{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,8]],"date-time":"2025-10-08T00:06:01Z","timestamp":1759881961309,"version":"build-2065373602"},"reference-count":69,"publisher":"Elsevier","isbn-type":[{"type":"print","value":"9780443313943"}],"license":[{"start":{"date-parts":[[2025,1,1]],"date-time":"2025-01-01T00:00:00Z","timestamp":1735689600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,1,1]],"date-time":"2025-01-01T00:00:00Z","timestamp":1735689600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,1,1]],"date-time":"2025-01-01T00:00:00Z","timestamp":1735689600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2025,1,1]],"date-time":"2025-01-01T00:00:00Z","timestamp":1735689600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2025,1,1]],"date-time":"2025-01-01T00:00:00Z","timestamp":1735689600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2025,1,1]],"date-time":"2025-01-01T00:00:00Z","timestamp":1735689600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2025,1,1]],"date-time":"2025-01-01T00:00:00Z","timestamp":1735689600000},"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":[[2025]]},"DOI":"10.1016\/bs.enz.2025.05.001","type":"book-chapter","created":{"date-parts":[[2025,7,23]],"date-time":"2025-07-23T09:46:31Z","timestamp":1753263991000},"page":"1-20","source":"Crossref","is-referenced-by-count":0,"title":["Overview on fungal and protozoan carbonic anhydrases"],"prefix":"10.1016","member":"78","reference":[{"issue":"6","key":"10.1016\/bs.enz.2025.05.001_bib0001","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1517\/13543776.2013.778245","article-title":"Anti-infective carbonic anhydrase inhibitors: a patent and literature review","volume":"23","author":"Capasso","year":"2013","journal-title":"Expert Opin. Ther. Pat."},{"issue":"12","key":"10.1016\/bs.enz.2025.05.001_bib0002","doi-asserted-by":"crossref","first-page":"1689","DOI":"10.1517\/14728222.2015.1067685","article-title":"Bacterial, fungal and protozoan carbonic anhydrases as drug targets","volume":"19","author":"Capasso","year":"2015","journal-title":"Expert Opin. Ther. Targets"},{"issue":"6","key":"10.1016\/bs.enz.2025.05.001_bib0003","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1080\/13543776.2024.2332663","article-title":"Carbonic anhydrase and bacterial metabolism: a chance for antibacterial drug discovery","volume":"34","author":"Capasso","year":"2024","journal-title":"Expert Opin. Ther. Pat."},{"issue":"9","key":"10.1016\/bs.enz.2025.05.001_bib0004","doi-asserted-by":"crossref","first-page":"4324","DOI":"10.3390\/ijms22094324","article-title":"A highlight on the inhibition of fungal carbonic anhydrases as drug targets for the antifungal armamentarium","volume":"22","author":"Supuran","year":"2021","journal-title":"Int. J. Mol. Sci."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.001_bib0005","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."},{"issue":"6","key":"10.1016\/bs.enz.2025.05.001_bib0006","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":"1","key":"10.1016\/bs.enz.2025.05.001_bib0007","doi-asserted-by":"crossref","first-page":"490","DOI":"10.1080\/21505594.2019.1614383","article-title":"Basic principles of the virulence of Cryptococcus","volume":"10","author":"Zaragoza","year":"2019","journal-title":"Virulence"},{"issue":"8","key":"10.1016\/bs.enz.2025.05.001_bib0008","doi-asserted-by":"crossref","first-page":"2521","DOI":"10.1016\/j.bmcl.2011.02.057","article-title":"Carbonic anhydrase inhibitors. Inhibition of the beta-class enzymes from the fungal pathogens Candida albicans and Cryptococcus neoformans with branched aliphatic\/aromatic carboxylates and their derivatives","volume":"21","author":"Carta","year":"2011","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"8","key":"10.1016\/bs.enz.2025.05.001_bib0009","doi-asserted-by":"crossref","first-page":"2508","DOI":"10.1016\/j.bmcl.2010.02.103","article-title":"Carbonic anhydrase inhibitors. The beta-carbonic anhydrases from the fungal pathogens Cryptococcus neoformans and Candida albicans are strongly inhibited by substituted-phenyl-1H-indole-5-sulfonamides","volume":"20","author":"Guzel","year":"2010","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"7","key":"10.1016\/bs.enz.2025.05.001_bib0010","doi-asserted-by":"crossref","first-page":"2654","DOI":"10.1016\/j.bmc.2009.02.058","article-title":"Carbonic anhydrase inhibitors. Inhibition of the beta-class enzymes from the fungal pathogens Candida albicans and Cryptococcus neoformans with aliphatic and aromatic carboxylates","volume":"17","author":"Innocenti","year":"2009","journal-title":"Bioorg. Med. Chem."},{"issue":"13","key":"10.1016\/bs.enz.2025.05.001_bib0011","doi-asserted-by":"crossref","first-page":"4503","DOI":"10.1016\/j.bmc.2009.05.002","article-title":"Carbonic anhydrase inhibitors. Inhibition and homology modeling studies of the fungal beta-carbonic anhydrase from Candida albicans with sulfonamides","volume":"17","author":"Innocenti","year":"2009","journal-title":"Bioorg. Med. Chem."},{"issue":"3","key":"10.1016\/bs.enz.2025.05.001_bib0012","doi-asserted-by":"crossref","first-page":"1034","DOI":"10.1016\/j.bmc.2009.12.058","article-title":"Carbonic anhydrase activators: activation of the beta-carbonic anhydrases from the pathogenic fungi Candida albicans and Cryptococcus neoformans with amines and amino acids","volume":"18","author":"Innocenti","year":"2010","journal-title":"Bioorg. Med. Chem."},{"issue":"18","key":"10.1016\/bs.enz.2025.05.001_bib0013","doi-asserted-by":"crossref","first-page":"5066","DOI":"10.1016\/j.bmcl.2008.07.122","article-title":"Carbonic anhydrase inhibitors: inhibition of the beta-class enzymes from the fungal pathogens Candida albicans and Cryptococcus neoformans with simple anions","volume":"18","author":"Innocenti","year":"2008","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"10","key":"10.1016\/bs.enz.2025.05.001_bib0014","doi-asserted-by":"crossref","first-page":"2642","DOI":"10.1016\/j.bmcl.2009.03.147","article-title":"Carbonic anhydrase inhibitors. Inhibition of the fungal beta-carbonic anhydrases from Candida albicans and Cryptococcus neoformans with boronic acids","volume":"19","author":"Innocenti","year":"2009","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"2","key":"10.1016\/bs.enz.2025.05.001_bib0015","doi-asserted-by":"crossref","first-page":"859","DOI":"10.1016\/j.bmcl.2011.12.033","article-title":"Dithiocarbamates are strong inhibitors of the beta-class fungal carbonic anhydrases from Cryptococcus neoformans, Candida albicans and Candida glabrata","volume":"22","author":"Monti","year":"2012","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2025.05.001_bib0016","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.bioorg.2019.01.030","article-title":"Benzenesulfonamides incorporating nitrogenous bases show effective inhibition of beta-carbonic anhydrases from the pathogenic fungi Cryptococcus neoformans, Candida glabrata and Malassezia globosa","volume":"86","author":"Bua","year":"2019","journal-title":"Bioorg. Chem."},{"issue":"4","key":"10.1016\/bs.enz.2025.05.001_bib0017","doi-asserted-by":"crossref","first-page":"1207","DOI":"10.1016\/j.jmb.2008.11.037","article-title":"Structure and inhibition of the CO2-sensing carbonic anhydrase Can2 from the pathogenic fungus Cryptococcus neoformans","volume":"385","author":"Schlicker","year":"2009","journal-title":"J. Mol. Biol."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.001_bib0018","doi-asserted-by":"crossref","first-page":"644","DOI":"10.1080\/14756366.2019.1571273","article-title":"Inhibition of alpha-, beta-, gamma-, delta-, zeta- and eta-class carbonic anhydrases from bacteria, fungi, algae, diatoms and protozoans with famotidine","volume":"34","author":"Angeli","year":"2019","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"21","key":"10.1016\/bs.enz.2025.05.001_bib0019","doi-asserted-by":"crossref","first-page":"6794","DOI":"10.1016\/j.bmc.2015.10.006","article-title":"Poly(amidoamine) dendrimers show carbonic anhydrase inhibitory activity against alpha-, beta-, gamma- and eta-class enzymes","volume":"23","author":"Carta","year":"2015","journal-title":"Bioorg. Med. Chem."},{"issue":"39","key":"10.1016\/bs.enz.2025.05.001_bib0020","doi-asserted-by":"crossref","first-page":"5266","DOI":"10.2174\/0929867325666180326160121","article-title":"Are carbonic anhydrases suitable targets to fight protozoan parasitic diseases?","volume":"25","author":"D'Ambrosio","year":"2018","journal-title":"Curr. Med. Chem."},{"issue":"14","key":"10.1016\/bs.enz.2025.05.001_bib0021","doi-asserted-by":"crossref","first-page":"5773","DOI":"10.1021\/jm400418p","article-title":"A class of sulfonamides with strong inhibitory action against the alpha-carbonic anhydrase from Trypanosoma cruzi","volume":"56","author":"Guzel-Akdemir","year":"2013","journal-title":"J. Med. Chem."},{"issue":"4","key":"10.1016\/bs.enz.2025.05.001_bib0022","doi-asserted-by":"crossref","first-page":"1761","DOI":"10.1021\/jm4000616","article-title":"Cloning, characterization, and sulfonamide and thiol inhibition studies of an alpha-carbonic anhydrase from Trypanosoma cruzi, the causative agent of Chagas disease","volume":"56","author":"Pan","year":"2013","journal-title":"J. Med. Chem."},{"issue":"15","key":"10.1016\/bs.enz.2025.05.001_bib0023","doi-asserted-by":"crossref","first-page":"4472","DOI":"10.1016\/j.bmc.2013.05.058","article-title":"Anion inhibition studies of the alpha-carbonic anhydrase from the protozoan pathogen Trypanosoma cruzi, the causative agent of Chagas disease","volume":"21","author":"Pan","year":"2013","journal-title":"Bioorg. Med. Chem."},{"issue":"2","key":"10.1016\/bs.enz.2025.05.001_bib0024","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."},{"issue":"4","key":"10.1016\/bs.enz.2025.05.001_bib0025","doi-asserted-by":"crossref","first-page":"2719","DOI":"10.1074\/jbc.M308984200","article-title":"Characterization of CA XIII, a novel member of the carbonic anhydrase isozyme family","volume":"279","author":"Lehtonen","year":"2004","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.001_bib0026","doi-asserted-by":"crossref","first-page":"1988","DOI":"10.1080\/14756366.2021.1972995","article-title":"An overview on the recently discovered iota-carbonic anhydrases","volume":"36","author":"Nocentini","year":"2021","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"7","key":"10.1016\/bs.enz.2025.05.001_bib0027","doi-asserted-by":"crossref","first-page":"603","DOI":"10.2174\/138161208783877884","article-title":"Carbonic anhydrases\u2013an overview","volume":"14","author":"Supuran","year":"2008","journal-title":"Curr. Pharm. Des."},{"key":"10.1016\/bs.enz.2025.05.001_bib0028","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1186\/1471-2091-11-28","article-title":"Characterization of the first beta-class carbonic anhydrase from an arthropod (Drosophila melanogaster) and phylogenetic analysis of beta-class carbonic anhydrases in invertebrates","volume":"11","author":"Syrjanen","year":"2010","journal-title":"BMC Biochem."},{"issue":"3","key":"10.1016\/bs.enz.2025.05.001_bib0029","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.2025.05.001_bib0030","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/bs.enz.2024.05.003","article-title":"Bacterial iota-CAs","volume":"55","author":"Capasso","year":"2024","journal-title":"Enzymes"},{"key":"10.1016\/bs.enz.2025.05.001_bib0031","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":"5","key":"10.1016\/bs.enz.2025.05.001_bib0032","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1080\/13543776.2024.2365407","article-title":"Biomedical applications of prokaryotic carbonic anhydrases: an update","volume":"34","author":"Capasso","year":"2024","journal-title":"Expert Opin. Ther. Pat."},{"issue":"2","key":"10.1016\/bs.enz.2025.05.001_bib0033","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1007\/s00294-009-0238-x","article-title":"Evolution of carbonic anhydrases in fungi","volume":"55","author":"Elleuche","year":"2009","journal-title":"Curr. Genet."},{"issue":"Pt 1","key":"10.1016\/bs.enz.2025.05.001_bib0034","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1099\/mic.0.032581-0","article-title":"Carbonic anhydrases in fungi","volume":"156","author":"Elleuche","year":"2010","journal-title":"Microbiology (Reading)"},{"issue":"11","key":"10.1016\/bs.enz.2025.05.001_bib0035","doi-asserted-by":"crossref","first-page":"1194","DOI":"10.1021\/acsmedchemlett.7b00369","article-title":"Benzoxaboroles as efficient inhibitors of the beta-carbonic anhydrases from pathogenic fungi: Activity and Modeling Study","volume":"8","author":"Nocentini","year":"2017","journal-title":"ACS Med. Chem. Lett."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.001_bib0036","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1186\/s12915-021-01039-8","article-title":"Characterization of a novel type of carbonic anhydrase that acts without metal cofactors","volume":"19","author":"Hirakawa","year":"2021","journal-title":"BMC Biol."},{"issue":"90","key":"10.1016\/bs.enz.2025.05.001_bib0037","first-page":"29","article-title":"Evolution and distribution of the carbonic anhydrase gene families","author":"Hewett-Emmett","year":"2000","journal-title":"EXS"},{"issue":"1","key":"10.1016\/bs.enz.2025.05.001_bib0038","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1006\/mpev.1996.0006","article-title":"Functional diversity, conservation, and convergence in the evolution of the alpha-, beta-, and gamma-carbonic anhydrase gene families","volume":"5","author":"Hewett-Emmett","year":"1996","journal-title":"Mol. Phylogenet. Evol."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.001_bib0039","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/j.jsb.2019.07.011","article-title":"The structural basis of the low catalytic activities of the two minor beta-carbonic anhydrases of the filamentous fungus Aspergillus fumigatus","volume":"208","author":"Kim","year":"2019","journal-title":"J. Struct. Biol."},{"issue":"2","key":"10.1016\/bs.enz.2025.05.001_bib0040","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1111\/j.1365-2958.2005.04560.x","article-title":"The gene NCE103 (YNL036w) from Saccharomyces cerevisiae encodes a functional carbonic anhydrase and its transcription is regulated by the concentration of inorganic carbon in the medium","volume":"56","author":"Amoroso","year":"2005","journal-title":"Mol. Microbiol."},{"issue":"10A","key":"10.1016\/bs.enz.2025.05.001_bib0041","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1002\/(SICI)1097-0061(199907)15:10A<855::AID-YEA425>3.0.CO;2-C","article-title":"Deletion of the carbonic anhydrase-like gene NCE103 of the yeast Saccharomyces cerevisiae causes an oxygen-sensitive growth defect","volume":"15","author":"Gotz","year":"1999","journal-title":"Yeast"},{"issue":"6","key":"10.1016\/bs.enz.2025.05.001_bib0042","doi-asserted-by":"crossref","first-page":"1662","DOI":"10.1016\/j.bmcl.2009.01.105","article-title":"Carbonic anhydrase activators: activation of the beta-carbonic anhydrase Nce103 from the yeast Saccharomyces cerevisiae with amines and amino acids","volume":"19","author":"Isik","year":"2009","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/bs.enz.2025.05.001_bib0043","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1186\/1472-6807-9-67","article-title":"Structural insights into the substrate tunnel of Saccharomyces cerevisiae carbonic anhydrase Nce103","volume":"9","author":"Teng","year":"2009","journal-title":"BMC Struct. Biol."},{"issue":"19","key":"10.1016\/bs.enz.2025.05.001_bib0044","doi-asserted-by":"crossref","first-page":"12045","DOI":"10.3390\/ijms231912045","article-title":"\u03b1-CAs from photosynthetic organisms","volume":"23","author":"Langella","year":"2022","journal-title":"Int. J. Mol. Sci."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.001_bib0045","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1080\/14756366.2019.1706089","article-title":"Inhibition survey with phenolic compounds against the delta- and eta-class carbonic anhydrases from the marine diatom thalassiosira weissflogii and protozoan Plasmodium falciparum","volume":"35","author":"Alissa","year":"2020","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"15","key":"10.1016\/bs.enz.2025.05.001_bib0046","doi-asserted-by":"crossref","first-page":"4181","DOI":"10.1016\/j.bmc.2015.06.050","article-title":"Inhibition studies of bacterial, fungal and protozoan beta-class carbonic anhydrases with Schiff bases incorporating sulfonamide moieties","volume":"23","author":"Ceruso","year":"2015","journal-title":"Bioorg. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.001_bib0047","doi-asserted-by":"crossref","first-page":"1164","DOI":"10.1080\/14756366.2019.1626375","article-title":"Appraisal of anti-protozoan activity of nitroaromatic benzenesulfonamides inhibiting carbonic anhydrases from Trypanosoma cruzi and Leishmania donovani","volume":"34","author":"Nocentini","year":"2019","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"5","key":"10.1016\/bs.enz.2025.05.001_bib0048","doi-asserted-by":"crossref","first-page":"1543","DOI":"10.1016\/j.bmc.2017.01.034","article-title":"Carbonic anhydrases from Trypanosoma and Leishmania as anti-protozoan drug targets","volume":"25","author":"Vermelho","year":"2017","journal-title":"Bioorg. Med. Chem."},{"issue":"5","key":"10.1016\/bs.enz.2025.05.001_bib0049","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":"18","key":"10.1016\/bs.enz.2025.05.001_bib0050","doi-asserted-by":"crossref","first-page":"7372","DOI":"10.1021\/jm400939k","article-title":"Cloning, characterization, and inhibition studies of a beta-carbonic anhydrase from Leishmania donovani chagasi, the protozoan parasite responsible for leishmaniasis","volume":"56","author":"Syrjanen","year":"2013","journal-title":"J. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.001_bib0051","doi-asserted-by":"crossref","first-page":"22","DOI":"10.3390\/metabo8010022","article-title":"An update on the metabolic roles of carbonic anhydrases in the model alga chlamydomonas reinhardtii","volume":"8","author":"Aspatwar","year":"2018","journal-title":"Metabolites"},{"key":"10.1016\/bs.enz.2025.05.001_bib0052","first-page":"257","article-title":"Carbonic anhydrases in fungi and fungal-like organisms - functional distribution and evolution of a gene family","volume":"14","author":"Elleuche","year":"2011","journal-title":"Mycota"},{"issue":"3","key":"10.1016\/bs.enz.2025.05.001_bib0053","doi-asserted-by":"crossref","first-page":"93","DOI":"10.3390\/metabo10030093","article-title":"Anion inhibition studies of the beta-class carbonic anhydrase CAS3 from the filamentous ascomycete sordaria macrospora","volume":"10","author":"Vullo","year":"2020","journal-title":"Metabolites"},{"issue":"5","key":"10.1016\/bs.enz.2025.05.001_bib0054","doi-asserted-by":"crossref","first-page":"1036","DOI":"10.3390\/molecules25051036","article-title":"Sulfonamide inhibition studies of the beta-class carbonic anhydrase CAS3 from the filamentous ascomycete sordaria macrospora","volume":"25","author":"Vullo","year":"2020","journal-title":"Molecules"},{"issue":"1","key":"10.1016\/bs.enz.2025.05.001_bib0055","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1128\/EC.5.1.103-111.2006","article-title":"senses CO through the carbonic anhydrase Can2 and the adenylyl cyclase Cac1","volume":"5","author":"Mogensen","year":"2006","journal-title":"Euk. Cell"},{"issue":"22","key":"10.1016\/bs.enz.2025.05.001_bib0056","doi-asserted-by":"crossref","first-page":"2013","DOI":"10.1016\/j.cub.2005.09.047","article-title":"Carbonic anhydrase and CO2 sensing during cryptococcus neoformans growth, differentiation, and virulence","volume":"15","author":"Bahn","year":"2005","journal-title":"Curr. Biol."},{"issue":"10","key":"10.1016\/bs.enz.2025.05.001_bib0057","doi-asserted-by":"crossref","first-page":"8146","DOI":"10.1074\/jbc.M111130200","article-title":"Acidocalcisomes are functionally linked to the contractile vacuole of dictyostelium discoideum","volume":"277","author":"Marchesini","year":"2002","journal-title":"J. Biol. Chem."},{"issue":"3","key":"10.1016\/bs.enz.2025.05.001_bib0058","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1016\/S0959-437X(05)80304-1","article-title":"cAMP signal transduction pathways regulating development of dictyostelium discoideum","volume":"1","author":"Kimmel","year":"1991","journal-title":"Curr. Opin. Genet. Dev."},{"year":"2019","author":"Aspatwar","series-title":"Carbonic anhydrases from pathogens: protozoan CAs and related inhibitors as potential antiprotozoal agents","key":"10.1016\/bs.enz.2025.05.001_bib0059"},{"issue":"1","key":"10.1016\/bs.enz.2025.05.001_bib0060","doi-asserted-by":"crossref","DOI":"10.1002\/ardp.202400626","article-title":"The carbonic anhydrase enzymes as new targets for the management of neglected tropical diseases","volume":"358","author":"Renzi","year":"2025","journal-title":"Arch. Pharm."},{"key":"10.1016\/bs.enz.2025.05.001_bib0061","doi-asserted-by":"crossref","DOI":"10.3389\/fcimb.2020.566726","article-title":"Uncovering the cyclic AMP signaling pathway of the protozoan parasite entamoeba histolytica and understanding its role in phagocytosis","volume":"10","author":"Agarwal","year":"2020","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"10.1016\/bs.enz.2025.05.001_bib0062","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/j.bioorg.2018.06.002","article-title":"The first activation studies of the eta-carbonic anhydrase from the malaria parasite plasmodium falciparum with amines and amino acids","volume":"80","author":"Angeli","year":"2018","journal-title":"Bioorg. Chem."},{"issue":"sup4","key":"10.1016\/bs.enz.2025.05.001_bib0063","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1080\/14756366.2016.1217856","article-title":"Cloning, expression and purification of the complete domain of the eta-carbonic anhydrase from plasmodium falciparum","volume":"31","author":"Del Prete","year":"2016","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"17","key":"10.1016\/bs.enz.2025.05.001_bib0064","doi-asserted-by":"crossref","first-page":"4184","DOI":"10.1016\/j.bmcl.2016.07.060","article-title":"Cloning, expression, purification and sulfonamide inhibition profile of the complete domain of the eta-carbonic anhydrase from Plasmodium falciparum","volume":"26","author":"Del Prete","year":"2016","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"7","key":"10.1016\/bs.enz.2025.05.001_bib0065","doi-asserted-by":"crossref","first-page":"1385","DOI":"10.1016\/j.bmcl.2015.02.046","article-title":"The zinc coordination pattern in the eta-carbonic anhydrase from Plasmodium falciparum is different from all other carbonic anhydrase genetic families","volume":"25","author":"De Simone","year":"2015","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"6","key":"10.1016\/bs.enz.2025.05.001_bib0066","doi-asserted-by":"crossref","first-page":"920","DOI":"10.3109\/14756366.2014.990963","article-title":"Protonography, a technique applicable for the analysis of eta-carbonic anhydrase activity","volume":"30","author":"Del Prete","year":"2015","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"18","key":"10.1016\/bs.enz.2025.05.001_bib0067","doi-asserted-by":"crossref","first-page":"4410","DOI":"10.1016\/j.bmc.2016.07.034","article-title":"Anion inhibition profiles of the complete domain of the eta-carbonic anhydrase from plasmodium falciparum","volume":"24","author":"Del Prete","year":"2016","journal-title":"Bioorg. Med. Chem."},{"issue":"18","key":"10.1016\/bs.enz.2025.05.001_bib0068","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\u2013the eta-carbonic anhydrases","volume":"24","author":"Del Prete","year":"2014","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"3","key":"10.1016\/bs.enz.2025.05.001_bib0069","doi-asserted-by":"crossref","first-page":"526","DOI":"10.1016\/j.bmc.2014.12.009","article-title":"Sulfonamide inhibition studies of the eta-class carbonic anhydrase from the malaria pathogen plasmodium falciparum","volume":"23","author":"Vullo","year":"2015","journal-title":"Bioorg. Med. Chem."}],"container-title":["The Enzymes","Fungal and Protozoan Carbonic Anhydrases"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874604725000034?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874604725000034?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,7]],"date-time":"2025-10-07T01:32:59Z","timestamp":1759800779000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1874604725000034"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025]]},"ISBN":["9780443313943"],"references-count":69,"URL":"https:\/\/doi.org\/10.1016\/bs.enz.2025.05.001","relation":{},"ISSN":["1874-6047"],"issn-type":[{"type":"print","value":"1874-6047"}],"subject":[],"published":{"date-parts":[[2025]]}}}