{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,8]],"date-time":"2026-09-08T02:40:55Z","timestamp":1788835255504,"version":"build-2803163510"},"reference-count":223,"publisher":"Elsevier","isbn-type":[{"value":"9780443470868","type":"print"}],"license":[{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026]]},"DOI":"10.1016\/bs.enz.2026.06.005","type":"book-chapter","created":{"date-parts":[[2026,6,30]],"date-time":"2026-06-30T11:50:19Z","timestamp":1782820219000},"page":"29-67","source":"Crossref","is-referenced-by-count":1,"title":["Carbonic anhydrases I and II"],"prefix":"10.1016","author":[{"given":"Claudiu T.","family":"Supuran","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Clemente","family":"Capasso","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/bs.enz.2026.06.005_bib0001","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1113\/jphysiol.1933.sp003077","article-title":"Carbonic anhydrase. Its preparation and properties","volume":"80","author":"Meldrum","year":"1933","journal-title":"J. Physiol."},{"key":"10.1016\/bs.enz.2026.06.005_bib0002","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1152\/physrev.1967.47.4.595","article-title":"Carbonic anhydrase: chemistry, physiology, and inhibition","volume":"47","author":"Maren","year":"1967","journal-title":"Physiol. Rev."},{"key":"10.1016\/bs.enz.2026.06.005_bib0003","doi-asserted-by":"crossref","first-page":"1129","DOI":"10.1016\/S0021-9258(18)60295-9","article-title":"Metal binding and catalytic activity in bovine carbonic anhydrase","volume":"237","author":"Lindskog","year":"1962","journal-title":"J. Biol. Chem."},{"key":"10.1016\/bs.enz.2026.06.005_bib0004","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.2026.06.005_bib0005","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."},{"key":"10.1016\/bs.enz.2026.06.005_bib0006","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1111\/j.1432-1033.1967.tb19504.x","article-title":"Studies of the esterase activity and the anion inhibition of bovine zinc and cobalt carbonic anhydrases","volume":"3","author":"Thorslund","year":"1967","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/bs.enz.2026.06.005_bib0007","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":"Nature Rev. Drug Discov."},{"key":"10.1016\/bs.enz.2026.06.005_bib0008","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.2026.06.005_bib0009","doi-asserted-by":"crossref","first-page":"325","DOI":"10.3109\/14756366.2014.910202","article-title":"An overview of the alpha-, beta- and gamma-carbonic anhydrases from bacteria: can bacterial carbonic anhydrases shed new light on evolution of bacteria?","volume":"30","author":"Capasso","year":"2015","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2026.06.005_bib0010","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.2026.06.005_bib0011","doi-asserted-by":"crossref","first-page":"12128","DOI":"10.1021\/bi001416s","article-title":"The active site structure of Thalassiosira weissflogii carbonic anhydrase 1","volume":"39","author":"Cox","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/bs.enz.2026.06.005_bib0012","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1038\/nature06636","article-title":"Structure and metal exchange in the cadmium carbonic anhydrase of marine diatoms","volume":"452","author":"Xu","year":"2008","journal-title":"Nature"},{"key":"10.1016\/bs.enz.2026.06.005_bib0013","doi-asserted-by":"crossref","first-page":"4389","DOI":"10.1016\/j.bmcl.2014.08.015","article-title":"Discovery of a new family of carbonic anhydrases in the malaria pathogen Plasmodium falciparum-the \u03b7-carbonic anhydrases","volume":"24","author":"Del Prete","year":"2014","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2026.06.005_bib0014","doi-asserted-by":"crossref","first-page":"9828","DOI":"10.1073\/pnas.1603112113","article-title":"Thylakoid luminal theta-carbonic anhydrase critical for growth and photosynthesis in the marine diatom Phaeodactylum tricornutum","volume":"113","author":"Kikutani","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/bs.enz.2026.06.005_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.2026.06.005_bib0016","doi-asserted-by":"crossref","first-page":"2094","DOI":"10.1038\/s41396-019-0426-8","article-title":"A new widespread subclass of carbonic anhydrase in marine phytoplankton","volume":"13","author":"Jensen","year":"2019","journal-title":"ISME J."},{"key":"10.1016\/bs.enz.2026.06.005_bib0017","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/bs.enz.2025.04.002","article-title":"Sordaria macrospora carbonic anhydrases","volume":"57","author":"Paoletti","year":"2025","journal-title":"Enzymes"},{"key":"10.1016\/bs.enz.2026.06.005_bib0018","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.2026.06.005_bib0019","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.2026.06.005_bib0020","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"},{"key":"10.1016\/bs.enz.2026.06.005_bib0021","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"},{"key":"10.1016\/bs.enz.2026.06.005_bib0022","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."},{"key":"10.1016\/bs.enz.2026.06.005_bib0023","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."},{"issue":"26","key":"10.1016\/bs.enz.2026.06.005_bib0024","doi-asserted-by":"crossref","first-page":"15184","DOI":"10.1073\/pnas.96.26.15184","article-title":"Carbonic anhydrase is an ancient enzyme widespread in prokaryotes","volume":"96","author":"Smith","year":"1999","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/bs.enz.2026.06.005_bib0025","doi-asserted-by":"crossref","DOI":"10.1155\/2012\/324549","article-title":"Dispensabilities of carbonic anhydrase in proteobacteria","volume":"2012","author":"Ueda","year":"2012","journal-title":"Int. J. Evol. Biol."},{"issue":"3","key":"10.1016\/bs.enz.2026.06.005_bib0026","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."},{"issue":"3","key":"10.1016\/bs.enz.2026.06.005_bib0027","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1016\/S0014-5793(98)00690-5","article-title":"Unexpected expression of carbonic anhydrase I and selenium-binding protein as the only major non-heme proteins in erythrocytes of the subterranean mole rat (Spalax ehrenbergi)","volume":"430","author":"Yang","year":"1998","journal-title":"FEBS Lett."},{"issue":"2","key":"10.1016\/bs.enz.2026.06.005_bib0028","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1016\/0167-4838(82)90471-X","article-title":"Purification, properties, partial sequence and evolutionary relationships of marsupial erythrocyte carbonic anhydrase","volume":"709","author":"Jones","year":"1982","journal-title":"Biochim. Biophys. Acta."},{"issue":"8","key":"10.1016\/bs.enz.2026.06.005_bib0029","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.2026.06.005_bib0030","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":"4226","key":"10.1016\/bs.enz.2026.06.005_bib0031","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1126\/science.813299","article-title":"Inhibition by anions of human red cell carbonic anhydrase B: physiological and biochemical implications","volume":"191","author":"Maren","year":"1976","journal-title":"Science"},{"key":"10.1016\/bs.enz.2026.06.005_bib0032","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1126\/science.406674","article-title":"Erythrocyte carbonic anhydrase I: inherited deficiency in humans","volume":"197","author":"Kendall","year":"1977","journal-title":"Science"},{"key":"10.1016\/bs.enz.2026.06.005_bib0033","doi-asserted-by":"crossref","first-page":"2752","DOI":"10.1073\/pnas.80.9.2752","article-title":"Carbonic anhydrase II deficiency identified as the primary defect in the autosomal recessive syndrome of osteopetrosis with renal tubular acidosis and cerebral calcification","volume":"80","author":"Sly","year":"1983","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/bs.enz.2026.06.005_bib0034","doi-asserted-by":"crossref","first-page":"648","DOI":"10.1126\/science.1262110","article-title":"Human genomics. The Genotype-Tissue Expression (GTEx) pilot analysis: multitissue gene regulation in humans","volume":"348","year":"2015","journal-title":"Science"},{"issue":"4","key":"10.1016\/bs.enz.2026.06.005_bib0035","doi-asserted-by":"crossref","first-page":"R176","DOI":"10.1186\/ar3929","article-title":"Carbonic anhydrase I (CA1) is involved in the process of bone formation and is susceptible to ankylosing spondylitis","volume":"14","author":"Chang","year":"2012","journal-title":"Arthritis. Res. Ther."},{"key":"10.1016\/bs.enz.2026.06.005_bib0036","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1016\/j.jad.2024.12.064","article-title":"Hippocampus carbonic anhydrase 1 via ERK pathway may be involved in depressive like behaviors","volume":"373","author":"Cheng","year":"2025","journal-title":"J. Affect. Disord."},{"issue":"2","key":"10.1016\/bs.enz.2026.06.005_bib0037","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1038\/nm1534","article-title":"Extracellular carbonic anhydrase mediates hemorrhagic retinal and cerebral vascular permeability through prekallikrein activation","volume":"13","author":"Gao","year":"2007","journal-title":"Nat. Med."},{"issue":"5 Pt 1","key":"10.1016\/bs.enz.2026.06.005_bib0038","doi-asserted-by":"crossref","first-page":"1151","DOI":"10.1016\/S0016-5085(85)80074-3","article-title":"Amount and distribution of carbonic anhydrases CA I and CA II in the gastrointestinal tract","volume":"88","author":"L\u00f6nnerholm","year":"1985","journal-title":"Gastroenterology"},{"issue":"5","key":"10.1016\/bs.enz.2026.06.005_bib0039","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1007\/BF00489754","article-title":"Immunohistochemical localization of carbonic anhydrase isoenzymes I and II in human bone, cartilage and giant cell tumor","volume":"81","author":"V\u00e4\u00e4n\u00e4nen","year":"1984","journal-title":"Histochemistry"},{"issue":"5","key":"10.1016\/bs.enz.2026.06.005_bib0040","doi-asserted-by":"crossref","first-page":"646","DOI":"10.1136\/gut.35.5.646","article-title":"Distribution of the carbonic anhydrase isoenzymes I, II, and VI in the human alimentary tract","volume":"35","author":"Parkkila","year":"1994","journal-title":"Gut"},{"issue":"2","key":"10.1016\/bs.enz.2026.06.005_bib0041","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1111\/j.1471-4159.1979.tb05199.x","article-title":"Estimation of glial contamination of synaptosomal-mitochondrial fractions of rat brain by radioimmunoassay of carbonic anhydrase (CA II)","volume":"33","author":"Delaunoy","year":"1979","journal-title":"J. Neurochem."},{"issue":"3","key":"10.1016\/bs.enz.2026.06.005_bib0042","doi-asserted-by":"crossref","first-page":"734","DOI":"10.1111\/j.1471-4159.1982.tb07954.x","article-title":"Immunocytochemical and biochemical analysis of carbonic anhydrase in primary astrocyte cultures from rat brain","volume":"39","author":"Kimelberg","year":"1982","journal-title":"J. Neurochem."},{"issue":"4","key":"10.1016\/bs.enz.2026.06.005_bib0043","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1177\/30.4.6801110","article-title":"Immunohistochemical localization of carbonic anhydrase isoenzyme C in the central and peripheral nervous system of the mouse","volume":"30","author":"Kumpulainen","year":"1982","journal-title":"J. Histochem. Cytochem."},{"issue":"2","key":"10.1016\/bs.enz.2026.06.005_bib0044","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1002\/j.1460-2075.1983.tb01405.x","article-title":"Induction of oligodendrocyte-like properties in a primitive hypothalamic cell line by cholesterol, an eye derived growth factor and brain extract","volume":"2","author":"de Vitry","year":"1983","journal-title":"EMBO J."},{"issue":"2\u20133","key":"10.1016\/bs.enz.2026.06.005_bib0045","first-page":"145","article-title":"Carbonic anhydrase in the anterior uvea of the rabbit","volume":"24","author":"Wistrand","year":"1951","journal-title":"Acta. Physiol. Scand."},{"issue":"1","key":"10.1016\/bs.enz.2026.06.005_bib0046","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/0002-9394(54)92027-9","article-title":"Decrease in intraocular pressure in man by a carbonic anhydrase inhibitor, diamox; a preliminary report","volume":"37","author":"Becker","year":"1954","journal-title":"Am. J. Ophthalmol."},{"issue":"3","key":"10.1016\/bs.enz.2026.06.005_bib0047","first-page":"419","article-title":"Carbonic anhydrase isoenzymes CA I and CA II in the human eye","volume":"27","author":"Wistrand","year":"1986","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"issue":"1","key":"10.1016\/bs.enz.2026.06.005_bib0048","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1006\/excr.1998.4071","article-title":"Carbonic anhydrase II plays a major role in osteoclast differentiation and bone resorption by effecting the steady state intracellular pH and Ca2+","volume":"242","author":"Lehenkari","year":"1998","journal-title":"Exp. Cell. Res."},{"issue":"3","key":"10.1016\/bs.enz.2026.06.005_bib0049","first-page":"250","article-title":"Immunohistochemical localization of carbonic anhydrase I and II in eccrine sweat glands from control subjects and patients with cystic fibrosis","volume":"112","author":"Briggman","year":"1983","journal-title":"Am. J. Pathol."},{"issue":"3","key":"10.1016\/bs.enz.2026.06.005_bib0050","doi-asserted-by":"crossref","first-page":"59","DOI":"10.2535\/ofaj.90.59","article-title":"Expression of carbonic anhydrase in the fetal eye and extra-ocular tissues","volume":"90","author":"Abe","year":"2013","journal-title":"Okajimas Folia Anat. Jpn."},{"issue":"1","key":"10.1016\/bs.enz.2026.06.005_bib0051","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1111\/j.1748-1716.1986.tb07788.x","article-title":"Carbonic anhydrase isoenzymes in the rat kidney. Effects of chronic acetazolamide treatment","volume":"126","author":"L\u00f6nnerholm","year":"1986","journal-title":"Acta. Physiol. Scand."},{"issue":"6","key":"10.1016\/bs.enz.2026.06.005_bib0052","doi-asserted-by":"crossref","first-page":"1350","DOI":"10.1095\/biolreprod52.6.1350","article-title":"Expression of carbonic anhydrase isoenzymes IV and II in rat epididymal duct","volume":"52","author":"Kaunisto","year":"1995","journal-title":"Biol. Reprod."},{"issue":"5","key":"10.1016\/bs.enz.2026.06.005_bib0053","first-page":"440","article-title":"Immunohistochemical study of carbonic anhydrase isozymes in human skin","volume":"13","author":"Mastrolorenzo","year":"2003","journal-title":"Eur. J. Dermatol."},{"issue":"2","key":"10.1016\/bs.enz.2026.06.005_bib0054","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1016\/0378-1119(90)90236-K","article-title":"Structure and methylation patterns of the gene encoding human carbonic anhydrase I","volume":"93","author":"Lowe","year":"1990","journal-title":"Gene"},{"issue":"14","key":"10.1016\/bs.enz.2026.06.005_bib0055","doi-asserted-by":"crossref","first-page":"4437","DOI":"10.1073\/pnas.80.14.4437","article-title":"Polymorphic gene for human carbonic anhydrase II: a molecular disease marker located on chromosome 8","volume":"80","author":"Venta","year":"1983","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/bs.enz.2026.06.005_bib0056","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1111\/j.1749-6632.1984.tb12314.x","article-title":"Structure, refinement, and function of carbonic anhydrase isozymes: refinement of human carbonic anhydrase I","volume":"429","author":"Kannan","year":"1984","journal-title":"Ann. N.Y. Acad. Sci."},{"issue":"1","key":"10.1016\/bs.enz.2026.06.005_bib0057","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1002\/prot.340150110","article-title":"Crystallographic analysis of Thr-200\u2013>His human carbonic anhydrase II and its complex with the substrate, HCO3-","volume":"15","author":"Xue","year":"1993","journal-title":"Proteins"},{"key":"10.1016\/bs.enz.2026.06.005_bib0058","doi-asserted-by":"crossref","first-page":"2505","DOI":"10.1073\/pnas.70.9.2505","article-title":"The catalytic mechanism of carbonic anhydrase","volume":"70","author":"Lindskog","year":"1973","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"issue":"19","key":"10.1016\/bs.enz.2026.06.005_bib0059","doi-asserted-by":"crossref","first-page":"7913","DOI":"10.1021\/bi00445a054","article-title":"Role of histidine 64 in the catalytic mechanism of human carbonic anhydrase II studied with a site-specific mutant","volume":"28","author":"Tu","year":"1989","journal-title":"Biochemistry"},{"issue":"34","key":"10.1016\/bs.enz.2026.06.005_bib0060","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"},{"key":"10.1016\/bs.enz.2026.06.005_bib0061","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1038\/newbio235131a0","article-title":"Crystal structure of human carbonic anhydrase C","volume":"235","author":"Liljas","year":"1972","journal-title":"Nat. New. Biol."},{"issue":"2","key":"10.1016\/bs.enz.2026.06.005_bib0062","doi-asserted-by":"crossref","first-page":"226","DOI":"10.1006\/jmbi.1994.1491","article-title":"Enzyme-substrate interactions. Structure of human carbonic anhydrase I complexed with bicarbonate","volume":"241","author":"Kumar","year":"1994","journal-title":"J. Mol. Biol."},{"issue":"1","key":"10.1016\/bs.enz.2026.06.005_bib0063","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1002\/prot.340170112","article-title":"Structural analysis of the zinc hydroxide-Thr-199-Glu-106 hydrogen-bond network in human carbonic anhydrase II","volume":"17","author":"Xue","year":"1993","journal-title":"Proteins"},{"issue":"2","key":"10.1016\/bs.enz.2026.06.005_bib0064","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1016\/0006-291X(91)91229-6","article-title":"Structural properties of human carbonic anhydrase II at pH 9.5","volume":"181","author":"Nair","year":"1991","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"1","key":"10.1016\/bs.enz.2026.06.005_bib0065","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1002\/pro.5560030115","article-title":"Positions of His-64 and a bound water in human carbonic anhydrase II upon binding three structurally related inhibitors","volume":"3","author":"Smith","year":"1994","journal-title":"Protein. Sci."},{"issue":"1","key":"10.1016\/bs.enz.2026.06.005_bib0066","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/0167-4838(92)90427-F","article-title":"Buffer dependence of CO2 hydration catalyzed by human carbonic anhydrase I","volume":"1120","author":"Ren","year":"1992","journal-title":"Biochim. Biophys. Acta."},{"issue":"3","key":"10.1016\/bs.enz.2026.06.005_bib0067","first-page":"696","article-title":"Catalytic and inhibitor-binding properties of some active-site mutants of human carbonic anhydrase I","volume":"229","author":"Engstrand","year":"1995","journal-title":"Eur. J. Biochem."},{"issue":"1","key":"10.1016\/bs.enz.2026.06.005_bib0068","doi-asserted-by":"crossref","first-page":"1450","DOI":"10.1080\/14756366.2020.1781846","article-title":"Human carbonic anhydrases and post-translational modifications: a hidden world possibly affecting protein properties and functions","volume":"35","author":"Di Fiore","year":"2020","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"4","key":"10.1016\/bs.enz.2026.06.005_bib0069","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1007\/s00726-021-03063-y","article-title":"Post-translational modifications in tumor-associated carbonic anhydrases","volume":"54","author":"Di Fiore","year":"2022","journal-title":"Amino Acids"},{"key":"10.1016\/bs.enz.2026.06.005_bib0070","doi-asserted-by":"crossref","DOI":"10.1016\/j.abb.2024.110182","article-title":"Phosphorylation strongly affects the inhibition of human carbonic anhydrase I CO2 hydration activity","volume":"761","author":"Angeli","year":"2024","journal-title":"Arch. Biochem. Biophys."},{"issue":"15","key":"10.1016\/bs.enz.2026.06.005_bib0071","doi-asserted-by":"crossref","first-page":"5498","DOI":"10.1016\/j.bmc.2010.06.056","article-title":"Mutation of Phe91 to Asn in human carbonic anhydrase I unexpectedly enhanced both catalytic activity and affinity for sulfonamide inhibitors","volume":"18","author":"Kockar","year":"2010","journal-title":"Bioorg. Med. Chem."},{"issue":"4","key":"10.1016\/bs.enz.2026.06.005_bib0072","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1002\/humu.1380040411","article-title":"Marked zinc activation of ester hydrolysis by a mutation, 67-His (CAT) to Arg (CGT), in the active site of human carbonic anhydrase I","volume":"4","author":"Chegwidden","year":"1994","journal-title":"Hum. Mutat."},{"issue":"20","key":"10.1016\/bs.enz.2026.06.005_bib0073","doi-asserted-by":"crossref","first-page":"6237","DOI":"10.1021\/bi0120446","article-title":"Crystal structure of a zinc-activated variant of human carbonic anhydrase I, CA I Michigan 1: evidence for a second zinc binding site involving arginine coordination","volume":"41","author":"Ferraroni","year":"2002","journal-title":"Biochemistry"},{"issue":"7","key":"10.1016\/bs.enz.2026.06.005_bib0074","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."},{"key":"10.1016\/bs.enz.2026.06.005_bib0075","doi-asserted-by":"crossref","first-page":"30766","DOI":"10.1074\/jbc.M805353200","article-title":"Entrapment of carbon dioxide in the active site of carbonic anhydrase II","volume":"283","author":"Domsic","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/bs.enz.2026.06.005_bib0076","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1111\/j.1432-1033.1975.tb02449.x","article-title":"The catalytic mechanism of carbonic anhydrase","volume":"59","author":"Steiner","year":"1975","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/bs.enz.2026.06.005_bib0077","doi-asserted-by":"crossref","first-page":"10609","DOI":"10.1073\/pnas.0904184106","article-title":"Structural study of x-ray induced activation of carbonic anhydrase","volume":"106","author":"Sj\u00f6blom","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"issue":"8","key":"10.1016\/bs.enz.2026.06.005_bib0078","doi-asserted-by":"crossref","first-page":"2561","DOI":"10.1016\/S0021-9258(18)62326-9","article-title":"The carbon dioxide hydration activity of carbonic anhydrase: I. Stop-flow kinetic studies on the native human isoenzymes B and C","volume":"246","author":"Khalifah","year":"1971","journal-title":"J. Biol. Chem."},{"issue":"28","key":"10.1016\/bs.enz.2026.06.005_bib0079","doi-asserted-by":"crossref","first-page":"13000","DOI":"10.1016\/S0021-9258(18)69261-0","article-title":"Steady-state kinetic studies of superoxide dismutases. Saturative behavior of the copper- and zinc-containing protein","volume":"261","author":"Fee","year":"1986","journal-title":"J. Biol. Chem."},{"issue":"3","key":"10.1016\/bs.enz.2026.06.005_bib0080","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1111\/j.1432-1033.1989.tb15050.x","article-title":"Effect of evolution on the kinetic properties of enzymes","volume":"184","author":"Pettersson","year":"1989","journal-title":"Eur. J. Biochem."},{"issue":"1","key":"10.1016\/bs.enz.2026.06.005_bib0081","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1080\/14756360801907143","article-title":"Carbonic anhydrase inhibitors. Cloning, characterization and inhibition studies of the cytosolic isozyme III with anions","volume":"24","author":"Nishimori","year":"2009","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"10","key":"10.1016\/bs.enz.2026.06.005_bib0082","doi-asserted-by":"crossref","first-page":"3818","DOI":"10.1021\/ja307735e","article-title":"Carbonyl sulfide hydrolase from Thiobacillus thioparus strain THI115 is one of the \u03b2-carbonic anhydrase family enzymes","volume":"135","author":"Ogawa","year":"2013","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/bs.enz.2026.06.005_bib0083","doi-asserted-by":"crossref","first-page":"3427","DOI":"10.1016\/j.csbj.2021.05.057","article-title":"Zeta-carbonic anhydrases show CS2 hydrolase activity: a new metabolic carbon acquisition pathway in diatoms?","volume":"19","author":"Alterio","year":"2021","journal-title":"Comput. Struct. Biotechnol. J."},{"issue":"7369","key":"10.1016\/bs.enz.2026.06.005_bib0084","doi-asserted-by":"crossref","first-page":"412","DOI":"10.1038\/nature10464","article-title":"Evolution of a new enzyme for carbon disulphide conversion by an acidothermophilic archaeon","volume":"478","author":"Smeulders","year":"2011","journal-title":"Nature"},{"key":"10.1016\/bs.enz.2026.06.005_bib0085","doi-asserted-by":"crossref","first-page":"528","DOI":"10.1007\/s007750050375","article-title":"Carbonic anhydrase catalyzes cyanamide hydration to urea: is it mimicking the physiological reaction ?","volume":"4","author":"Briganti","year":"1999","journal-title":"J. Biol. Inorg. Chem."},{"key":"10.1016\/bs.enz.2026.06.005_bib0086","doi-asserted-by":"crossref","first-page":"12391","DOI":"10.1021\/bi000937c","article-title":"Mechanism of cyanamide hydration catalyzed by carbonic anhydrase II suggested by cryogenic x-ray diffraction","volume":"39","author":"Guerri","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/bs.enz.2026.06.005_bib0087","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1002\/(SICI)1097-0134(199702)27:2<272::AID-PROT12>3.0.CO;2-J","article-title":"Is cyanate a carbonic anhydrase substrate?","volume":"27","author":"Supuran","year":"1997","journal-title":"Proteins: Struct. Funct. Genet."},{"issue":"1","key":"10.1016\/bs.enz.2026.06.005_bib0088","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1021\/bi00853a037","article-title":"The catalytic versatility of erythrocyte carbonic anhydrase. II. Kinetic studies of the enzyme-catalyzed hydration of pyridine aldehydes","volume":"6","author":"Pocker","year":"1967","journal-title":"Biochemistry"},{"issue":"3","key":"10.1016\/bs.enz.2026.06.005_bib0089","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1021\/ja00979a029","article-title":"A comparative study of enzymatic and metal ion catalyzed hydration of pyridine aldehydes","volume":"89","author":"Pocker","year":"1967","journal-title":"J. Am. Chem. Soc."},{"issue":"5","key":"10.1016\/bs.enz.2026.06.005_bib0090","doi-asserted-by":"crossref","first-page":"1995","DOI":"10.1021\/bi00845a050","article-title":"The catalytic versatility of erythrocyte carbonic anhydrase. V. Kinetic studies of enzyme-catalyzed hydrations of aliphatic aldehydes","volume":"7","author":"Pocker","year":"1968","journal-title":"Biochemistry"},{"issue":"9","key":"10.1016\/bs.enz.2026.06.005_bib0091","doi-asserted-by":"crossref","first-page":"3021","DOI":"10.1021\/bi00849a001","article-title":"The catalytic versatility of erythrocyte carbonic anhydrase. VII. Kinetic studies of esterase activity and competitive inhibition by substrate analogs","volume":"7","author":"Pocker","year":"1968","journal-title":"Biochemistry"},{"issue":"13","key":"10.1016\/bs.enz.2026.06.005_bib0092","doi-asserted-by":"crossref","first-page":"2475","DOI":"10.1021\/bi00737a017","article-title":"Stopped-flow studies of high pH activity and acetazolamide inhibition of bovine carbonic anhydrase. Enzyme-catalyzed hydrolyses of 3-pyridyl and nitro-3-pyridyl acetates","volume":"12","author":"Pocker","year":"1973","journal-title":"Biochemistry"},{"issue":"7","key":"10.1016\/bs.enz.2026.06.005_bib0093","doi-asserted-by":"crossref","first-page":"1411","DOI":"10.1021\/bi00704a015","article-title":"Alpha-keto esters as substrates of erythrocyte carbonic anhydrase. Kinetic studies of enzyme-catalyzed hydration of methyl and ethyl pyruvate","volume":"13","author":"Pocker","year":"1974","journal-title":"Biochemistry"},{"issue":"18","key":"10.1016\/bs.enz.2026.06.005_bib0094","doi-asserted-by":"crossref","first-page":"4221","DOI":"10.1016\/S0021-9258(18)95800-X","article-title":"Esterase activities of human carbonic anhydrases B and C","volume":"242","author":"Verpoorte","year":"1967","journal-title":"J. Biol. Chem."},{"issue":"6","key":"10.1016\/bs.enz.2026.06.005_bib0095","doi-asserted-by":"crossref","first-page":"880","DOI":"10.3109\/14756366.2011.637202","article-title":"Simple methanesulfonates are hydrolyzed by the sulfatase carbonic anhydrase activity","volume":"27","author":"Kazancio\u011flu","year":"2012","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2026.06.005_bib0096","doi-asserted-by":"crossref","first-page":"148","DOI":"10.3109\/14756366.2011.629198","article-title":"\u03b1-Carbonic anhydrases are sulfatases with cyclic diol monosulfate esters","volume":"27","author":"Cavdar","year":"2012","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"7","key":"10.1016\/bs.enz.2026.06.005_bib0097","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."},{"key":"10.1016\/bs.enz.2026.06.005_bib0098","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1006\/abbi.2000.1793","article-title":"Carbonic anhydrase III: the phosphatase activity is extrinsic","volume":"377","author":"Kim","year":"2000","journal-title":"Arch. Biochem. Biophys."},{"issue":"3","key":"10.1016\/bs.enz.2026.06.005_bib0099","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1021\/ml500470b","article-title":"\u03b1-carbonic anhydrases possess thioesterase activity","volume":"6","author":"Tanc","year":"2015","journal-title":"ACS Med. Chem. Lett."},{"issue":"32","key":"10.1016\/bs.enz.2026.06.005_bib0100","doi-asserted-by":"crossref","first-page":"4444","DOI":"10.1039\/D0CC00995D","article-title":"Selenolesterase enzyme activity of carbonic anhydrases","volume":"56","author":"Angeli","year":"2020","journal-title":"Chem. Commun. (Camb)."},{"issue":"7990","key":"10.1016\/bs.enz.2026.06.005_bib0101","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1038\/s41586-023-06716-y","article-title":"Plant carbonic anhydrase-like enzymes in neuroactive alkaloid biosynthesis","volume":"624","author":"Nett","year":"2023","journal-title":"Nature"},{"key":"10.1016\/bs.enz.2026.06.005_bib0102","doi-asserted-by":"crossref","first-page":"321","DOI":"10.3109\/14756366.2014.913587","article-title":"Recent advances in the discovery of zinc-binding motifs for the development of carbonic anhydrase inhibitors","volume":"30","author":"Winum","year":"2015","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"80","key":"10.1016\/bs.enz.2026.06.005_bib0103","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)."},{"key":"10.1016\/bs.enz.2026.06.005_bib0104","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2025.118043","article-title":"Design, anticancer activity, and mechanistic evaluation of a novel class of selective human carbonic anhydrase IX inhibitors featuring a trifluorodihydroxypropanone pharmacophore","volume":"298","author":"Pala","year":"2025","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.06.005_bib0105","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.2026.06.005_bib0106","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":"31","key":"10.1016\/bs.enz.2026.06.005_bib0107","doi-asserted-by":"crossref","first-page":"7840","DOI":"10.1002\/chem.201800941","article-title":"Deciphering the mechanism of human carbonic anhydrases inhibition with sulfocoumarins: computational and experimental studies","volume":"24","author":"Nocentini","year":"2018","journal-title":"Chemistry"},{"key":"10.1016\/bs.enz.2026.06.005_bib0108","doi-asserted-by":"crossref","first-page":"3057","DOI":"10.1021\/ja809683v","article-title":"Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new class of suicide inhibitors","volume":"131","author":"Maresca","year":"2009","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/bs.enz.2026.06.005_bib0109","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":"1","key":"10.1016\/bs.enz.2026.06.005_bib0110","doi-asserted-by":"crossref","DOI":"10.1002\/ardp.202400705","article-title":"Lactonase activity of \u03b1-carbonic anhydrases allows identification of novel inhibitors","volume":"358","author":"Giovannuzzi","year":"2025","journal-title":"Arch. Pharm. (Weinheim)"},{"issue":"9","key":"10.1016\/bs.enz.2026.06.005_bib0111","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.2026.06.005_bib0112","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1039\/C4CC07320G","article-title":"Out of the active site binding pocket for carbonic anhydrase inhibitors","volume":"51","author":"D\u2019Ambrosio","year":"2015","journal-title":"Chem. Commun."},{"issue":"1","key":"10.1016\/bs.enz.2026.06.005_bib0113","doi-asserted-by":"crossref","DOI":"10.1002\/ardp.202400776","article-title":"Unprecedented carbonic anhydrase inhibition mechanism: targeting histidine 64 side chain through a halogen bond","volume":"358","author":"Paciotti","year":"2025","journal-title":"Arch. Pharm. (Weinheim)"},{"key":"10.1016\/bs.enz.2026.06.005_bib0114","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."},{"key":"10.1016\/bs.enz.2026.06.005_bib0115","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.2026.06.005_bib0116","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1042\/bj0430525","article-title":"Inhibition of carbonic anhydrase by sulphonamides","volume":"43","author":"Krebs","year":"1948","journal-title":"Biochem. J."},{"issue":"10","key":"10.1016\/bs.enz.2026.06.005_bib0117","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.2026.06.005_bib0118","doi-asserted-by":"crossref","first-page":"1185","DOI":"10.1056\/NEJMoa2203094","article-title":"Acetazolamide in acute decompensated heart failure with volume overload","volume":"387","author":"Mullens","year":"2022","journal-title":"N. Engl. J. Med."},{"issue":"10","key":"10.1016\/bs.enz.2026.06.005_bib0119","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":"11","key":"10.1016\/bs.enz.2026.06.005_bib0120","doi-asserted-by":"crossref","first-page":"863","DOI":"10.1212\/WNL.4.11.863","article-title":"Diamox; a carbonic anhydrase inhibitor; its use in epilepsy","volume":"4","author":"Merlis","year":"1954","journal-title":"Neurology"},{"issue":"4968","key":"10.1016\/bs.enz.2026.06.005_bib0121","doi-asserted-by":"crossref","first-page":"650","DOI":"10.1136\/bmj.1.4968.650","article-title":"Acetazolamide in treatment of epilepsy","volume":"1","author":"Ansell","year":"1956","journal-title":"Br. Med. J."},{"issue":"1","key":"10.1016\/bs.enz.2026.06.005_bib0122","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1111\/j.1528-1157.1989.tb05285.x","article-title":"Use of acetazolamide as an adjunct to carbamazepine in refractory partial seizures","volume":"30","author":"Oles","year":"1989","journal-title":"Epilepsia"},{"issue":"5","key":"10.1016\/bs.enz.2026.06.005_bib0123","doi-asserted-by":"crossref","first-page":"514","DOI":"10.1177\/106002809603000515","article-title":"Acetazolamide in the treatment of seizures","volume":"30","author":"Reiss","year":"1996","journal-title":"Ann. Pharmacother."},{"issue":"2","key":"10.1016\/bs.enz.2026.06.005_bib0124","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/S0920-1211(02)00019-0","article-title":"Effects of antiepileptic drugs on extracellular pH regulation in the hippocampal CA1 region in vivo","volume":"49","author":"Aribi","year":"2002","journal-title":"Epilepsy Res."},{"issue":"5","key":"10.1016\/bs.enz.2026.06.005_bib0125","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1046\/j.1528-1157.2002.32601.x","article-title":"Carbonic anhydrase inhibitor sulthiame reduces intracellular pH and epileptiform activity of hippocampal CA3 neurons","volume":"43","author":"Leniger","year":"2002","journal-title":"Epilepsia"},{"key":"10.1016\/bs.enz.2026.06.005_bib0126","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1016\/j.lfs.2017.03.018","article-title":"Hypercapnia-induced brain acidosis: effects and putative mechanisms on acute kainate induced seizures","volume":"176","author":"Shi","year":"2017","journal-title":"Life Sci."},{"issue":"Suppl 1","key":"10.1016\/bs.enz.2026.06.005_bib0127","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":"7","key":"10.1016\/bs.enz.2026.06.005_bib0128","doi-asserted-by":"crossref","first-page":"661","DOI":"10.2174\/138161208783877956","article-title":"Anticonvulsant sulfonamides\/sulfamates\/sulfamides with carbonic anhydrase inhibitory activity: drug design and mechanism of action","volume":"14","author":"Thiry","year":"2008","journal-title":"Curr. Pharm. Des."},{"issue":"6","key":"10.1016\/bs.enz.2026.06.005_bib0129","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1517\/13543776.2013.782394","article-title":"Anticonvulsant\/antiepileptic carbonic anhydrase inhibitors: a patent review","volume":"23","author":"Aggarwal","year":"2013","journal-title":"Expert Opin. Ther. Pat."},{"issue":"5","key":"10.1016\/bs.enz.2026.06.005_bib0130","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":"17","key":"10.1016\/bs.enz.2026.06.005_bib0131","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":"3","key":"10.1016\/bs.enz.2026.06.005_bib0132","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1111\/j.1747-0285.2009.00857.x","article-title":"Which carbonic anhydrases are targeted by the antiepileptic sulfonamides and sulfamates?","volume":"74","author":"De Simone","year":"2009","journal-title":"Chem. Biol. Drug Des."},{"issue":"7","key":"10.1016\/bs.enz.2026.06.005_bib0133","doi-asserted-by":"crossref","first-page":"655","DOI":"10.2174\/138161208783877820","article-title":"Are carbonic anhydrase inhibitors suitable for obtaining antiobesity drugs?","volume":"14","author":"De Simone","year":"2008","journal-title":"Curr. Pharm. Des."},{"issue":"6","key":"10.1016\/bs.enz.2026.06.005_bib0134","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1517\/13543776.2013.790957","article-title":"Antiobesity carbonic anhydrase inhibitors: a literature and patent review","volume":"23","author":"Scozzafava","year":"2013","journal-title":"Expert Opin. Ther. Pat."},{"issue":"1","key":"10.1016\/bs.enz.2026.06.005_bib0135","doi-asserted-by":"crossref","first-page":"2478","DOI":"10.1080\/14756366.2022.2121393","article-title":"Anti-obesity carbonic anhydrase inhibitors: challenges and opportunities","volume":"37","author":"Supuran","year":"2022","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"2","key":"10.1016\/bs.enz.2026.06.005_bib0136","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.2026.06.005_bib0137","first-page":"883","article-title":"Acetazolamide plus low-dose dexamethasone is better than acetazolamide alone to ameliorate symptoms of acute mountain sickness","volume":"69","author":"Bernhard","year":"1998","journal-title":"Aviat. Space Environ. Med."},{"key":"10.1016\/bs.enz.2026.06.005_bib0138","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1055\/s-2007-1024597","article-title":"Acetazolamide and high altitude disease","volume":"13","author":"Bradwell","year":"1992","journal-title":"Int. J. Sports Med."},{"key":"10.1016\/bs.enz.2026.06.005_bib0139","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1164\/rccm.200608-1199OC","article-title":"Effects of acetazolamide on ventilatory, cerebrovascular, and pulmonary vascular responses to hypoxia","volume":"175","author":"Teppema","year":"2007","journal-title":"Am. J. Respir. Crit. Care Med."},{"key":"10.1016\/bs.enz.2026.06.005_bib0140","first-page":"6656","article-title":"Acetazolamide pre-treatment before ascending to high altitudes: sustained effect on systemic blood pressure during submaximal exercise","volume":"9","author":"Burtscher","year":"2016","journal-title":"Int. J. Clin. Exp. Med."},{"key":"10.1016\/bs.enz.2026.06.005_bib0141","doi-asserted-by":"crossref","first-page":"851","DOI":"10.1586\/14737175.2015.1066675","article-title":"Acetazolamide for the treatment of idiopathic intracranial hypertension","volume":"15","author":"Supuran","year":"2015","journal-title":"Expert Rev. Neurother."},{"key":"10.1016\/bs.enz.2026.06.005_bib0142","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.neulet.2017.02.032","article-title":"Acetazolamide lowers intracranial pressure and modulates the cerebrospinal fluid secretion pathway in healthy rats","volume":"645","author":"Uldall","year":"2017","journal-title":"Neurosci. Lett."},{"issue":"3","key":"10.1016\/bs.enz.2026.06.005_bib0143","doi-asserted-by":"crossref","first-page":"450","DOI":"10.3390\/medicina61030450","article-title":"Effectiveness of topiramate versus acetazolamide in the management of idiopathic intracranial hypertension: a systematic review and meta-analysis","volume":"61","author":"Almaqhawi","year":"2025","journal-title":"Medicina. (Kaunas)"},{"key":"10.1016\/bs.enz.2026.06.005_bib0144","doi-asserted-by":"crossref","first-page":"961","DOI":"10.1080\/14737175.2016.1193009","article-title":"Carbonic anhydrase inhibition and the management of neuropathic pain","volume":"16","author":"Supuran","year":"2016","journal-title":"Expert Rev. Neurother."},{"key":"10.1016\/bs.enz.2026.06.005_bib0145","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1016\/j.pain.2009.11.015","article-title":"Acetazolamide and midazolam act synergistically to inhibit neuropathic pain","volume":"148","author":"Asiedu","year":"2010","journal-title":"Pain"},{"key":"10.1016\/bs.enz.2026.06.005_bib0146","doi-asserted-by":"crossref","first-page":"1828","DOI":"10.1016\/j.bmc.2015.02.027","article-title":"A class of sulfonamide carbonic anhydrase inhibitors with neuropathic pain modulating effects","volume":"23","author":"Carta","year":"2015","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/bs.enz.2026.06.005_bib0147","doi-asserted-by":"crossref","first-page":"894","DOI":"10.3109\/14756366.2015.1113407","article-title":"Carbonic anhydrase inhibition for the management of cerebral ischemia: in vivo evaluation of sulfonamide and coumarin inhibitors","volume":"31","author":"Di Cesare Mannelli","year":"2016","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"9","key":"10.1016\/bs.enz.2026.06.005_bib0148","doi-asserted-by":"crossref","first-page":"5029","DOI":"10.3390\/ijms22095029","article-title":"Role of carbonic anhydrase in cerebral ischemia and carbonic anhydrase inhibitors as putative protective agents","volume":"22","author":"Bulli","year":"2021","journal-title":"Int. J. Mol. Sci."},{"issue":"1","key":"10.1016\/bs.enz.2026.06.005_bib0149","doi-asserted-by":"crossref","first-page":"964","DOI":"10.1080\/14756366.2021.1907575","article-title":"Protective effects of carbonic anhydrase inhibition in brain ischaemia in vitro and in vivo models","volume":"36","author":"Dettori","year":"2021","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2026.06.005_bib0150","doi-asserted-by":"crossref","first-page":"e750","DOI":"10.1016\/j.wneu.2024.02.123","article-title":"Treatment Effects of acetazolamide on ischemic stroke: a meta-analysis and systematic review","volume":"185","author":"Liu","year":"2024","journal-title":"World Neurosurg."},{"issue":"4","key":"10.1016\/bs.enz.2026.06.005_bib0151","doi-asserted-by":"crossref","DOI":"10.1016\/j.heliyon.2025.e42457","volume":"11","author":"Amiranda","year":"2025","journal-title":"Heliyon"},{"key":"10.1016\/bs.enz.2026.06.005_bib0152","doi-asserted-by":"crossref","first-page":"4961","DOI":"10.1021\/acs.jmedchem.8b00420","article-title":"Discovery of novel nonsteroidal anti-inflammatory drugs and carbonic anhydrase inhibitors hybrids (NSAIDs-CAIs) for the management of rheumatoid arthritis","volume":"61","author":"Akgul","year":"2018","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.06.005_bib0153","doi-asserted-by":"crossref","first-page":"1159","DOI":"10.1021\/acs.jmedchem.6b01607","article-title":"Design and synthesis of novel nonsteroidal anti-inflammatory drugs and carbonic anhydrase inhibitors hybrids (NSAIDs-CAIs) for the treatment of rheumatoid arthritis","volume":"60","author":"Bua","year":"2017","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2026.06.005_bib0154","doi-asserted-by":"crossref","first-page":"7233","DOI":"10.1021\/acs.jmedchem.9b00845","article-title":"Synthesis and evaluation of carbonic anhydrase inhibitors with carbon monoxide releasing properties for the management of rheumatoid arthritis","volume":"62","author":"Berrino","year":"2019","journal-title":"J. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2026.06.005_bib0155","doi-asserted-by":"crossref","first-page":"56","DOI":"10.3390\/antiox10010056","article-title":"Dual carbonic anhydrase IX\/XII inhibitors and carbon monoxide releasing molecules modulate LPS-mediated inflammation in mouse macrophages","volume":"10","author":"Berrino","year":"2021","journal-title":"Antioxidants (Basel)"},{"key":"10.1016\/bs.enz.2026.06.005_bib0156","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."},{"key":"10.1016\/bs.enz.2026.06.005_bib0157","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.nbd.2015.11.006","article-title":"The carbonic anhydrase inhibitor methazolamide prevents amyloid beta-induced mitochondrial dysfunction and caspase activation protecting neuronal and glial cells in vitro and in the mouse brain","volume":"86","author":"Fossati","year":"2016","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/bs.enz.2026.06.005_bib0158","doi-asserted-by":"crossref","DOI":"10.1111\/acel.12787","article-title":"Carbonic anhydrase inhibition selectively prevents amyloid \u03b2 neurovascular mitochondrial toxicity","volume":"17","author":"Solesio","year":"2018","journal-title":"Aging Cell"},{"issue":"11","key":"10.1016\/bs.enz.2026.06.005_bib0159","doi-asserted-by":"crossref","first-page":"5048","DOI":"10.1002\/alz.13063","article-title":"FDA-approved carbonic anhydrase inhibitors reduce amyloid \u03b2 pathology and improve cognition, by ameliorating cerebrovascular health and glial fitness","volume":"19","author":"Canepa","year":"2023","journal-title":"Alzheimers Dement."},{"issue":"24","key":"10.1016\/bs.enz.2026.06.005_bib0160","doi-asserted-by":"crossref","first-page":"2840","DOI":"10.3390\/cells12242840","article-title":"Amyloid beta oligomers activate death receptors and mitochondria-mediated apoptotic pathways in cerebral vascular smooth muscle cells; protective effects of carbonic anhydrase inhibitors","volume":"12","author":"Anzovino","year":"2023","journal-title":"Cells"},{"issue":"4","key":"10.1016\/bs.enz.2026.06.005_bib0161","doi-asserted-by":"crossref","DOI":"10.1002\/alz.70122","article-title":"Cerebral proteome adaptations to amyloid angiopathy are prevented by carbonic anhydrase inhibitors","volume":"21","author":"Carlsen","year":"2025","journal-title":"Alzheimers Dement."},{"issue":"3","key":"10.1016\/bs.enz.2026.06.005_bib0162","doi-asserted-by":"crossref","DOI":"10.1002\/alz.70023","article-title":"Carbonic anhydrase inhibitors prevent presymptomatic capillary flow disturbances in a model of cerebral amyloidosis","volume":"21","author":"Guti\u00e9rrez-Jim\u00e9nez","year":"2025","journal-title":"Alzheimers Dement."},{"key":"10.1016\/bs.enz.2026.06.005_bib0163","doi-asserted-by":"crossref","first-page":"3019","DOI":"10.2147\/JIR.S413358","article-title":"M1-type macrophages secrete TNF-\u03b1 to stimulate vascular calcification by upregulating CA1 and CA2 expression in VSMCs","volume":"16","author":"Song","year":"2023","journal-title":"J. Inflamm. Res."},{"key":"10.1016\/bs.enz.2026.06.005_bib0164","doi-asserted-by":"crossref","DOI":"10.1155\/2024\/5009637","article-title":"Methazolamide can treat atherosclerosis by increasing immunosuppressive cells and decreasing expressions of genes related to proinflammation, calcification, and tissue remodeling","volume":"2024","author":"Zhou","year":"2024","journal-title":"J. Immunol. Res."},{"key":"10.1016\/bs.enz.2026.06.005_bib0165","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1016\/j.athplu.2025.03.003","article-title":"ApoE [-\/-] CA1-overexpressing knock-in mice aggravated atherosclerosis by increasing M1 macrophages","volume":"60","author":"Zong","year":"2025","journal-title":"Atheroscler. Plus"},{"key":"10.1016\/bs.enz.2026.06.005_bib0166","doi-asserted-by":"crossref","first-page":"256","DOI":"10.1186\/1471-2474-13-256","article-title":"Transgenic mice over-expressing carbonic anhydrase I showed aggravated joint inflammation and tissue destruction","volume":"13","author":"Zheng","year":"2012","journal-title":"BMC Musculoskelet. Disord."},{"issue":"5","key":"10.1016\/bs.enz.2026.06.005_bib0167","doi-asserted-by":"crossref","first-page":"413","DOI":"10.7150\/ijms.8.413","article-title":"Treat ankylosing spondylitis with methazolamide","volume":"8","author":"Chang","year":"2011","journal-title":"Int. J. Med. Sci."},{"key":"10.1016\/bs.enz.2026.06.005_bib0168","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1186\/1471-2474-11-279","article-title":"Increased expression of carbonic anhydrase I in the synovium of patients with ankylosing spondylitis","volume":"11","author":"Chang","year":"2010","journal-title":"BMC Musculoskelet. Disord."},{"issue":"6","key":"10.1016\/bs.enz.2026.06.005_bib0169","doi-asserted-by":"crossref","first-page":"963","DOI":"10.1189\/jlb.1212612","article-title":"Oral administration of carbonic anhydrase I ameliorates murine experimental colitis induced by Foxp3-CD4+CD25- T cells","volume":"93","author":"Mori","year":"2013","journal-title":"J. Leukoc. Biol."},{"issue":"8","key":"10.1016\/bs.enz.2026.06.005_bib0170","doi-asserted-by":"crossref","first-page":"1835","DOI":"10.1097\/MIB.0000000000000781","article-title":"Carbonic anhydrate I epitope peptide improves inflammation in a murine model of inflammatory bowel disease","volume":"22","author":"Yagi","year":"2016","journal-title":"Inflamm. Bowel Dis."},{"issue":"1","key":"10.1016\/bs.enz.2026.06.005_bib0171","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-022-22455-y","article-title":"Oral administration of human carbonic anhydrase I suppresses colitis in a murine inflammatory bowel disease model","volume":"12","author":"Tange","year":"2022","journal-title":"Sci. Rep."},{"issue":"1","key":"10.1016\/bs.enz.2026.06.005_bib0172","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-025-96677-1","article-title":"A case-control study on the role of carbonic anhydrase autoantibodies in the pathogenesis and diagnosis of fibromyalgia","volume":"15","author":"K\u0131l\u0131\u00e7","year":"2025","journal-title":"Sci. Rep."},{"issue":"1","key":"10.1016\/bs.enz.2026.06.005_bib0173","first-page":"26","article-title":"Carbonic anhydrase I and II autoantibodies in Beh\u00e7et\u2019s disease","volume":"42","author":"Mentese","year":"2017","journal-title":"Acta. Reumatol. Port."},{"issue":"4","key":"10.1016\/bs.enz.2026.06.005_bib0174","doi-asserted-by":"crossref","first-page":"382","DOI":"10.1097\/00006676-200005000-00008","article-title":"Elevated serum levels of antibodies to carbonic anhydrase I and II in patients with chronic pancreatitis","volume":"20","author":"Frulloni","year":"2000","journal-title":"Pancreas"},{"issue":"22","key":"10.1016\/bs.enz.2026.06.005_bib0175","doi-asserted-by":"crossref","first-page":"3637","DOI":"10.1111\/jcmm.17970","article-title":"Spontaneous regression of tumours. Possible cross reactivity of autoantibodies against carbonic anhydrase I","volume":"27","author":"Lakota","year":"2023","journal-title":"J. Cell. Mol. Med."},{"key":"10.1016\/bs.enz.2026.06.005_bib0176","doi-asserted-by":"crossref","DOI":"10.1155\/mi\/9981131","article-title":"Inhibitory effect of human anti-CA I autoantibodies and development of monoclonal antibody mAb 2B8 targeting carbonic anhydrase I","volume":"2024","author":"Chalova","year":"2024","journal-title":"Mediators Inflamm."},{"issue":"4","key":"10.1016\/bs.enz.2026.06.005_bib0177","doi-asserted-by":"crossref","first-page":"842","DOI":"10.4269\/ajtmh.16-0021","article-title":"Serum carbonic anhydrase 1 is a biomarker for diagnosis of human Schistosoma mansoni Infection","volume":"96","author":"Kardoush","year":"2017","journal-title":"Am. J. Trop. Med. Hyg."},{"issue":"1","key":"10.1016\/bs.enz.2026.06.005_bib0178","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1007\/s13277-015-3834-z","article-title":"Carbonic anhydrase 1 is a promising biomarker for early detection of non-small cell lung cancer","volume":"37","author":"Wang","year":"2016","journal-title":"Tumour Biol."},{"issue":"10","key":"10.1016\/bs.enz.2026.06.005_bib0179","doi-asserted-by":"crossref","first-page":"2179","DOI":"10.1023\/A:1011910931210","article-title":"Differential expression of cytoplasmic carbonic anhydrases, CA I and II, and membrane-associated isozymes, CA IX and XII, in normal mucosa of large intestine and in colorectal tumors","volume":"46","author":"Kivela","year":"2001","journal-title":"Dig. Dis. Sci."},{"issue":"34","key":"10.1016\/bs.enz.2026.06.005_bib0180","first-page":"998","article-title":"Expression of carbonic anhydrase I or II and correlation to clinical aspects of colorectal cancer","volume":"47","author":"Bekku","year":"2000","journal-title":"Hepatogastroenterology"},{"issue":"2","key":"10.1016\/bs.enz.2026.06.005_bib0181","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1016\/j.chest.2025.09.019","article-title":"Acetazolamide plus atomoxetine for obesity hypoventilation syndrome treatment","volume":"169","author":"Perger","year":"2026","journal-title":"Chest"},{"issue":"2","key":"10.1016\/bs.enz.2026.06.005_bib0182","first-page":"97","article-title":"Role of carbonic anhydrase in bone: plasma acetazolamide concentrations associated with inhibition of bone loss","volume":"31","author":"Kenny","year":"1985","journal-title":"Pharmacology"},{"issue":"4","key":"10.1016\/bs.enz.2026.06.005_bib0183","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1002\/jbmr.5650060406","article-title":"Effect of chronic carbonic anhydrase inhibitor therapy on bone mineral density in white women","volume":"6","author":"Pierce","year":"1991","journal-title":"J. Bone Miner. Res."},{"issue":"5","key":"10.1016\/bs.enz.2026.06.005_bib0184","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."},{"key":"10.1016\/bs.enz.2026.06.005_bib0185","first-page":"411","article-title":"Carbonic anhydrase activators. Part 4. A general mechanism of action for activators of isozymes I, II and III","volume":"37","author":"Supuran","year":"1994","journal-title":"Rev. Roum. Chim."},{"key":"10.1016\/bs.enz.2026.06.005_bib0186","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.2026.06.005_bib0187","first-page":"107","article-title":"Carbonic anhydrase activators. Part 8. pKa-activation relationship in a series of amino acid derivatives activators of isozyme II","volume":"39","author":"Supuran","year":"1994","journal-title":"Rev. Roum. Chim."},{"issue":"15","key":"10.1016\/bs.enz.2026.06.005_bib0188","doi-asserted-by":"crossref","first-page":"3955","DOI":"10.1016\/j.bmcl.2006.05.023","article-title":"Carbonic anhydrase activators: activation of isozyme XIII with amino acids and amines","volume":"16","author":"Parkkila","year":"2006","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"5","key":"10.1016\/bs.enz.2026.06.005_bib0189","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."},{"issue":"23","key":"10.1016\/bs.enz.2026.06.005_bib0190","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.2026.06.005_bib0191","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.2026.06.005_bib0192","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.2026.06.005_bib0193","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.2026.06.005_bib0194","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.2026.06.005_bib0195","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.2026.06.005_bib0196","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."},{"issue":"15","key":"10.1016\/bs.enz.2026.06.005_bib0197","doi-asserted-by":"crossref","first-page":"4107","DOI":"10.1016\/j.bmcl.2007.05.052","article-title":"Carbonic anhydrase activators: activation of the human isoforms VII (cytosolic) and XIV (transmembrane) with amino acids and amines","volume":"17","author":"Vullo","year":"2007","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"5","key":"10.1016\/bs.enz.2026.06.005_bib0198","doi-asserted-by":"crossref","first-page":"1336","DOI":"10.1016\/j.bmcl.2006.11.075","article-title":"Carbonic anhydrase activators: an activation study of the human mitochondrial isoforms VA and VB with amino acids and amines","volume":"17","author":"Vullo","year":"2007","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"15","key":"10.1016\/bs.enz.2026.06.005_bib0199","doi-asserted-by":"crossref","first-page":"5351","DOI":"10.1016\/j.bmc.2007.03.004","article-title":"Carbonic anhydrase activators: the first activation study of the human secretory isoform VI with amino acids and amines","volume":"15","author":"Nishimori","year":"2007","journal-title":"Bioorg. Med. Chem."},{"issue":"13","key":"10.1016\/bs.enz.2026.06.005_bib0200","doi-asserted-by":"crossref","first-page":"3430","DOI":"10.1016\/j.bmcl.2009.05.026","article-title":"Carbonic anhydrase activators. Activation of the membrane-associated isoform XV with amino acids and amines","volume":"19","author":"Innocenti","year":"2009","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2026.06.005_bib0201","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.2026.06.005_bib0202","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.2026.06.005_bib0203","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.2026.06.005_bib0204","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.2026.06.005_bib0205","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.2026.06.005_bib0206","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.2026.06.005_bib0207","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.2026.06.005_bib0208","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.2026.06.005_bib0209","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.2026.06.005_bib0210","doi-asserted-by":"crossref","DOI":"10.2174\/0115680266373008250723064558","article-title":"Exploring the carbonic anhydrase activation properties of 4-arylazo-3,5- diamino-1H-pyrazoles against hCA I, II, IV, and VII isoenzymes","author":"Akocak","year":"2025","journal-title":"Curr. Top. Med. Chem."},{"issue":"18","key":"10.1016\/bs.enz.2026.06.005_bib0211","doi-asserted-by":"crossref","first-page":"16873","DOI":"10.1021\/acs.jmedchem.4c01866","article-title":"Enhanced recognition memory through dual modulation of brain carbonic anhydrases and cholinesterases","volume":"67","author":"Nocentini","year":"2024","journal-title":"J. Med. Chem."},{"issue":"14","key":"10.1016\/bs.enz.2026.06.005_bib0212","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":"10","key":"10.1016\/bs.enz.2026.06.005_bib0213","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":"7","key":"10.1016\/bs.enz.2026.06.005_bib0214","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":"6","key":"10.1016\/bs.enz.2026.06.005_bib0215","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":"1","key":"10.1016\/bs.enz.2026.06.005_bib0216","doi-asserted-by":"crossref","first-page":"84","DOI":"10.18632\/oncotarget.422","article-title":"Recent developments in targeting carbonic anhydrase IX for cancer therapeutics","volume":"3","author":"McDonald","year":"2012","journal-title":"Oncotarget"},{"issue":"6","key":"10.1016\/bs.enz.2026.06.005_bib0217","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":"1","key":"10.1016\/bs.enz.2026.06.005_bib0218","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."},{"issue":"43","key":"10.1016\/bs.enz.2026.06.005_bib0219","doi-asserted-by":"crossref","first-page":"23068","DOI":"10.1002\/anie.202103211","article-title":"Modulating the efficacy of carbonic anhydrase inhibitors through fluorine substitution","volume":"60","author":"Berrino","year":"2021","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"10.1016\/bs.enz.2026.06.005_bib0220","series-title":"Targets in Heterocyclic Systems\u2014Chemistry and Properties","first-page":"116","article-title":"Heterocycles in the design of carbonic anhydrase inhibitors","volume":"28","author":"Paoletti","year":"2024"},{"key":"10.1016\/bs.enz.2026.06.005_bib0221","series-title":"Metalloenzymes\u2014From Bench to Bedside","first-page":"139","article-title":"Carbonic anhydrases","author":"Supuran","year":"2024"},{"key":"10.1016\/bs.enz.2026.06.005_bib0222","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1002\/humu.9266","article-title":"Carbonic anhydrase II deficiency syndrome (osteopetrosis with renal tubular acidosis and brain calcification): novel mutations in CA2 identified by direct sequencing expand the opportunity for genotype-phenotype correlation","volume":"24","author":"Shah","year":"2004","journal-title":"Hum. Mutat."},{"issue":"5","key":"10.1016\/bs.enz.2026.06.005_bib0223","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1038\/sj.bjp.0705850","article-title":"Topiramate modulates pH of hippocampal CA3 neurons by combined effects on carbonic anhydrase and Cl-\/HCO3- exchange","volume":"142","author":"Leniger","year":"2004","journal-title":"Br. J. Pharmacol."}],"container-title":["The Enzymes","Vertebrate Carbonic Anhydrases"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874604726000181?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874604726000181?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,7,22]],"date-time":"2026-07-22T15:16:07Z","timestamp":1784733367000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1874604726000181"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026]]},"ISBN":["9780443470868"],"references-count":223,"URL":"https:\/\/doi.org\/10.1016\/bs.enz.2026.06.005","relation":{},"ISSN":["1874-6047"],"issn-type":[{"value":"1874-6047","type":"print"}],"subject":[],"published":{"date-parts":[[2026]]}}}