References
- Capasso C, Supuran CT. Sulfa and trimethoprim-like drugs – antimetabolites acting as carbonic anhydrase, dihydropteroate synthase and dihydrofolate reductase inhibitors. J Enzyme Inhib Med Chem 2014;29:379-87
- Capasso C, Supuran CT. Anti-infective carbonic anhydrase inhibitors: a patent and literature review. Expert Opin Ther Pat 2013;23:693–704
- Vullo D, Del Prete S, Osman SM, et al. Sulfonamide inhibition studies of the gamma-carbonic anhydrase from the oral pathogen Porphyromonas gingivalis. Bioorg Med Chem Lett 2014;24:240–4
- Nishimori I, Vullo D, Minakuchi T, et al. Anion inhibition studies of two new beta-carbonic anhydrases from the bacterial pathogen Legionella pneumophila. Bioorg Med Chem Lett 2014;24:1127–32
- Nishimori I, Vullo D, Minakuchi T, et al. Sulfonamide inhibition studies of two beta-carbonic anhydrases from the bacterial pathogen Legionella pneumophila. Bioorg Med Chem 2014;22:2939–46
- Del Prete S, De Luca V, Scozzafava A, et al. Biochemical properties of a new alpha-carbonic anhydrase from the human pathogenic bacterium, Vibrio cholerae. J Enzyme Inhib Med Chem 2014;29:23–7
- 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 2014. [Epub ahead of print]. doi: 10.3109/14756366.2014.910202.
- Alafeefy AM, Abdel-Aziz HA, Vullo D, et al. 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 2014;22:141–7
- Vullo D, De Luca V, Scozzafava A, et al. The alpha-carbonic anhydrase from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1 is highly susceptible to inhibition by sulfonamides. Bioorg Med Chem 2013;21:1534–8
- De Luca V, Vullo D, Scozzafava A, et al. An alpha-carbonic anhydrase from the thermophilic bacterium Sulphurihydrogenibium azorense is the fastest enzyme known for the CO2 hydration reaction. Bioorg Med Chem 2013;21:1465–9
- Del Prete S, Vullo D, De Luca V, et al. 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 2013;23:4067–71
- Akdemir A, Vullo D, De Luca V, et al. 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 2013;23:1087–90
- Vullo D, De Luca V, Scozzafava A, et al. The first activation study of a bacterial carbonic anhydrase (CA). The thermostable alpha-CA from Sulfurihydrogenibium yellowstonense YO3AOP1 is highly activated by amino acids and amines. Bioorg Med Chem Lett 2012;22:6324–7
- Vullo D, De Luca V, Scozzafava A, et al. Anion inhibition studies of the fastest carbonic anhydrase (CA) known, the extremo-CA from the bacterium Sulfurihydrogenibium azorense. Bioorg Med Chem Lett 2012;22:7142–5
- De Luca V, Vullo D, Scozzafava A, et al. Anion inhibition studies of an alpha-carbonic anhydrase from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1. Bioorg Med Chem Lett 2012;22:5630–4
- Capasso C, De Luca V, Carginale V, et al. Biochemical properties of a novel and highly thermostable bacterial alpha-carbonic anhydrase from Sulfurihydrogenibium yellowstonense YO3AOP1. J Enzyme Inhib Med Chem 2012;27:892–7
- Supuran CT. Bacterial carbonic anhydrases as drug targets: toward novel antibiotics? Front Pharmacol 2011;2:34. doi: 10.3389/fphar.2011.00034
- Vullo D, Kupriyanova EV, Scozzafava A, et al. Anion inhibition study of the beta-carbonic anhydrase (CahB1) from the cyanobacterium Coleofasciculus chthonoplastes (ex-Microcoleus chthonoplastes). Bioorg Med Chem 2014;22:1667–71
- Vullo D, Flemetakis E, Scozzafava A, et al. Anion inhibition studies of two alpha-carbonic anhydrases from Lotus japonicus, LjCAA1 and LjCAA2. J Inorg Biochem 2014;136C:67–72
- Vullo D, Del Prete S, Osman SM, et al. Sulfonamide inhibition studies of the delta-carbonic anhydrase from the diatom Thalassiosira weissflogii. Bioorg Med Chem Lett 2014;24:275–9
- Rodrigues GC, Feijo DF, Bozza MT, et al. Design, synthesis, and evaluation of hydroxamic acid derivatives as promising agents for the management of Chagas disease. J Med Chem 2014;57:298–308
- Migliardini F, De Luca V, Carginale V, et al. Biomimetic CO2 capture using a highly thermostable bacterial alpha-carbonic anhydrase immobilized on a polyurethane foam. J Enzyme Inhib Med Chem 2014;29:146–50
- Del Prete S, Vullo D, Scozzafava A, et al. Cloning, characterization and anion inhibition study of the delta-class carbonic anhydrase (TweCA) from the marine diatom Thalassiosira weissflogii. Bioorg Med Chem 2014;22:531–7
- Del Prete S, Vullo D, De Luca V, et al. Biochemical characterization of the delta-carbonic anhydrase from the marine diatom Thalassiosira weissflogii, TweCA. J Enzyme Inhib Med Chem 2014. [Epub ahead of print]. doi: 10.3109/14756366.2013.868599
- Alafeefy AM, Abdel-Aziz HA, Vullo D, et al. 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 2014. [Epub ahead of print]. doi: 10.3109/14756366.2013.877897
- Vullo D, Leewattanapasuk W, Muhlschlegel FA, et al. Carbonic anhydrase inhibitors: inhibition of the beta-class enzyme from the pathogenic yeast Candida glabrata with sulfonamides, sulfamates and sulfamides. Bioorg Med Chem Lett 2013;23:2647–52
- Vullo D, De Luca V, Scozzafava A, et al. The extremo-alpha-carbonic anhydrase from the thermophilic bacterium Sulfurihydrogenibium azorense is highly inhibited by sulfonamides. Bioorg Med Chem 2013;21:4521–5
- Russo ME, Olivieri G, Capasso C, et al. Kinetic study of a novel thermo-stable alpha-carbonic anhydrase for biomimetic CO2 capture. Enzyme Microb Technol 2013;53:271–7
- Nishimori I, Vullo D, Minakuchi T, et al. 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 2013;23:256–60
- Di Fiore A, Capasso C, De Luca V, et al. 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 2013;69:1150–9
- Vullo D, Isik S, Del Prete S, et al. Anion inhibition studies of the alpha-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae. Bioorg Med Chem Lett 2013;23:1636–8
- Del Prete S, De Luca V, Vullo D, et al. Biochemical characterization of the gamma-carbonic anhydrase from the oral pathogen Porphyromonas gingivalis, PgiCA. J Enzyme Inhib Med Chem 2013. [Epub ahead of print]. doi: 10.3109/14756366.2013.822371
- Mysak J, Podzimek S, Sommerova P, et al. Porphyromonas gingivalis: major periodontopathic pathogen overview. J Immunol Res 2014;2014:1–8
- Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970;227:680–5
- 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
- Innocenti A, Supuran CT. Paraoxon, 4-nitrophenyl phosphate and acetate are substrates of alpha- but not of beta-, gamma- and zeta-carbonic anhydrases. Bioorg Med Chem Lett 2010;20:6208–12
- Innocenti A, Scozzafava A, Supuran CT. Carbonic anhydrase inhibitors. Inhibition of transmembrane isoforms IX, XII, and XIV with less investigated anions including trithiocarbonate and dithiocarbamate. Bioorg Med Chem Lett 2010;20:1548–50
- Maresca A, Scozzafava A, Kohler S, et al. Inhibition of beta-carbonic anhydrases from the bacterial pathogen Brucella suis with inorganic anions. J Inorg Biochem 2012;110:36–9
- Guindon S, Dufayard JF, Lefort V, et al. New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0. Syst Biol 2010;59:307–21
- Zolfaghari Emameh R, Barker H, Tolvanen ME, et al. Bioinformatic analysis of beta carbonic anhydrase sequences from protozoans and metazoans. Parasit Vectors 2014;7:1–12
- Larkin MA, Blackshields G, Brown NP, et al. Clustal W and Clustal X version 2.0. Bioinformatics 2007;23:2947–8