Chem."},{"issue":"25","key":"10.1016\/bs.enz.2026.03.003_bib0067","doi-asserted-by":"crossref","first-page":"8329","DOI":"10.1021\/ja061574s","article-title":"Carbonic anhydrase inhibitors: X-ray and molecular modeling study for the interaction of a fluorescent antitumor sulfonamide with isozyme II and IX","volume":"128","author":"Alterio","year":"2006","journal-title":"J. Am. Chem. Soc."},{"issue":"15","key":"10.1016\/bs.enz.2026.03.003_bib0068","doi-asserted-by":"crossref","first-page":"4201","DOI":"10.1016\/j.bmcl.2007.05.045","article-title":"Carbonic anhydrase inhibitors: inhibition of human, bacterial, and archaeal isozymes with benzene-1,3-disulfonamides\u2014solution and crystallographic studies","volume":"17","author":"Alterio","year":"2007","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"24","key":"10.1016\/bs.enz.2026.03.003_bib0069","doi-asserted-by":"crossref","first-page":"6204","DOI":"10.1016\/j.bmcl.2006.09.022","article-title":"Carbonic anhydrase inhibitors: X-ray crystallographic studies for the binding of 5-amino-1,3,4-thiadiazole-2-sulfonamide and 5-(4-amino-3-chloro-5-fluorophenylsulfonamido)-1,3,4-thiadiazole-2-sulfonamide to human isoform II","volume":"16","author":"Menchise","year":"2006","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0070","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1016\/j.bmcl.2003.09.062","article-title":"Carbonic anhydrase inhibitors: E7070, a sulfonamide anticancer agent, potently inhibits cytosolic isozymes I and II, and transmembrane, tumor-associated isozyme IX","volume":"14","author":"Abbate","year":"2004","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"9","key":"10.1016\/bs.enz.2026.03.003_bib0071","doi-asserted-by":"crossref","first-page":"2357","DOI":"10.1016\/j.bmcl.2004.01.096","article-title":"Carbonic anhydrase inhibitors: X-ray crystallographic structure of the adduct of human isozyme II with a topically acting antiglaucoma sulfonamide","volume":"14","author":"Abbate","year":"2004","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0072","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1016\/j.bmcl.2007.10.110","article-title":"Carbonic anhydrase inhibitors. Interaction of 2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide with 12 mammalian isoforms: kinetic and X-ray crystallographic studies","volume":"18","author":"G\u00fczel","year":"2008","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"20","key":"10.1016\/bs.enz.2026.03.003_bib0073","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":"Bioorg. Med. Chem."},{"issue":"12","key":"10.1016\/bs.enz.2026.03.003_bib0074","doi-asserted-by":"crossref","first-page":"3170","DOI":"10.1016\/j.bmcl.2009.04.123","article-title":"Carbonic anhydrase inhibitors. Phenacetyl-, pyridylacetyl- and thienylacetyl-substituted aromatic sulfonamides act as potent and selective isoform VII inhibitors","volume":"19","author":"G\u00fczel","year":"2009","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"12","key":"10.1016\/bs.enz.2026.03.003_bib0075","doi-asserted-by":"crossref","first-page":"3732","DOI":"10.1016\/j.bmc.2011.05.006","article-title":"Conformational variability of different sulfonamide inhibitors with thienyl-acetamido moieties attributes to differential binding in the active site of cytosolic human carbonic anhydrase isoforms","volume":"19","author":"Biswas","year":"2011","journal-title":"Bioorg. Med. Chem."},{"issue":"6","key":"10.1016\/bs.enz.2026.03.003_bib0076","doi-asserted-by":"crossref","first-page":"1896","DOI":"10.1021\/jm101541x","article-title":"Ureido-substituted benzenesulfonamides potently inhibit carbonic anhydrase IX and show antimetastatic activity in a model of breast cancer metastasis","volume":"54","author":"Pacchiano","year":"2011","journal-title":"J. Med. Chem."},{"issue":"14","key":"10.1016\/bs.enz.2026.03.003_bib0077","doi-asserted-by":"crossref","first-page":"3297","DOI":"10.3390\/cancers14143297","article-title":"Cancer therapeutic targeting of hypoxia induced carbonic anhydrase IX: from bench to bedside","volume":"14","author":"McDonald","year":"2022","journal-title":"Cancers (Basel)"},{"issue":"7","key":"10.1016\/bs.enz.2026.03.003_bib0078","doi-asserted-by":"crossref","first-page":"484","DOI":"10.1097\/COC.0000000000000691","article-title":"A phase 1 study of SLC-0111, a novel inhibitor of carbonic anhydrase IX, in patients with advanced solid tumors","volume":"43","author":"McDonald","year":"2020","journal-title":"Am. J. Clin. Oncol."},{"issue":"44","key":"10.1016\/bs.enz.2026.03.003_bib0079","doi-asserted-by":"crossref","first-page":"8371","DOI":"10.1039\/c0cc02707c","article-title":"Selective hydrophobic pocket binding observed within the carbonic anhydrase II active site accommodate different 4-substituted-ureido-benzenesulfonamides and correlate to inhibitor potency","volume":"46","author":"Pacchiano","year":"2010","journal-title":"Chem. Commun. (Camb)"},{"key":"10.1016\/bs.enz.2026.03.003_bib0080","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1016\/j.ejmech.2017.03.026","article-title":"Structure activity study of carbonic anhydrase IX: selective inhibition with ureido-substituted benzenesulfonamides","volume":"132","author":"Mboge","year":"2017","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0081","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2020.113035","article-title":"Handling drug-target selectivity: a study on ureido containing carbonic anhydrase inhibitors","volume":"212","author":"Akgul","year":"2021","journal-title":"Eur. J. Med. Chem."},{"issue":"3","key":"10.1016\/bs.enz.2026.03.003_bib0082","doi-asserted-by":"crossref","first-page":"1494","DOI":"10.1021\/jm501798g","article-title":"Carbonic anhydrase inhibitors with dual-tail moieties to match the hydrophobic and hydrophilic halves of the carbonic anhydrase active site","volume":"58","author":"Tanpure","year":"2015","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0083","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."},{"issue":"6","key":"10.1016\/bs.enz.2026.03.003_bib0084","doi-asserted-by":"crossref","first-page":"3317","DOI":"10.1021\/acs.jmedchem.9b02090","article-title":"Discovery of potent dual-tailed benzenesulfonamide inhibitors of human carbonic anhydrases implicated in glaucoma and in vivo profiling of their intraocular pressure-lowering action","volume":"63","author":"Fares","year":"2020","journal-title":"J. Med. Chem."},{"issue":"2","key":"10.1016\/bs.enz.2026.03.003_bib0085","doi-asserted-by":"crossref","first-page":"1863","DOI":"10.1021\/acs.jmedchem.4c02586","article-title":"Novel 3-sulfonamide dual-tail pyrrol-2-one bridged molecules as potent Human carbonic anhydrase isoform inhibitors: design, synthesis, molecular modeling investigation, and anticancer activity in MeWo, SK-BR-3, and MG-63 cell lines","volume":"68","author":"Al-Matarneh","year":"2025","journal-title":"J. Med. Chem."},{"issue":"13","key":"10.1016\/bs.enz.2026.03.003_bib0086","doi-asserted-by":"crossref","first-page":"7422","DOI":"10.1021\/acs.jmedchem.0c00733","article-title":"Sulfonamide inhibitors of human carbonic anhydrases designed through a three-tails approach: improving ligand\/isoform matching and selectivity of action","volume":"63","author":"Bonardi","year":"2020","journal-title":"J. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0087","doi-asserted-by":"crossref","first-page":"930","DOI":"10.1080\/14756366.2022.2053526","article-title":"The three-tails approach as a new strategy to improve selectivity of action of sulphonamide inhibitors against tumour-associated carbonic anhydrase IX and XII","volume":"37","author":"Bonardi","year":"2022","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"3","key":"10.1016\/bs.enz.2026.03.003_bib0088","doi-asserted-by":"crossref","first-page":"3115","DOI":"10.1021\/acs.jmedchem.5c03037","article-title":"First-in-class dual PDGFR\/Carbonic anhydrase IX\/XII inhibitors: 6,7-dimethoxyquinoline-sulfonamides as promising antileukemic agents","volume":"69","author":"Roshdy","year":"2026","journal-title":"J. Med. Chem."},{"issue":"3","key":"10.1016\/bs.enz.2026.03.003_bib0089","doi-asserted-by":"crossref","first-page":"3289","DOI":"10.1021\/acs.jmedchem.5c03157","article-title":"Targeting metabolic and pH regulatory pathways in cancer via dual inhibition of nicotinamide phosphoribosyltransferase and carbonic anhydrases IX and XII","volume":"69","author":"Paoletti","year":"2026","journal-title":"J. Med. Chem."},{"issue":"2","key":"10.1016\/bs.enz.2026.03.003_bib0090","doi-asserted-by":"crossref","first-page":"1454","DOI":"10.1021\/acs.jmedchem.5c02930","article-title":"Hybridization approach applied to umbelliferon and vanilloids toward new inhibitors of carbonic anhydrases IX and XII with in vitro antiproliferative and anti-inflammatory activities","volume":"69","author":"Melfi","year":"2026","journal-title":"J. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0091","doi-asserted-by":"crossref","DOI":"10.1002\/ddr.70214","article-title":"Multitargeted anti-inflammatory agents: novel pyrazole and pyrazolo[1,5-a]pyrimidine carbonic anhydrase and COX-2 inhibitors with optimal in vivo efficacy and low toxicity","volume":"87","author":"Fakhry","year":"2026","journal-title":"Drug. Dev. Res."},{"key":"10.1016\/bs.enz.2026.03.003_bib0092","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2025.118504","article-title":"Ketoconazole-carbonic anhydrase inhibitors as potential anticancer agents","volume":"304","author":"Andreucci","year":"2026","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0093","article-title":"Exploring dual inhibitors carbonic anhydrases and phosphodiesterase 5 as potential agents for treatment Alzheimer\u2019s disease","volume":"303","author":"Angeli","year":"2026","journal-title":"Eur. J. Med. Chem."},{"issue":"Pt 1","key":"10.1016\/bs.enz.2026.03.003_bib0094","article-title":"Click-modifiable isatin hydrazones as COX-2, VEGFR-2, and carbonic anhydrase inhibitors: A multi-target approach to cancer therapy","volume":"302","author":"El-Attar","year":"2026","journal-title":"Eur. J. Med. Chem."},{"issue":"21","key":"10.1016\/bs.enz.2026.03.003_bib0095","doi-asserted-by":"crossref","first-page":"22874","DOI":"10.1021\/acs.jmedchem.5c01788","article-title":"Discovery of first-in-class carbonic anhydrase\/histone deacetylase dual inhibitors with antiproliferative activity in cancer cells","volume":"68","author":"Bozdag","year":"2025","journal-title":"J. Med. Chem."},{"issue":"9","key":"10.1016\/bs.enz.2026.03.003_bib0096","doi-asserted-by":"crossref","first-page":"1387","DOI":"10.3390\/ph18091387","article-title":"Hybrid and chimeric heterocycles for the inhibition of carbonic anhydrases","volume":"18","author":"Paoletti","year":"2025","journal-title":"Pharmaceuticals (Basel)"},{"key":"10.1016\/bs.enz.2026.03.003_bib0097","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2025.118107","article-title":"Dual inhibition of carbonic anhydrase IX and glutathione peroxidase 4 as a novel strategy for ferroptosis-induced tumor cell death","volume":"300","author":"Renzi","year":"2025","journal-title":"Eur. J. Med. Chem."},{"issue":"17","key":"10.1016\/bs.enz.2026.03.003_bib0098","doi-asserted-by":"crossref","first-page":"18579","DOI":"10.1021\/acs.jmedchem.5c01459","article-title":"Repurposing drug metabolites into dual \u03b2-adrenergic receptor-carbonic anhydrase modulators as potential tools for ocular disorders","volume":"68","author":"Ammara","year":"2025","journal-title":"J. Med. Chem."},{"issue":"9","key":"10.1016\/bs.enz.2026.03.003_bib0099","doi-asserted-by":"crossref","first-page":"4316","DOI":"10.1039\/D5MD00109A","article-title":"Pegylation approach applied to erlotinib-carbonic anhydrase inhibitors hybrids towards anticancer agents","volume":"16","author":"Filiberti","year":"2025","journal-title":"RSC Med. Chem."},{"issue":"6","key":"10.1016\/bs.enz.2026.03.003_bib0100","doi-asserted-by":"crossref","first-page":"1627","DOI":"10.1021\/acsptsci.5c00011","article-title":"Multi-target glitazones for modulating peroxisome proliferator-activated receptor-\u03b3, cyclooxygenase-2, and carbonic anhydrases for the management of metabolic dysfunction","volume":"8","author":"Elzahhar","year":"2025","journal-title":"ACS Pharmacol. Transl. Sci."},{"key":"10.1016\/bs.enz.2026.03.003_bib0101","doi-asserted-by":"crossref","first-page":"687","DOI":"10.1016\/0223-5234(96)88286-9","article-title":"Carbonic anhydrase inhibitors. Part 24. A quantitative structure-activity study of positively-charged sulfonamide inhibitors","volume":"30","author":"Supuran","year":"1995","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0102","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1016\/S0223-5234(98)80017-2","article-title":"Carbonic anhydrase inhibitors. Part 53. Synthesis of substituted-pyridinium derivatives of aromatic sulfonamides: the first non-polymeric membrane-impermeable inhibitors with selectivity for isozyme IV","volume":"33","author":"Supuran","year":"1998","journal-title":"Eur. J. Med. Chem."},{"issue":"2","key":"10.1016\/bs.enz.2026.03.003_bib0103","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1021\/jm990479+","article-title":"Carbonic anhydrase inhibitors: synthesis of membrane-impermeant low molecular weight sulfonamides possessing in vivo selectivity for the membrane-bound versus cytosolic isozymes","volume":"43","author":"Scozzafava","year":"2000","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0104","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2020.104204","article-title":"Pyridinium derivatives of 3-aminobenzenesulfonamide are nanomolar-potent inhibitors of tumor-expressed carbonic anhydrase isozymes CA IX and CA XII","volume":"103","author":"Akocak","year":"2020","journal-title":"Bioorg. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0105","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1016\/S0223-5234(97)81681-9","article-title":"Carbonic anhydrase inhibitors. Part 43. Schiff bases derived from aromatic sulfonamides: towards more specific inhibitors for membrane-bound versus cytosolic isozymes","volume":"32","author":"Supuran","year":"1997","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0106","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/S0223-5234(98)80033-0","article-title":"Carbonic anhydrase inhibitors. Part 49. Synthesis of substituted ureido- and thioureido derivatives of aromatic\/heterocyclic sulfonamides with increased affinities for isozyme I","volume":"33","author":"Supuran","year":"1998","journal-title":"Eur. J. Med. Chem."},{"issue":"21","key":"10.1016\/bs.enz.2026.03.003_bib0107","doi-asserted-by":"crossref","first-page":"5427","DOI":"10.1016\/j.bmcl.2004.07.087","article-title":"Carbonic anhydrase inhibitors: synthesis and inhibition of cytosolic\/tumor-associated carbonic anhydrase isozymes I, II, and IX with sulfonamides incorporating 1,2,4-triazine moieties","volume":"14","author":"Garaj","year":"2004","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"12","key":"10.1016\/bs.enz.2026.03.003_bib0108","doi-asserted-by":"crossref","first-page":"3102","DOI":"10.1016\/j.bmcl.2005.04.056","article-title":"Carbonic anhydrase inhibitors: novel sulfonamides incorporating 1,3,5-triazine moieties as inhibitors of the cytosolic and tumour-associated carbonic anhydrase isozymes I, II and IX","volume":"15","author":"Garaj","year":"2005","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"10","key":"10.1016\/bs.enz.2026.03.003_bib0109","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":"Bioorg. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0110","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1016\/j.bioorg.2018.08.005","article-title":"Novel sulfonamides incorporating 1,3,5-triazine and amino acid structural motifs as inhibitors of the physiological carbonic anhydrase isozymes I, II and IV and tumor-associated isozyme IX","volume":"81","author":"Miku\u0161","year":"2018","journal-title":"Bioorg. Chem."},{"issue":"24","key":"10.1016\/bs.enz.2026.03.003_bib0111","doi-asserted-by":"crossref","first-page":"6332","DOI":"10.1016\/j.bmcl.2008.10.093","article-title":"Carbonic anhydrase inhibitors: 2-substituted-1,3,4-thiadiazole-5-sulfamides act as powerful and selective inhibitors of the mitochondrial isozymes VA and VB over the cytosolic and membrane-associated carbonic anhydrases I, II and IV","volume":"18","author":"Smaine","year":"2008","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"14","key":"10.1016\/bs.enz.2026.03.003_bib0112","doi-asserted-by":"crossref","first-page":"4894","DOI":"10.1016\/j.bmc.2009.06.006","article-title":"Carbonic anhydrase inhibitors. Aromatic\/heterocyclic sulfonamides incorporating phenacetyl, pyridylacetyl and thienylacetyl tails act as potent inhibitors of human mitochondrial isoforms VA and VB","volume":"17","author":"G\u00fczel","year":"2009","journal-title":"Bioorg. Med. Chem."},{"issue":"9","key":"10.1016\/bs.enz.2026.03.003_bib0113","doi-asserted-by":"crossref","first-page":"3364","DOI":"10.1158\/0008-5472.CAN-10-4261","article-title":"Targeting tumor hypoxia: suppression of breast tumor growth and metastasis by novel carbonic anhydrase IX inhibitors","volume":"71","author":"Lou","year":"2011","journal-title":"Cancer Res."},{"issue":"44","key":"10.1016\/bs.enz.2026.03.003_bib0114","doi-asserted-by":"crossref","first-page":"5210","DOI":"10.1038\/onc.2012.550","article-title":"Targeting carbonic anhydrase IX depletes breast cancer stem cells within the hypoxic niche","volume":"32","author":"Lock","year":"2013","journal-title":"Oncogene"},{"issue":"35","key":"10.1016\/bs.enz.2026.03.003_bib0115","doi-asserted-by":"crossref","first-page":"eabj0364","DOI":"10.1126\/sciadv.abj0364","article-title":"Genome-wide synthetic lethal screen unveils novel CAIX-NFS1\/xCT axis as a targetable vulnerability in hypoxic solid tumors","volume":"7","author":"Chafe","year":"2021","journal-title":"Sci. Adv."},{"issue":"9","key":"10.1016\/bs.enz.2026.03.003_bib0116","doi-asserted-by":"crossref","first-page":"2569","DOI":"10.1016\/j.bmc.2017.03.027","article-title":"Synthesis and carbonic anhydrase inhibition of a series of SLC-0111 analogs","volume":"25","author":"Carta","year":"2017","journal-title":"Bioorg. Med. Chem."},{"issue":"5","key":"10.1016\/bs.enz.2026.03.003_bib0117","doi-asserted-by":"crossref","first-page":"976","DOI":"10.1016\/j.bmc.2016.01.019","article-title":"Kinetic and X-ray crystallographic investigations on carbonic anhydrase isoforms I, II, IX and XII of a thioureido analog of SLC-0111","volume":"24","author":"Lomelino","year":"2016","journal-title":"Bioorg. Med. Chem."},{"issue":"14","key":"10.1016\/bs.enz.2026.03.003_bib0118","doi-asserted-by":"crossref","first-page":"6328","DOI":"10.1021\/acs.jmedchem.8b00770","article-title":"Discovery of 4-hydroxy-3-(3-(phenylureido)benzenesulfonamides as SLC-0111 analogues for the treatment of hypoxic tumors overexpressing carbonic anhydrase IX","volume":"61","author":"Bozdag","year":"2018","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0119","doi-asserted-by":"crossref","first-page":"542","DOI":"10.1016\/j.bioorg.2018.02.015","article-title":"Design and synthesis of novel 1,3-diaryltriazene-substituted sulfonamides as potent and selective carbonic anhydrase II inhibitors","volume":"77","author":"Lolak","year":"2018","journal-title":"Bioorg. Chem."},{"issue":"9","key":"10.1016\/bs.enz.2026.03.003_bib0120","doi-asserted-by":"crossref","first-page":"963","DOI":"10.1021\/acsmedchemlett.7b00280","article-title":"Discovery of new selenoureido analogues of 4-(4-Fluorophenylureido)benzenesulfonamide as carbonic anhydrase inhibitors","volume":"8","author":"Angeli","year":"2017","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2026.03.003_bib0121","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1016\/j.bioorg.2018.11.014","article-title":"SLC-0111 enaminone analogs, 3\/4-(3-aryl-3-oxopropenyl) aminobenzenesulfonamides, as novel selective subnanomolar inhibitors of the tumor-associated carbonic anhydrase isoform IX","volume":"83","author":"Eldehna","year":"2019","journal-title":"Bioorg. Chem."},{"issue":"18","key":"10.1016\/bs.enz.2026.03.003_bib0122","doi-asserted-by":"crossref","first-page":"3850","DOI":"10.1016\/j.bmcl.2015.07.060","article-title":"Synthesis of sulfonamides incorporating piperazinyl-ureido moieties and their carbonic anhydrase I, II, IX and XII inhibitory activity","volume":"25","author":"Congiu","year":"2015","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2026.03.003_bib0123","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2020.103728","article-title":"Appliance of the piperidinyl-hydrazidoureido linker to benzenesulfonamide compounds: synthesis, in vitro and in silico evaluation of potent carbonic anhydrase II, IX and XII inhibitors","volume":"98","author":"Moi","year":"2020","journal-title":"Bioorg. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0124","doi-asserted-by":"crossref","first-page":"794","DOI":"10.1016\/j.bioorg.2019.04.002","article-title":"Novel synthesized SLC-0111 thiazole and thiadiazole analogues: determination of their carbonic anhydrase inhibitory activity and molecular modeling studies","volume":"87","author":"Abo-Ashour","year":"2019","journal-title":"Bioorg. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0125","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2020.112745","article-title":"3-Methylthiazolo[3,2-a]benzimidazole-benzenesulfonamide conjugates as novel carbonic anhydrase inhibitors endowed with anticancer activity: design, synthesis, biological and molecular modeling studies","volume":"207","author":"Alkhaldi","year":"2020","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0126","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1016\/j.ejmech.2018.10.068","article-title":"Enhancement of the tail hydrophobic interactions within the carbonic anhydrase IX active site via structural extension: design and synthesis of novel N-substituted isatins-SLC-0111 hybrids as carbonic anhydrase inhibitors and antitumor agents","volume":"162","author":"Eldehna","year":"2019","journal-title":"Eur. J. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0127","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1186\/s40164-025-00690-z","article-title":"An ureido-substituted benzenesulfonamide carbonic anhydrase inhibitor exerts a potent antitumor effect in vitro and in vivo","volume":"14","author":"Gazzaroli","year":"2025","journal-title":"Exp. Hematol. Oncol."},{"key":"10.1016\/bs.enz.2026.03.003_bib0128","doi-asserted-by":"crossref","DOI":"10.1016\/j.bmc.2025.118304","article-title":"Discovery of novel thiourea benzenesulfonamides based 1,8-naphthalimide derivatives as carbonic anhydrase IX inhibitors that induce ferroptosis and inhibit triple-negative breast cancer metastasis","volume":"129","author":"Liu","year":"2025","journal-title":"Bioorg. Med. Chem."},{"issue":"14","key":"10.1016\/bs.enz.2026.03.003_bib0129","doi-asserted-by":"crossref","first-page":"15151","DOI":"10.1021\/acs.jmedchem.5c01392","article-title":"Design, synthesis, and In vitro anticancer evaluation of thiazole-based chalcones linked to sulfanilamide as tumor-associated carbonic anhydrase IX and XII inhibitors","volume":"68","author":"Elshamsy","year":"2025","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0130","doi-asserted-by":"crossref","DOI":"10.3389\/fchem.2025.1571646","article-title":"Discovery of a novel 4-pyridyl SLC-0111 analog targeting tumor-associated carbonic anhydrase isoform IX through tail-based design approach with potent anticancer activity","volume":"13","author":"Hashem","year":"2025","journal-title":"Front. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0131","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2025.108335","article-title":"Development of novel amino-benzenesulfonamide derivatives and their analogues as carbonic anhydrase inhibitors: design, synthesis, anticancer activity assessment, and pharmacokinetic studies using UPLC-MS\/MS","volume":"159","author":"Elsayad","year":"2025","journal-title":"Bioorg. Chem."},{"issue":"3","key":"10.1016\/bs.enz.2026.03.003_bib0132","doi-asserted-by":"crossref","DOI":"10.1002\/jbt.70217","article-title":"Investigating the anti-inflammatory potential of SLC-0111: A carbonic anhydrase inhibitor targeting cyclooxygenase-mediated inflammatory pathways in a carrageenan-induced rat model","volume":"39","author":"Do\u011fan","year":"2025","journal-title":"J. Biochem. Mol. Toxicol."},{"issue":"8","key":"10.1016\/bs.enz.2026.03.003_bib0133","doi-asserted-by":"crossref","DOI":"10.1002\/ardp.202400157","article-title":"In-vitro and in-silico investigations of SLC-0111 hydrazinyl analogs as human carbonic anhydrase I, II, IX, and XII inhibitors","volume":"357","author":"Sharma","year":"2024","journal-title":"Arch. Pharm. (Weinheim)"},{"key":"10.1016\/bs.enz.2026.03.003_bib0134","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2024.107192","article-title":"A comparative study of diaryl urea molecules with and without sulfonamide group on carbonic anhydrase IX and XII inhibition and its consequence on breast cancer cells","volume":"145","author":"Debnath","year":"2024","journal-title":"Bioorg. Chem."},{"issue":"10","key":"10.1016\/bs.enz.2026.03.003_bib0135","doi-asserted-by":"crossref","first-page":"755","DOI":"10.2174\/0118715206285326240207045249","article-title":"1,3-Diaryl triazenes incorporating disulfonamides show both antiproliferative activity and effective inhibition of tumor-associated carbonic anhydrases IX and XII","volume":"24","author":"Lolak","year":"2024","journal-title":"Anticancer Agents Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0136","doi-asserted-by":"crossref","DOI":"10.1016\/j.canlet.2023.216338","article-title":"The CAIX inhibitor SLC-0111 exerts anti-cancer activity on gastric cancer cell lines and resensitizes resistant cells to 5-Fluorouracil, taxane-derived, and platinum-based drugs","volume":"571","author":"Andreucci","year":"2023","journal-title":"Cancer Lett."},{"issue":"15","key":"10.1016\/bs.enz.2026.03.003_bib0137","doi-asserted-by":"crossref","first-page":"10558","DOI":"10.1021\/acs.jmedchem.3c00721","article-title":"1,5-Diaryl-1,2,4-triazole ureas as new SLC-0111 analogues endowed with dual carbonic anhydrase and VEGFR-2 inhibitory activities","volume":"66","author":"Elsawi","year":"2023","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0138","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2023.115538","article-title":"Design and synthesis of 6-arylpyridine-tethered sulfonamides as novel selective inhibitors of carbonic anhydrase IX with promising antitumor features toward the human colorectal cancer","volume":"258","author":"Eldehna","year":"2023","journal-title":"Eur. J. Med. Chem."},{"issue":"6","key":"10.1016\/bs.enz.2026.03.003_bib0139","doi-asserted-by":"crossref","first-page":"810","DOI":"10.1021\/acsmedchemlett.3c00094","article-title":"Discovery of novel hydroxyimine-tethered benzenesulfonamides as potential Human carbonic anhydrase IX\/XII inhibitors","volume":"14","author":"Peerzada","year":"2023","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2026.03.003_bib0140","doi-asserted-by":"crossref","DOI":"10.3389\/fonc.2023.1118268","article-title":"SLC-0111, an inhibitor of carbonic anhydrase IX, attenuates hepatoblastoma cell viability and migration","volume":"13","author":"Eloranta","year":"2023","journal-title":"Front. Oncol."},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0141","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1080\/14756366.2022.2132485","article-title":"Design and synthesis of some new benzoylthioureido benzenesulfonamide derivatives and their analogues as carbonic anhydrase inhibitors","volume":"38","author":"Oudah","year":"2023","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"24","key":"10.1016\/bs.enz.2026.03.003_bib0142","doi-asserted-by":"crossref","first-page":"11039","DOI":"10.1111\/jcmm.17027","article-title":"Pharmacological inhibition of Carbonic anhydrase IX and XII to enhance targeting of acute myeloid leukaemia cells under hypoxic conditions","volume":"25","author":"Chen","year":"2021","journal-title":"J. Cell. Mol. Med."},{"issue":"4","key":"10.1016\/bs.enz.2026.03.003_bib0143","doi-asserted-by":"crossref","first-page":"3066","DOI":"10.1021\/acs.jmedchem.3c02254","article-title":"Novel carbonic anhydrase inhibitors with dual-tail core sulfonamide show potent and lasting effects for glaucoma therapy","volume":"67","author":"Angeli","year":"2024","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0144","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/bs.accb.2025.09.003","article-title":"Carbohydrate-modified carbonic anhydrase inhibitors: advances and challenges","volume":"87","author":"Giovannuzzi","year":"2025","journal-title":"Adv. Carbohydr. Chem. Biochem."},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0145","doi-asserted-by":"crossref","DOI":"10.1080\/14756366.2023.2202360","article-title":"Discovery of the first-in-class potent and isoform-selective human carbonic anhydrase III inhibitors","volume":"38","author":"Giovannuzzi","year":"2023","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"13","key":"10.1016\/bs.enz.2026.03.003_bib0146","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":"48","author":"Carta","year":"2012","journal-title":"Chem. Commun. (Camb)"},{"issue":"4","key":"10.1016\/bs.enz.2026.03.003_bib0147","doi-asserted-by":"crossref","first-page":"1721","DOI":"10.1021\/jm300031j","article-title":"Dithiocarbamates strongly inhibit carbonic anhydrases and show antiglaucoma action in vivo","volume":"55","author":"Carta","year":"2012","journal-title":"J. Med. Chem."},{"issue":"12","key":"10.1016\/bs.enz.2026.03.003_bib0148","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":"59","author":"Vullo","year":"2016","journal-title":"J. Med. Chem."},{"issue":"11","key":"10.1016\/bs.enz.2026.03.003_bib0149","doi-asserted-by":"crossref","first-page":"4691","DOI":"10.1021\/jm400414j","article-title":"Xanthates and trithiocarbonates strongly inhibit carbonic anhydrases and show antiglaucoma effects in vivo","volume":"56","author":"Carta","year":"2013","journal-title":"J. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0150","doi-asserted-by":"crossref","DOI":"10.1080\/14756366.2023.2201403","article-title":"Effect of hydrophobic extension of aryl enaminones and pyrazole-linked compounds combined with sulphonamide, sulfaguanidine, or carboxylic acid functionalities on carbonic anhydrase inhibitory potency and selectivity","volume":"38","author":"Allam","year":"2023","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0151","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2021.114008","article-title":"Natural inspired ligustrazine-based SLC-0111 analogues as novel carbonic anhydrase inhibitors","volume":"228","author":"Elimam","year":"2022","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0152","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2021.113800","article-title":"Natural inspired piperine-based sulfonamides and carboxylic acids as carbonic anhydrase inhibitors: design, synthesis and biological evaluation","volume":"225","author":"Elimam","year":"2021","journal-title":"Eur. J. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0153","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1016\/j.bmc.2015.11.034","article-title":"Inhibition of carbonic anhydrase isoforms I, II, IV, VII and XII with carboxylates and sulfonamides incorporating phthalimide\/phthalic anhydride scaffolds","volume":"24","author":"El-Azab","year":"2016","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0154","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2023.106976","article-title":"Boron-containing carbonic anhydrases inhibitors","volume":"143","author":"Giovannuzzi","year":"2024","journal-title":"Bioorg. Chem."},{"issue":"12","key":"10.1016\/bs.enz.2026.03.003_bib0155","doi-asserted-by":"crossref","first-page":"1241","DOI":"10.1080\/13543776.2025.2576513","article-title":"Therapeutic applications of benzoxaborole compounds: a patent and literature analysis (2019-2024)","volume":"35","author":"Giovannuzzi","year":"2025","journal-title":"Expert. Opin. Ther. Pat."},{"issue":"20","key":"10.1016\/bs.enz.2026.03.003_bib0156","doi-asserted-by":"crossref","first-page":"18221","DOI":"10.1021\/acs.jmedchem.4c01516","article-title":"Benzoxaborinine, new chemotype for carbonic anhydrase inhibition: ex novo synthesis, crystallography, in silico studies, and anti-melanoma cell line activity","volume":"67","author":"Giovannuzzi","year":"2024","journal-title":"J. Med. Chem."},{"issue":"4","key":"10.1016\/bs.enz.2026.03.003_bib0157","doi-asserted-by":"crossref","DOI":"10.1111\/cbdd.70108","article-title":"A journey around boronic acids: sulfonyl hydrazone-containing derivatives as carbonic anhydrase inhibitors","volume":"105","author":"Anak\u00f6k","year":"2025","journal-title":"Chem. Biol. Drug. Des."},{"issue":"Pt 2","key":"10.1016\/bs.enz.2026.03.003_bib0158","article-title":"Exploring the binding mode of phenyl and vinyl boronic acids to human carbonic anhydrases","volume":"282","author":"Esposito","year":"2024","journal-title":"Int. J. Biol. Macromol."},{"issue":"8","key":"10.1016\/bs.enz.2026.03.003_bib0159","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."},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0160","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."},{"issue":"15","key":"10.1016\/bs.enz.2026.03.003_bib0161","doi-asserted-by":"crossref","first-page":"4511","DOI":"10.1016\/j.bmcl.2010.06.040","article-title":"Coumarins incorporating hydroxy- and chloro-moieties selectively inhibit the transmembrane, tumor-associated carbonic anhydrase isoforms IX and XII over the cytosolic ones I and II","volume":"20","author":"Maresca","year":"2010","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"24","key":"10.1016\/bs.enz.2026.03.003_bib0162","doi-asserted-by":"crossref","first-page":"7255","DOI":"10.1016\/j.bmcl.2010.10.094","article-title":"7,8-disubstituted- but not 6,7-disubstituted coumarins selectively inhibit the transmembrane, tumor-associated carbonic anhydrase isoforms IX and XII over the cytosolic ones I and II in the low nanomolar\/subnanomolar range","volume":"20","author":"Maresca","year":"2010","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"24","key":"10.1016\/bs.enz.2026.03.003_bib0163","doi-asserted-by":"crossref","first-page":"8271","DOI":"10.1021\/jm200983e","article-title":"Glycosyl coumarin carbonic anhydrase IX and XII inhibitors strongly attenuate the growth of primary breast tumors","volume":"54","author":"Touisni","year":"2011","journal-title":"J. Med. Chem."},{"issue":"7","key":"10.1016\/bs.enz.2026.03.003_bib0164","doi-asserted-by":"crossref","first-page":"2266","DOI":"10.1016\/j.bmc.2012.02.014","article-title":"Novel coumarins and 2-thioxo-coumarins as inhibitors of the tumor-associated carbonic anhydrases IX and XII","volume":"20","author":"Carta","year":"2012","journal-title":"Bioorg. Med. Chem."},{"issue":"21","key":"10.1016\/bs.enz.2026.03.003_bib0165","doi-asserted-by":"crossref","first-page":"6955","DOI":"10.1016\/j.bmc.2015.09.041","article-title":"Click-tailed coumarins with potent and selective inhibitory action against the tumor-associated carbonic anhydrases IX and XII","volume":"23","author":"Nocentini","year":"2015","journal-title":"Bioorg. Med. Chem."},{"issue":"2","key":"10.1016\/bs.enz.2026.03.003_bib0166","doi-asserted-by":"crossref","first-page":"677","DOI":"10.1016\/j.bmc.2016.11.039","article-title":"Coumarins and other fused bicyclic heterocycles with selective tumor-associated carbonic anhydrase isoforms inhibitory activity","volume":"25","author":"Bozdag","year":"2017","journal-title":"Bioorg. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0167","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":"59","author":"Ferraroni","year":"2016","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0168","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.ejmech.2018.01.033","article-title":"Structural investigations on coumarins leading to chromeno[4,3-c]pyrazol-4-ones and pyrano[4,3-c]pyrazol-4-ones: new scaffolds for the design of the tumor-associated carbonic anhydrase isoforms IX and XII","volume":"146","author":"Bonardi","year":"2018","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0169","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1016\/j.bioorg.2019.04.004","article-title":"Synthesis and biological evaluation of coumarin-1,3,4-oxadiazole hybrids as selective carbonic anhydrase IX and XII inhibitors","volume":"87","author":"Narella","year":"2019","journal-title":"Bioorg. Chem."},{"issue":"9","key":"10.1016\/bs.enz.2026.03.003_bib0170","doi-asserted-by":"crossref","first-page":"947","DOI":"10.1021\/acsmedchemlett.8b00362","article-title":"Heterocoumarins are selective carbonic anhydrase IX and XII inhibitors with cytotoxic effects against cancer cells lines","volume":"9","author":"Angeli","year":"2018","journal-title":"ACS Med. Chem. Lett."},{"issue":"7","key":"10.1016\/bs.enz.2026.03.003_bib0171","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1021\/acsmedchemlett.8b00170","article-title":"Targeting tumor associated carbonic anhydrases IX and XII: highly isozyme selective coumarin and psoralen inhibitors","volume":"9","author":"Melis","year":"2018","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2026.03.003_bib0172","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2020.112897","article-title":"Novel 3-substituted coumarins as selective human carbonic anhydrase IX and XII inhibitors: synthesis, biological and molecular dynamics analysis","volume":"209","author":"Abdelrahman","year":"2021","journal-title":"Eur. J. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0173","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."},{"issue":"8","key":"10.1016\/bs.enz.2026.03.003_bib0174","doi-asserted-by":"crossref","first-page":"1252","DOI":"10.1002\/cmdc.202000915","article-title":"Coumarin-Thiourea hybrids show potent carbonic anhydrase IX and XIII inhibitory action","volume":"16","author":"Thacker","year":"2021","journal-title":"Chem. Med. Chem."},{"issue":"11","key":"10.1016\/bs.enz.2026.03.003_bib0175","doi-asserted-by":"crossref","first-page":"9401","DOI":"10.3390\/ijms24119401","article-title":"Conformationally restricted glycoconjugates derived from arylsulfonamides and coumarins: new families of tumour-associated carbonic anhydrase inhibitors","volume":"24","author":"Mart\u00ednez-Montiel","year":"2023","journal-title":"Int. J. Mol. Sci."},{"issue":"6","key":"10.1016\/bs.enz.2026.03.003_bib0176","doi-asserted-by":"crossref","first-page":"5787","DOI":"10.1021\/acsomega.2c07459","article-title":"Tail-approach-based design and synthesis of coumarin-monoterpenes as carbonic anhydrase inhibitors and anticancer agents","volume":"8","author":"Zengin Kurt","year":"2023","journal-title":"ACS Omega"},{"issue":"9","key":"10.1016\/bs.enz.2026.03.003_bib0177","doi-asserted-by":"crossref","first-page":"7406","DOI":"10.1021\/acs.jmedchem.4c00239","article-title":"Discovery and mechanistic studies of dual-target hits for Carbonic anhydrase IX and VEGFR-2 as potential agents for solid tumors: X-ray, in vitro, in vivo, and in silico investigations of coumarin-based thiazoles","volume":"67","author":"Hefny","year":"2024","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0178","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2024.107168","article-title":"Coumarins-lipophilic cations conjugates: efficient mitocans targeting carbonic anhydrases","volume":"145","author":"Fuentes-Aguilar","year":"2024","journal-title":"Bioorg. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0179","doi-asserted-by":"crossref","DOI":"10.1002\/ardp.202400482","article-title":"New 7-hydroxycoumarin acetamide derivatives as human carbonic anhydrase IX and XII inhibitors: design, synthesis, biological evaluation and molecular docking studies","volume":"358","author":"Maddipatla","year":"2025","journal-title":"Arch. Pharm. (Weinheim)"},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0180","doi-asserted-by":"crossref","first-page":"743","DOI":"10.1080\/14756366.2022.2041630","article-title":"Isocoumarins: a new class of selective carbonic anhydrase IX and XII inhibitors","volume":"37","author":"Ony\u0131lmaz","year":"2022","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"13","key":"10.1016\/bs.enz.2026.03.003_bib0181","doi-asserted-by":"crossref","first-page":"1347","DOI":"10.1080\/17568919.2024.2350875","article-title":"Isocoumarins incorporating chalcone moieties act as isoform selective tumor-associated carbonic anhydrase inhibitors","volume":"16","author":"Onyilmaz","year":"2024","journal-title":"Future Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0182","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1021\/jm301625s","article-title":"Sulfocoumarins (1,2-benzoxathiine-2,2-dioxides): a class of potent and isoform-selective inhibitors of tumor-associated carbonic anhydrases","volume":"56","author":"Tars","year":"2013","journal-title":"J. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0183","doi-asserted-by":"crossref","DOI":"10.1080\/14756366.2023.2166503","article-title":"Click chemistry approaches for developing carbonic anhydrase inhibitors and their applications","volume":"38","author":"Angeli","year":"2023","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"80","key":"10.1016\/bs.enz.2026.03.003_bib0184","doi-asserted-by":"crossref","first-page":"11983","DOI":"10.1039\/C6CC06399C","article-title":"Benzoxaborole as a new chemotype for carbonic anhydrase inhibition","volume":"52","author":"Alterio","year":"2016","journal-title":"Chem. Commun. (Camb)"},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0185","doi-asserted-by":"crossref","first-page":"1498","DOI":"10.1080\/14756366.2019.1653291","article-title":"Exploring benzoxaborole derivatives as carbonic anhydrase inhibitors: a structural and computational analysis reveals their conformational variability as a tool to increase enzyme selectivity","volume":"34","author":"Langella","year":"2019","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"15","key":"10.1016\/bs.enz.2026.03.003_bib0186","doi-asserted-by":"crossref","first-page":"5511","DOI":"10.1021\/jm1003667","article-title":"Polyamines inhibit carbonic anhydrases by anchoring to the zinc-coordinated water molecule","volume":"53","author":"Carta","year":"2010","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0187","doi-asserted-by":"crossref","first-page":"3659","DOI":"10.1021\/ja00087a086","article-title":"Two-site binding of phenol in the active site of human carbonic anhydrase II: structural implications for substrate association","volume":"116","author":"Nair","year":"1994","journal-title":"J. Am. Chem. Soc."},{"issue":"21","key":"10.1016\/bs.enz.2026.03.003_bib0188","doi-asserted-by":"crossref","first-page":"19460","DOI":"10.1021\/acs.jmedchem.4c01795","article-title":"Superacid-synthesized fluorinated diamines act as selective hCA IV inhibitors","volume":"67","author":"Berrino","year":"2024","journal-title":"J. Med. Chem."},{"issue":"5","key":"10.1016\/bs.enz.2026.03.003_bib0189","doi-asserted-by":"crossref","first-page":"648","DOI":"10.1039\/C8CC08562E","article-title":"Selenols: a new class of carbonic anhydrase inhibitors","volume":"55","author":"Angeli","year":"2019","journal-title":"Chem. Commun. (Camb)"},{"key":"10.1016\/bs.enz.2026.03.003_bib0190","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."},{"issue":"20","key":"10.1016\/bs.enz.2026.03.003_bib0191","doi-asserted-by":"crossref","DOI":"10.1002\/cmdc.202400345","article-title":"Thia- and Seleno-Michael Reactions for the Synthesis of Carbonic Anhydrases Inhibitors","volume":"19","author":"Angeli","year":"2024","journal-title":"ChemMedChem"},{"issue":"5","key":"10.1016\/bs.enz.2026.03.003_bib0192","doi-asserted-by":"crossref","first-page":"1583","DOI":"10.1016\/j.bmcl.2008.01.077","article-title":"Carbonic anhydrase inhibitors: interactions of phenols with the 12 catalytically active mammalian isoforms (CA I-XIV)","volume":"18","author":"Innocenti","year":"2008","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"15","key":"10.1016\/bs.enz.2026.03.003_bib0193","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":"Bioorg. Med. Chem."},{"issue":"6","key":"10.1016\/bs.enz.2026.03.003_bib0194","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":"Bioorg. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0195","doi-asserted-by":"crossref","first-page":"34","DOI":"10.3389\/fphar.2011.00034","article-title":"Bacterial carbonic anhydrases as drug targets: toward novel antibiotics?","volume":"2","author":"Supuran","year":"2011","journal-title":"Front. Pharmacol."},{"issue":"19","key":"10.1016\/bs.enz.2026.03.003_bib0196","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":"10","key":"10.1016\/bs.enz.2026.03.003_bib0197","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":"6","key":"10.1016\/bs.enz.2026.03.003_bib0198","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.2026.03.003_bib0199","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":"7","key":"10.1016\/bs.enz.2026.03.003_bib0200","doi-asserted-by":"crossref","first-page":"622","DOI":"10.2174\/138161208783877875","article-title":"The alpha and beta classes carbonic anhydrases from Helicobacter pylori as novel drug targets","volume":"14","author":"Nishimori","year":"2008","journal-title":"Curr. Pharm. Des."},{"issue":"5","key":"10.1016\/bs.enz.2026.03.003_bib0201","article-title":"Structural basis for the inhibition of Helicobacter pylori \u03b1-carbonic anhydrase by sulfonamides","volume":"10","author":"Modak","year":"2015","journal-title":"PLoS One"},{"issue":"24","key":"10.1016\/bs.enz.2026.03.003_bib0202","doi-asserted-by":"crossref","first-page":"11098","DOI":"10.1021\/acs.jmedchem.6b01333","article-title":"Structure-activity relationship for sulfonamide inhibition of Helicobacter pylori \u03b1-carbonic anhydrase","volume":"59","author":"Modak","year":"2016","journal-title":"J. Med. Chem."},{"issue":"4","key":"10.1016\/bs.enz.2026.03.003_bib0203","doi-asserted-by":"crossref","first-page":"527","DOI":"10.3109\/14756366.2015.1051042","article-title":"The history and rationale of using carbonic anhydrase inhibitors in the treatment of peptic ulcers. In memoriam Ioan Pu\u015fca\u015f (1932-2015)","volume":"31","author":"Buz\u00e1s","year":"2016","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0204","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1111\/j.1749-6632.1984.tb12392.x","article-title":"Treatment of gastroduodenal ulcers with carbonic anhydrase inhibitors","volume":"429","author":"Pu\u015fca\u015f","year":"1984","journal-title":"Ann. N. Y. Acad. Sci."},{"issue":"6","key":"10.1016\/bs.enz.2026.03.003_bib0205","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1080\/13543776.2024.2367005","article-title":"Management of Neisseria gonorrhoeae infection: from drug resistance to drug repurposing","volume":"34","author":"Pisano","year":"2024","journal-title":"Expert. Opin. Ther. Pat."},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0206","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":"7","key":"10.1016\/bs.enz.2026.03.003_bib0207","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":"Hewitt","year":"2021","journal-title":"ACS Infect. Dis."},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0208","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.2026.03.003_bib0209","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":"1","key":"10.1016\/bs.enz.2026.03.003_bib0210","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":"1","key":"10.1016\/bs.enz.2026.03.003_bib0211","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":"37","author":"Giovannuzzi","year":"2022","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0212","doi-asserted-by":"crossref","DOI":"10.1080\/14756366.2023.2284119","article-title":"Inhibition of pathogenic bacterial carbonic anhydrases by monothiocarbamates","volume":"38","author":"Giovannuzzi","year":"2023","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0213","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":"36","author":"Nocentini","year":"2021","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0214","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. Enzyme Inhib. Med. Chem."},{"issue":"11","key":"10.1016\/bs.enz.2026.03.003_bib0215","doi-asserted-by":"crossref","first-page":"9613","DOI":"10.1021\/acs.jmedchem.4c00740","article-title":"Development of penicillin-based carbonic anhydrase inhibitors targeting multidrug-resistant Neisseria gonorrhoeae","volume":"67","author":"Bonardi","year":"2024","journal-title":"J. Med. Chem."},{"issue":"17","key":"10.1016\/bs.enz.2026.03.003_bib0216","doi-asserted-by":"crossref","first-page":"15537","DOI":"10.1021\/acs.jmedchem.4c01187","article-title":"Optimization of ethoxzolamide analogs with improved pharmacokinetic properties for in vivo efficacy against Neisseria gonorrhoeae","volume":"67","author":"Youse","year":"2024","journal-title":"J. Med. Chem."},{"issue":"7","key":"10.1016\/bs.enz.2026.03.003_bib0217","doi-asserted-by":"crossref","first-page":"857","DOI":"10.3390\/antibiotics11070857","article-title":"Enterococcus virulence and resistant traits associated with its permanence in the hospital environment","volume":"11","author":"Geraldes","year":"2022","journal-title":"Antibiotics (Basel)"},{"issue":"17","key":"10.1016\/bs.enz.2026.03.003_bib0218","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":"4","key":"10.1016\/bs.enz.2026.03.003_bib0219","doi-asserted-by":"crossref","first-page":"e01715","DOI":"10.1128\/AAC.01715-20","article-title":"In vivo antibacterial activity of acetazolamide","volume":"65","author":"Abutaleb","year":"2021","journal-title":"Antimicrob. Agents Chemother."},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0220","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.2026.03.003_bib0221","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.2026.03.003_bib0222","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2025.117620","article-title":"Redesigning oxazolidinones as carbonic anhydrase inhibitors against vancomycin-resistant enterococci","volume":"291","author":"Ammara","year":"2025","journal-title":"Eur. J. Med. Chem."},{"issue":"17","key":"10.1016\/bs.enz.2026.03.003_bib0223","doi-asserted-by":"crossref","first-page":"18597","DOI":"10.1021\/acs.jmedchem.5c01584","article-title":"Hit-to-lead optimization of acetazolamide-based bacterial carbonic anhydrase inhibitors with efficacy in vivo for treatment of vancomycin-resistant enterococci septicemia","volume":"68","author":"Holly","year":"2025","journal-title":"J. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0224","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1021\/acsinfecdis.5c00736","article-title":"Bacterial carbonic anhydrase inhibitor CAI0019 demonstrates efficacy in Enterococcus faecium septicemic peritonitis mouse model while sparing the microbiome","volume":"12","author":"Abutaleb","year":"2026","journal-title":"ACS Infect. Dis."},{"issue":"21","key":"10.1016\/bs.enz.2026.03.003_bib0225","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."},{"issue":"7","key":"10.1016\/bs.enz.2026.03.003_bib0226","doi-asserted-by":"crossref","first-page":"2267","DOI":"10.1016\/j.bmcl.2008.03.012","article-title":"Investigations of the esterase, phosphatase, and sulfatase activities of the cytosolic mammalian carbonic anhydrase isoforms I, II, and XIII with 4-nitrophenyl esters as substrates","volume":"18","author":"Innocenti","year":"2008","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"45","key":"10.1016\/bs.enz.2026.03.003_bib0227","doi-asserted-by":"crossref","first-page":"18452","DOI":"10.1021\/ja207855c","article-title":"Promiscuity of carbonic anhydrase II. Unexpected ester hydrolysis of carbohydrate-based sulfamate inhibitors","volume":"133","author":"Lopez","year":"2011","journal-title":"J. Am. Chem. Soc."},{"issue":"34","key":"10.1016\/bs.enz.2026.03.003_bib0228","doi-asserted-by":"crossref","first-page":"10384","DOI":"10.1021\/bi970760v","article-title":"Carbonic anhydrase activators: X-ray crystallographic and spectroscopic investigations for the interaction of isozymes I and II with histamine","volume":"36","author":"Briganti","year":"1997","journal-title":"Biochemistry"},{"issue":"5","key":"10.1016\/bs.enz.2026.03.003_bib0229","doi-asserted-by":"crossref","first-page":"561","DOI":"10.4155\/fmc-2017-0223","article-title":"Carbonic anhydrase activators","volume":"10","author":"Supuran","year":"2018","journal-title":"Future Med. Chem."},{"issue":"22","key":"10.1016\/bs.enz.2026.03.003_bib0230","doi-asserted-by":"crossref","first-page":"2025","DOI":"10.4155\/fmc-2023-0193","article-title":"State of the art of carbonic anhydrase activators","volume":"15","author":"Fiorentino","year":"2023","journal-title":"Future Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0231","doi-asserted-by":"crossref","first-page":"768","DOI":"10.1002\/jps.2600830603","article-title":"Carbonic anhydrase activators. 3: structure-activity correlations for a series of isozyme II activators","volume":"83","author":"Clare","year":"1994","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/bs.enz.2026.03.003_bib0232","first-page":"107","article-title":"Carbonic anhydrase activators. Part 8. pKa\u2014activation relationship in a series of amino acid derivatives activators of isozyme II","volume":"39","author":"Supuran","year":"1994","journal-title":"Rev. Roum. Chim."},{"issue":"23","key":"10.1016\/bs.enz.2026.03.003_bib0233","doi-asserted-by":"crossref","first-page":"5136","DOI":"10.1016\/j.bmcl.2005.08.069","article-title":"Carbonic anhydrase activators: X-ray crystal structure of the adduct of human isozyme II with L-histidine as a platform for the design of stronger activators","volume":"15","author":"Temperini","year":"2005","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"27","key":"10.1016\/bs.enz.2026.03.003_bib0234","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"},{"issue":"19","key":"10.1016\/bs.enz.2026.03.003_bib0235","doi-asserted-by":"crossref","first-page":"5152","DOI":"10.1016\/j.bmcl.2006.07.021","article-title":"Carbonic anhydrase activators: the first X-ray crystallographic study of an adduct of isoform I","volume":"16","author":"Temperini","year":"2006","journal-title":"Bioorg. Med. Chem. Lett.."},{"issue":"10","key":"10.1016\/bs.enz.2026.03.003_bib0236","doi-asserted-by":"crossref","first-page":"3019","DOI":"10.1021\/jm0603320","volume":"49","author":"Temperini","year":"2006","journal-title":"J. Med. Chem."},{"issue":"3","key":"10.1016\/bs.enz.2026.03.003_bib0237","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":"Bioorg. Med. Chem. Lett."},{"issue":"18","key":"10.1016\/bs.enz.2026.03.003_bib0238","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":"Bioorg. Med. Chem."},{"issue":"9","key":"10.1016\/bs.enz.2026.03.003_bib0239","doi-asserted-by":"crossref","first-page":"7431","DOI":"10.1007\/s12035-017-0854-2","article-title":"Crystal structure of carbonic anhydrase II in complex with an activating ligand: implications in neuronal function","volume":"55","author":"Bhatt","year":"2018","journal-title":"Mol. Neurobiol."},{"key":"10.1016\/bs.enz.2026.03.003_bib0240","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2021.113875","article-title":"Binding site comparison for coumarin inhibitors and amine\/amino acid activators of human carbonic anhydrases","volume":"226","author":"Petreni","year":"2021","journal-title":"Eur. J. Med. Chem."},{"issue":"3","key":"10.1016\/bs.enz.2026.03.003_bib0241","doi-asserted-by":"crossref","first-page":"961","DOI":"10.1016\/S0022-3565(24)29621-X","article-title":"Pharmacological enhancement of synaptic efficacy, spatial learning, and memory through carbonic anhydrase activation in rats","volume":"297","author":"Sun","year":"2001","journal-title":"J. Pharmacol. Exp. Ther."},{"issue":"2","key":"10.1016\/bs.enz.2026.03.003_bib0242","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/S0165-6147(02)01899-0","article-title":"Carbonic anhydrase gating of attention: memory therapy and enhancement","volume":"23","author":"Sun","year":"2002","journal-title":"Trends Pharmacol. Sci."},{"key":"10.1016\/bs.enz.2026.03.003_bib0243","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1016\/j.neuropharm.2017.03.009","article-title":"Carbonic anhydrase activation enhances object recognition memory in mice through phosphorylation of the extracellular signal-regulated kinase in the cortex and the hippocampus","volume":"118","author":"Canto de Souza","year":"2017","journal-title":"Neuropharmacology"},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0244","doi-asserted-by":"crossref","first-page":"1206","DOI":"10.1080\/14756366.2020.1766455","article-title":"Carbonic anhydrase modulation of emotional memory. Implications for the treatment of cognitive disorders","volume":"35","author":"Blandina","year":"2020","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"27","key":"10.1016\/bs.enz.2026.03.003_bib0245","doi-asserted-by":"crossref","first-page":"16000","DOI":"10.1073\/pnas.1910690117","article-title":"The role of carbonic anhydrases in extinction of contextual fear memory","volume":"117","author":"Schmidt","year":"2020","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"1","key":"10.1016\/bs.enz.2026.03.003_bib0246","doi-asserted-by":"crossref","first-page":"719","DOI":"10.1080\/14756366.2021.1891051","article-title":"Activation of carbonic anhydrase isoforms involved in modulation of emotional memory and cognitive disorders with histamine agonists, antagonists and derivatives","volume":"36","author":"Provensi","year":"2021","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0247","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1016\/j.neuroscience.2022.03.025","article-title":"Modulation of carbonic anhydrases activity in the hippocampus or prefrontal cortex differentially affects social recognition memory in rats","volume":"497","author":"Schmidt","year":"2022","journal-title":"Neuroscience"},{"key":"10.1016\/bs.enz.2026.03.003_bib0248","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2022.114828","article-title":"New \u03b2-arylchalcogeno amines with procognitive properties targeting carbonic anhydrases and monoamine oxidases","volume":"244","author":"Provensi","year":"2022","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0249","first-page":"343","article-title":"Carbonic anhydrase activators. Part 5. CA II activation by 2,4,6-trisubstituted pyridinium cations with 1-(\u03c9-aminoalkyl) side chains","volume":"38","author":"Supuran","year":"1993","journal-title":"Rev. Roum. Chim."},{"key":"10.1016\/bs.enz.2026.03.003_bib0250","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1016\/0223-5234(96)89555-9","article-title":"Carbonic anhydrase activators. Part 14. Synthesis of mono- and bis- pyridinium salt derivatives of 2-amino-5-(2-aminoethyl)- and 2-amino-5-(3-aminopropyl)-1,3,4-thiadiazole, and their interaction with isozyme II","volume":"31","author":"Supuran","year":"1996","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0251","doi-asserted-by":"crossref","first-page":"911","DOI":"10.1016\/S0223-5234(97)82777-8","article-title":"Carbonic anhydrase activators. Part 17. Synthesis and activation study of a series of 1-(1,2,4-triazole-(1H)-3-yl)-2,4,6-trisubstituted-pyridinium salts against isozymes I, II and IV","volume":"32","author":"Ilies","year":"1997","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0252","doi-asserted-by":"crossref","first-page":"504","DOI":"10.1021\/jm011031n","article-title":"Carbonic anhydrase activators: design of high affinity isozymes I, II, and IV activators, incorporating tri-\/tetrasubstituted-pyridinium-azole moieties","volume":"45","author":"Ilies","year":"2002","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0253","doi-asserted-by":"crossref","first-page":"2790","DOI":"10.1039\/c0ob00703j","article-title":"Pyridinium derivatives of histamine are potent activators of cytosolic carbonic anhydrase isoforms I, II and VII","volume":"9","author":"K","year":"2011","journal-title":"Org. Biomol. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0254","doi-asserted-by":"crossref","first-page":"2764","DOI":"10.1016\/j.bmcl.2010.10.045","article-title":"An inhibitor-like binding mode of a carbonic anhydrase activator within the active site of isoform II","volume":"21","author":"K","year":"2011","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2026.03.003_bib0255","doi-asserted-by":"crossref","first-page":"2915","DOI":"10.1016\/S0968-0896(99)00227-8","article-title":"Carbonic anhydrase activators: amino acyl\/dipeptidyl histamine derivatives bind with high affinity to isozymes I, II and IV and act as efficient activators","volume":"7","author":"Supuran","year":"1999","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0256","doi-asserted-by":"crossref","first-page":"2043","DOI":"10.1016\/S0960-894X(99)00310-8","article-title":"Novel carbonic anhydrase isozymes I, II and IV activators incorporating sulfonyl-histamino moieties","volume":"9","author":"Briganti","year":"1999","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2026.03.003_bib0257","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1080\/14756360009030347","article-title":"Carbonic anhydrase activators: synthesis of high affinity isozymes I, II and IV activators, derivatives of 4-(4-tosylureido-amino acyl)ethyl-1H-imidazole (histamine derivatives)","volume":"15","author":"Scozzafava","year":"2000","journal-title":"J. Enzyme Inhib."},{"key":"10.1016\/bs.enz.2026.03.003_bib0258","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/S0223-5234(00)00102-1","article-title":"Carbonic anhydrase activators\u2014part 21. Novel activators of isozymes I, II and IV incorporating carboxamido and ureido histamine moieties","volume":"35","author":"Scozzafava","year":"2000","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0259","doi-asserted-by":"crossref","first-page":"471","DOI":"10.3109\/14756360009040703","article-title":"Carbonic anhydrase activators: synthesis of high affinity isozymes I, II and IV activators, derivatives of 4-(arylsulfonylureido-amino acyl)ethyl-1H-imidazole","volume":"15","author":"Supuran","year":"2000","journal-title":"J. Enzyme Inhib."},{"key":"10.1016\/bs.enz.2026.03.003_bib0260","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/S0928-0987(99)00086-X","article-title":"Carbonic anhydrase activators. Part 24. High affinity isozymes I, II and IV activators, derivatives of 4-(4-chlorophenylsulfonylureido-amino acyl)ethyl-1H-imidazole","volume":"10","author":"Scozzafava","year":"2000","journal-title":"Eur. J. Pharm. Sci."},{"key":"10.1016\/bs.enz.2026.03.003_bib0261","doi-asserted-by":"crossref","first-page":"4884","DOI":"10.1016\/j.bmcl.2011.06.030","article-title":"Carbonic anhydrase I and II activation with mono- and dihalogenated histamine derivatives","volume":"21","author":"Saada","year":"2011","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2026.03.003_bib0262","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":"Bioorg. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0263","doi-asserted-by":"crossref","first-page":"5980","DOI":"10.1039\/C4CC02346C","article-title":"Ethylene bis-imidazoles are highly potent and selective activators for isozymes VA and VII of carbonic anhydrase, with a potential nootropic effect","volume":"50","author":"Draghici","year":"2014","journal-title":"Chem. Commun. (Camb)"},{"key":"10.1016\/bs.enz.2026.03.003_bib0264","doi-asserted-by":"crossref","first-page":"1681","DOI":"10.1016\/j.bmc.2017.01.031","article-title":"Carbonic anhydrases activation with 3-amino-1H-1,2,4-triazole-1-carboxamides: discovery of subnanomolar isoform II activators","volume":"25","author":"Y","year":"2017","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0265","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1080\/14756366.2016.1232254","article-title":"A class of carbonic anhydrase \u2014iselective activators","volume":"32","author":"Licsandru","year":"2017","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0266","doi-asserted-by":"crossref","first-page":"1177","DOI":"10.1016\/S0960-894X(02)00121-X","article-title":"Carbonic anhydrase activators: human isozyme II is strongly activated by oligopeptides incorporating the carboxyterminal sequence of the bicarbonate anion exchanger AE1","volume":"12","author":"Scozzafava","year":"2002","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2026.03.003_bib0267","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1021\/jm010958k","article-title":"Carbonic anhydrase activators: high affinity isozymes I, II, and IV activators, incorporating a beta-alanyl-histidine scaffold","volume":"45","author":"Scozzafava","year":"2002","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.03.003_bib0268","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.2026.03.003_bib0269","doi-asserted-by":"crossref","first-page":"2440","DOI":"10.1016\/j.bmcl.2009.03.050","article-title":"Carbonic anhydrase activators: activation of human isozymes I, II and IX with phenylsulfonylhydrazido l-histidine derivatives","volume":"19","author":"Abdo","year":"2009","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2026.03.003_bib0270","doi-asserted-by":"crossref","first-page":"4053","DOI":"10.1039\/C6CC00796A","article-title":"Dynamic encapsulation and activation of carbonic anhydrase in multivalent dynameric host matrices","volume":"52","author":"Zhang","year":"2016","journal-title":"Chem. Commun. (Camb)"}],"container-title":["The Enzymes","Vertebrate Carbonic Anhydrases"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S187460472600003X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S187460472600003X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,7,22]],"date-time":"2026-07-22T15:14:00Z","timestamp":1784733240000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S187460472600003X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026]]},"ISBN":["9780443470868"],"references-count":270,"URL":"https:\/\/doi.org\/10.1016\/bs.enz.2026.03.003","relation":{},"ISSN":["1874-6047"],"issn-type":[{"value":"1874-6047","type":"print"}],"subject":[],"published":{"date-parts":[[2026]]}}}