Activation studies of the β-carbonic anhydrases from Malassezia restricta with amines and amino acids

References

• (a) Supuran CT. Carbonic anhydrases: novel therapeutic applications for inhibitors and activators. Nat Rev Drug Discov 2008;7:168–81.
   PubMed Web of Science ®Google Scholar
  (b) Nocentini A, Supuran CT. Advances in the structural annotation of human carbonic anhydrases and impact on future drug discovery. Expert Opin Drug Discov 2019;14:1175–97.
   PubMed Web of Science ®Google Scholar
• (a) Supuran CT. How many carbonic anhydrase inhibition mechanisms exist?. J Enzyme Inhib Med Chem 2016;31:345–60.
   PubMed Web of Science ®Google Scholar
  (b) Supuran CT. Advances in structure-based drug discovery of carbonic anhydrase inhibitors. Expert Opin Drug Discov 2017;12:61–88. (c) Supuran CT. Structure and function of carbonic anhydrases. Biochem J 2016;473:2023–32.
   PubMed Web of Science ®Google Scholar
• (a) Supuran CT. Carbonic anhydrase activators. Future Med Chem 2018;10:561–73.
   PubMed Web of Science ®Google Scholar
  (b) Temperini C, Scozzafava A, Supuran CT. Carbonic anhydrase activation and the drug design. Curr Pharm Des 2008;14:708–15. (c) Akocak S, Supuran CT. Activation of α-, β-, γ- δ-, ζ- and η- class of carbonic anhydrases with amines and amino acids: a review. J Enzyme Inhib Med Chem 2019;34:1652–9.
   PubMed Web of Science ®Google Scholar
• (a) Zoccola D, Innocenti A, Bertucci A, et al. Coral carbonic anhydrases: regulation by ocean acidification. Mar Drugs 2016;14:109.
   Web of Science ®Google Scholar
  (b) Bertucci A, Moya A, Tambutté S, et al. Carbonic anhydrases in anthozoan corals – a review. Bioorg Med Chem 2013;21:1437–50. (c) Del Prete S, Vullo D, Zoccola D, et al. Activation profile analysis of CruCA4, an α-carbonic anhydrase involved in skeleton formation of the mediterranean red coral, Corallium rubrum. Molecules 2017;23:66.(d) Dathan NA, Alterio V, Troiano E, et al. Biochemical characterization of the chloroplastic β-carbonic anhydrase from Flaveria bidentis (L.) "Kuntze". J Enzyme Inhib Med Chem 2014;29:500–4.
   PubMed Web of Science ®Google Scholar
• (a) Capasso C, Supuran CT. An overview of the alpha-, beta- and gamma-carbonic anhydrases from Bacteria: can bacterial carbonic anhydrases shed new light on evolution of bacteria?. J Enzyme Inhib Med Chem 2015;30:325–32.
   PubMed Web of Science ®Google Scholar
  (b) Smith KS, Jakubzick C, Whittam TS, Ferry JG. Carbonic anhydrase is an ancient enzyme widespread in prokaryotes. Proc Natl Acad Sci USA 1999;96:15184–9.
   PubMed Web of Science ®Google Scholar
• (a) Supuran CT. Applications of carbonic anhydrases inhibitors in renal and central nervous system diseases. Expert Opin Ther Pat 2018;28:713–21.
   PubMed Web of Science ®Google Scholar
  (b) Supuran CT. Carbonic anhydrase inhibitors and their potential in a range of therapeutic areas. Expert Opin Ther Pat 2018;28:709–12. (c) Supuran CT. Carbonic anhydrase inhibitors as emerging agents for the treatment and imaging of hypoxic tumors. Expert Opin Investig Drugs 2018;27:963–70. (d) Nocentini A, Supuran CT. Carbonic anhydrase inhibitors as antitumor/antimetastatic agents: a patent review (2008–2018). Expert Opin Ther Pat 201828:729–40.
   PubMed Web of Science ®Google Scholar
• (a) Supuran CT, Capasso C. The eta-class carbonic anhydrases as drug targets for antimalarial agents. Expert Opin Ther Targets 2015;19:551–63.
   PubMed Web of Science ®Google Scholar
  (b) Capasso C, Supuran CT. Bacterial, fungal and protozoan carbonic anhydrases as drug targets. Expert Opin Ther Targets 2015;19:1689–704. (c) Supuran CT, Capasso C. Biomedical applications of prokaryotic carbonic anhydrases. Expert Opin Ther Pat 2018;28:745–54.
   PubMed Web of Science ®Google Scholar
• (a) Ozensoy Guler O, Capasso C, Supuran CT. A magnificent enzyme superfamily: carbonic anhydrases, their purification and characterization. J Enzym Inhib Med Chem 2016;31:689–94.
   PubMed Web of Science ®Google Scholar
  (b) De Simone G, Supuran CT. (In)organic anions as carbonic anhydrase inhibitors. J Inorg Biochem 2012;111:117–29. (c) Supuran CT. Carbonic anhydrase inhibition and the management of hypoxic tumors. Metabolites 2017;7:E48.
   PubMed Web of Science ®Google Scholar
• (a) Alterio V, Esposito D, Monti SM, et al. Crystal structure of the human carbonic anhydrase II adduct with 1-(4-sulfamoylphenyl-ethyl)-2,4,6-triphenylpyridinium perchlorate, a membrane-impermeant, isoform selective inhibitor. J Enzyme Inhib Med Chem 2018;33:151–7.
   PubMed Web of Science ®Google Scholar
  (b) Innocenti A, Vullo D, Scozzafava A, et al. Carbonic anhydrase inhibitors. Inhibition of mammalian isoforms I–XIV with a series of substituted phenols including paracetamol and salicylic acid. Bioorg Med Chem 2008;16:7424–8. (c) Nocentini A, Bonardi A, Gratteri P, et al. Steroids interfere with human carbonic anhydrase activity by using alternative binding mechanisms. J Enzyme Inhib Med Chem 2018;33:1453–9. (d) Tars K, Vullo D, Kazaks A, et al. Sulfocoumarins (1,2-benzoxathiine-2,2-dioxides): a class of potent and isoform-selective inhibitors of tumor-associated carbonic anhydrases. J Med Chem 2013;56:293–300.
   PubMed Web of Science ®Google Scholar
• (a) Del Prete S, Vullo D, Scozzafava A, et al. Cloning, characterization and anion inhibition study of the δ-class carbonic anhydrase (TweCA) from the marine diatom Thalassiosira weissflogii. Bioorg Med Chem 2014;22:531–7.
   PubMed Web of Science ®Google Scholar
  (b) Vullo D, Del Prete S, Osman SM, et al. Sulfonamide inhibition studies of the δ-carbonic anhydrase from the diatom Thalassiosira weissflogii. Bioorg Med Chem Lett 2014;24:275–9. (c) Del Prete S, Vullo D, De Luca V, et al. Biochemical characterization of the δ-carbonic anhydrase from the marine diatom Thalassiosira weissflogii. J Enzyme Inhib Med Chem 2014;29:906–11.
   PubMed Web of Science ®Google Scholar
• (a) Supuran CT, Capasso C. An overview of the bacterial carbonic anhydrases. Metabolites 2017; 7:56.
   PubMed Web of Science ®Google Scholar
  (b) Clare BW, Supuran CT. Carbonic anhydrase activators. 3: structure–activity correlations for a series of isozyme II activators. J Pharm Sci 1994;83:768–73. (c) Supuran CT. Carbonic anhydrases and metabolism. Metabolites 2018;8:25. (d) Supuran CT. Carbon- versus sulphur-based zinc binding groups for carbonic anhydrase inhibitors? J Enzyme Inhib Med Chem 2018;33:485–95.
   PubMed Web of Science ®Google Scholar
• (a) Del Prete S, Vullo D, Fisher GM, et al. Discovery of new family of carbonic anhydrases in the malaria pathogen Plasmodium falciparum- the η-carbonic anhydrases. Bioorg Med Chem 2014;24:4389–96.
   Web of Science ®Google Scholar
  (b) De Simone G, Di Fiore A, Capasso C, Supuran CT. The zinc coordination pattern in the η-carbonic anhydrase from Plasmodium falciparum is different from all other carbonic anhydrase genetic families. Bioorg Med Chem Lett 2015;25:1385–9.
   PubMed Web of Science ®Google Scholar
• Jensen EL, Clement R, Kosta A, et al. A new widespread subclass of carbonic anhydrase in marine phytoplankton. ISME J 2019;13:2094–106.
   PubMed Web of Science ®Google Scholar
• (a) 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.
   PubMed Web of Science ®Google Scholar
  (b) Briganti F, Pierattelli R, Scozzafava A, Supuran CT. Carbonic anhydrase inhibitors. Part 37. Novel classes of carbonic anhydrase inhibitors and their interaction with the native and cobalt-substituted enzyme: kinetic and spectroscopic investigations. Eur J Med Chem 1996;31:1001–10. (c) Neri D, Supuran CT. Interfering with pH regulation in tumours as a therapeutic strategy. Nat Rev Drug Discov 2011;10:767–77. (e) Supuran CT, Vullo D, Manole G, et al. Designing of novel carbonic anhydrase inhibitors and activators. Curr Med Chem Cardiovasc Hematol Agents 2004;2:49–68.
   Web of Science ®Google Scholar
• (a) Pacchiano F, Carta F, McDonald PC, et al. Ureido-substituted benzenesulfonamides potently inhibit carbonic anhydrase IX and show antimetastatic activity in a model of breast cancer metastasis. J Med Chem 2011;54:1896–902.
   PubMed Web of Science ®Google Scholar
  (b) Lou Y, McDonald PC, Oloumi A, et al. Targeting tumor hypoxia: suppression of breast tumor growth and metastasis by novel carbonic anhydrase IX inhibitors. Cancer Res 2011;71:3364–76. (c) Pacchiano F, Aggarwal M, Avvaru BS, et al. Selective hydrophobic pocket binding observed within the carbonic anhydrase II active site accommodate different 4-substituted-ureido-benzenesulfonamides and correlate to inhibitor potency. Chem Commun (Camb) 2010;46:8371–3. (d) Köhler K, Hillebrecht A, Schulze Wischeler J, et al. Saccharin inhibits carbonic anhydrases: possible explanation for its unpleasant metallic aftertaste. Angew Chem Int Ed Engl 2007;46:7697–9.
   PubMed Web of Science ®Google Scholar
• (a) Krall N, Pretto F, Decurtins W, et al. A small‐molecule drug conjugate for the treatment of carbonic anhydrase IX expressing tumors. Angew Chem Int Ed Engl 2014;53:4231–5.
   PubMed Web of Science ®Google Scholar
  (b) El-Gazzar MG, Nafie NH, Nocentini A, et al. Carbonic anhydrase inhibition with a series of novel benzenesulfonamide-triazole conjugates. J Enzyme Inhib Med Chem 2005;20:333–40. (c) Eldehna WM, Abo-Ashour MF, Berrino E, et al. SLC-0111 enaminone analogs, 3/4-(3-aryl-3-oxopropenyl) aminobenzenesulfonamides, as novel selective subnanomolar inhibitors of the tumor-associated carbonic anhydrase isoform IX. Bioorg Chem 2019;83:549–58. (d) Abo-Ashour MF, Eldehna WM, Nocentini A, et al. Novel synthesized SLC-0111 thiazole and thiadiazole analogues: Determination of their carbonic anhydrase inhibitory activity and molecular modeling studies. Bioorg Chem 2019;87:794–802.
   PubMed Web of Science ®Google Scholar
• (a) Akocak S, Lolak N, Nocentini A, et al. Synthesis and biological evaluation of novel aromatic and heterocyclic bis-sulfonamide Schiff bases as carbonic anhydrase I, II, VII and IX inhibitors. Bioorg Med Chem 2017;25:3093–7.
   PubMed Web of Science ®Google Scholar
  (b) Akocak S, Lolak N, Bua S, et al. Synthesis and biological evaluation of novel N,N`-diaryl cyanoguanidines acting as potent and selective carbonic anhydrase II inhibitors. Bioorg Chem 2018;77:245–51. (c) Lolak N, Akocak S, Bua S, et al. Design and synthesis of novel 1,3-diaryltriazene-substituted sulfonamides as potent and selective carbonic anhydrase II inhibitors. Bioorg Chem 2018; 77542–7. (d) Akocak S, Lolak N, Bua S, et al. Discovery of novel 1,3-diaryltriazene sulfonamides as carbonic anhydrase I, II, VII, and IX inhibitors. J Enzyme Inhib Med Chem 2018; 33:1575–80.
   PubMed Web of Science ®Google Scholar
• (a) Lolak N, Akocak S, Bua S, Supuran CT. Design, synthesis and biological evaluation of novel ureido benzenesulfonamides incorporating 1,3,5-triazine moieties as potent carbonic anhydrase IX inhibitors. Bioorg Chem 2019;82:117–22.
   PubMed Web of Science ®Google Scholar
  (b) Lolak N, Akocak S, Bua S, et al. Discovery of new ureido benzenesulfonamides incorporating 1,3,5-triazine moieties as carbonic anhydrase I, II, IX and inhibitors. Bioorg Med Chem 2019;27:1588–94. (c) Shabana AM, Mondal UK, Alam R, et al. pH-sensitive multiligand gold nanoplatform targeting carbonic anhydrase IX enhances the delivery of Doxorubicin to hypoxic tumor spheroids and overcomes the hypoxia-induced chemoresistance. ACS Appl Mater Interfaces 2018;10:17792–808.
   PubMed Web of Science ®Google Scholar
• (a) Briganti F, Mangani S, Orioli P, et al. Carbonic anhydrase activators: X-ray crystallographic and spectroscopic investigations for the interaction of isozymes I and II with histamine. Biochemistry 1997;36:10384–92.
   PubMed Web of Science ®Google Scholar
  (b) Temperini C, Scozzafava A, Vullo D, Supuran CT. Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and crystallographic analysis of their adducts with isoform II: engineering proton-transfer processes within the active site of an enzyme. Chemistry 2006;12:7057–66. (c) Temperini C, Scozzafava A, Vullo D, Supuran CT. Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII, and XIV with L- and D-phenylalanine and crystallographic analysis of their adducts with isozyme II: stereospecific recognition within the active site of an enzyme and its consequences for the drug design. J Med Chem 2006;49:3019–27. (d) Temperini C, Innocenti A, Scozzafava A, Supuran CT. Carbonic anhydrase activators: kinetic and X-ray crystallographic study for the interaction of D- and L-tryptophan with the mammalian isoforms I-XIV. Bioorg Med Chem 2008;16:8373–8. (e) Temperini C, Innocenti A, Scozzafava A, et al. Carbonic anhydrase activators: L-Adrenaline plugs the active site entrance of isozyme II, activating better isoforms I, IV, VA, VII, and XIV. Bioorg Med Chem Lett 2007;17:628–35.
   PubMed Web of Science ®Google Scholar
• (a) De Simone G, Di Fiore A, Truppo E, et al. Exploration of the residues modulating the catalytic features of human carbonic anhydrase XIII by a site-specific mutagenesis approach. J Enzyme Inhib Med Chem 2019;34:1506–10.
   PubMed Web of Science ®Google Scholar
  (b) Buonanno M, Di Fiore A, Langella E, et al. The crystal structure of a hCA VII variant provides insights into the molecular determinants responsible for its catalytic behavior. Int J Mol Sci 2018;19:1571. (c) Mikulski R, West D, Sippel KH, et al. Water networks in fast proton transfer during catalysis by human carbonic anhydrase II. Biochemistry 2013;52:125–31.
   Web of Science ®Google Scholar
• (a) Akocak S, Lolak N, Vullo D, et al. Synthesis and biological evaluation of histamine Schiff bases as carbonic anhydrase I, II, IV, VII, and IX activators. J Enzyme Inhib Med Chem 2017;32:1305–12.
   PubMed Web of Science ®Google Scholar
  (b) Akocak S, Lolak N, Bua S, et al. α-Carbonic anhydrases are strongly activated by spinaceamine derivatives. Bioorg Med Chem 2019;27:800–4. (c) Akocak S, Lolak N, Bua S, et al. Activation of human α-carbonic anhydrase isoforms I, II, IV and VII with bis-histamine Schiff bases and bis-spinaceamine substituted derivatives. J Enzyme Inhib Med Chem 2019;34:1193–8. (d) Dave K, Scozzafava A, Vullo D, et al. Pyridinium derivatives of histamine are potent activators of cytosolic carbonic anhydrase isoforms, I, II and VII. Org Biomol Chem 2011;9:2790–800. (e) Dave K, Ilies MA, Scozzafava A, et al. An inhibitor-like binding mode of a carbonic anhydrase activator within the active site of isoform II. Bioorg Med Chem Lett 2011;21:2764–8.
   PubMed Web of Science ®Google Scholar
• (a) Bhatt A, Mondal UK, Supuran CT, et al. Crystal structure of carbonic anhydrase ii in complex with an activating ligand: implications in neuronal function. Mol Neurobiol 2018;55:7431–7.
   PubMed Web of Science ®Google Scholar
  (b) Temperini C, Scozzafava A, Supuran CT. Carbonic anhydrase activators: the first X-ray crystallographic study of an adduct of isoform I. Bioorg Med Chem Lett 2006;16:5152–6. (c) Temperini C, Scozzafava A, Puccetti L, Supuran CT. Carbonic anhydrase activators: X-ray crystal structure of the adduct of human isozyme II with L-histidine as a platform for the design of stronger activators. Bioorg Med Chem Lett 2005;15:5136–41. (d) Draghici B, Vullo D, Akocak S, et al. Ethylene bis-imidazoles are highly potent and selective activators for isozymes VA and VII of carbonic anhydrase, with a potential nootropic effect. Chem Commun 2014;50:5980–3.
   PubMed Web of Science ®Google Scholar
• (a) Canto de Souza L, Provensi G, Vullo D, et al. Carbonic anhydrase activation enhances object recognition memory in mice through phosphorylation of the extracellular signal-regulated kinase in the cortex and the hippocampus. Neuropharmacology 2017;118:148–56.
   PubMed Web of Science ®Google Scholar
  (b) Sanku RKK, John JS, Salkovitz M, et al. Potential learning and memory disruptors and enhancers in a simple, 1-day operant task in mice. Behavioural Pharmacol 2018;29:482–92. (c) Wang X, Schröder HC, Schlossmacher U, et al. Modulation of the initial mineralization process of SaOS-2 cells by carbonic anhydrase activators and polyphosphate. Calcif Tissue Int 2014;94:495–509.
   PubMed Web of Science ®Google Scholar
• (a) Del Prete S, Vullo D, Ghobril C, et al. Cloning, purification, and characterization of a β-carbonic anhydrase from Malassezia restricta, an opportunistic pathogen involved in dandruff and seborrheic dermatitis. Int J Mol Sci 2019;20:2447.
   PubMed Web of Science ®Google Scholar
  (b) Prete SD, Angeli A, Ghobril C, et al. Anion inhibition profile of the β-carbonic anhydrase from the opportunist pathogenic fungus Malassezia restricta involved in dandruff and seborrheic dermatitis. Metabolites 2019;9:E147. (c) Del Prete S, Angeli A, Ghobril C, et al. Sulfonamide inhibition profile of the β-carbonic anhydrase from Malassezia restricta, an opportunistic pathogen triggering scalp conditions. Metabolites 2020;10:39.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• (a) Vullo D, Innocenti A, Nishimori I, et al. Carbonic anhydrase activators: Activation of the human isoforms VII (cytosolic) and XIV (transmembrane) with amino acids and amines. Bioorg Med Chem Lett 2007;17:4107–12.
   PubMed Web of Science ®Google Scholar
  (b) Pastorekova S, Vullo D, Nishimori I, et al. Carbonic anhydrase activators: Activation of the human tumor-associated isozymes IX and XII with amino acids and amines. Bioorg Med Chem 2008;16:3530–6. (c) Innocenti A, Hilvo M, Parkkila S, et al. Carbonic anhydrase activators: activation of the membrane-associated isoform XV with amino acids and amines. Bioorg Med Chem Lett 2009;19:3430–3.
   PubMed Web of Science ®Google Scholar
• (a) Innocenti A, Zimmerman SA, Scozzafava A, et al. Carbonic anhydrase activators: Activation of the archaeal β-class (Cab) and γ-class (Cam) carbonic anhydrases with amino acids and amines. Bioorg Med Chem Lett 2008;18:6194–8.
   PubMed Web of Science ®Google Scholar
  (b) Vullo D, Del Prete S, Capasso C, Supuran CT. Carbonic anhydrase activators: activation of the β-carbonic anhydrase from Malassezia globosa with amino acids and amines. Bioorg Med Chem Lett 2016;26:1381–5. (c) Isik S, Kockar F, Aydin M, et al. Carbonic anhydrase activators: activation of the β-carbonic anhydrase Nce103 from the yeast Saccharomyces cerevisiae with amino acids and amines. Bioorg Med Chem Lett 2009;19:1662–5.
   PubMed Web of Science ®Google Scholar
• Innocenti A, Leewattanapasuk W, Manole G, et al. Carbonic anhydrase activators: activation of the β-carbonic anhydrase from the pathogenic yeast Candida glabrata with amino acids and amines. Bioorg Med Chem Lett 2010;20:1701–4.
   PubMed Web of Science ®Google Scholar
• (a) Angeli A, Del Prete S, Osman SM, et al. Activation studies of the α- and β-carbonic anhydrases from the pathogenic bacterium Vibrio cholerae with amines and amino acids. J Enzyme Inhib Med Chem 2018;33:227–33.
   PubMed Web of Science ®Google Scholar
  (b) Angeli A, Del Prete S, Donald WA, et al. The γ-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae is potently activated by amines and amino acids. Bioorg Chem 2018;77:1–5. (c) Angeli A, Del Prete S, Osman SM, et al. Activation studies with amines and amino acids of the β-carbonic anhydrase encoded by the Rv3273 gene from the pathogenic bacterium Mycobacterium tuberculosis. J Enzyme Inhib Med Chem 2018;33:364–9.
   PubMed Web of Science ®Google Scholar
• (a) Angeli A, Del Prete S, Pinteala M, et al. The first activation study of the β-carbonic anhydrases from the pathogenic bacteria Brucella suis and Francisella tularensis with amines and amino acids. J Enzyme Inhib Med Chem 2019;34:1178–85.
   PubMed Web of Science ®Google Scholar
  (b) Stefanucci A, Angeli A, Dimmito MP, et al. Activation of β- and γ-carbonic anhydrases from pathogenic bacteria with tripeptides. J Enzyme Inhib Med Chem 2018;33:945–50. (c) Bua S, Haapanen S, Kuuslahti M, et al. Activation studies of the β-carbonic anhydrase from the pathogenic protozoan Entamoeba histolytica with amino acids and amines. Metabolites 2019;9:26–33.
   PubMed Web of Science ®Google Scholar
• (a) Vullo D, Del Prete S, Osman SM, et al. Burkholderia pseudomallei γ-carbonic anhydrase is strongly activated by amino acids and amines. Bioorg Med Chem Lett 2017;27:77–80.
   PubMed Web of Science ®Google Scholar
  (b) Vullo D, Del Prete S, Osman SM, et al. Comparison of the amine/amino acid activation profiles of the β- and γ-carbonic anhydrases from the pathogenic bacterium Burkholderia pseudomallei. J Enzyme Inhib Med Chem 2018;33:25–30.
   PubMed Web of Science ®Google Scholar
• (a) Angeli A, Del Prete S, Osman SM, et al. Activation studies of the γ-carbonic anhydrases from the Antarctic marine bacteria Pseudoalteromonas haloplanktis and Colwellia psychrerythraea with amino acids and amines. Marine Drugs 2019;17:238–46.
   Web of Science ®Google Scholar
  (b) Angeli A, Alasmary FAS, Del Prete S, et al. The first study of a δ-carbonic anhydrase: TweCAδ from the diatom Thalassiosira weissflogii is effectively activated by amines and amino acids. J Enzyme Inhib Med Chem 2018;33:680–5. (c) Angeli A, Buonanno M, Donald WA, et al. The zinc – but not cadmium – containing ζ-carbonic from the diatom Thalassiosira weissflogii is potently activated by amines and amino acids. Bioorg Chem 2018;80:261–5.
   PubMed Web of Science ®Google Scholar
• (a) Angeli A, Del Prete S, Alasmary FAS, et al. The first activation studies of the η-carbonic anhydrase from the malaria parasite Plasmodium falciparum with amines and amino acids. Bioorg Chem 2018; 80:94–8.
   PubMed Web of Science ®Google Scholar
  (b) Angeli A, Donald WA, Parkkila S, Supuran CT. Activation studies with amines and amino acids of the β-carbonic anhydrase from the pathogenic protozoan Leishmania donovani chagasi. Bioorg Chem 2018;78:406–10.
   PubMed Web of Science ®Google Scholar
• Capasso C, Supuran CT, Protozoan, fungal and bacterial carbonic anhydrases targeting for obtaining antiinfectives. In: Supuran CT, Capasso, C. ed. Targeting carbonic anhydrases. London: Future Science Ltd.; 2014:133–141.
   Google Scholar
  (b) Schlicker C, Hall RA, Vullo D, et al. Structure and inhibition of the CO2-sensing carbonic anhydrase Can2 from the pathogenic fungus Cryptococcus neoformans. J Mol Biol 2009;385:1207–20.
   PubMed Web of Science ®Google Scholar
• Hewitson KS, Vullo D, Scozzafava A, et al. Molecular cloning, characterization and inhibition studies of a β-carbonic anhydrase from Malassezia globosa, a potential antidandruff target. J Med Chem 2012;55:3513–20.
   PubMed Web of Science ®Google Scholar
• Nguyen GTH, Tran TN, Podgorski MN, et al. Nanoscale ion emitters in native mass spectrometry for measuring ligand-protein binding affinities. ACS Cent Sci 2019;5:308–18.
   PubMed Web of Science ®Google Scholar