References
- Supuran CT. Structure and function of carbonic anhydrases. Biochem J 2016;473:2023–32.
- Supuran CT. Carbonic anhydrases: novel therapeutic applications for inhibitors and activators. Nat Rev Drug Discov 2008;7:168–81.
- Supuran CT. Carbonic anhydrase inhibitors. Bioorg Med Chem Lett 2010;20:3467–74.
- Supuran CT. Carbonic anhydrase inhibitors and activators for novel therapeutic applications. Future Med Chem 2011;3:1165–80.
- Supuran CT. Emerging role of carbonic anhydrase inhibitors. Clin Sci 2021;135:1233–49.
- Angeli A, Abdel-Aziz AAM, Nocentini A, et al. Synthesis and carbonic anhydrase inhibition of polycyclic imides incorporating N-benzenesulfonamide moieties. Bioorg Med Chem 2017;25:5373–9.
- Kurt BZ, Sonmez F, Ozturk D, et al. Synthesis of coumarin-sulfonamide derivatives and determination of their cytotoxicity, carbonic anhydrase inhibitory and molecular docking studies. Eur J Med Chem 2019;183:111702.
- Kurt BZ, Dag A, Doğan B, et al. Synthesis, biological activity and multiscale molecular modeling studies of bis-coumarins as selective carbonic anhydrase IX and XII inhibitors with effective cytotoxicity against hepatocellular carcinoma. Bioorg Chem 2019;87:838–50.
- Awadallah FM, Bua S, Mahmoud WR, et al. Inhibition studies on a panel of human carbonic anhydrases with N1-substituted secondary sulfonamides incorporating thiazolinone or imidazolone-indole tails. J Enzyme Inhib Med Chem 2018;33:629–38.
- Awadallah FM, El-Waei TA, Hanna MM, et al. Synthesis, carbonic anhydrase inhibition and cytotoxic activity of novel chromone-based sulfonamide derivatives. Eur J Med Chem 2015;96:425–35.
- Masini E, Carta F, Scozzafava A, Supuran CT. Antiglaucoma carbonic anhydrase inhibitors: a patent review. Expert Opin Ther Pat 2013;23:705–16.
- Alterio V, Di Fiore A, D’Ambrosio K, et al. Multiple binding modes of inhibitors to carbonic anhydrases: how to design specific drugs targeting 15 different isoforms? Chem Rev 2012;112:4421–68.
- Marini AM, Maresca A, Aggarwal M, et al. Tricyclic sulfonamides incorporating benzothiopyrano[4,3-c]pyrazole and pyridothiopyrano[4,3-c]pyrazole effectively inhibit α- and β-carbonic anhydrase: X-ray crystallography and solution investigations on 15 isoforms. J Med Chem 2012;55:9619–29.
- Barresi E, Salerno S, Marini AM, et al. Sulfonamides incorporating heteropolycyclic scaffolds show potent inhibitory action against carbonic anhydrase isoforms I, II, IX and XII. Bioorg Med Chem 2016;24:921–7.
- Salerno S, Barresi E, Amendola G, et al. 4-Substituted benzenesulfonamides incorporating bi/tricyclic moieties act as potent and isoform-selective carbonic anhydrase II/IX inhibitors. J Med Chem 2018;61:5765–70.
- Salerno S, Amendola G, Angeli A, et al. Inhibition studies on carbonic anhydrase isoforms I, II, IV and IX with N-arylsubstituted secondary sulfonamides featuring a bicyclic tetrahydroindazole scaffold. Eur J Med Chem 2021;220:113490.
- Wilkinson BL, Bornaghi LF, Houston TA, et al. A novel class of carbonic anhydrase inhibitors: glycoconjugate benzene sulfonamides prepared by “click-tailing”. J Med Chem 2006;49:6539–48.
- Güzel-Akdemir Ö, Akdemir A, Isik S, et al. O-Benzenedisulfonimido-sulfonamides are potent inhibitors of the tumor-associated carbonic anhydrase isoforms CA IX and CA XII. Bioorg Med Chem 2013;21:1386–91.
- Liu F, Martin-Mingot A, Lecornué F, et al. Carbonic anhydrases inhibitory effects of new benzenesulfonamides synthesized by using superacid chemistry. J Enzyme Inhib Med Chem 2012;27:886–91.
- Métayer B, Mingot A, Vullo D, et al. New superacid synthesized (fluorinated) tertiary benzenesulfonamides acting as selective HCA IX inhibitors: toward a new mode of carbonic anhydrase inhibition by sulfonamides. Chem Commun 2013;49:6015–7.
- Coviello V, Marchi B, Sartini S, et al. 1,2-Benzisothiazole derivatives bearing 4-, 5-, or 6-alkyl/arylcarboxamide moieties inhibit carbonic anhydrase isoform IX (CAIX) and cell proliferation under hypoxic conditions. J Med Chem 2016;59:6547–52.
- Ammazzalorso A, Carradori S, Angeli A, et al. Fibrate-based N-acylsulphonamides targeting carbonic anhydrases: synthesis, biochemical evaluation, and docking studies. J Enzyme Inhib Med Chem 2019;34:1051–61.
- D'Ascenzio M, Guglielmi P, Carradori S, et al. Open saccharin-based secondary sulfonamides as potent and selective inhibitors of cancer-related carbonic anhydrase IX and XII isoforms. J Enzyme Inhib Med Chem 2017;32:51–9.
- Moeker J, Peat TS, Bornaghi LF, et al. Cyclic secondary sulfonamides: unusually good inhibitors of cancer-related carbonic anhydrase enzymes. J Med Chem 2014;57:3522–31.
- Alp C, Maresca A, Alp NA, et al. Secondary/tertiary benzenesulfonamides with inhibitory action against the cytosolic human carbonic anhydrase isoforms I and II. J Enzyme Inhib Med Chem 2013;28:294–8.
- Supuran CT. How many carbonic anhydrase inhibition mechanisms exist? J Enzyme Inhib Med Chem 2016;31:345–60.
- Schenone P, Mosti L, Menozzi G. Reaction of 2-dimethylaminomethylene-1,3-diones with dinucleophiles. I. Synthesis of 1,5-disubstituted 4-acylpyrazoles. J Heterocycl Chem 1982;19:1355–61.
- Khalifah RG. The carbon dioxide hydration activity of carbonic anhydrase. I. Stop-flow kinetic studies on the native human isoenzymes B and C. J Biol Chem 1971;246:2561–73.
- Santos-Martins D, Solis-Vasquez L, Tillack AF, et al. Accelerating AutoDock4 with GPUs and gradient-based local search. J Chem Theory Comput 2021;17:1060–73.
- Morris G, Ruth H, Lindstrom W, et al. AutoDock4 and AutoDockTools4: automated docking with selective receptor flexibility. J Comput Chem 2009;30:2785–91.
- Leitans J, Kazaks A, Balode A, et al. Efficient expression and crystallization system of cancer-associated carbonic anhydrase isoform IX. J Med Chem 2015;58:9004–9.
- Chiaramonte N, Bua S, Ferraroni M, et al. 2-Benzylpiperazine: a new scaffold for potent human carbonic anhydrase inhibitors. Synthesis, enzyme inhibition, enantioselectivity, computational and crystallographic studies and in vivo activity for a new class of intraocular pressure lowering agents. Eur J Med Chem 2018;151:363–75.
- Behnke CA, Le Trong I, Godden JW, et al. Atomic resolution studies of carbonic anhydrase II. Acta Crystallogr D Biol Crystallogr 2010;66:616–27.
- Schrödinger Release 2020-2: Protein Preparation Wizard; Epik, Schrödinger, LLC, New York, NY, 2020; Impact, Schrödinger, LLC, New York, NY; Prime, Schrödinger, LLC, New York, NY, 2020.
- Sastry GM, Adzhigirey M, Day T, Annabhimoju R, Sherman W. Protein and ligand preparation: Parameters, protocols, and influence on virtual screening enrichments. J Comput Aid Mol Des 2013; 27:221–34.
- Santos-Martins D, Forli S, Ramos MJ, Olson AJ. AutoDock4(Zn): an improved AutoDock force field for small-molecule docking to zinc metalloproteins. J Chem Inf Model 2014;54:2371–9.
- Milite C, Amendola G, Nocentini A, et al. Novel 2-substituted-benzimidazole-6-sulfonamides as carbonic anhydrase inhibitors: synthesis, biological evaluation against isoforms I, II, IX and XII and molecular docking studies. J Enzyme Inhib Med Chem 2019;34:1697–710.
- Kennedy CR, Goya Grocin A, Kovačič T, et al. A probe for NLRP3 inflammasome inhibitor MCC950 identifies carbonic anhydrase 2 as a novel target. ACS Chem Biol 2021;16:982–990.
- Nocentini A, Angeli A, Carta F, et al. Reconsidering anion inhibitors in the general context of drug design studies of modulators of activity of the classical enzyme carbonic anhydrase. J Enzyme Inhib Med Chem 2021;36:561–80.
- Pettersen EF, Goddard TD, Huang CC, et al. UCSF Chimera—a visualization system for exploratory research and analysis. J Comput Chem 2004;25:1605–12.