{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,8]],"date-time":"2025-10-08T00:06:04Z","timestamp":1759881964473,"version":"build-2065373602"},"reference-count":115,"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.2025.05.003","type":"book-chapter","created":{"date-parts":[[2025,7,23]],"date-time":"2025-07-23T09:46:15Z","timestamp":1753263975000},"page":"129-182","source":"Crossref","is-referenced-by-count":0,"title":["Trypanosoma cruzi and Leishmania spp. CAs"],"prefix":"10.1016","member":"78","reference":[{"year":"2025","series-title":"Neglected tropical diseases","key":"10.1016\/bs.enz.2025.05.003_bib0001"},{"key":"10.1016\/bs.enz.2025.05.003_bib0002","series-title":"Handbook of medical and health sciences in developing countries","first-page":"1","article-title":"Neglected diseases in developing countries I","author":"Sapkota","year":"2023"},{"key":"10.1016\/bs.enz.2025.05.003_bib0003","article-title":"An insight into the success, challenges, and future perspectives of eliminating neglected tropical disease","volume":"24","author":"Hudu","year":"2024","journal-title":"Sci. Afr."},{"issue":"11","key":"10.1016\/bs.enz.2025.05.003_bib0004","doi-asserted-by":"crossref","first-page":"2058","DOI":"10.1021\/acsmedchemlett.0c00446","article-title":"Challenges and opportunities for drug discovery in developing countries: the example of cutaneous Leishmaniasis","volume":"11","author":"Surur","year":"2020","journal-title":"ACS Med. Chem. Lett."},{"issue":"6","key":"10.1016\/bs.enz.2025.05.003_bib0005","doi-asserted-by":"crossref","first-page":"e1391","DOI":"10.1093\/cid\/ciab350","article-title":"Supporting drug development for neglected tropical diseases using mathematical modeling","volume":"73","author":"Walker","year":"2021","journal-title":"Clin. Infect. Dis."},{"key":"10.1016\/bs.enz.2025.05.003_bib0006","first-page":"32","article-title":"Advances and challenges in molecular docking applied to neglected tropical diseases","author":"De Angelo","year":"2025","journal-title":"Curr. Med. Chem."},{"issue":"20","key":"10.1016\/bs.enz.2025.05.003_bib0007","doi-asserted-by":"crossref","first-page":"7719","DOI":"10.1021\/jm400362b","article-title":"Drug discovery for neglected diseases: molecular target-based and phenotypic approaches: miniperspectives series on phenotypic screening for antiinfective targets","volume":"56","author":"Gilbert","year":"2013","journal-title":"J. Med. Chem."},{"key":"10.1016\/bs.enz.2025.05.003_bib0008","doi-asserted-by":"crossref","DOI":"10.7189\/jogh.15.03002","article-title":"AI-powered drug discovery for neglected diseases: accelerating public health solutions in the developing world","volume":"15","author":"Nishan","year":"2025","journal-title":"J. Glob. Health"},{"issue":"1","key":"10.1016\/bs.enz.2025.05.003_bib0009","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1016\/j.drudis.2020.10.010","article-title":"Artificial intelligence in drug discovery and development","volume":"26","author":"Paul","year":"2021","journal-title":"Drug Discov. Today"},{"key":"10.1016\/bs.enz.2025.05.003_bib0010","doi-asserted-by":"crossref","DOI":"10.3389\/fcimb.2023.1199715","article-title":"Editorial: Chagas disease novel drug targets and treatments","volume":"13","author":"Duschak","year":"2023","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"10.1016\/bs.enz.2025.05.003_bib0011","doi-asserted-by":"crossref","DOI":"10.3389\/fchem.2021.614073","article-title":"Use of artificial intelligence and machine learning for discovery of drugs for neglected tropical diseases","volume":"9","author":"Winkler","year":"2021","journal-title":"Front. Chem"},{"issue":"11","key":"10.1016\/bs.enz.2025.05.003_bib0012","doi-asserted-by":"crossref","first-page":"1161","DOI":"10.1080\/17460441.2019.1652593","article-title":"Advances in preclinical approaches to Chagas disease drug discovery","volume":"14","author":"Villalta","year":"2019","journal-title":"Expert Opin. Drug Discov"},{"issue":"22","key":"10.1016\/bs.enz.2025.05.003_bib0013","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"},{"key":"10.1016\/bs.enz.2025.05.003_bib0014","series-title":"Recent advances in parasitomics","first-page":"65","article-title":"CRISPR-cas in parasites: advances and challenges in the study of neglected tropical diseases","author":"Mej\u00eda-Jaramillo","year":"2025"},{"key":"10.1016\/bs.enz.2025.05.003_bib0015","doi-asserted-by":"crossref","DOI":"10.1016\/j.actatropica.2025.107598","article-title":"Basic research on chagas disease: Fifty years of a successful initiative","volume":"265","author":"Goldenberg","year":"2025","journal-title":"Acta Trop."},{"issue":"2","key":"10.1016\/bs.enz.2025.05.003_bib0016","doi-asserted-by":"crossref","first-page":"e00024","DOI":"10.1128\/msystems.00038-24","article-title":"System-based insights into parasitological and clinical treatment failure in Chagas disease","volume":"10","author":"Ernst","year":"2025","journal-title":"mSystems"},{"issue":"6","key":"10.1016\/bs.enz.2025.05.003_bib0017","doi-asserted-by":"crossref","first-page":"1107","DOI":"10.1021\/acsinfecdis.2c00123","article-title":"An updated view of the Trypanosoma cruzi life cycle: intervention points for an effective treatment","volume":"8","author":"Mart\u00edn-Escolano","year":"2022","journal-title":"ACS Infect. Dis."},{"issue":"2","key":"10.1016\/bs.enz.2025.05.003_bib0018","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.pt.2011.10.005","article-title":"Dormancy in mammalian malaria","volume":"28","author":"Markus","year":"2012","journal-title":"Trends Parasitol."},{"issue":"3","key":"10.1016\/bs.enz.2025.05.003_bib0019","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1111\/j.1574-6976.2011.00305.x","article-title":"Mechanisms of Toxoplasma gondii persistence and latency","volume":"36","author":"Sullivan","year":"2012","journal-title":"FEMS Microbiol. Rev."},{"issue":"5","key":"10.1016\/bs.enz.2025.05.003_bib0020","doi-asserted-by":"crossref","first-page":"712","DOI":"10.1111\/mmi.13653","article-title":"Recently differentiated epimastigotes from Trypanosoma cruzi are infective to the mammalian host","volume":"104","author":"Kessler","year":"2017","journal-title":"Mol. Microbiol."},{"issue":"7","key":"10.1016\/bs.enz.2025.05.003_bib0021","doi-asserted-by":"crossref","first-page":"1051","DOI":"10.1590\/S0074-02762009000700021","article-title":"A new consensus for Trypanosoma cruzi intraspecific nomenclature: second revision meeting recommends TcI to TcVI","volume":"104","author":"Zingales","year":"2009","journal-title":"Mem. Inst. Oswaldo Cruz."},{"issue":"6","key":"10.1016\/bs.enz.2025.05.003_bib0022","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1017\/S0031182009005861","article-title":"A new genotype of Trypanosoma cruzi associated with bats evidenced by phylogenetic analyses using SSU rDNA, cytochrome b and Histone H2B genes and genotyping based on ITS1 rDNA","volume":"136","author":"Marcili","year":"2009","journal-title":"Parasitology"},{"key":"10.1016\/bs.enz.2025.05.003_bib0023","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1016\/j.meegid.2016.01.029","article-title":"Reconsideration of the seven discrete typing units within the species Trypanosoma cruzi, a new proposal of three reliable mitochondrial clades","volume":"39","author":"Barnab\u00e9","year":"2016","journal-title":"Infect. Genet. Evol."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.003_bib0024","doi-asserted-by":"crossref","first-page":"26","DOI":"10.5334\/gh.484","article-title":"WHF IASC roadmap on chagas disease","volume":"15","author":"Echeverr\u00eda","year":"2020","journal-title":"Glob. Heart"},{"issue":"6","key":"10.1016\/bs.enz.2025.05.003_bib0025","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1080\/17460441.2024.2349155","article-title":"New drug discovery strategies for the treatment of benznidazole-resistance in Trypanosoma cruzi, the causative agent of Chagas disease","volume":"19","author":"Murta","year":"2024","journal-title":"Expert Opin. Drug Discov"},{"issue":"2","key":"10.1016\/bs.enz.2025.05.003_bib0026","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pntd.0012849","article-title":"Redefining the treatment of Chagas disease: a review of recent clinical and pharmacological data for a novel formulation of nifurtimox","volume":"19","author":"Altcheh","year":"2025","journal-title":"PLoS Negl. Trop. Dis."},{"issue":"2","key":"10.1016\/bs.enz.2025.05.003_bib0027","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":"3","key":"10.1016\/bs.enz.2025.05.003_bib0028","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1080\/13543776.2023.2176219","article-title":"Are patents important indicators of innovation for Chagas disease treatment?","volume":"33","author":"Caroli","year":"2023","journal-title":"Expert Opin. Ther. Pat."},{"key":"10.1016\/bs.enz.2025.05.003_bib0029","article-title":"Kinetoplastid diseases: Insights into the mechanisms of drug action and resistance for novel drug discovery","volume":"5","author":"Tauheed","year":"2025","journal-title":"Asp Mol Med"},{"issue":"1","key":"10.1016\/bs.enz.2025.05.003_bib0030","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1186\/1756-3305-6-112","article-title":"Identification of Trypanosoma cruzi Discrete Typing Units (DTUs) through the implementation of a High-Resolution Melting (HRM) genotyping assay","volume":"6","author":"Higuera","year":"2013","journal-title":"Parasit. Vectors"},{"issue":"12","key":"10.1016\/bs.enz.2025.05.003_bib0031","doi-asserted-by":"crossref","DOI":"10.1016\/j.heliyon.2022.e12380","article-title":"New metabolic signature for Chagas disease reveals sex steroid perturbation in humans and mice","volume":"8","author":"Golizeh","year":"2022","journal-title":"Heliyon"},{"key":"10.1016\/bs.enz.2025.05.003_bib0032","doi-asserted-by":"crossref","first-page":"402","DOI":"10.3389\/fcimb.2020.00402","article-title":"Gut dysbiosis in chagas disease. a possible link to the pathogenesis","volume":"10","author":"Souza-Basqueira","year":"2020","journal-title":"Front. Cell. Infect. Microbiol."},{"issue":"7","key":"10.1016\/bs.enz.2025.05.003_bib0033","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pntd.0011490","article-title":"Chagas disease is related to structural changes of the gut microbiota in adults with chronic infection (TRIPOBIOME study)","volume":"17","author":"P\u00e9rez-Molina","year":"2023","journal-title":"PLoS Negl. Trop. Dis."},{"issue":"2","key":"10.1016\/bs.enz.2025.05.003_bib0034","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1080\/17460913.2024.2431417","article-title":"Parasite-microbiota interactions: a pathway to innovative interventions for Chagas disease, leishmaniasis, and ascariasis","volume":"20","author":"Ram\u00edrez","year":"2025","journal-title":"Future Microbiol"},{"key":"10.1016\/bs.enz.2025.05.003_bib0035","doi-asserted-by":"crossref","first-page":"333","DOI":"10.3762\/bjnano.15.30","article-title":"Nanomedicines against Chagas disease: a critical review","volume":"15","author":"Morilla","year":"2024","journal-title":"Beilstein J. Nanotechnol."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.003_bib0036","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":"18","key":"10.1016\/bs.enz.2025.05.003_bib0037","doi-asserted-by":"crossref","DOI":"10.3390\/ijms241813778","article-title":"From benznidazole to new drugs: nanotechnology contribution in chagas disease","volume":"24","author":"Gomes","year":"2023","journal-title":"Int J Mol Sci."},{"issue":"10","key":"10.1016\/bs.enz.2025.05.003_bib0038","doi-asserted-by":"crossref","first-page":"911","DOI":"10.1080\/14728222.2023.2264512","article-title":"Molecular targets for Chagas disease: validation, challenges and lead compounds for widely exploited targets","volume":"27","author":"Souza","year":"2023","journal-title":"Expert Opin. Ther. Targets"},{"issue":"1","key":"10.1016\/bs.enz.2025.05.003_bib0039","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1080\/14756366.2019.1677638","article-title":"A structure-based approach towards the identification of novel antichagasic compounds: Trypanosoma cruzi carbonic anhydrase inhibitors","volume":"35","author":"Llanos","year":"2020","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"8","key":"10.1016\/bs.enz.2025.05.003_bib0040","doi-asserted-by":"crossref","first-page":"1129","DOI":"10.1016\/S1473-3099(20)30844-6","article-title":"New regimens of benznidazole monotherapy and in combination with fosravuconazole for treatment of Chagas disease (BENDITA): a phase 2, double-blind, randomised trial","volume":"21","author":"Torrico","year":"2021","journal-title":"Lancet Infect. Dis."},{"issue":"14","key":"10.1016\/bs.enz.2025.05.003_bib0041","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":"5","key":"10.1016\/bs.enz.2025.05.003_bib0042","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":"2","key":"10.1016\/bs.enz.2025.05.003_bib0043","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1007\/s10822-022-00491-0","article-title":"A combined ligand and target-based virtual screening strategy to repurpose drugs as putrescine uptake inhibitors with trypanocidal activity","volume":"37","author":"Llanos","year":"2023","journal-title":"J Comput Aided Mol Des"},{"key":"10.1016\/bs.enz.2025.05.003_bib0044","doi-asserted-by":"crossref","DOI":"10.1590\/0074-02760240161","article-title":"Investigation of the activity of 4-aminoquinolines as cysteine protease inhibitors with application in the treatment of Chagas disease","volume":"120","author":"Sheu-Idrees","year":"2025","journal-title":"Mem. Inst. Oswaldo Cruz."},{"issue":"4","key":"10.1016\/bs.enz.2025.05.003_bib0045","doi-asserted-by":"crossref","first-page":"2067","DOI":"10.1128\/AAC.00617-13","article-title":"Sesquiterpene lactone in nanostructured parenteral dosage form is efficacious in experimental chagas disease","volume":"58","author":"Branquinho","year":"2014","journal-title":"Antimicrob. Agents Chemother."},{"issue":"3","key":"10.1016\/bs.enz.2025.05.003_bib0046","doi-asserted-by":"crossref","first-page":"fuad020","DOI":"10.1093\/femsre\/fuad020","article-title":"Targeting the nucleotide metabolism of Trypanosoma brucei and other trypanosomatids","volume":"47","author":"Hofer","year":"2023","journal-title":"FEMS Microbiol. Rev."},{"issue":"9","key":"10.1016\/bs.enz.2025.05.003_bib0047","doi-asserted-by":"crossref","first-page":"2943","DOI":"10.1007\/s00436-020-06779-0","article-title":"Repositioning of leishmanicidal (1,2,3)Triazolo(1,5-a)pyridinium salts for Chagas disease treatment: Trypanosoma cruzi cell death involving mitochondrial membrane depolarisation and Fe-SOD inhibition","volume":"119","author":"Mart\u00edn-Escolano","year":"2020","journal-title":"Parasitol. Res."},{"issue":"3","key":"10.1016\/bs.enz.2025.05.003_bib0048","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1016\/j.ijpddr.2015.05.002","article-title":"An in vitro iron superoxide dismutase inhibitor decreases the parasitemia levels of Trypanosoma cruzi in BALB\/c mouse model during acute phase","volume":"5","author":"Olmo","year":"2015","journal-title":"Int J Parasitol Drugs Drug Resist"},{"issue":"6","key":"10.1016\/bs.enz.2025.05.003_bib0049","doi-asserted-by":"crossref","first-page":"586","DOI":"10.1097\/QCO.0b013e32834c630e","article-title":"Boron-based drugs as antiprotozoals","volume":"24","author":"Jacobs","year":"2011","journal-title":"Curr. Opin. Infect. Dis."},{"issue":"7","key":"10.1016\/bs.enz.2025.05.003_bib0050","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1005058","article-title":"Utilizing chemical genomics to identify cytochrome b as a novel drug target for chagas disease. Phillips MA, organizador","volume":"11","author":"Khare","year":"2015","journal-title":"PLoS Pathog."},{"issue":"3","key":"10.1016\/bs.enz.2025.05.003_bib0051","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1021\/acsinfecdis.9b00426","article-title":"The Qi Site of cytochrome b is a promiscuous drug target in Trypanosoma cruzi and Leishmania donovani","volume":"6","author":"Wall","year":"2020","journal-title":"ACS Infect Dis."},{"issue":"6652","key":"10.1016\/bs.enz.2025.05.003_bib0052","doi-asserted-by":"crossref","first-page":"1349","DOI":"10.1126\/science.adh0614","article-title":"Cyanotriazoles are selective topoisomerase II poisons that rapidly cure trypanosome infections","volume":"380","author":"Rao","year":"2023","journal-title":"Science"},{"issue":"10","key":"10.1016\/bs.enz.2025.05.003_bib0053","doi-asserted-by":"crossref","first-page":"1207","DOI":"10.1038\/s41564-020-0745-6","article-title":"Targeting the trypanosome kinetochore with CLK1 protein kinase inhibitors","volume":"5","author":"Saldivia","year":"2020","journal-title":"Nat. Microbiol."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.003_bib0054","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-022-23941-z","article-title":"Fexinidazole interferes with the growth and structural organization of Trypanosoma cruzi","volume":"12","author":"Zuma","year":"2022","journal-title":"Sci. Rep."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.003_bib0055","doi-asserted-by":"crossref","DOI":"10.1016\/j.arcmed.2024.103084","article-title":"New drugs and promising drug combinations in the treatment of chagas disease in Brazil: a systematic review and meta-analysis","volume":"56","author":"Freire","year":"2025","journal-title":"Arch. Med. Res."},{"issue":"6","key":"10.1016\/bs.enz.2025.05.003_bib0056","doi-asserted-by":"crossref","first-page":"2117","DOI":"10.1021\/jm0512600","article-title":"Carbonic anhydrase inhibitors: DNA cloning and inhibition studies of the \u03b1-carbonic anhydrase from helicobacter pylori, a new target for developing sulfonamide and sulfamate gastric drugs","volume":"49","author":"Nishimori","year":"2006","journal-title":"J. Med. Chem."},{"issue":"18","key":"10.1016\/bs.enz.2025.05.003_bib0057","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 \u2014the \u03b7-carbonic anhydrases","volume":"24","author":"Del Prete","year":"2014","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"18","key":"10.1016\/bs.enz.2025.05.003_bib0058","doi-asserted-by":"crossref","first-page":"5066","DOI":"10.1016\/j.bmcl.2008.07.122","article-title":"Carbonic anhydrase inhibitors: Inhibition of the \u03b2-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":"4","key":"10.1016\/bs.enz.2025.05.003_bib0059","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":"2019","journal-title":"ACS Med. Chem. Lett."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.003_bib0060","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."},{"key":"10.1016\/bs.enz.2025.05.003_bib0061","series-title":"Carbonic anhydrases","first-page":"449","article-title":"Carbonic anhydrases from pathogens","author":"Aspatwar","year":"2019"},{"issue":"1","key":"10.1016\/bs.enz.2025.05.003_bib0062","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":"4","key":"10.1016\/bs.enz.2025.05.003_bib0063","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":"6","key":"10.1016\/bs.enz.2025.05.003_bib0064","doi-asserted-by":"crossref","first-page":"901","DOI":"10.3390\/ph16060901","article-title":"Targeting metalloenzymes: the \u201cAchilles\u2019 heel\u201d of viruses and parasites","volume":"16","author":"Moianos","year":"2023","journal-title":"Pharmaceuticals"},{"issue":"10","key":"10.1016\/bs.enz.2025.05.003_bib0065","doi-asserted-by":"crossref","first-page":"1147","DOI":"10.1080\/17460441.2022.2117295","article-title":"Discovery of novel drugs for Chagas disease: is carbonic anhydrase a target for antiprotozoal drugs?","volume":"17","author":"Vermelho","year":"2022","journal-title":"Expert Opin Drug Discov"},{"issue":"39","key":"10.1016\/bs.enz.2025.05.003_bib0066","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\u2019Ambrosio","year":"2019","journal-title":"Curr. Med. Chem."},{"issue":"3","key":"10.1016\/bs.enz.2025.05.003_bib0067","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. mar\u00e7o de"},{"issue":"15","key":"10.1016\/bs.enz.2025.05.003_bib0068","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":"1","key":"10.1016\/bs.enz.2025.05.003_bib0069","doi-asserted-by":"crossref","first-page":"330","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":"4","key":"10.1016\/bs.enz.2025.05.003_bib0070","doi-asserted-by":"crossref","first-page":"581","DOI":"10.3109\/14756366.2014.956309","article-title":"A new class of quinazoline-sulfonamides acting as efficient inhibitors against the \u03b1-carbonic anhydrase from Trypanosoma cruzi","volume":"30","author":"Alafeefy","year":"2015","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.003_bib0071","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":"13","key":"10.1016\/bs.enz.2025.05.003_bib0072","doi-asserted-by":"crossref","first-page":"7422","DOI":"10.1021\/acs.jmedchem.0c00733","article-title":"Sulfonamide inhibitors of human carbonic anhydrases designed through a three-tails approach: improving ligand\/isoform matching and selectivity of action","volume":"63","author":"Bonardi","year":"2020","journal-title":"J. Med. Chem."},{"issue":"4","key":"10.1016\/bs.enz.2025.05.003_bib0073","doi-asserted-by":"crossref","first-page":"1721","DOI":"10.1021\/jm300031j","article-title":"Dithiocarbamates strongly inhibit carbonic anhydrases and show antiglaucoma action in vivo","volume":"55","author":"Carta","year":"2012","journal-title":"J. Med. Chem."},{"issue":"12","key":"10.1016\/bs.enz.2025.05.003_bib0075","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":"15","key":"10.1016\/bs.enz.2025.05.003_bib0074","doi-asserted-by":"crossref","first-page":"2806","DOI":"10.3390\/molecules24152806","article-title":"Application of dithiocarbamates as potential new antitrypanosomatids-drugs: approach chemistry, functional and biological","volume":"24","author":"Oliveira","year":"2019","journal-title":"Molecules"},{"issue":"2","key":"10.1016\/bs.enz.2025.05.003_bib0076","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.2025.05.003_bib0077","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":"Menezes","year":"2016","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.003_bib0078","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":"726","key":"10.1016\/bs.enz.2025.05.003_bib0079","doi-asserted-by":"crossref","first-page":"eadg8105","DOI":"10.1126\/scitranslmed.adg8105","article-title":"Short-course combination treatment for experimental chronic Chagas disease","volume":"15","author":"Gonz\u00e1lez","year":"2023","journal-title":"Sci. Transl. Med."},{"issue":"4","key":"10.1016\/bs.enz.2025.05.003_bib0080","doi-asserted-by":"crossref","first-page":"54","DOI":"10.3390\/tropicalmed7040054","article-title":"Immune responses in leishmaniasis: an overview","volume":"7","author":"Silva","year":"2022","journal-title":"Trop Med Infect Dis"},{"year":"2024","series-title":"Leishmaniasis","key":"10.1016\/bs.enz.2025.05.003_bib0081"},{"year":"2023","series-title":"Leishmaniasis","key":"10.1016\/bs.enz.2025.05.003_bib0082"},{"issue":"2","key":"10.1016\/bs.enz.2025.05.003_bib0083","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1007\/s40475-021-00232-7","article-title":"A review of leishmaniasis: current knowledge and future directions","volume":"8","author":"Mann","year":"2021","journal-title":"Curr. Trop. Med. Rep."},{"key":"10.1016\/bs.enz.2025.05.003_bib0084","series-title":"Antiprotozoal drug development and delivery","first-page":"143","article-title":"Polyamine and trypanothione pathways as targets for novel antileishmanial drugs","author":"Rodrigues","year":"2021"},{"issue":"3","key":"10.1016\/bs.enz.2025.05.003_bib0085","doi-asserted-by":"crossref","first-page":"516","DOI":"10.1111\/ced.14919","article-title":"Treatment options for leishmaniasis","volume":"47","author":"Pradhan","year":"2022","journal-title":"Clin. Exp. Dermatol."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.003_bib0086","doi-asserted-by":"crossref","first-page":"1100","DOI":"10.1080\/14756366.2019.1616182","article-title":"Leishmania infantum arginase: biochemical characterization and inhibition by naturally occurring phenolic substances","volume":"34","author":"Garcia","year":"2019","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"18","key":"10.1016\/bs.enz.2025.05.003_bib0087","doi-asserted-by":"crossref","first-page":"3216","DOI":"10.3390\/molecules24183216","article-title":"Leishmania mexicana Trypanothione Reductase Inhibitors: Computational and Biological Studies","volume":"24","author":"Matadamas-Mart\u00ednez","year":"2019","journal-title":"Molecules"},{"issue":"9","key":"10.1016\/bs.enz.2025.05.003_bib0088","doi-asserted-by":"crossref","first-page":"1020","DOI":"10.3390\/pathogens11091020","article-title":"In vitro and in silico analyses of new cinnamid and rosmarinic acid-derived compounds biosynthesized in Escherichia coli as Leishmania amazonensis arginase inhibitors","volume":"11","author":"Come","year":"2022","journal-title":"Pathogens"},{"key":"10.1016\/bs.enz.2025.05.003_bib0089","doi-asserted-by":"crossref","unstructured":"C.F. Prada, R. \u00c1lvarez-Velilla, R. Bala\u00f1a-Fouce, C. Prieto, E. Calvo-\u00c1lvarez, J.M. Escudero-Mart\u00ednez, J.M. Requena, C. Ord\u00f3\u00f1e, A. Desideri, Y. P\u00e9rez-Pertejo, R.M. Reguera, Gimatecan and other camptothecin derivatives poison Leishmania DNA-topoisomerase IB leading to a strong leishmanicidal effect, Biochem. Pharmacol. 85 (10) (2013) 1433\u20131440.","DOI":"10.1016\/j.bcp.2013.02.024"},{"issue":"1","key":"10.1016\/bs.enz.2025.05.003_bib0090","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-017-09725-w","article-title":"MAPK1 of Leishmania donovani interacts and phosphorylates HSP70 and HSP90 subunits of foldosome complex","volume":"7","author":"Kaur","year":"2017","journal-title":"Sci. Rep."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.003_bib0091","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-019-52774-6","article-title":"Biochemical characterization and chemical validation of Leishmania MAP Kinase-3 as a potential drug target","volume":"9","author":"Raj","year":"2019","journal-title":"Sci. Rep."},{"issue":"8","key":"10.1016\/bs.enz.2025.05.003_bib0092","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":"18","key":"10.1016\/bs.enz.2025.05.003_bib0093","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":"21","key":"10.1016\/bs.enz.2025.05.003_bib0094","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":"5","key":"10.1016\/bs.enz.2025.05.003_bib0095","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0292152","article-title":"Leishmania ribosomal protein (RP) paralogous genes compensate each other\u2019s expression maintaining protein native levels","volume":"19","author":"Borges","year":"2024","journal-title":"PLoS One"},{"issue":"2","key":"10.1016\/bs.enz.2025.05.003_bib0096","doi-asserted-by":"crossref","first-page":"606","DOI":"10.1007\/s11686-022-00519-3","article-title":"Host\u2013parasite interactions: regulation of Leishmania infection in Sand Fly","volume":"67","author":"Omondi","year":"2022","journal-title":"Acta Parasitol"},{"issue":"4","key":"10.1016\/bs.enz.2025.05.003_bib0097","doi-asserted-by":"crossref","first-page":"754","DOI":"10.1242\/jcs.199422","article-title":"Interplay between a cytosolic and a cell surface carbonic anhydrase in pH homeostasis and acid tolerance of Leishmania","volume":"130","author":"Pal","year":"2017","journal-title":"J. Cell Sci."},{"key":"10.1016\/bs.enz.2025.05.003_bib0098","series-title":"Antiprotozoal drug development and delivery","first-page":"83","article-title":"Targeting carbonic anhydrases from Trypanosoma cruzi and Leishmania spp. as a therapeutic strategy to obtain new antiprotozoal drugs","author":"Nocentini","year":"2021"},{"issue":"12","key":"10.1016\/bs.enz.2025.05.003_bib0099","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pntd.0006052","article-title":"Drug resistance and treatment failure in leishmaniasis: a 21st century challenge","volume":"11","author":"Ponte-Sucre","year":"2017","journal-title":"PLoS Negl. Trop. Dis."},{"key":"10.1016\/bs.enz.2025.05.003_bib0100","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/B978-0-12-407679-2.00005-3","article-title":"Mechanisms of immune evasion in leishmaniasis","volume":"82","author":"Gupta","year":"2013","journal-title":"Adv. Appl. Microbiol."},{"key":"10.1016\/bs.enz.2025.05.003_bib0101","article-title":"Functional partnership between carbonic anhydrase and malic enzyme in promoting gluconeogenesis in Leishmania major","author":"Mondal","year":"2020","journal-title":"Biorxiv"},{"issue":"3","key":"10.1016\/bs.enz.2025.05.003_bib0102","doi-asserted-by":"crossref","first-page":"310","DOI":"10.3390\/pathogens11030310","article-title":"The role of nuclear factor Kappa B (NF-\u03baB) in the immune response against parasites","volume":"11","author":"B\u0105ska","year":"2022","journal-title":"Pathogens"},{"key":"10.1016\/bs.enz.2025.05.003_bib0103","doi-asserted-by":"crossref","DOI":"10.3389\/fimmu.2021.748325","article-title":"Determinants of innate immunity in visceral leishmaniasis and their implication in vaccine development","volume":"12","author":"Volpedo","year":"2021","journal-title":"Front. Immunol."},{"key":"10.1016\/bs.enz.2025.05.003_bib0104","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.cyto.2018.07.001","article-title":"The impact of IL-10 dynamic modulation on host immune response against visceral leishmaniasis","volume":"112","author":"Mesquita","year":"2018","journal-title":"Cytokine"},{"issue":"7","key":"10.1016\/bs.enz.2025.05.003_bib0105","doi-asserted-by":"crossref","first-page":"993","DOI":"10.1007\/s00249-021-01561-1","article-title":"Structure and mechanism of secondary sulfonamide binding to carbonic anhydrases","volume":"50","author":"Baronas","year":"2021","journal-title":"Eur. Biophys. J."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.003_bib0106","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":"4","key":"10.1016\/bs.enz.2025.05.003_bib0109","doi-asserted-by":"crossref","first-page":"2144","DOI":"10.1128\/AAC.05146-14","article-title":"Identification of metal dithiocarbamates as a novel class of antileishmanial agents","volume":"59","author":"Pal","year":"2015","journal-title":"Antimicrob. Agents Chemother."},{"issue":"1","key":"10.1016\/bs.enz.2025.05.003_bib0113","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":"Cardoso","year":"2018","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"5","key":"10.1016\/bs.enz.2025.05.003_bib0107","doi-asserted-by":"crossref","first-page":"1520","DOI":"10.1021\/acsinfecdis.4c00163","article-title":"Metalloenzyme inhibitors against zoonotic infections: focus on Leishmania and Schistosoma","volume":"10","author":"Rossi","year":"2024","journal-title":"ACS Infect Dis"},{"key":"10.1016\/bs.enz.2025.05.003_bib0108","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2021.104733","article-title":"Synthesis and antiplasmodial evaluation of 1H-1,2,3-triazole grafted 4-aminoquinoline-benzoxaborole hybrids and benzoxaborole analogues","volume":"109","author":"Saini","year":"2021","journal-title":"Bioorganic Chem"},{"issue":"20","key":"10.1016\/bs.enz.2025.05.003_bib0110","doi-asserted-by":"crossref","first-page":"3677","DOI":"10.1021\/jm000027t","article-title":"Carbonic anhydrase and matrix metalloproteinase inhibitors: sulfonylated amino acid hydroxamates with MMP inhibitory properties act as efficient inhibitors of CA Isozymes I, II, and IV, and N -Hydroxysulfonamides inhibit both these zinc enzymes","volume":"43","author":"Scozzafava","year":"2000","journal-title":"J. Med. Chem."},{"issue":"70","key":"10.1016\/bs.enz.2025.05.003_bib0111","doi-asserted-by":"crossref","first-page":"8838","DOI":"10.1039\/c2cc34275h","article-title":"Hydroxamate represents a versatile zinc binding group for the development of new carbonic anhydrase inhibitors","volume":"48","author":"Di Fiore","year":"2012","journal-title":"Chem. Commun."},{"issue":"11","key":"10.1016\/bs.enz.2025.05.003_bib0112","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."},{"key":"10.1016\/bs.enz.2025.05.003_bib0114","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":"Bioorganic Chem"},{"issue":"2","key":"10.1016\/bs.enz.2025.05.003_bib0115","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1021\/acs.chemmater.2c03003","article-title":"The future of drug delivery","volume":"35","author":"Gao","year":"2023","journal-title":"Chem. Mater."}],"container-title":["The Enzymes","Fungal and Protozoan Carbonic Anhydrases"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874604725000058?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874604725000058?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,7]],"date-time":"2025-10-07T01:34:07Z","timestamp":1759800847000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1874604725000058"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025]]},"ISBN":["9780443313943"],"references-count":115,"URL":"https:\/\/doi.org\/10.1016\/bs.enz.2025.05.003","relation":{},"ISSN":["1874-6047"],"issn-type":[{"type":"print","value":"1874-6047"}],"subject":[],"published":{"date-parts":[[2025]]}}}