{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,8]],"date-time":"2025-10-08T00:06:43Z","timestamp":1759882003239,"version":"build-2065373602"},"reference-count":144,"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.2025.05.005","type":"book-chapter","created":{"date-parts":[[2025,7,30]],"date-time":"2025-07-30T11:16:41Z","timestamp":1753874201000},"page":"229-250","source":"Crossref","is-referenced-by-count":0,"title":["Challenges for developing selective fungal\/protozoal carbonic anhydrase inhibitors as anti-infectives"],"prefix":"10.1016","member":"78","reference":[{"issue":"Pt 1","key":"10.1016\/bs.enz.2025.05.005_bib0001","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":"20","key":"10.1016\/bs.enz.2025.05.005_bib0002","doi-asserted-by":"crossref","first-page":"8433","DOI":"10.1007\/s00253-014-5993-z","article-title":"A matter of structure: structural comparison of fungal carbonic anhydrases","volume":"98","author":"Lehneck","year":"2014","journal-title":"Appl. Microbiol. Biotechnol."},{"issue":"2","key":"10.1016\/bs.enz.2025.05.005_bib0003","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1038\/nrd2467","article-title":"Carbonic anhydrases: novel therapeutic applications for inhibitors and activators","volume":"7","author":"Supuran","year":"2008","journal-title":"Nat. Rev. Drug Discov."},{"issue":"9","key":"10.1016\/bs.enz.2025.05.005_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."},{"key":"10.1016\/bs.enz.2025.05.005_bib0005","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.2025.05.005_bib0006","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":"22","key":"10.1016\/bs.enz.2025.05.005_bib0007","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":"22","key":"10.1016\/bs.enz.2025.05.005_bib0008","doi-asserted-by":"crossref","first-page":"2021","DOI":"10.1016\/j.cub.2005.10.040","article-title":"Fungal adenylyl cyclase integrates CO2 sensing with cAMP signaling and virulence","volume":"15","author":"Klengel","year":"2005","journal-title":"Curr. Biol."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.005_bib0009","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1128\/EC.5.1.103-111.2006","article-title":"Cryptococcus neoformans senses CO2 through the carbonic anhydrase Can2 and the adenylyl cyclase Cac1","volume":"5","author":"Mogensen","year":"2006","journal-title":"Euk. Cell"},{"issue":"6","key":"10.1016\/bs.enz.2025.05.005_bib0010","doi-asserted-by":"crossref","first-page":"572","DOI":"10.1016\/j.mib.2006.09.003","article-title":"CO2 sensing in fungi and beyond","volume":"9","author":"Bahn","year":"2006","journal-title":"Curr. Opin. Microbiol."},{"issue":"6","key":"10.1016\/bs.enz.2025.05.005_bib0011","doi-asserted-by":"crossref","first-page":"1549","DOI":"10.1016\/j.bmc.2012.05.053","article-title":"Carbonic anhydrase regulation and CO(2) sensing in the fungal pathogen Candida glabrata involves a novel Rca1p ortholog","volume":"21","author":"Cottier","year":"2013","journal-title":"Bioorg. Med. Chem."},{"issue":"4","key":"10.1016\/bs.enz.2025.05.005_bib0012","doi-asserted-by":"crossref","first-page":"1207","DOI":"10.1534\/genetics.110.118315","article-title":"Comparative transcriptome analysis of the CO2 sensing pathway via differential expression of carbonic anhydrase in Cryptococcus neoformans","volume":"185","author":"Kim","year":"2010","journal-title":"Genetics"},{"issue":"Suppl 2","key":"10.1016\/bs.enz.2025.05.005_bib0013","first-page":"32","article-title":"Molecular biology and biochemistry of malarial parasite pyrimidine biosynthetic pathway","volume":"34","author":"Krungkrai","year":"2003","journal-title":"Southeast Asian J. Trop. Med. Public Health"},{"issue":"9","key":"10.1016\/bs.enz.2025.05.005_bib0014","doi-asserted-by":"crossref","first-page":"909","DOI":"10.2174\/156802607780636744","article-title":"Malarial parasite carbonic anhydrase and its inhibitors","volume":"7","author":"Krungkrai","year":"2007","journal-title":"Curr. Top. Med. Chem."},{"issue":"7","key":"10.1016\/bs.enz.2025.05.005_bib0015","doi-asserted-by":"crossref","first-page":"631","DOI":"10.2174\/138161208783877901","article-title":"The alpha-carbonic anhydrase from the malaria parasite and its inhibition","volume":"14","author":"Krungkrai","year":"2008","journal-title":"Curr. Pharm. Des."},{"first-page":"1","year":"2022","series-title":"Antiprotozoal drug development and delivery","key":"10.1016\/bs.enz.2025.05.005_bib0016"},{"issue":"4","key":"10.1016\/bs.enz.2025.05.005_bib0017","doi-asserted-by":"crossref","DOI":"10.1111\/myc.70051","article-title":"Antifungal resistance in non-fumigatus aspergillus species","volume":"68","author":"Djenontin","year":"2025","journal-title":"Mycoses"},{"issue":"Supplement_1","key":"10.1016\/bs.enz.2025.05.005_bib0018","doi-asserted-by":"crossref","first-page":"i2","DOI":"10.1093\/jac\/dkaf004","article-title":"Clinical aspects and recent advances in fungal diseases impacting human health","volume":"80","author":"Pagano","year":"2025","journal-title":"J. Antimicrob. Chemother."},{"issue":"2","key":"10.1016\/bs.enz.2025.05.005_bib0019","doi-asserted-by":"crossref","first-page":"272","DOI":"10.3390\/microorganisms13020272","article-title":"Insights into virulence factors, complement evasion and antifungal drug resistance","volume":"13","author":"Gaffar","year":"2025","journal-title":"Microorganisms"},{"key":"10.1016\/bs.enz.2025.05.005_bib0020","article-title":"The evolution of antifungal therapy: Traditional agents, current challenges and future perspectives","volume":"8","author":"Souza","year":"2025","journal-title":"Curr. Res. Microb. Sci."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.005_bib0021","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1186\/s12941-025-00795-7","article-title":"Prevalence of antimalaria drug resistance-conferring mutations associated with sulphadoxine-pyrimethamineine-resistant Plasmodium falciparum in East Africa: a systematic review and meta-analysis","volume":"24","author":"Abebe","year":"2025","journal-title":"Ann Clin Microbiol Antimicrob"},{"issue":"11","key":"10.1016\/bs.enz.2025.05.005_bib0022","article-title":"Evolutionary biology of antimalarial drug resistance: Understanding of the evolutionary dynamics","volume":"104","author":"Igwe","year":"2025","journal-title":"Medicine (Baltimore)."},{"key":"10.1016\/bs.enz.2025.05.005_bib0023","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijpddr.2025.100586","article-title":"Recent in vitro advances in the ocular antimicrobial agents against Acanthamoeba","volume":"27","author":"Chen","year":"2025","journal-title":"Int J Parasitol Drugs Drug Resist"},{"key":"10.1016\/bs.enz.2025.05.005_bib0024","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1051\/parasite\/2025009","article-title":"Leishmaniases: strategies in treatment development","volume":"32","author":"Majoor","year":"2025","journal-title":"Parasite"},{"issue":"4","key":"10.1016\/bs.enz.2025.05.005_bib0025","doi-asserted-by":"crossref","DOI":"10.1128\/cmr.00109-24","article-title":"Artemisinin-resistant malaria","volume":"37","author":"White","year":"2024","journal-title":"Clin. Microbiol. Rev."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.005_bib0026","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1021\/acs.jmedchem.3c01020","article-title":"Novel drug screening assay for acanthamoeba castellanii and the anti-amoebic effect of carbonic anhydrase inhibitors","volume":"67","author":"Haapanen","year":"2024","journal-title":"J. Med. Chem."},{"issue":"3","key":"10.1016\/bs.enz.2025.05.005_bib0027","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1080\/13543776.2023.2201432","article-title":"Antiprotozoal drugs: challenges and opportunities","volume":"33","author":"Supuran","year":"2023","journal-title":"Expert Opin. Ther. Pat."},{"issue":"18","key":"10.1016\/bs.enz.2025.05.005_bib0028","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 \u03b7-carbonic anhydrases","volume":"24","author":"Del Prete","year":"2014","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"12","key":"10.1016\/bs.enz.2025.05.005_bib0029","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":"3","key":"10.1016\/bs.enz.2025.05.005_bib0030","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1080\/13543776.2023.2205586","article-title":"The management of Babesia, amoeba and other zoonotic diseases provoked by protozoa","volume":"33","author":"Capasso","year":"2023","journal-title":"Expert Opin. Ther. Pat."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.005_bib0031","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":"1","key":"10.1016\/bs.enz.2025.05.005_bib0032","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'Ambrosio","year":"2025","journal-title":"Chem. Rev."},{"issue":"10","key":"10.1016\/bs.enz.2025.05.005_bib0033","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.)"},{"issue":"4","key":"10.1016\/bs.enz.2025.05.005_bib0034","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.2025.05.005_bib0035","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1186\/s12900-018-0093-4","article-title":"Crystal structure of carbonic anhydrase CaNce103p from the pathogenic yeast Candida albicans","volume":"18","author":"Dost\u00e1l","year":"2018","journal-title":"BMC Struct. Biol."},{"key":"10.1016\/bs.enz.2025.05.005_bib0036","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":"7","key":"10.1016\/bs.enz.2025.05.005_bib0037","doi-asserted-by":"crossref","first-page":"1759","DOI":"10.1111\/febs.12738","article-title":"Crystal structures of two tetrameric \u03b2-carbonic anhydrases from the filamentous ascomycete Sordaria macrospora","volume":"281","author":"Lehneck","year":"2014","journal-title":"FEBS J."},{"issue":"9","key":"10.1016\/bs.enz.2025.05.005_bib0038","first-page":"831","article-title":"Crystal Structure of \u03b2-Carbonic Anhydrase CafA from the fungal pathogen Aspergillus fumigatus","volume":"43","author":"Kim","year":"2020","journal-title":"Mol. Cells"},{"issue":"7","key":"10.1016\/bs.enz.2025.05.005_bib0039","doi-asserted-by":"crossref","first-page":"1042","DOI":"10.1016\/j.febslet.2011.03.001","article-title":"Structure of a dimeric fungal \u03b1-type carbonic anhydrase","volume":"585","author":"Cuesta-Seijo","year":"2011","journal-title":"FEBS Lett."},{"issue":"18","key":"10.1016\/bs.enz.2025.05.005_bib0040","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":"6","key":"10.1016\/bs.enz.2025.05.005_bib0041","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."},{"issue":"3","key":"10.1016\/bs.enz.2025.05.005_bib0042","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":"16","key":"10.1016\/bs.enz.2025.05.005_bib0043","doi-asserted-by":"crossref","first-page":"4802","DOI":"10.1016\/j.bmcl.2009.06.048","article-title":"Carbonic anhydrase inhibitors. Inhibition of the beta-class enzyme from the pathogenic yeast Candida glabrata with anions","volume":"19","author":"Innocenti","year":"2009","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"5","key":"10.1016\/bs.enz.2025.05.005_bib0044","doi-asserted-by":"crossref","first-page":"1701","DOI":"10.1016\/j.bmcl.2010.01.054","article-title":"Carbonic anhydrase activators: Activation of the beta-carbonic anhydrase from the pathogenic yeast Candida glabrata with amines and amino acids","volume":"20","author":"Innocenti","year":"2010","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"24","key":"10.1016\/bs.enz.2025.05.005_bib0045","doi-asserted-by":"crossref","first-page":"6327","DOI":"10.1016\/j.bmcl.2008.10.100","article-title":"Carbonic anhydrase inhibitors. Inhibition of the beta-class enzyme from the yeast Saccharomyces cerevisiae with anions","volume":"18","author":"Isik","year":"2008","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"7","key":"10.1016\/bs.enz.2025.05.005_bib0046","doi-asserted-by":"crossref","first-page":"3513","DOI":"10.1021\/jm300203r","article-title":"Molecular cloning, characterization, and inhibition studies of a \u03b2-carbonic anhydrase from Malassezia globosa, a potential antidandruff target","volume":"55","author":"Hewitson","year":"2012","journal-title":"J. Med. Chem."},{"issue":"6","key":"10.1016\/bs.enz.2025.05.005_bib0047","doi-asserted-by":"crossref","first-page":"1156","DOI":"10.3109\/14756366.2015.1102137","article-title":"A new procedure for the cloning, expression and purification of the \u03b2-carbonic anhydrase from the pathogenic yeast Malassezia globosa, an anti-dandruff drug target","volume":"31","author":"Del Prete","year":"2016","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"10","key":"10.1016\/bs.enz.2025.05.005_bib0048","doi-asserted-by":"crossref","first-page":"2447","DOI":"10.3390\/ijms20102447","article-title":"Cloning, purification, and characterization of a \u03b2-carbonic anhydrase from Malassezia restricta, an opportunistic pathogen involved in dandruff and seborrheic dermatitis","volume":"20","author":"Del Prete","year":"2019","journal-title":"Int. J. Mol. Sci."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.005_bib0049","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1080\/14756366.2021.1994559","article-title":"Heterologous expression and biochemical characterisation of the recombinant \u03b2-carbonic anhydrase (MpaCA) from the warm-blooded vertebrate pathogen Malassezia pachydermatis","volume":"37","author":"De Luca","year":"2022","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"3","key":"10.1016\/bs.enz.2025.05.005_bib0050","doi-asserted-by":"crossref","first-page":"93","DOI":"10.3390\/metabo10030093","article-title":"Anion inhibition studies of the \u03b2-class carbonic anhydrase CAS3 from the filamentous Ascomycete Sordaria macrospora","volume":"10","author":"Vullo","year":"2020","journal-title":"Metabolites"},{"issue":"13","key":"10.1016\/bs.enz.2025.05.005_bib0051","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":"8","key":"10.1016\/bs.enz.2025.05.005_bib0052","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":"G\u00fczel","year":"2010","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"10","key":"10.1016\/bs.enz.2025.05.005_bib0053","doi-asserted-by":"crossref","first-page":"3105","DOI":"10.1016\/j.bmc.2011.04.005","article-title":"Sulfonamides incorporating 1,3,5-triazine moieties selectively and potently inhibit carbonic anhydrase transmembrane isoforms IX, XII and XIV over cytosolic isoforms I and II: Solution and X-ray crystallographic studies","volume":"19","author":"Carta","year":"2011","journal-title":"Bioorg. Med. Chem."},{"issue":"15","key":"10.1016\/bs.enz.2025.05.005_bib0054","doi-asserted-by":"crossref","first-page":"4181","DOI":"10.1016\/j.bmc.2015.06.050","article-title":"Inhibition studies of bacterial, fungal and protozoan \u03b2-class carbonic anhydrases with Schiff bases incorporating sulfonamide moieties","volume":"23","author":"Ceruso","year":"2015","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/bs.enz.2025.05.005_bib0055","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 \u03b2-carbonic anhydrases from the pathogenic fungi Cryptococcus neoformans, Candida glabrata and Malassezia globosa","volume":"86","author":"Bua","year":"2019","journal-title":"Bioorg. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.005_bib0056","doi-asserted-by":"crossref","first-page":"644","DOI":"10.1080\/14756366.2019.1571273","article-title":"Inhibition of \u03b1-, \u03b2-, \u03b3-, \u03b4-, \u03b6- and \u03b7-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":"7","key":"10.1016\/bs.enz.2025.05.005_bib0057","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":"8","key":"10.1016\/bs.enz.2025.05.005_bib0058","doi-asserted-by":"crossref","first-page":"2521","DOI":"10.1016\/j.bmcl.2011.02.057","article-title":"Carbonic anhydrase inhibitors. Inhibition of the \u03b2-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":"10","key":"10.1016\/bs.enz.2025.05.005_bib0059","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":"18","key":"10.1016\/bs.enz.2025.05.005_bib0060","doi-asserted-by":"crossref","first-page":"4406","DOI":"10.1016\/j.bmc.2016.07.035","article-title":"Bortezomib inhibits bacterial and fungal \u03b2-carbonic anhydrases","volume":"24","author":"Supuran","year":"2016","journal-title":"Bioorg. Med. Chem."},{"issue":"11","key":"10.1016\/bs.enz.2025.05.005_bib0061","doi-asserted-by":"crossref","first-page":"1194","DOI":"10.1021\/acsmedchemlett.7b00369","article-title":"Benzoxaboroles as efficient inhibitors of the \u03b2-carbonic anhydrases from pathogenic fungi: Activity and Modeling Study","volume":"8","author":"Nocentini","year":"2017","journal-title":"ACS Med. Chem. Lett."},{"issue":"2","key":"10.1016\/bs.enz.2025.05.005_bib0062","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."},{"issue":"6","key":"10.1016\/bs.enz.2025.05.005_bib0063","doi-asserted-by":"crossref","first-page":"1682","DOI":"10.1021\/jm1013242","article-title":"Natural product-based phenols as novel probes for mycobacterial and fungal carbonic anhydrases","volume":"54","author":"Davis","year":"2011","journal-title":"J. Med. Chem."},{"issue":"22","key":"10.1016\/bs.enz.2025.05.005_bib0064","doi-asserted-by":"crossref","DOI":"10.3390\/ijms232214115","article-title":"Benzenesulfonamides incorporating hydantoin moieties effectively inhibit eukaryotic and human carbonic anhydrases","volume":"23","author":"Abdoli","year":"2022","journal-title":"Int. J. Mol. Sci."},{"issue":"9","key":"10.1016\/bs.enz.2025.05.005_bib0065","doi-asserted-by":"crossref","first-page":"2647","DOI":"10.1016\/j.bmcl.2013.02.092","article-title":"Carbonic anhydrase inhibitors: inhibition of the \u03b2-class enzyme from the pathogenic yeast Candida glabrata with sulfonamides, sulfamates and sulfamides","volume":"23","author":"Vullo","year":"2013","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"sup2","key":"10.1016\/bs.enz.2025.05.005_bib0066","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1080\/14756366.2016.1187143","article-title":"A substituted sulfonamide and its Co (II), Cu (II), and Zn (II) complexes as potential antifungal agents","volume":"31","author":"Diaz","year":"2016","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"21","key":"10.1016\/bs.enz.2025.05.005_bib0067","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 \u03b1-, \u03b2-, \u03b3- and \u03b7-class enzymes","volume":"23","author":"Carta","year":"2015","journal-title":"Bioorg. Med. Chem."},{"issue":"3","key":"10.1016\/bs.enz.2025.05.005_bib0068","doi-asserted-by":"crossref","first-page":"1158","DOI":"10.1016\/j.bmc.2008.12.035","article-title":"Carbonic anhydrase inhibitors: inhibition of the beta-class enzyme from the yeast Saccharomyces cerevisiae with sulfonamides and sulfamates","volume":"17","author":"Isik","year":"2009","journal-title":"Bioorg. Med. Chem."},{"issue":"12","key":"10.1016\/bs.enz.2025.05.005_bib0069","doi-asserted-by":"crossref","first-page":"3570","DOI":"10.1016\/j.bmcl.2013.04.028","article-title":"Carbonic anhydrase inhibitors. Benzenesulfonamides incorporating cyanoacrylamide moieties strongly inhibit Saccharomyces cerevisiae \u03b2-carbonic anhydrase","volume":"23","author":"Alafeefy","year":"2013","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"29","key":"10.1016\/bs.enz.2025.05.005_bib0070","doi-asserted-by":"crossref","first-page":"3327","DOI":"10.2174\/138161210793429878","article-title":"Saccharomyces cerevisiae \u03b2-carbonic anhydrase: inhibition and activation studies","volume":"16","author":"Isik","year":"2010","journal-title":"Curr. Pharm. Des."},{"issue":"4","key":"10.1016\/bs.enz.2025.05.005_bib0071","doi-asserted-by":"crossref","first-page":"495","DOI":"10.3109\/14756366.2013.806497","article-title":"Carbonic anhydrase inhibitors. Phenols incorporating 2- or 3-pyridyl-ethenylcarbonyl and tertiary amine moieties strongly inhibit Saccharomyces cerevisiae \u03b2-carbonic anhydrase","volume":"29","author":"Bilginer","year":"2014","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.005_bib0072","doi-asserted-by":"crossref","first-page":"132","DOI":"10.3109\/14756366.2015.1010529","article-title":"Dithiocarbamates with potent inhibitory activity against the Saccharomyces cerevisiae \u03b2-carbonic anhydrase","volume":"31","author":"Bozdag","year":"2016","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"22","key":"10.1016\/bs.enz.2025.05.005_bib0073","doi-asserted-by":"crossref","first-page":"5194","DOI":"10.1016\/j.bmcl.2015.09.068","article-title":"Anion inhibition studies of the dandruff-producing fungus Malassezia globosa \u03b2-carbonic anhydrase MgCA","volume":"25","author":"Del Prete","year":"2015","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"16","key":"10.1016\/bs.enz.2025.05.005_bib0074","doi-asserted-by":"crossref","first-page":"3612","DOI":"10.1016\/j.bmc.2016.05.072","article-title":"N-Nitrosulfonamides: A new chemotype for carbonic anhydrase inhibition","volume":"24","author":"Nocentini","year":"2016","journal-title":"Bioorg. Med. Chem."},{"issue":"3","key":"10.1016\/bs.enz.2025.05.005_bib0075","doi-asserted-by":"crossref","first-page":"1260","DOI":"10.1016\/j.bmc.2016.12.040","article-title":"Dithiocarbamates effectively inhibit the \u03b2-carbonic anhydrase from the dandruff-producing fungus Malassezia globosa","volume":"25","author":"Vullo","year":"2017","journal-title":"Bioorg. Med. Chem."},{"issue":"9","key":"10.1016\/bs.enz.2025.05.005_bib0076","doi-asserted-by":"crossref","first-page":"2577","DOI":"10.1016\/j.bmc.2017.03.026","article-title":"Inhibition of Malassezia globosa carbonic anhydrase with phenols","volume":"25","author":"Entezari Heravi","year":"2017","journal-title":"Bioorg. Med. Chem."},{"issue":"6","key":"10.1016\/bs.enz.2025.05.005_bib0077","doi-asserted-by":"crossref","first-page":"1558","DOI":"10.1080\/14786419.2021.1880406","article-title":"Phenols from Origanum dictamnus L. and Thymus vulgaris L. and their activity against Malassezia globosa carbonic anhydrase","volume":"36","author":"Paloukopoulou","year":"2022","journal-title":"Nat. Prod. Res."},{"issue":"7","key":"10.1016\/bs.enz.2025.05.005_bib0078","doi-asserted-by":"crossref","first-page":"147","DOI":"10.3390\/metabo9070147","article-title":"Anion inhibition profile of the \u03b2-carbonic anhydrase from the opportunist pathogenic fungus Malassezia restricta involved in dandruff and seborrheic dermatitis","volume":"9","author":"Prete","year":"2019","journal-title":"Metabolites"},{"issue":"1","key":"10.1016\/bs.enz.2025.05.005_bib0079","doi-asserted-by":"crossref","first-page":"39","DOI":"10.3390\/metabo10010039","article-title":"Sulfonamide inhibition profile of the \u03b2-carbonic anhydrase from Malassezia restricta, an opportunistic pathogen triggering scalp conditions","volume":"10","author":"Del Prete","year":"2020","journal-title":"Metabolites"},{"issue":"22","key":"10.1016\/bs.enz.2025.05.005_bib0080","doi-asserted-by":"crossref","DOI":"10.3390\/ijms222212601","article-title":"Inhibitory effects of sulfonamide derivatives on the \u03b2-carbonic anhydrase (MpaCA) from Malassezia pachydermatis, a commensal, pathogenic fungus present in domestic animals","volume":"22","author":"De Luca","year":"2021","journal-title":"Int. J. Mol. Sci."},{"issue":"9","key":"10.1016\/bs.enz.2025.05.005_bib0081","doi-asserted-by":"crossref","first-page":"1905","DOI":"10.1021\/acsinfecdis.2c00250","article-title":"Seleno containing compounds as potent and selective antifungal agents","volume":"8","author":"Angeli","year":"2022","journal-title":"ACS Infect Dis."},{"issue":"3","key":"10.1016\/bs.enz.2025.05.005_bib0082","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1111\/vde.13336","article-title":"Comparative efficacy of selenoureido carbonic anhydrase inhibitors and azole antifungal drugs against clinical isolates of Malassezia pachydermatis","volume":"36","author":"Spadini","year":"2025","journal-title":"Vet. Dermatol."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.005_bib0083","doi-asserted-by":"crossref","first-page":"390","DOI":"10.1080\/14756366.2018.1425687","article-title":"Sulfonamide inhibition studies of two \u03b2-carbonic anhydrases from the ascomycete fungus Sordaria macrospora, CAS1 and CAS2","volume":"33","author":"Vullo","year":"2018","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"5","key":"10.1016\/bs.enz.2025.05.005_bib0084","doi-asserted-by":"crossref","first-page":"1036","DOI":"10.3390\/molecules25051036","article-title":"Sulfonamide inhibition studies of the \u03b2-class carbonic anhydrase CAS3 from the Filamentous Ascomycete Sordaria macrospora","volume":"25","author":"Vullo","year":"2020","journal-title":"Molecules"},{"key":"10.1016\/bs.enz.2025.05.005_bib0085","unstructured":"F. Carta, A. Angeli, S. Selleri, C.T. Supuran, C.S. Cabassi, C. Spadini Carbamoselenoyl derivative sas anti-infective agents. WO Patent 2023\/073634."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.005_bib0086","doi-asserted-by":"crossref","first-page":"1292","DOI":"10.1080\/14756366.2020.1774572","article-title":"Biochemical and structural characterisation of a protozoan beta-carbonic anhydrase from Trichomonas vaginalis","volume":"35","author":"Urba\u0144ski","year":"2020","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"4","key":"10.1016\/bs.enz.2025.05.005_bib0087","doi-asserted-by":"crossref","first-page":"1761","DOI":"10.1021\/jm4000616","article-title":"Cloning, characterization, and sulfonamide and thiol inhibition studies of an \u03b1-carbonic anhydrase from Trypanosoma cruzi, the causative agent of Chagas disease","volume":"56","author":"Pan","year":"2013","journal-title":"J. Med. Chem."},{"issue":"14","key":"10.1016\/bs.enz.2025.05.005_bib0088","doi-asserted-by":"crossref","first-page":"5773","DOI":"10.1021\/jm400418p","article-title":"A class of sulfonamides with strong inhibitory action against the \u03b1-carbonic anhydrase from Trypanosoma cruzi","volume":"56","author":"G\u00fczel-Akdemir","year":"2013","journal-title":"J. Med. Chem."},{"issue":"15","key":"10.1016\/bs.enz.2025.05.005_bib0089","doi-asserted-by":"crossref","first-page":"4472","DOI":"10.1016\/j.bmc.2013.05.058","article-title":"Anion inhibition studies of the \u03b1-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.2025.05.005_bib0090","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1021\/jm400902y","article-title":"Design, synthesis, and evaluation of hydroxamic acid derivatives as promising agents for the management of Chagas disease","volume":"57","author":"Rodrigues","year":"2014","journal-title":"J. Med. Chem."},{"issue":"6","key":"10.1016\/bs.enz.2025.05.005_bib0091","doi-asserted-by":"crossref","first-page":"964","DOI":"10.3109\/14756366.2015.1077330","article-title":"Hydroxamic acid derivatives: a promising scaffold for rational compound optimization in Chagas disease","volume":"31","author":"de Menezes Dda","year":"2016","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.005_bib0092","doi-asserted-by":"crossref","first-page":"286","DOI":"10.1080\/14756366.2017.1414808","article-title":"Carbonic anhydrases from Trypanosoma cruzi and Leishmania donovani chagasi are inhibited by benzoxaboroles","volume":"33","author":"Nocentini","year":"2018","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"4","key":"10.1016\/bs.enz.2025.05.005_bib0093","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1021\/acsmedchemlett.8b00430","article-title":"N-Nitrosulfonamides as carbonic anhydrase inhibitors: a promising chemotype for targeting chagas disease and leishmaniasis","volume":"10","author":"Bonardi","year":"2018","journal-title":"ACS Med. Chem. Lett."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.005_bib0094","doi-asserted-by":"crossref","first-page":"2417","DOI":"10.1080\/14756366.2022.2119965","article-title":"Inhibition studies of the protozoan \u03b1-carbonic anhydrase from Trypanosoma cruzi with phenols","volume":"37","author":"Bonardi","year":"2022","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.005_bib0095","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1080\/14756366.2017.1405264","article-title":"Nanoemulsions of sulfonamide carbonic anhydrase inhibitors strongly inhibit the growth of Trypanosoma cruzi","volume":"33","author":"Vermelho","year":"2018","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"3","key":"10.1016\/bs.enz.2025.05.005_bib0096","doi-asserted-by":"crossref","first-page":"311","DOI":"10.4155\/fmc.15.185","article-title":"Inhibition of carbonic anhydrase from Trypanosoma cruzi for the management of Chagas disease: an underexplored therapeutic opportunity","volume":"8","author":"Supuran","year":"2016","journal-title":"Future Med Chem"},{"issue":"2","key":"10.1016\/bs.enz.2025.05.005_bib0097","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1080\/17460441.2020.1681394","article-title":"Why hasn\u2019t there been more progress in new Chagas disease drug discovery?","volume":"15","author":"Vermelho","year":"2020","journal-title":"Expert Opin Drug Discov"},{"issue":"22","key":"10.1016\/bs.enz.2025.05.005_bib0098","doi-asserted-by":"crossref","first-page":"5483","DOI":"10.3390\/molecules25225483","article-title":"Chagas disease: perspectives on the past and present and challenges in drug discovery","volume":"25","author":"Mansoldo","year":"2020","journal-title":"Molecules"},{"issue":"18","key":"10.1016\/bs.enz.2025.05.005_bib0099","doi-asserted-by":"crossref","first-page":"7372","DOI":"10.1021\/jm400939k","article-title":"Cloning, characterization, and inhibition studies of a \u03b2-carbonic anhydrase from Leishmania donovani chagasi, the protozoan parasite responsible for leishmaniasis","volume":"56","author":"Syrj\u00e4nen","year":"2013","journal-title":"J. Med. Chem."},{"issue":"15","key":"10.1016\/bs.enz.2025.05.005_bib0100","doi-asserted-by":"crossref","first-page":"4181","DOI":"10.1016\/j.bmc.2015.06.050","article-title":"Inhibition studies of bacterial, fungal and protozoan \u03b2-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.2025.05.005_bib0101","doi-asserted-by":"crossref","first-page":"850","DOI":"10.1080\/14756366.2018.1463221","article-title":"Antileishmanial activity of sulphonamide nanoemulsions targeting the \u03b2-carbonic anhydrase from Leishmania species","volume":"33","author":"da Silva Cardoso","year":"2018","journal-title":"J. Enzyme Inhib. Med. Chem."},{"key":"10.1016\/bs.enz.2025.05.005_bib0102","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1016\/j.bioorg.2019.01.069","article-title":"Discovery of new organoselenium compounds as antileishmanial agents","volume":"86","author":"Al-Tamimi","year":"2019","journal-title":"Bioorg. Chem."},{"issue":"8","key":"10.1016\/bs.enz.2025.05.005_bib0103","doi-asserted-by":"crossref","first-page":"4306","DOI":"10.1021\/acs.jmedchem.0c00211","article-title":"Tellurides bearing sulfonamides as novel inhibitors of leishmanial carbonic anhydrase with potent antileishmanial activity","volume":"63","author":"Angeli","year":"2020","journal-title":"J. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.005_bib0104","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1080\/14756366.2019.1681987","article-title":"Phosphonamidates are the first phosphorus-based zinc binding motif to show inhibition of \u03b2-class carbonic anhydrases from bacteria, fungi, and protozoa","volume":"35","author":"Alissa","year":"2020","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.005_bib0105","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 (Weinheim)"},{"issue":"7","key":"10.1016\/bs.enz.2025.05.005_bib0106","doi-asserted-by":"crossref","first-page":"631","DOI":"10.2174\/138161208783877901","article-title":"The alpha-carbonic anhydrase from the malaria parasite and its inhibition","volume":"14","author":"Krungkrai","year":"2008","journal-title":"Curr. Pharm. Des."},{"issue":"18","key":"10.1016\/bs.enz.2025.05.005_bib0107","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 \u03b7-carbonic anhydrases","volume":"24","author":"Del Prete","year":"2014","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"3","key":"10.1016\/bs.enz.2025.05.005_bib0108","doi-asserted-by":"crossref","first-page":"526","DOI":"10.1016\/j.bmc.2014.12.009","article-title":"Sulfonamide inhibition studies of the \u03b7-class carbonic anhydrase from the malaria pathogen Plasmodium falciparum","volume":"23","author":"Vullo","year":"2015","journal-title":"Bioorg. Med. Chem."},{"issue":"18","key":"10.1016\/bs.enz.2025.05.005_bib0109","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 \u03b7-carbonic anhydrase from Plasmodium falciparum","volume":"24","author":"Del Prete","year":"2016","journal-title":"Bioorg. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.005_bib0110","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1080\/14756366.2019.1706089","article-title":"Inhibition survey with phenolic compounds against the \u03b4- and \u03b7-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":"1","key":"10.1016\/bs.enz.2025.05.005_bib0111","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1080\/14756366.2022.2036986","article-title":"Coumarins inhibit \u03b7-class carbonic anhydrase from Plasmodium falciparum","volume":"37","author":"Giovannuzzi","year":"2022","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"21","key":"10.1016\/bs.enz.2025.05.005_bib0112","doi-asserted-by":"crossref","DOI":"10.1002\/cmdc.202300267","article-title":"Antimalarial agents targeting plasmodium falciparum carbonic anhydrase: towards artesunate hybrid compounds with dual mechanism of action","volume":"18","author":"D'Agostino","year":"2023","journal-title":"ChemMedChem"},{"issue":"12","key":"10.1016\/bs.enz.2025.05.005_bib0113","doi-asserted-by":"crossref","first-page":"3112","DOI":"10.3390\/molecules23123112","article-title":"Cloning, characterization and anion inhibition studies of a \u03b2-carbonic anhydrase from the pathogenic protozoan entamoeba histolytica","volume":"23","author":"Haapanen","year":"2018","journal-title":"Molecules"},{"issue":"12","key":"10.1016\/bs.enz.2025.05.005_bib0114","doi-asserted-by":"crossref","first-page":"3946","DOI":"10.3390\/ijms19123946","article-title":"Sulfonamide inhibition studies of a new \u03b2-carbonic anhydrase from the pathogenic protozoan entamoeba histolytica","volume":"19","author":"Bua","year":"2018","journal-title":"Int. J. Mol. Sci."},{"issue":"2","key":"10.1016\/bs.enz.2025.05.005_bib0115","doi-asserted-by":"crossref","first-page":"26","DOI":"10.3390\/metabo9020026","article-title":"Activation studies of the \u03b2-carbonic anhydrase from the pathogenic protozoan entamoeba histolytica with amino acids and amines","volume":"9","author":"Bua","year":"2019","journal-title":"Metabolites."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.005_bib0116","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1007\/s00109-021-02148-1","article-title":"Biochemical and structural characterization of beta-carbonic anhydrase from the parasite Trichomonas vaginalis","volume":"100","author":"Urba\u0144ski","year":"2022","journal-title":"J Mol Med (Berl)"},{"key":"10.1016\/bs.enz.2025.05.005_bib0117","doi-asserted-by":"crossref","DOI":"10.1016\/j.jinorgbio.2020.111274","article-title":"Inhibition of the newly discovered \u03b2\u2011carbonic anhydrase from the protozoan pathogen Trichomonas vaginalis with inorganic anions and small molecules","volume":"213","author":"Urba\u0144ski","year":"2020","journal-title":"J. Inorg. Biochem."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.005_bib0118","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1080\/14756366.2020.1863958","article-title":"Inhibition of the \u03b2-carbonic anhydrase from the protozoan pathogen Trichomonas vaginalis with sulphonamides","volume":"36","author":"Urba\u0144ski","year":"2021","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.005_bib0119","doi-asserted-by":"crossref","first-page":"758","DOI":"10.1080\/14756366.2021.1897802","article-title":"Activation of the \u03b2-carbonic anhydrase from the protozoan pathogen Trichomonas vaginalis with amines and amino acids","volume":"36","author":"Angeli","year":"2021","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.005_bib0120","doi-asserted-by":"crossref","DOI":"10.1080\/14756366.2024.2346523","article-title":"Cloning, expression, and purification of an \u03b1-carbonic anhydrase from Toxoplasma gondii to unveil its kinetic parameters and anion inhibition profile","volume":"39","author":"De Luca","year":"2024","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.005_bib0121","doi-asserted-by":"crossref","first-page":"116","DOI":"10.3390\/ijms26010116","article-title":"Exploring the Inhibition of Toxoplasma gondii \u03b1-Carbonic Anhydrase by Sulfonamides: Insights into Potential Drug Targeting","volume":"26","author":"Giovannuzzi","year":"2024","journal-title":"Int. J. Mol. Sci."},{"issue":"4","key":"10.1016\/bs.enz.2025.05.005_bib0122","doi-asserted-by":"crossref","first-page":"1721","DOI":"10.1021\/jm300031j","article-title":"Dithiocarbamates strongly inhibit carbonic anhydrases and show antiglaucoma action in vivo","volume":"55","author":"Carta","year":"2012","journal-title":"J. Med. Chem."},{"issue":"13","key":"10.1016\/bs.enz.2025.05.005_bib0123","doi-asserted-by":"crossref","first-page":"1868","DOI":"10.1039\/c2cc16395k","article-title":"Dithiocarbamates: a new class of carbonic anhydrase inhibitors. Crystallographic and kinetic investigations","volume":"48","author":"Carta","year":"2012","journal-title":"Chem. Commun. (Camb.)"},{"issue":"2","key":"10.1016\/bs.enz.2025.05.005_bib0124","doi-asserted-by":"crossref","first-page":"407","DOI":"10.3109\/14756366.2011.641015","article-title":"Dithiocarbamates strongly inhibit the \u03b2-class carbonic anhydrases from Mycobacterium tuberculosis","volume":"28","author":"Maresca","year":"2013","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"2","key":"10.1016\/bs.enz.2025.05.005_bib0125","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1016\/j.bmc.2004.10.015","article-title":"Carbonic anhydrase inhibitors. Inhibition of Plasmodium falciparum carbonic anhydrase with aromatic sulfonamides: towards antimalarials with a novel mechanism of action?","volume":"13","author":"Krungkrai","year":"2005","journal-title":"Bioorg. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.005_bib0126","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/j.ijpddr.2017.01.003","article-title":"Investigating the antiplasmodial activity of primary sulfonamide compounds identified in open source malaria data","volume":"7","author":"Fisher","year":"2017","journal-title":"Int J Parasitol Drugs Drug Resist"},{"key":"10.1016\/bs.enz.2025.05.005_bib0127","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1016\/bs.enz.2024.05.006","article-title":"Challenges for developing bacterial CA inhibitors as novel antibiotics","volume":"55","author":"Supuran","year":"2024","journal-title":"Enzymes"},{"issue":"21","key":"10.1016\/bs.enz.2025.05.005_bib0128","doi-asserted-by":"crossref","first-page":"19077","DOI":"10.1021\/acs.jmedchem.4c01555","article-title":"Inhibition of pseudomonas aeruginosa carbonic anhydrases, exploring ciprofloxacin functionalization toward new antibacterial agents: an in-depth multidisciplinary study","volume":"67","author":"Marinacci","year":"2024","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2025.05.005_bib0129","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1016\/bs.enz.2024.05.012","article-title":"Mycobacterial \u03b2-carbonic anhydrases: molecular biology, role in the pathogenesis of tuberculosis and inhibition studies","volume":"55","author":"Parkkinen","year":"2024","journal-title":"Enzymes"},{"key":"10.1016\/bs.enz.2025.05.005_bib0130","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.2025.05.005_bib0131","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2025.117620","article-title":"Redesigning oxazolidinones as carbonic anhydrase inhibitors against vancomycin-resistant enterococci","volume":"291","author":"Ammara","year":"2025","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/bs.enz.2025.05.005_bib0132","series-title":"Antiprotozoal drug development and delivery","first-page":"321","article-title":"Challenges and promises for obtaining new antiprotozoal drugs: what\u2019s going wrong ?","author":"Vermelho","year":"2022"},{"issue":"3","key":"10.1016\/bs.enz.2025.05.005_bib0133","doi-asserted-by":"crossref","first-page":"2802","DOI":"10.3390\/ijms24032802","article-title":"Synthesis, biological and in silico studies of griseofulvin and Usnic acid sulfonamide derivatives as fungal, bacterial and human carbonic anhydrase inhibitors","volume":"24","author":"Angeli","year":"2023","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/bs.enz.2025.05.005_bib0134","doi-asserted-by":"crossref","DOI":"10.1128\/mbio.02475-23","article-title":"Signaling pathways governing the pathobiological features and antifungal drug resistance of Candida auris","author":"Cha","year":"2025","journal-title":"mBio"},{"key":"10.1016\/bs.enz.2025.05.005_bib0135","doi-asserted-by":"crossref","DOI":"10.1590\/0037-8682-0328-2024","article-title":"Fluconazole resistance and heteroresistance in Cryptococcus spp.: mechanisms and Implications","volume":"58","author":"Moreira","year":"2025","journal-title":"Rev. Soc. Bras. Med. Trop."},{"issue":"4","key":"10.1016\/bs.enz.2025.05.005_bib0136","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/j.riam.2024.11.001","article-title":"Antifungal pipeline: New tools for the treatment of mycoses","volume":"41","author":"Wolfgruber","year":"2024","journal-title":"Rev. Iberoam. Micol"},{"key":"10.1016\/bs.enz.2025.05.005_bib0137","article-title":"The evolution of antifungal therapy: Traditional agents, current challenges and future perspectives","volume":"8","author":"Souza","year":"2025","journal-title":"Curr. Res. Microb. Sci."},{"issue":"6734","key":"10.1016\/bs.enz.2025.05.005_bib0138","doi-asserted-by":"crossref","first-page":"eadq6241","DOI":"10.1126\/science.adq6241","article-title":"The essential genome of Plasmodium knowlesi reveals determinants of antimalarial susceptibility","volume":"387","author":"Elsworth","year":"2025","journal-title":"Science"},{"issue":"10","key":"10.1016\/bs.enz.2025.05.005_bib0139","doi-asserted-by":"crossref","first-page":"835","DOI":"10.3390\/pathogens13100835","article-title":"Molecular mechanisms of drug resistance in Leishmania spp","volume":"13","author":"Moncada-Diaz","year":"2024","journal-title":"Pathogens"},{"issue":"3","key":"10.1016\/bs.enz.2025.05.005_bib0140","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1007\/s11046-025-00944-8","article-title":"Keep the hospital clean: diagnostic performance of ten different molecular and culture-based methods to detect Candidozyma (Candida) auris","volume":"190","author":"Korsten","year":"2025","journal-title":"Mycopathologia"},{"issue":"4","key":"10.1016\/bs.enz.2025.05.005_bib0141","doi-asserted-by":"crossref","first-page":"myaf033","DOI":"10.1093\/mmy\/myaf033","article-title":"Clustered cases of Candida auris colonization: roles of the infection prevention and control department and the mycology laboratory in controlling transmission","volume":"63","author":"Cottrel","year":"2025","journal-title":"Med. Mycol."},{"key":"10.1016\/bs.enz.2025.05.005_bib0142","doi-asserted-by":"crossref","DOI":"10.1128\/mbio.02475-23","article-title":"Signaling pathways governing the pathobiological features and antifungal drug resistance of Candida auris","author":"Cha","year":"2025","journal-title":"mBio"},{"issue":"3","key":"10.1016\/bs.enz.2025.05.005_bib0143","doi-asserted-by":"crossref","first-page":"652","DOI":"10.3390\/microorganisms13030652","article-title":"A continuing threat","volume":"13","author":"Bhargava","year":"2025","journal-title":"Microorganisms."},{"issue":"7","key":"10.1016\/bs.enz.2025.05.005_bib0144","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1080\/13543776.2020.1760838","article-title":"A deadly spillover: SARS-CoV-2 outbreak","volume":"30","author":"Mori","year":"2020","journal-title":"Expert Opin. Ther. Pat."}],"container-title":["The Enzymes","Fungal and Protozoan Carbonic Anhydrases"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874604725000071?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874604725000071?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,7]],"date-time":"2025-10-07T01:33:30Z","timestamp":1759800810000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1874604725000071"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025]]},"ISBN":["9780443313943"],"references-count":144,"URL":"https:\/\/doi.org\/10.1016\/bs.enz.2025.05.005","relation":{},"ISSN":["1874-6047"],"issn-type":[{"type":"print","value":"1874-6047"}],"subject":[],"published":{"date-parts":[[2025]]}}}