*

Institute of Biosciences and Bioresources

National Research Council of Italy

Clemente Capasso

Role: Researcher
Section: Researchers and Technologists
Division: Naples
Tel: (39) 081-6132559-081-6132558
E-mail: clemente.capasso@ibbr.cnr.it


Name: Clemente Capasso

Date and Place of Birth: 22.07.1965, Napoli, Italy

Address: Institute of Biosciences and Bioresources, National Research Council, - Via Pietro Castellino 111- 80131, Napoli, Italy,

Tel: ++39 0816132558,

E-mail: clemente.capasso@ibbr.cnr.it

Education and Training

(From 1992-present)

1992 Achieved the master degree in Biology cum laude at University of Naples “Federico II”.

1993-1994 Post-Laurea training: University Federico II of Naples, Department of Evolutionary and Comparative Biology. Mentor: Prof. Elio Parisi.-Works on metallothioneins (MTs) in marine and terrestrial organisms

1993-1994 Awarded a C.N.R. fellowship: CNR. Institute of Protein Biochemistry and Enzymology of Naples. Mentor: Prof. Elio Parisi. Continues work on MTs.

1/10/1994-1/12/1994 Visiting Scientist: Biological Station of Roscoff (France, CNR/CNRS cooperation). Works on metal-binding proteins in bacteria.

1995-1996 Awarded a CNR fellowship: University of Genova, Italy. Works on protein crystallization (serine proteinases, superoxide dismutase, and hexokinase).

1/10/1996-31/12/2013 Researcher at CNR-Institute of Protein Biochemistry and Enzymology, Naples, Italy. Principal investigator of the scientific project: "Cloning, heterologous expression and structure of proteins and enzymes from Antarctic organisms". Works on multigene family proteins (metallothioneins, aspartic proteinases, and carbonic anhydrases).

12/05/1997-09/07/1997 Visiting Scientist: School of Molecular and Medical Biosciences, University College, Cardiff. Works on the expression of heterologous proteins (MTs and aspartic proteinases) in E. coli.

2003-2004 Research Associate: University of Southern California Keck School of Medicine, Los Angeles, CA. Works on human 5-lipoxygenase.

1/12/2014-present Researcher at CNR- Institute of Biosciences and Bioresources (IBBR). Principal investigator of the scientific projects: 1) Evolution, adaptation, and biodiversity of carbonic anhydrases from Antarctic organisms; 2) Capture of the CO2 from flue gases by using enzymes from moderately thermophilic microorganisms.

Scientific Activities

Clemente Capasso obtained his MSc in biology cum laude at the University of Naples ‘Federico II’ (Italy). His research interest at the Italian National Research Council (CNR; Rome, Italy) from 1992 to date has been the study of the structure/function relationship of both native and recombinant proteins from terrestrial and marine organisms. In particular, he studied metallothioneins and aspartic proteinases in Echinoderms and Antarctic fish. This research activity has allowed him to acquire extensive knowledge of most protein purification procedures as well as kinetic, chemical-physical, and structural characterization of enzymes. He also has experience with molecular biology techniques, such as nucleic acid isolation, cloning, and expression of recombinant proteins and enzymes in Escherichia coli. Recently, his research activity has been focused on the investigation of enzymes involved in the hydration of CO2 (carbonic anhydrases) in extremophilic microorganisms. The preliminary results of this study are helpful in developing new methodologies for the use of enzymatic systems in biotechnologies. All of these activities have led to more than 150 publications in peer-reviewed journals. He has a long and strong scientific background, developed over 15 years of experience acquired by intense training in Italian and international laboratories. He is the Associate Editor of Journal of Enzyme Inhibition and Medicinal Chemistry and is on the Editorial Board of the Expert Opinion on Therapeutic Patents, Current Enzyme Inhibition, and International Journal of Molecular Science.

Recent publications

Journal Articles

[1] M. Mori, C. Capasso, F. Carta, W.A. Donald, C.T. Supuran, A deadly spillover: SARS-CoV-2 outbreak, Expert Opin Ther Pat (2020) 1-5.

[2] G. Salbitani, S. Del Prete, F. Bolinesi, O. Mangoni, V. De Luca, V. Carginale, W.A. Donald, C.T. Supuran, S. Carfagna, C. Capasso, Use of an immobilised thermostable alpha-CA (SspCA) for enhancing the metabolic efficiency of the freshwater green microalga Chlorella sorokiniana, J Enzyme Inhib Med Chem 35(1) (2020) 913-920.

[3] O. Ozensoy Guler, C.T. Supuran, C. Capasso, Carbonic anhydrase IX as a novel candidate in liquid biopsy, J Enzyme Inhib Med Chem 35(1) (2020) 255-260.

[4] M. Logozzi, D. Mizzoni, C. Capasso, S. Del Prete, R. Di Raimo, M. Falchi, D.F. Angelini, A. Sciarra, M. Maggi, C.T. Supuran, S. Fais, Plasmatic exosomes from prostate cancer patients show increased carbonic anhydrase IX expression and activity and low pH, J Enzyme Inhib Med Chem 35(1) (2020) 280-288.

[5] S. Del Prete, A. Nocentini, C.T. Supuran, C. Capasso, Bacterial iota-carbonic anhydrase: a new active class of carbonic anhydrase identified in the genome of the Gram-negative bacterium Burkholderia territorii, J Enzyme Inhib Med Chem 35(1) (2020) 1060-1068.

[6] S. Del Prete, A. Angeli, C. Ghobril, J. Hitce, C. Clavaud, X. Marat, C.T. Supuran, C. Capasso, Sulfonamide Inhibition Profile of the beta-Carbonic Anhydrase from Malassezia restricta, An Opportunistic Pathogen Triggering Scalp Conditions, Metabolites 10(1) (2020).

[7] A. Angeli, S.D. Prete, C. Ghobril, J. Hitce, C. Clavaud, X. Marrat, W.A. Donald, C. Capasso, C.T. Supuran, Activation studies of the beta-carbonic anhydrases from Malassezia restricta with amines and amino acids, J Enzyme Inhib Med Chem 35(1) (2020) 824-830.

[8] A. Angeli, M. Pinteala, S.S. Maier, B.C. Simionescu, A. Milaneschi, G. Abbas, S. Del Prete, C. Capasso, A. Capperucci, D. Tanini, F. Carta, C.T. Supuran, Evaluation of Thio- and Seleno-Acetamides Bearing Benzenesulfonamide as Inhibitor of Carbonic Anhydrases from Different Pathogenic Bacteria, Int J Mol Sci 21(2) (2020).

[9] S.A. Alissa, H.A. Alghulikah, A.L. ZA, S.M. Osman, S. Del Prete, C. Capasso, A. Nocentini, C.T. Supuran, Inhibition survey with phenolic compounds against the delta- and eta-class carbonic anhydrases from the marine diatom thalassiosira weissflogii and protozoan Plasmodium falciparum, J Enzyme Inhib Med Chem 35(1) (2020) 377-382.

[10] S.A. Alissa, H.A. Alghulikah, Z.A. Alothman, S.M. Osman, S. Del Prete, C. Capasso, A. Nocentini, C.T. Supuran, Phosphonamidates are the first phosphorus-based zinc binding motif to show inhibition of beta-class carbonic anhydrases from bacteria, fungi, and protozoa, J Enzyme Inhib Med Chem 35(1) (2020) 59-64.

[11] M. Ronci, S. Del Prete, V. Puca, S. Carradori, V. Carginale, R. Muraro, G. Mincione, A. Aceto, F. Sisto, C.T. Supuran, R. Grande, C. Capasso, Identification and characterization of the alpha-CA in the outer membrane vesicles produced by Helicobacter pylori, J Enzyme Inhib Med Chem 34(1) (2019) 189-195.

[12] A. Rogato, S. Del Prete, A. Nocentini, V. Carginale, C.T. Supuran, C. Capasso, Phaeodactylum tricornutum as a model organism for testing the membrane penetrability of sulphonamide carbonic anhydrase inhibitors, J Enzyme Inhib Med Chem 34(1) (2019) 510-518.

[13] S.D. Prete, A. Angeli, C. Ghobril, J. Hitce, C. Clavaud, X. Marat, C.T. Supuran, C. Capasso, Anion Inhibition Profile of the beta-Carbonic Anhydrase from the Opportunist Pathogenic Fungus Malassezia Restricta Involved in Dandruff and Seborrheic Dermatitis, Metabolites 9(7) (2019).

[14] A. Nocentini, S.M. Osman, S. Del Prete, C. Capasso, A.L. ZA, C.T. Supuran, Extending the gamma-class carbonic anhydrases inhibition profiles with phenolic compounds, Bioorg Chem 93 (2019) 103336.

[15] R. Merlo, S. Del Prete, A. Valenti, R. Mattossovich, V. Carginale, C.T. Supuran, C. Capasso, G. Perugino, An AGT-based protein-tag system for the labelling and surface immobilization of enzymes on E. coli outer membrane, J Enzyme Inhib Med Chem 34(1) (2019) 490-499.

[16] M. Logozzi, C. Capasso, R. Di Raimo, S. Del Prete, D. Mizzoni, M. Falchi, C.T. Supuran, S. Fais, Prostate cancer cells and exosomes in acidic condition show increased carbonic anhydrase IX expression and activity, J Enzyme Inhib Med Chem 34(1) (2019) 272-278.

[17] H. Kucukbay, N. Bugday, F.Z. Kucukbay, E. Berrino, G. Bartolucci, S. Del Prete, C. Capasso, C.T. Supuran, Synthesis and carbonic anhydrase inhibitory properties of novel 4-(2-aminoethyl)benzenesulfonamide-dipeptide conjugates, Bioorg Chem 83 (2019) 414-423.

[18] R. Gitto, L. De Luca, F. Mancuso, S. Del Prete, D. Vullo, C.T. Supuran, C. Capasso, Seeking new approach for therapeutic treatment of cholera disease via inhibition of bacterial carbonic anhydrases: experimental and theoretical studies for sixteen benzenesulfonamide derivatives, J Enzyme Inhib Med Chem 34(1) (2019) 1186-1192.

[19] S. Distinto, R. Meleddu, F. Ortuso, F. Cottiglia, S. Deplano, L. Sequeira, C. Melis, B. Fois, A. Angeli, C. Capasso, R. Angius, S. Alcaro, C.T. Supuran, E. Maccioni, Exploring new structural features of the 4-[(3-methyl-4-aryl-2.3-dihydro-1.3-thiazol-2-ylidene)amino]benzenesulphonamide scaffold for the inhibition of human carbonic anhydrases, J Enzyme Inhib Med Chem 34(1) (2019) 1526-1533.

[20] S. Del Prete, D. Vullo, C. Ghobril, J. Hitce, C. Clavaud, X. Marat, C. Capasso, C.T. Supuran, Cloning, Purification, and Characterization of a beta-Carbonic Anhydrase from Malassezia restricta, an Opportunistic Pathogen Involved in Dandruff and Seborrheic Dermatitis, Int J Mol Sci 20(10) (2019).

[21] S. Del Prete, R. Merlo, A. Valenti, R. Mattossovich, M. Rossi, V. Carginale, C.T. Supuran, G. Perugino, C. Capasso, Thermostability enhancement of the alpha-carbonic anhydrase from Sulfurihydrogenibium yellowstonense by using the anchoring-and-self-labelling-protein-tag system (ASL(tag)), J Enzyme Inhib Med Chem 34(1) (2019) 946-954.

[22] S. Del Prete, S. Bua, F.A.S. Alasmary, Z. AlOthman, S. Tambutte, D. Zoccola, C.T. Supuran, C. Capasso, Comparison of the Sulfonamide Inhibition Profiles of the alpha-Carbonic Anhydrase Isoforms (SpiCA1, SpiCA2 and SpiCA3) Encoded by the Genome of the Scleractinian Coral Stylophora pistillata, Mar Drugs 17(3) (2019).

[23] S. Bua, S.M. Osman, S. Del Prete, C. Capasso, Z. AlOthman, A. Nocentini, C.T. Supuran, Click-tailed benzenesulfonamides as potent bacterial carbonic anhydrase inhibitors for targeting Mycobacterium tuberculosis and Vibrio cholerae, Bioorg Chem 86 (2019) 183-186.

[24] A. Angeli, M. Pinteala, S.S. Maier, S. Del Prete, C. Capasso, B.C. Simionescu, C.T. Supuran, Inhibition of alpha-, beta-, gamma-, delta-, zeta- and eta-class carbonic anhydrases from bacteria, fungi, algae, diatoms and protozoans with famotidine, J Enzyme Inhib Med Chem 34(1) (2019) 644-650.

[25] A. Angeli, M. Pinteala, S.S. Maier, S. Del Prete, C. Capasso, B.C. Simionescu, C.T. Supuran, Inhibition of bacterial alpha-, beta- and gamma-class carbonic anhydrases with selenazoles incorporating benzenesulfonamide moieties, J Enzyme Inhib Med Chem 34(1) (2019) 244-249.

[26] A. Angeli, S. Del Prete, M. Pinteala, S.S. Maier, W.A. Donald, B.C. Simionescu, C. Capasso, C.T. Supuran, The first activation study of the beta-carbonic anhydrases from the pathogenic bacteria Brucella suis and Francisella tularensis with amines and amino acids, J Enzyme Inhib Med Chem 34(1) (2019) 1178-1185.

[27] A. Angeli, S. Del Prete, S.M. Osman, Z. AlOthman, W.A. Donald, C. Capasso, C.T. Supuran, Activation Studies of the gamma-Carbonic Anhydrases from the Antarctic Marine Bacteria Pseudoalteromonas haloplanktis and Colwellia psychrerythraea with Amino Acids and Amines, Mar Drugs 17(4) (2019).

[28] D. Vullo, S. Del Prete, S.M. Osman, F.A.S. Alasmary, Z. AlOthman, W.A. Donald, C. Capasso, C.T. Supuran, Comparison of the amine/amino acid activation profiles of the beta- and gamma-carbonic anhydrases from the pathogenic bacterium Burkholderia pseudomallei, J Enzyme Inhib Med Chem 33(1) (2018) 25-30.

[29] C.T. Supuran, C. Capasso, Biomedical applications of prokaryotic carbonic anhydrases, Expert Opin Ther Pat 28(10) (2018) 745-754.

[30] A. Stefanucci, A. Angeli, M.P. Dimmito, G. Luisi, S. Del Prete, C. Capasso, W.A. Donald, A. Mollica, C.T. Supuran, Activation of beta- and gamma-carbonic anhydrases from pathogenic bacteria with tripeptides, J Enzyme Inhib Med Chem 33(1) (2018) 945-950.

[31] A. Nocentini, S. Bua, S. Del Prete, Y.E. Heravi, A.A. Saboury, A. Karioti, A.R. Bilia, C. Capasso, P. Gratteri, C.T. Supuran, Natural Polyphenols Selectively Inhibit beta-Carbonic Anhydrase from the Dandruff-Producing Fungus Malassezia globosa: Activity and Modeling Studies, ChemMedChem 13(8) (2018) 816-823.

[32] C. Melis, S. Distinto, G. Bianco, R. Meleddu, F. Cottiglia, B. Fois, D. Taverna, R. Angius, S. Alcaro, F. Ortuso, M. Gaspari, A. Angeli, S. Del Prete, C. Capasso, C.T. Supuran, E. Maccioni, Targeting Tumor Associated Carbonic Anhydrases IX and XII: Highly Isozyme Selective Coumarin and Psoralen Inhibitors, ACS Med Chem Lett 9(7) (2018) 725-729.

[33] R. Meleddu, S. Distinto, F. Cottiglia, R. Angius, M. Gaspari, D. Taverna, C. Melis, A. Angeli, G. Bianco, S. Deplano, B. Fois, S. Del Prete, C. Capasso, S. Alcaro, F. Ortuso, M. Yanez, C.T. Supuran, E. Maccioni, Tuning the Dual Inhibition of Carbonic Anhydrase and Cyclooxygenase by Dihydrothiazole Benzensulfonamides, ACS Med Chem Lett 9(10) (2018) 1045-1050.

[34] S. Del Prete, D. Vullo, N. Caminiti-Segonds, D. Zoccola, S. Tambutte, C.T. Supuran, C. Capasso, Protonography and anion inhibition profile of the alpha-carbonic anhydrase (CruCA4) identified in the Mediterranean red coral Corallium rubrum, Bioorg Chem 76 (2018) 281-287.

[35] S. Del Prete, S. Bua, D. Zoccola, F.A.S. Alasmary, Z. AlOthman, L.S. Alqahtani, N. Techer, C.T. Supuran, S. Tambutte, C. Capasso, Comparison of the Anion Inhibition Profiles of the alpha-CA Isoforms (SpiCA1, SpiCA2 and SpiCA3) from the Scleractinian Coral Stylophora pistillata, Int J Mol Sci 19(7) (2018).

[36] L. De Luca, F. Mancuso, S. Ferro, M.R. Buemi, A. Angeli, S. Del Prete, C. Capasso, C.T. Supuran, R. Gitto, Inhibitory effects and structural insights for a novel series of coumarin-based compounds that selectively target human CA IX and CA XII carbonic anhydrases, Eur J Med Chem 143 (2018) 276-282.

[37] S. Bua, M. Bozdag, S. Del Prete, F. Carta, W.A. Donald, C. Capasso, C.T. Supuran, Mono- and di-thiocarbamate inhibition studies of the delta-carbonic anhydrase TweCAdelta from the marine diatom Thalassiosira weissflogii, J Enzyme Inhib Med Chem 33(1) (2018) 707-713.

[38] S. Bua, E. Berrino, S. Del Prete, V.S. Murthy, V. Vijayakumar, Y. Tamboli, C. Capasso, E. Cerbai, A. Mugelli, F. Carta, C.T. Supuran, Synthesis of novel benzenesulfamide derivatives with inhibitory activity against human cytosolic carbonic anhydrase I and II and Vibrio cholerae alpha- and beta-class enzymes, J Enzyme Inhib Med Chem 33(1) (2018) 1125-1136.

[39] E. Berrino, M. Bozdag, S. Del Prete, F.A.S. Alasmary, L.S. Alqahtani, Z. AlOthman, C. Capasso, C.T. Supuran, Inhibition of alpha-, beta-, gamma-, and delta-carbonic anhydrases from bacteria and diatoms with N’-aryl-N-hydroxy-ureas, J Enzyme Inhib Med Chem 33(1) (2018) 1194-1198.

[40] G. Annunziato, L. Giovati, A. Angeli, M. Pavone, S. Del Prete, M. Pieroni, C. Capasso, A. Bruno, S. Conti, W. Magliani, C.T. Supuran, G. Costantino, Discovering a new class of antifungal agents that selectively inhibits microbial carbonic anhydrases, J Enzyme Inhib Med Chem 33(1) (2018) 1537-1544.

[41] A. Angeli, S. Del Prete, S.M. Osman, F.A.S. Alasmary, Z. AlOthman, W.A. Donald, C. Capasso, C.T. Supuran, Activation studies of the alpha- and beta-carbonic anhydrases from the pathogenic bacterium Vibrio cholerae with amines and amino acids, J Enzyme Inhib Med Chem 33(1) (2018) 227-233.

[42] A. Angeli, S. Del Prete, S.M. Osman, F.A.S. Alasmary, Z. AlOthman, W.A. Donald, C. Capasso, C.T. Supuran, Activation studies with amines and amino acids of the beta-carbonic anhydrase encoded by the Rv3273 gene from the pathogenic bacterium Mycobacterium tuberculosis, J Enzyme Inhib Med Chem 33(1) (2018) 364-369.

[43] A. Angeli, S. Del Prete, W.A. Donald, C. Capasso, C.T. Supuran, The gamma-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae is potently activated by amines and amino acids, Bioorg Chem 77 (2018) 1-5.

[44] A. Angeli, S. Del Prete, F.A.S. Alasmary, L.S. Alqahtani, Z. AlOthman, W.A. Donald, C. Capasso, C.T. Supuran, The first activation studies of the eta-carbonic anhydrase from the malaria parasite Plasmodium falciparum with amines and amino acids, Bioorg Chem 80 (2018) 94-98.

[45] A. Angeli, F.A.S. Alasmary, S. Del Prete, S.M. Osman, Z. AlOthman, W.A. Donald, C. Capasso, C.T. Supuran, The first activation study of a delta-carbonic anhydrase: TweCAdelta from the diatom Thalassiosira weissflogii is effectively activated by amines and amino acids, J Enzyme Inhib Med Chem 33(1) (2018) 680-685.

[46] A. Angeli, G. Abbas, S. Del Prete, C. Capasso, C.T. Supuran, Selenides bearing benzenesulfonamide show potent inhibition activity against carbonic anhydrases from pathogenic bacteria Vibrio cholerae and Burkholderia pseudomallei, Bioorg Chem 79 (2018) 319-322.

[47] D. Vullo, S. Del Prete, S.M. Osman, Z. AlOthman, C. Capasso, W.A. Donald, C.T. Supuran, Burkholderia pseudomallei gamma-carbonic anhydrase is strongly activated by amino acids and amines, Bioorg Med Chem Lett 27(1) (2017) 77-80.

[48] D. Vullo, S. Del Prete, A. Nocentini, S.M. Osman, Z. AlOthman, C. Capasso, M. Bozdag, F. Carta, P. Gratteri, C.T. Supuran, Dithiocarbamates effectively inhibit the beta-carbonic anhydrase from the dandruff-producing fungus Malassezia globosa, Bioorg Med Chem 25(3) (2017) 1260-1265.

[49] D. Vullo, S. Del Prete, P. Di Fonzo, V. Carginale, W.A. Donald, C.T. Supuran, C. Capasso, Comparison of the Sulfonamide Inhibition Profiles of the beta- and gamma-Carbonic Anhydrases from the Pathogenic Bacterium Burkholderia pseudomallei, Molecules 22(3) (2017).

[50] C.T. Supuran, C. Capasso, Carbonic Anhydrase from Porphyromonas Gingivalis as a Drug Target, Pathogens 6(3) (2017).

[51] C.T. Supuran, C. Capasso, An Overview of the Bacterial Carbonic Anhydrases, Metabolites 7(4) (2017).

[52] R. Perfetto, S. Del Prete, D. Vullo, G. Sansone, C.M.A. Barone, M. Rossi, C.T. Supuran, C. Capasso, Production and covalent immobilisation of the recombinant bacterial carbonic anhydrase (SspCA) onto magnetic nanoparticles, J Enzyme Inhib Med Chem 32(1) (2017) 759-766.

[53] R. Perfetto, S. Del Prete, D. Vullo, G. Sansone, C.M.A. Barone, M. Rossi, C.T. Supuran, C. Capasso, Sequence Analysis, Kinetic Constants, and Anion Inhibition Profile of the Nacrein-Like Protein (CgiNAP2X1) from the Pacific Oyster Magallana gigas (Ex-Crassostrea gigas), Mar Drugs 15(9) (2017).

[54] R. Perfetto, S. Del Prete, D. Vullo, G. Sansone, C. Barone, M. Rossi, C.T. Supuran, C. Capasso, Biochemical characterization of the native alpha-carbonic anhydrase purified from the mantle of the Mediterranean mussel, Mytilus galloprovincialis, J Enzyme Inhib Med Chem 32(1) (2017) 632-639.

[55] R. Perfetto, S. Del Prete, D. Vullo, V. Carginale, G. Sansone, C.M.A. Barone, M. Rossi, F.A.S. Alasmary, S.M. Osman, Z. AlOthman, C.T. Supuran, C. Capasso, Cloning, expression and purification of the alpha-carbonic anhydrase from the mantle of the Mediterranean mussel, Mytilus galloprovincialis, J Enzyme Inhib Med Chem 32(1) (2017) 1029-1035.

[56] A. Nocentini, D. Vullo, S. Del Prete, S.M. Osman, F.A.S. Alasmary, Z. AlOthman, C. Capasso, F. Carta, P. Gratteri, C.T. Supuran, Inhibition of the beta-carbonic anhydrase from the dandruff-producing fungus Malassezia globosa with monothiocarbamates, J Enzyme Inhib Med Chem 32(1) (2017) 1064-1070.

[57] A. Nocentini, R. Cadoni, S. Del Prete, C. Capasso, P. Dumy, P. Gratteri, C.T. Supuran, J.Y. Winum, Benzoxaboroles as Efficient Inhibitors of the beta-Carbonic Anhydrases from Pathogenic Fungi: Activity and Modeling Study, ACS Med Chem Lett 8(11) (2017) 1194-1198.

[58] C. Melis, R. Meleddu, A. Angeli, S. Distinto, G. Bianco, C. Capasso, F. Cottiglia, R. Angius, C.T. Supuran, E. Maccioni, Isatin: a privileged scaffold for the design of carbonic anhydrase inhibitors, J Enzyme Inhib Med Chem 32(1) (2017) 68-73.

[59] R. Kumar, S. Bua, S. Ram, S. Del Prete, C. Capasso, C.T. Supuran, P.K. Sharma, Benzenesulfonamide bearing imidazothiadiazole and thiazolotriazole scaffolds as potent tumor associated human carbonic anhydrase IX and XII inhibitors, Bioorg Med Chem 25(3) (2017) 1286-1293.

[60] G.M. Fisher, S. Bua, S. Del Prete, M.S. Arnold, C. Capasso, C.T. Supuran, K.T. Andrews, S.A. Poulsen, Investigating the antiplasmodial activity of primary sulfonamide compounds identified in open source malaria data, Int J Parasitol Drugs Drug Resist 7(1) (2017) 61-70.

[61] Y. Entezari Heravi, S. Bua, A. Nocentini, S. Del Prete, A.A. Saboury, H. Sereshti, C. Capasso, P. Gratteri, C.T. Supuran, Inhibition of Malassezia globosa carbonic anhydrase with phenols, Bioorg Med Chem 25(9) (2017) 2577-2582.

[62] S. Del Prete, D. Vullo, D. Zoccola, S. Tambutte, C.T. Supuran, C. Capasso, Activation Profile Analysis of CruCA4, an alpha-Carbonic Anhydrase Involved in Skeleton Formation of the Mediterranean Red Coral, Corallium rubrum, Molecules 23(1) (2017).

[63] S. Del Prete, D. Vullo, D. Zoccola, S. Tambutte, C. Capasso, C.T. Supuran, Kinetic properties and affinities for sulfonamide inhibitors of an alpha-carbonic anhydrase (CruCA4) involved in coral biomineralization in the Mediterranean red coral Corallium rubrum, Bioorg Med Chem 25(13) (2017) 3525-3530.

[64] S. Del Prete, D. Vullo, S.M. Osman, Z. AlOthman, C.T. Supuran, C. Capasso, Sulfonamide inhibition profiles of the beta-carbonic anhydrase from the pathogenic bacterium Francisella tularensis responsible of the febrile illness tularemia, Bioorg Med Chem 25(13) (2017) 3555-3561.

[65] S. Del Prete, D. Vullo, S.M. Osman, Z. AlOthman, W.A. Donald, J.Y. Winum, C.T. Supuran, C. Capasso, Anion inhibitors of the beta-carbonic anhydrase from the pathogenic bacterium responsible of tularemia, Francisella tularensis, Bioorg Med Chem 25(17) (2017) 4800-4804.

[66] S. Del Prete, D. Vullo, P. Di Fonzo, S.M. Osman, Z. AlOthman, C.T. Supuran, C. Capasso, Anion inhibition profiles of the gamma-carbonic anhydrase from the pathogenic bacterium Burkholderia pseudomallei responsible of melioidosis and highly drug resistant to common antibiotics, Bioorg Med Chem 25(2) (2017) 575-580.

[67] S. Del Prete, D. Vullo, P. Di Fonzo, S.M. Osman, Z. AlOthman, W.A. Donald, C.T. Supuran, C. Capasso, Sulfonamide inhibition profile of the gamma-carbonic anhydrase identified in the genome of the pathogenic bacterium Burkholderia pseudomallei the etiological agent responsible of melioidosis, Bioorg Med Chem Lett 27(3) (2017) 490-495.

[68] S. Del Prete, D. Vullo, P. di Fonzo, V. Carginale, C.T. Supuran, C. Capasso, Comparison of the anion inhibition profiles of the beta- and gamma-carbonic anhydrases from the pathogenic bacterium Burkholderia pseudomallei, Bioorg Med Chem 25(6) (2017) 2010-2015.

[69] S. Del Prete, R. Perfetto, M. Rossi, F.A.S. Alasmary, S.M. Osman, Z. AlOthman, C.T. Supuran, C. Capasso, A one-step procedure for immobilising the thermostable carbonic anhydrase (SspCA) on the surface membrane of Escherichia coli, J Enzyme Inhib Med Chem 32(1) (2017) 1120-1128.

[70] D. De Vita, A. Angeli, F. Pandolfi, M. Bortolami, R. Costi, R. Di Santo, E. Suffredini, M. Ceruso, S. Del Prete, C. Capasso, L. Scipione, C.T. Supuran, Inhibition of the alpha-carbonic anhydrase from Vibrio cholerae with amides and sulfonamides incorporating imidazole moieties, J Enzyme Inhib Med Chem 32(1) (2017) 798-804.

[71] C. Capasso, C.T. Supuran, Inhibition of Bacterial Carbonic Anhydrases as a Novel Approach to Escape Drug Resistance, Curr Top Med Chem 17(11) (2017) 1237-1248.

[72] A. Angeli, G. Abbas, S. Del Prete, F. Carta, C. Capasso, C.T. Supuran, Acyl selenoureido benzensulfonamides show potent inhibitory activity against carbonic anhydrases from the pathogenic bacterium Vibrio cholerae, Bioorg Chem 75 (2017) 170-172.

[73] S. Angapelly, P.V.S. Ramya, A. Angeli, S. Del Prete, C. Capasso, M. Arifuddin, C.T. Supuran, Development of sulfonamides incorporating phenylacrylamido functionalities as carbonic anhydrase isoforms I, II, IX and XII inhibitors, Bioorg Med Chem 25(20) (2017) 5726-5732.

[74] D. Vullo, S. Del Prete, V. De Luca, V. Carginale, M. Ferraroni, N. Dedeoglu, S.M. Osman, Z. AlOthman, C. Capasso, C.T. Supuran, Anion inhibition studies of the beta-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae, Bioorg Med Chem Lett 26(5) (2016) 1406-10.

[75] D. Vullo, S. Del Prete, C. Capasso, C.T. Supuran, Carbonic anhydrase activators: Activation of the beta-carbonic anhydrase from Malassezia globosa with amines and amino acids, Bioorg Med Chem Lett 26(5) (2016) 1381-5.

[76] D. Vullo, V. De Luca, S. Del Prete, V. Carginale, A. Scozzafava, S.M. Osman, Z. AlOthman, C. Capasso, C.T. Supuran, Sulfonamide inhibition studies of the gamma-carbonic anhydrase from the Antarctic bacterium Colwellia psychrerythraea, Bioorg Med Chem Lett 26(4) (2016) 1253-9.

[77] C.T. Supuran, C. Capasso, New light on bacterial carbonic anhydrases phylogeny based on the analysis of signal peptide sequences, J Enzyme Inhib Med Chem 31(6) (2016) 1254-60.

[78] O. Ozensoy Guler, C. Capasso, C.T. Supuran, A magnificent enzyme superfamily: carbonic anhydrases, their purification and characterization, J Enzyme Inhib Med Chem 31(5) (2016) 689-94.

[79] S. Del Prete, D. Vullo, V. De Luca, V. Carginale, S.M. Osman, Z. AlOthman, C.T. Supuran, C. Capasso, Comparison of the sulfonamide inhibition profiles of the alpha-, beta- and gamma-carbonic anhydrases from the pathogenic bacterium Vibrio cholerae, Bioorg Med Chem Lett 26(8) (2016) 1941-6.

[80] S. Del Prete, D. Vullo, V. De Luca, V. Carginale, S.M. Osman, Z. AlOthman, C.T. Supuran, C. Capasso, Cloning, expression, purification and sulfonamide inhibition profile of the complete domain of the eta-carbonic anhydrase from Plasmodium falciparum, Bioorg Med Chem Lett 26(17) (2016) 4184-90.

[81] S. Del Prete, D. Vullo, V. De Luca, V. Carginale, M. Ferraroni, S.M. Osman, Z. AlOthman, C.T. Supuran, C. Capasso, Sulfonamide inhibition studies of the beta-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae, Bioorg Med Chem 24(5) (2016) 1115-20.

[82] S. Del Prete, D. Vullo, V. De Luca, V. Carginale, P. di Fonzo, S.M. Osman, Z. AlOthman, C.T. Supuran, C. Capasso, Anion inhibition profiles of alpha-, beta- and gamma-carbonic anhydrases from the pathogenic bacterium Vibrio cholerae, Bioorg Med Chem 24(16) (2016) 3413-7.

[83] S. Del Prete, D. Vullo, V. De Luca, V. Carginale, P. di Fonzo, S.M. Osman, Z. AlOthman, C.T. Supuran, C. Capasso, Anion inhibition profiles of the complete domain of the eta-carbonic anhydrase from Plasmodium falciparum, Bioorg Med Chem 24(18) (2016) 4410-4414.

[84] S. Del Prete, V. De Luca, D. Vullo, S.M. Osman, Z. AlOthman, V. Carginale, C.T. Supuran, C. Capasso, A new procedure for the cloning, expression and purification of the beta-carbonic anhydrase from the pathogenic yeast Malassezia globosa, an anti-dandruff drug target, J Enzyme Inhib Med Chem 31(6) (2016) 1156-61.

[85] S. Del Prete, V. De Luca, G. De Simone, C.T. Supuran, C. Capasso, Cloning, expression and purification of the complete domain of the eta-carbonic anhydrase from Plasmodium falciparum, J Enzyme Inhib Med Chem 31(sup4) (2016) 54-59.

[86] S. Del Prete, V. De Luca, C. Capasso, C.T. Supuran, V. Carginale, Recombinant thermoactive phosphoenolpyruvate carboxylase (PEPC) from Thermosynechococcus elongatus and its coupling with mesophilic/thermophilic bacterial carbonic anhydrases (CAs) for the conversion of CO2 to oxaloacetate, Bioorg Med Chem 24(2) (2016) 220-5.

[87] V. De Luca, D. Vullo, S. Del Prete, V. Carginale, S.M. Osman, Z. AlOthman, C.T. Supuran, C. Capasso, Cloning, characterization and anion inhibition studies of a gamma-carbonic anhydrase from the Antarctic bacterium Colwellia psychrerythraea, Bioorg Med Chem 24(4) (2016) 835-40.

[88] V. De Luca, S. Del Prete, D. Vullo, V. Carginale, P. Di Fonzo, S.M. Osman, Z. AlOthman, C.T. Supuran, C. Capasso, Expression and characterization of a recombinant psychrophilic gamma-carbonic anhydrase (NcoCA) identified in the genome of the Antarctic cyanobacteria belonging to the genus Nostoc, J Enzyme Inhib Med Chem 31(5) (2016) 810-7.

[89] C. Capasso, C.T. Supuran, An Overview of the Carbonic Anhydrases from Two Pathogens of the Oral Cavity: Streptococcus mutans and Porphyromonas gingivalis, Curr Top Med Chem 16(21) (2016) 2359-68.

[90] G. Annunziato, A. Angeli, F. D’Alba, A. Bruno, M. Pieroni, D. Vullo, V. De Luca, C. Capasso, C.T. Supuran, G. Costantino, Discovery of New Potential Anti-Infective Compounds Based on Carbonic Anhydrase Inhibitors by Rational Target-Focused Repurposing Approaches, ChemMedChem 11(17) (2016) 1904-14.

[91] N.M. Abdel Gawad, N.H. Amin, M.T. Elsaadi, F.M.M. Mohamed, A. Angeli, V. De Luca, C. Capasso, C.T. Supuran, Synthesis of 4-(thiazol-2-ylamino)-benzenesulfonamides with carbonic anhydrase I, II and IX inhibitory activity and cytotoxic effects against breast cancer cell lines, Bioorg Med Chem 24(13) (2016) 3043-3051.

[92] D. Vullo, S. Del Prete, G.M. Fisher, K.T. Andrews, S.A. Poulsen, C. Capasso, C.T. Supuran, Sulfonamide inhibition studies of the eta-class carbonic anhydrase from the malaria pathogen Plasmodium falciparum, Bioorg Med Chem 23(3) (2015) 526-31.

[93] D. Vullo, V. De Luca, S. Del Prete, V. Carginale, A. Scozzafava, C. Capasso, C.T. Supuran, Sulfonamide inhibition studies of the gamma-carbonic anhydrase from the Antarctic cyanobacterium Nostoc commune, Bioorg Med Chem 23(8) (2015) 1728-34.

[94] D. Vullo, V. De Luca, S. Del Prete, V. Carginale, A. Scozzafava, C. Capasso, C.T. Supuran, Sulfonamide inhibition studies of the gamma-carbonic anhydrase from the Antarctic bacterium Pseudoalteromonas haloplanktis, Bioorg Med Chem Lett 25(17) (2015) 3550-5.

[95] C.T. Supuran, C. Capasso, The eta-class carbonic anhydrases as drug targets for antimalarial agents, Expert Opin Ther Targets 19(4) (2015) 551-63.

[96] M. Ferraroni, S. Del Prete, D. Vullo, C. Capasso, C.T. Supuran, Crystal structure and kinetic studies of a tetrameric type II beta-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae, Acta Crystallogr D Biol Crystallogr 71(Pt 12) (2015) 2449-56.

[97] S. Del Prete, D. Vullo, S.M. Osman, Z. AlOthman, C. Capasso, C.T. Supuran, Anion inhibition studies of the dandruff-producing fungus Malassezia globosa beta-carbonic anhydrase MgCA, Bioorg Med Chem Lett 25(22) (2015) 5194-8.

[98] S. Del Prete, D. Vullo, V. De Luca, Z. AlOthman, S.M. Osman, C.T. Supuran, C. Capasso, Biochemical characterization of recombinant beta-carbonic anhydrase (PgiCAb) identified in the genome of the oral pathogenic bacterium Porphyromonas gingivalis, J Enzyme Inhib Med Chem 30(3) (2015) 366-70.

[99] S. Del Prete, V. De Luca, C.T. Supuran, C. Capasso, Protonography, a technique applicable for the analysis of eta-carbonic anhydrase activity, J Enzyme Inhib Med Chem 30(6) (2015) 920-4.

[100] S. Del Prete, V. De Luca, E. Iandolo, C.T. Supuran, C. Capasso, Protonography, a powerful tool for analyzing the activity and the oligomeric state of the gamma-carbonic anhydrase identified in the genome of Porphyromonas gingivalis, Bioorg Med Chem 23(13) (2015) 3747-50.

[101] N. Dedeoglu, V. DeLuca, S. Isik, H. Yildirim, F. Kockar, C. Capasso, C.T. Supuran, Sulfonamide inhibition study of the beta-class carbonic anhydrase from the caries producing pathogen Streptococcus mutans, Bioorg Med Chem Lett 25(11) (2015) 2291-7.

[102] N. Dedeoglu, V. De Luca, S. Isik, H. Yildirim, F. Kockar, C. Capasso, C.T. Supuran, Cloning, characterization and anion inhibition study of a beta-class carbonic anhydrase from the caries producing pathogen Streptococcus mutans, Bioorg Med Chem 23(13) (2015) 2995-3001.

[103] G. De Simone, S.M. Monti, V. Alterio, M. Buonanno, V. De Luca, M. Rossi, V. Carginale, C.T. Supuran, C. Capasso, A. Di Fiore, Crystal structure of the most catalytically effective carbonic anhydrase enzyme known, SazCA from the thermophilic bacterium Sulfurihydrogenibium azorense, Bioorg Med Chem Lett 25(9) (2015) 2002-6.

[104] G. De Simone, A. Di Fiore, C. Capasso, C.T. Supuran, The zinc coordination pattern in the eta-carbonic anhydrase from Plasmodium falciparum is different from all other carbonic anhydrase genetic families, Bioorg Med Chem Lett 25(7) (2015) 1385-9.

[105] V. De Luca, D. Vullo, S. Del Prete, V. Carginale, A. Scozzafava, S.M. Osman, Z. AlOthman, C.T. Supuran, C. Capasso, Cloning, characterization and anion inhibition studies of a new gamma-carbonic anhydrase from the Antarctic bacterium Pseudoalteromonas haloplanktis, Bioorg Med Chem 23(15) (2015) 4405-9.

[106] V. De Luca, S. Del Prete, C.T. Supuran, C. Capasso, Protonography, a new technique for the analysis of carbonic anhydrase activity, J Enzyme Inhib Med Chem 30(2) (2015) 277-82.

[107] V. De Luca, S. Del Prete, V. Carginale, D. Vullo, C.T. Supuran, C. Capasso, A failed tentative to design a super carbonic anhydrase having the biochemical properties of the most thermostable CA (SspCA) and the fastest (SazCA) enzymes, J Enzyme Inhib Med Chem 30(6) (2015) 989-94.

[108] V. De Luca, S. Del Prete, V. Carginale, D. Vullo, C.T. Supuran, C. Capasso, Cloning, characterization and anion inhibition studies of a gamma-carbonic anhydrase from the Antarctic cyanobacterium Nostoc commune, Bioorg Med Chem Lett 25(21) (2015) 4970-4975.

[109] F. Carta, S.M. Osman, D. Vullo, Z. AlOthman, S. Del Prete, C. Capasso, C.T. Supuran, Poly(amidoamine) dendrimers show carbonic anhydrase inhibitory activity against alpha-, beta-, gamma- and eta-class enzymes, Bioorg Med Chem 23(21) (2015) 6794-8.

[110] C. Capasso, C.T. Supuran, 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 30(2) (2015) 325-32.

[111] C. Capasso, C.T. Supuran, An Overview of the Selectivity and Efficiency of the Bacterial Carbonic Anhydrase Inhibitors, Curr Med Chem 22(18) (2015) 2130-9.

[112] C. Capasso, C.T. Supuran, Bacterial, fungal and protozoan carbonic anhydrases as drug targets, Expert Opin Ther Targets 19(12) (2015) 1689-704.

[113] M. Bejaoui, E. Pantazi, V. De Luca, A. Panisello, E. Folch-Puy, G. Hotter, C. Capasso, C.T. Supuran, J. Rosello-Catafau, Correction: Carbonic Anhydrase Protects Fatty Liver Grafts against Ischemic Reperfusion Damage, PLoS One 10(9) (2015) e0139411.

[114] A.M. Alafeefy, M. Ceruso, A.M. Al-Tamimi, S. Del Prete, C.T. Supuran, C. Capasso, Inhibition studies of quinazoline-sulfonamide derivatives against the gamma-CA (PgiCA) from the pathogenic bacterium, Porphyromonas gingivalis, J Enzyme Inhib Med Chem 30(4) (2015) 592-6.

[115] A.M. Alafeefy, H.A. Abdel-Aziz, D. Vullo, A.M. Al-Tamimi, A.S. Awaad, M.A. Mohamed, C. Capasso, C.T. Supuran, Inhibition of human carbonic anhydrase isozymes I, II, IX and XII with a new series of sulfonamides incorporating aroylhydrazone-, [1.2,4]triazolo[3.4-b][1.3,4]thiadiazinyl- or 2-(cyanophenylmethylene)-1.3,4-thiadiazol-3(2H)-yl moieties, J Enzyme Inhib Med Chem 30(1) (2015) 52-6.

[116] D. Vullo, E.V. Kupriyanova, A. Scozzafava, C. Capasso, C.T. Supuran, Anion inhibition study of the beta-carbonic anhydrase (CahB1) from the cyanobacterium Coleofasciculus chthonoplastes (ex-Microcoleus chthonoplastes), Bioorg Med Chem 22(5) (2014) 1667-71.

[117] D. Vullo, E. Flemetakis, A. Scozzafava, C. Capasso, C.T. Supuran, Anion inhibition studies of two alpha-carbonic anhydrases from Lotus japonicus, LjCAA1 and LjCAA2, J Inorg Biochem 136 (2014) 67-72.

[118] D. Vullo, S. Del Prete, S.M. Osman, A. Scozzafava, Z. Alothman, C.T. Supuran, C. Capasso, Anion inhibition study of the beta-class carbonic anhydrase (PgiCAb) from the oral pathogen Porphyromonas gingivalis, Bioorg Med Chem Lett 24(18) (2014) 4402-4406.

[119] D. Vullo, S. Del Prete, S.M. Osman, V. De Luca, A. Scozzafava, Z. Alothman, C.T. Supuran, C. Capasso, Sulfonamide inhibition studies of the delta-carbonic anhydrase from the diatom Thalassiosira weissflogii, Bioorg Med Chem Lett 24(1) (2014) 275-9.

[120] D. Vullo, S. Del Prete, S.M. Osman, V. De Luca, A. Scozzafava, Z. Alothman, C.T. Supuran, C. Capasso, Sulfonamide inhibition studies of the gamma-carbonic anhydrase from the oral pathogen Porphyromonas gingivalis, Bioorg Med Chem Lett 24(1) (2014) 240-4.

[121] G.C. Rodrigues, D.F. Feijo, M.T. Bozza, P. Pan, D. Vullo, S. Parkkila, C.T. Supuran, C. Capasso, A.P. Aguiar, A.B. Vermelho, Design, synthesis, and evaluation of hydroxamic acid derivatives as promising agents for the management of Chagas disease, J Med Chem 57(2) (2014) 298-308.

[122] S.D. Prete, D. Vullo, S.M. Osman, A. Scozzafava, Z. AlOthman, C. Capasso, C.T. Supuran, Sulfonamide inhibition study of the carbonic anhydrases from the bacterial pathogen Porphyromonas gingivalis: the beta-class (PgiCAb) versus the gamma-class (PgiCA) enzymes, Bioorg Med Chem 22(17) (2014) 4537-43.

[123] I. Nishimori, D. Vullo, T. Minakuchi, A. Scozzafava, S.M. Osman, Z. AlOthman, C. Capasso, C.T. Supuran, Anion inhibition studies of two new beta-carbonic anhydrases from the bacterial pathogen Legionella pneumophila, Bioorg Med Chem Lett 24(4) (2014) 1127-32.

[124] I. Nishimori, D. Vullo, T. Minakuchi, A. Scozzafava, C. Capasso, C.T. Supuran, Sulfonamide inhibition studies of two beta-carbonic anhydrases from the bacterial pathogen Legionella pneumophila, Bioorg Med Chem 22(11) (2014) 2939-46.

[125] F. Migliardini, V. De Luca, V. Carginale, M. Rossi, P. Corbo, C.T. Supuran, C. Capasso, Biomimetic CO2 capture using a highly thermostable bacterial alpha-carbonic anhydrase immobilized on a polyurethane foam, J Enzyme Inhib Med Chem 29(1) (2014) 146-50.

[126] S. Del Prete, D. Vullo, A. Scozzafava, C. Capasso, C.T. Supuran, Cloning, characterization and anion inhibition study of the delta-class carbonic anhydrase (TweCA) from the marine diatom Thalassiosira weissflogii, Bioorg Med Chem 22(1) (2014) 531-7.

[127] S. Del Prete, D. Vullo, G.M. Fisher, K.T. Andrews, S.A. Poulsen, C. Capasso, C.T. Supuran, Discovery of a new family of carbonic anhydrases in the malaria pathogen Plasmodium falciparum--the eta-carbonic anhydrases, Bioorg Med Chem Lett 24(18) (2014) 4389-4396.

[128] S. Del Prete, D. Vullo, V. De Luca, C.T. Supuran, C. Capasso, Biochemical characterization of the delta-carbonic anhydrase from the marine diatom Thalassiosira weissflogii, TweCA, J Enzyme Inhib Med Chem 29(6) (2014) 906-11.

[129] S. Del Prete, V. De Luca, D. Vullo, A. Scozzafava, V. Carginale, C.T. Supuran, C. Capasso, Biochemical characterization of the gamma-carbonic anhydrase from the oral pathogen Porphyromonas gingivalis, PgiCA, J Enzyme Inhib Med Chem 29(4) (2014) 532-7.

[130] S. Del Prete, V. De Luca, A. Scozzafava, V. Carginale, C.T. Supuran, C. Capasso, Biochemical properties of a new alpha-carbonic anhydrase from the human pathogenic bacterium, Vibrio cholerae, J Enzyme Inhib Med Chem 29(1) (2014) 23-7.

[131] M. Ceruso, S. Del Prete, Z. AlOthman, S.M. Osman, A. Scozzafava, C. Capasso, C.T. Supuran, Synthesis of sulfonamides with effective inhibitory action against Porphyromonas gingivalis gamma-carbonic anhydrase, Bioorg Med Chem Lett 24(16) (2014) 4006-10.

[132] M. Ceruso, S. Del Prete, Z. Alothman, C. Capasso, C.T. Supuran, Sulfonamides with Potent Inhibitory Action and Selectivity against the alpha-Carbonic Anhydrase from Vibrio cholerae, ACS Med Chem Lett 5(7) (2014) 826-30.

[133] C. Capasso, C.T. Supuran, Sulfa and trimethoprim-like drugs - antimetabolites acting as carbonic anhydrase, dihydropteroate synthase and dihydrofolate reductase inhibitors, J Enzyme Inhib Med Chem 29(3) (2014) 379-87.

[134] S. Bilginer, E. Unluer, H.I. Gul, E. Mete, S. Isik, D. Vullo, O. Ozensoy-Guler, S. Beyaztas, C. Capasso, C.T. Supuran, Carbonic anhydrase inhibitors. Phenols incorporating 2- or 3-pyridyl-ethenylcarbonyl and tertiary amine moieties strongly inhibit Saccharomyces cerevisiae beta-carbonic anhydrase, J Enzyme Inhib Med Chem 29(4) (2014) 495-9.

[135] A.M. Alafeefy, M. Ceruso, A.M. Al-Tamimi, S. Del Prete, C. Capasso, C.T. Supuran, Quinazoline-sulfonamides with potent inhibitory activity against the alpha-carbonic anhydrase from Vibrio cholerae, Bioorg Med Chem 22(19) (2014) 5133-40.

[136] A.M. Alafeefy, H.A. Abdel-Aziz, D. Vullo, A.M. Al-Tamimi, N.A. Al-Jaber, C. Capasso, C.T. Supuran, Inhibition of carbonic anhydrases from the extremophilic bacteria Sulfurihydrogenibium yellostonense (SspCA) and S. azorense (SazCA) with a new series of sulfonamides incorporating aroylhydrazone-, [1.2,4]triazolo[3.4-b][1.3,4]thiadiazinyl- or 2-(cyanophenylmethylene)-1.3,4-thiadiazol-3(2H)-yl moieties, Bioorg Med Chem 22(1) (2014) 141-7.

[137] D. Vullo, R.S. Sai Kumar, A. Scozzafava, C. Capasso, J.G. Ferry, C.T. Supuran, Anion inhibition studies of a beta-carbonic anhydrase from Clostridium perfringens, Bioorg Med Chem Lett 23(24) (2013) 6706-10.

[138] D. Vullo, V.D. Luca, A. Scozzafava, V. Carginale, M. Rossi, C.T. Supuran, C. Capasso, The alpha-carbonic anhydrase from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1 is highly susceptible to inhibition by sulfonamides, Bioorg Med Chem 21(6) (2013) 1534-8.

[139] D. Vullo, W. Leewattanapasuk, F.A. Muhlschlegel, A. Mastrolorenzo, C. Capasso, C.T. Supuran, Carbonic anhydrase inhibitors: inhibition of the beta-class enzyme from the pathogenic yeast Candida glabrata with sulfonamides, sulfamates and sulfamides, Bioorg Med Chem Lett 23(9) (2013) 2647-52.

[140] D. Vullo, S. Isik, S. Del Prete, V. De Luca, V. Carginale, A. Scozzafava, C.T. Supuran, C. Capasso, Anion inhibition studies of the alpha-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae, Bioorg Med Chem Lett 23(6) (2013) 1636-8.

[141] D. Vullo, V. De Luca, A. Scozzafava, V. Carginale, M. Rossi, C.T. Supuran, C. Capasso, The extremo-alpha-carbonic anhydrase from the thermophilic bacterium Sulfurihydrogenibium azorense is highly inhibited by sulfonamides, Bioorg Med Chem 21(15) (2013) 4521-5.

[142] L. Syrjanen, A.B. Vermelho, A. Rodrigues Ide, S. Corte-Real, T. Salonen, P. Pan, D. Vullo, S. Parkkila, C. Capasso, C.T. Supuran, Cloning, characterization, and inhibition studies of a beta-carbonic anhydrase from Leishmania donovani chagasi, the protozoan parasite responsible for leishmaniasis, J Med Chem 56(18) (2013) 7372-81.

[143] P. Pan, A.B. Vermelho, A. Scozzafava, S. Parkkila, C. Capasso, C.T. Supuran, Anion inhibition studies of the alpha-carbonic anhydrase from the protozoan pathogen Trypanosoma cruzi, the causative agent of Chagas disease, Bioorg Med Chem 21(15) (2013) 4472-6.

[144] P. Pan, A.B. Vermelho, G. Capaci Rodrigues, A. Scozzafava, M.E. Tolvanen, S. Parkkila, C. Capasso, C.T. Supuran, Cloning, characterization, and sulfonamide and thiol inhibition studies of an alpha-carbonic anhydrase from Trypanosoma cruzi, the causative agent of Chagas disease, J Med Chem 56(4) (2013) 1761-71.

[145] I. Nishimori, D. Vullo, T. Minakuchi, A. Scozzafava, C. Capasso, C.T. Supuran, Restoring catalytic activity to the human carbonic anhydrase (CA) related proteins VIII, X and XI affords isoforms with high catalytic efficiency and susceptibility to anion inhibition, Bioorg Med Chem Lett 23(1) (2013) 256-60.

[146] S.M. Monti, G. De Simone, N.A. Dathan, M. Ludwig, D. Vullo, A. Scozzafava, C. Capasso, C.T. Supuran, Kinetic and anion inhibition studies of a beta-carbonic anhydrase (FbiCA 1) from the C4 plant Flaveria bidentis, Bioorg Med Chem Lett 23(6) (2013) 1626-30.

[147] V.D. Luca, D. Vullo, A. Scozzafava, V. Carginale, M. Rossi, C.T. Supuran, C. Capasso, An alpha-carbonic anhydrase from the thermophilic bacterium Sulphurihydrogenibium azorense is the fastest enzyme known for the CO2 hydration reaction, Bioorg Med Chem 21(6) (2013) 1465-9.

[148] O. Guzel-Akdemir, A. Akdemir, P. Pan, A.B. Vermelho, S. Parkkila, A. Scozzafava, C. Capasso, C.T. Supuran, A class of sulfonamides with strong inhibitory action against the alpha-carbonic anhydrase from Trypanosoma cruzi, J Med Chem 56(14) (2013) 5773-81.

[149] A. Di Fiore, C. Capasso, V. De Luca, S.M. Monti, V. Carginale, C.T. Supuran, A. Scozzafava, C. Pedone, M. Rossi, G. De Simone, X-ray structure of the first extremo-alpha-carbonic anhydrase’, a dimeric enzyme from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1, Acta Crystallogr D Biol Crystallogr 69(Pt 6) (2013) 1150-9.

[150] S. Del Prete, D. Vullo, V. De Luca, V. Carginale, A. Scozzafava, C.T. Supuran, C. Capasso, A highly catalytically active gamma-carbonic anhydrase from the pathogenic anaerobe Porphyromonas gingivalis and its inhibition profile with anions and small molecules, Bioorg Med Chem Lett 23(14) (2013) 4067-71.

[151] C. Capasso, C.T. Supuran, Anti-infective carbonic anhydrase inhibitors: a patent and literature review, Expert Opin Ther Pat 23(6) (2013) 693-704.

[152] A.M. Alafeefy, S. Isik, N.A. Al-Jaber, D. Vullo, H.A. Abdel-Aziz, A.E. Ashour, A.S. Awaad, C. Capasso, C.T. Supuran, Carbonic anhydrase inhibitors. Benzenesulfonamides incorporating cyanoacrylamide moieties strongly inhibit Saccharomyces cerevisiae beta-carbonic anhydrase, Bioorg Med Chem Lett 23(12) (2013) 3570-5.

[153] A. Akdemir, D. Vullo, V. De Luca, A. Scozzafava, V. Carginale, M. Rossi, C.T. Supuran, C. Capasso, The extremo-alpha-carbonic anhydrase (CA) from Sulfurihydrogenibium azorense, the fastest CA known, is highly activated by amino acids and amines, Bioorg Med Chem Lett 23(4) (2013) 1087-90.

[154] A. Akdemir, O. Guzel-Akdemir, A. Scozzafava, C. Capasso, C.T. Supuran, Inhibition of tumor-associated human carbonic anhydrase isozymes IX and XII by a new class of substituted-phenylacetamido aromatic sulfonamides, Bioorg Med Chem 21(17) (2013) 5228-32.

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