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World Health Organization: Fact Sheets–Antibiotic Resistance. [(accessed on 16 October 2021)]. Available online: https://www.who.int/news-room/fact-sheets/detail/antibiotic-resistance.
Supuran C.T., Capasso C. An Overview of the Bacterial Carbonic Anhydrases. Metabolites. 2017;7:56. doi: 10.3390/metabo7040056.
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Supuran C.T., Capasso C. Antibacterial carbonic anhydrase inhibitors: An update on the recent literature. Expert Opin. Ther. Pat. 2020;30:963–982. doi: 10.1080/13543776.2020.1811853.
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Capasso C., Supuran C.T. Bacterial, fungal and protozoan carbonic anhydrases as drug targets. Expert Opin. Ther. Targets. 2015;19:1689–1704. doi: 10.1517/14728222.2015.1067685.
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Flaherty P., Seleem D.M.N., Supuran C.T. Bacterial carbonic anhydrases: Underexploited antibacterial therapeutic targets. Future Med. Chem. 2021;13:1619–1622. doi: 10.4155/fmc-2021-0207.
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Capasso C., Supuran C.T. An overview of the α-, β- and γ-carbonic anhydrases from Bacteria: Can bacterial carbonic anhydrases shed new light on evolution of bacteria? J. Enzyme Inhib. Med. Chem. 2015;30:325–332. doi: 10.3109/14756366.2014.910202.
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De Luca V., Petreni A., Nocentini A., Scaloni A., Supuran C.T., Capasso C. Effect of Sulfonamides and Their Structurally Related Derivatives on the Activity of ι-Carbonic Anhydrase from Burkholderia territorii. Int. J. Mol. Sci. 2021;22:571. doi: 10.3390/ijms22020571.
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Capasso C., Supuran C.T. An Overview of the Selectivity and Efficiency of the Bacterial Carbonic Anhydrase Inhibitors. Curr. Med. Chem. 2015;22:2130–2139. doi: 10.2174/0929867321666141012174921.
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Supuran C.T., Capasso C. Biomedical applications of prokaryotic carbonic anhydrases. Expert Opin. Ther. Pat. 2018;28:745–754. doi: 10.1080/13543776.2018.1497161.
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Bonardi A., Nocentini A., Osman S.M., Alasmary F.A., Almutairi T.M., Abdullah D.S., Gratteri P., Supuran C.T. Inhibition of α-, β- and γ-carbonic anhydrases from the pathogenic bacterium Vibrio cholerae with aromatic sulphonamides and clinically licenced drugs–a joint docking/molecular dynamics study. J. Enzyme Inhib. Med. Chem. 2021;36:469–479. doi: 10.1080/14756366.2020.1862102.
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Del Prete S., Isik S., Vullo D., De Luca V., Carginale V., Scozzafava A., Supuran C.T., Capasso C. DNA Cloning, Characterization, and Inhibition Studies of an α-Carbonic Anhydrase from the Pathogenic Bacterium Vibrio cholerae. J. Med. Chem. 2012;55:10742–10748. doi: 10.1021/jm301611m.
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Ceruso M., Del Prete S., Alothman Z., Capasso C., Supuran C.T. Sulfonamides with Potent Inhibitory Action and Selectivity against the α-Carbonic Anhydrase from Vibrio cholerae. ACS Med. Chem. Lett. 2014;5:826–830. doi: 10.1021/ml500192a.
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Bua S., Berrino E., Del Prete S., Murthy V.S., Vijayakumar V., Tamboli Y., Capasso C., Cerbai E., Mugelli A., Carta F., et al. Synthesis of novel benzenesulfamide derivatives with inhibitory activity against human cytosolic carbonic anhydrase I and II and Vibrio cholerae α- and β-class enzymes. J. Enzyme Inhib. Med. Chem. 2018;33:1125–1136. doi: 10.1080/14756366.2018.1467901.
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Bua S., Osman S.M., Del Prete S., Capasso C., Alothman Z., Nocentini A., Supuran C.T. Click-tailed benzenesulfonamides as potent bacterial carbonic anhydrase inhibitors for targeting Mycobacterium tuberculosis and Vibrio cholerae. Bioorg. Chem. 2019;86:183–186. doi: 10.1016/j.bioorg.2019.01.065.
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Ceruso M., Vullo D., Scozzafava A., Supuran C.T. Sulfonamides incorporating fluorine and 1,3,5-triazine moieties are effective inhibitors of three β -class carbonic anhydrases from Mycobacterium tuberculosis. J. Enzyme Inhib. Med. Chem. 2014;29:686–689. doi: 10.3109/14756366.2013.842233.
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Angeli A., Pinteala M., Maier S.S., Simionescu B.C., Milaneschi A., Abbas G., del Prete S., Capasso C., Capperucci A., Tanini D., et al. Evaluation of Thio- and Seleno-Acetamides Bearing Benzenesulfonamide as Inhibitor of Carbonic Anhydrases from Different Pathogenic Bacteria. Int. J. Mol. Sci. 2020;21:686–689. doi: 10.3390/ijms21020598.
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Carta F., Maresca A., Covarrubias A.S., Mowbray S.L., Jones T.A., Supuran C.T. Carbonic anhydrase inhibitors. Characterization and inhibition studies of the most active β-carbonic anhydrase from Mycobacterium tuberculosis, Rv3588c. Int. J. Mol. Sci. 2009;19:6649–6654. doi: 10.1016/j.bmcl.2009.10.009.
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Maresca A., Carta F., Vullo D., Scozzafava A., Supuran C.T. Carbonic anhydrase inhibitors. Inhibition of the Rv1284 and Rv3273 β-carbonic anhydrases from Mycobacterium tuberculosis with diazenylbenzenesulfonamides. Int. J. Mol. Sci. 2009;19:4929–4932. doi: 10.1016/j.bmcl.2009.07.088.
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Ali M., Angeli A., Bozdag M., Carta F., Capasso C., Farooq U., Supuran C.T. Benzylaminoethylureido-Tailed Benzenesulfonamides Show Potent Inhibitory Activity against Bacterial Carbonic Anhydrases. ChemMedChem. 2020;15:2444–2447. doi: 10.1002/cmdc.202000680.
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Nocentini A., Supuran C.T., Capasso C. An overview on the recently discovered iota-carbonic anhydrases. J. Enzyme Inhib. Med. Chem. 2021;36:1988–1995. doi: 10.1080/14756366.2021.1972995.
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Del Prete S., De Luca V., Bua S., Nocentini A., Carginale V., Supuran C.T., Capasso C. The Effect of Substituted Benzene-Sulfonamides and Clinically Licensed Drugs on the Catalytic Activity of CynT2, a Carbonic Anhydrase Crucial for Escherichia coli Life Cycle: Characterisation and effects of simple aromatic/heterocyclic sulphonamide inhibitors. Int. J. Mol. Sci. 2020;21:4175. doi: 10.3390/ijms21114175.
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Del Prete S., Bua S., Supuran C.T., Capasso C. Escherichia coli γ -carbonic anhydrase: Characterisation and effects of simple aromatic/heterocyclic sulphonamide inhibitors. J. Enzyme Inhib. Med. Chem. 2020;35:1545–1554. doi: 10.1080/14756366.2020.1800670.
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Smith S.V., Friedman D.I. The Idiopathic Intracranial Hypertension Treatment Trial: A Review of the Outcomes. Headache. 2017;57:1303–1310. doi: 10.1111/head.13144.
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Supuran C.T. Emerging role of carbonic anhydrase inhibitors: A Review of the Outcomes. Clin. Sci. 2021;135:1233–1249. doi: 10.1042/CS20210040.
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Angeli A., Carta F., Nocentini A., Winum J.-Y., Zalubovskis R., Akdemir A., Onnis V., Eldehna W.M., Capasso C., Simone G.D., et al. Carbonic Anhydrase Inhibitors Targeting Metabolism and Tumor Microenvironment: A Review of the Outcomes. Metabolites. 2020;10:412. doi: 10.3390/metabo10100412.
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Kumar S., Rulhania S., Jaswal S., Monga V. Recent advances in the medicinal chemistry of carbonic anhydrase inhibitors: A Review of the Outcomes. Eur. J. Med. Chem. 2021;209:1233–1249. doi: 10.1016/j.ejmech.2020.112923.
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Havránková E., Csöllei J., Vullo D., Garaj V., Pazdera P., Supuran C.T. Novel sulfonamide incorporating piperazine, aminoalcohol and 1,3,5-triazine structural motifs with carbonic anhydrase I, II and IX inhibitory action: Application of Cu(I) Supported on a Weakly Acidic Cation-Exchanger Resin in a Comparative Study. Bioorg. Chem. 2018;77:25–37. doi: 10.1016/j.bioorg.2017.12.034.
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Garaj V., Puccetti L., Fasolis G., Winum J.-Y., Montero J.-L., Scozzafava A., Vullo D., Innocenti A., Supuran C.T. Carbonic anhydrase inhibitors: Synthesis and inhibition of cytosolic/tumor-associated carbonic anhydrase isozymes I, II, and IX with sulfonamides incorporating 1,2,4-triazine moieties. J. Med. Chem. 2004;14:5427–5433. doi: 10.1016/j.bmcl.2004.07.087.
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Ekinci D., Karagoz L., Ekinci D., Senturk M., Supuran C.T. Carbonic anhydrase inhibitors: In vitro inhibition of α isoforms (hCA I, hCA II, bCA III, hCA IV) by flavonoids: Inhibition of human and bovine isoenzymes by benzenesulphonamides, cyclitols and phenolic compounds. J. Enzyme Inhib. Med. Chem. 2013;28:283–288. doi: 10.3109/14756366.2011.643303.
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Alp C., Maresca A., Alp N.A., Gültekin M.S., Ekinci D., Scozzafava A., Supuran C.T. Secondary/tertiary benzenesulfonamides with inhibitory action against the cytosolic human carbonic anhydrase isoforms I and II: Inhibition of human and bovine isoenzymes by benzenesulphonamides, cyclitols and phenolic compounds. J. Enzyme Inhib. Med. Chem. 2013;28:294–298. doi: 10.3109/14756366.2012.658788.
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