Compounds > 5-amino-1,3,4-thiadiazole-2-sulfonamide
Page last updated: 2024-08-25

5-amino-1,3,4-thiadiazole-2-sulfonamide and ethoxzolamide

5-amino-1,3,4-thiadiazole-2-sulfonamide has been researched along with ethoxzolamide in 52 studies

Research

Studies (52)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (1.92)18.2507
2000's23 (44.23)29.6817
2010's28 (53.85)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Briganti, F; Menabuoni, L; Mincione, F; Mincione, G; Scozzafava, A; Supuran, CT1
Menabuoni, L; Mincione, F; Scozzafava, A; Supuran, CT1
Franchi, M; Gallori, E; Pastorek, J; Pastorekova, S; Scozzafava, A; Supuran, CT; Vullo, D1
Caproiu, MT; Ilies, M; Ilies, MA; Pastorek, J; Pastorekova, S; Scozzafava, A; Supuran, CT; Vullo, D1
Jaiswal, M; Khadikar, PV; Scozzafava, A; Supuran, CT1
Durgun, M; Emul, M; Innocenti, A; Scozzafava, A; Supuran, CT; Turkmen, H; Vullo, D; Yilmaztekin, S1
Innocenti, A; Nishimori, I; Pastorek, J; Pastoreková, S; Scozzafava, A; Supuran, CT; Vullo, D1
Innocenti, A; Kaila, K; Ranki, H; Rivera, C; Scozzafava, A; Supuran, CT; Voipio, J; Vullo, D1
Antel, J; Firnges, MA; Innocenti, A; Scozzafava, A; Supuran, CT; Wurl, M1
Innocenti, A; Mastrolorenzo, A; Nishimori, I; Scozzafava, A; Supuran, CT; Vullo, D2
Minakuchi, T; Morimoto, K; Nishimori, I; Onishi, S; Scozzafava, A; Supuran, CT; Vullo, D1
Minakuchi, T; Morimoto, K; Nishimori, I; Onishi, S; Sano, S; Scozzafava, A; Supuran, CT; Takeuchi, H; Vullo, D1
Minakuchi, T; Nishimori, I; Onishi, S; Scozzafava, A; Supuran, CT; Vullo, D1
Kohsaki, T; Minakuchi, T; Nishimori, I; Onishi, S; Scozzafava, A; Supuran, CT; Takeuchi, H; Vullo, D1
Cecchi, A; Minakuchi, T; Nishimori, I; Onishi, S; Scozzafava, A; Supuran, CT; Vullo, D1
Arslan, O; Aydin, M; Guler, OO; Innocenti, A; Isik, S; Kockar, F; Scozzafava, A; Supuran, CT1
Hilvo, M; Innocenti, A; Kulomaa, MS; Parkkila, S; Salzano, AM; Scaloni, A; Scozzafava, A; Supuran, CT1
Eroğlu, E; Oltulu, O; Yaşar, MM1
Minakuchi, T; Nishimori, I; Scozzafava, A; Supuran, CT; Vullo, D2
Innocenti, A; Minakuchi, T; Nishimori, I; Scozzafava, A; Supuran, CT; Vullo, D1
Hall, RA; Innocenti, A; Mühlschlegel, FA; Schlicker, C; Scozzafava, A; Steegborn, C; Supuran, CT1
Bertucci, A; Innocenti, A; Scozzafava, A; Supuran, CT; Tambutté, S; Zoccola, D2
Carta, F; Covarrubias, AS; Jones, TA; Maresca, A; Mowbray, SL; Supuran, CT1
Joseph, P; Köhler, S; Minakuchi, T; Montero, JL; Nishimori, I; Ouahrani-Bettache, S; Scozzafava, A; Supuran, CT; Turtaut, F; Vullo, D; Winum, JY1
Arslan, O; Aydin, M; Güler, OO; Işik, S; Kockar, F; Maresca, A; Sinan, S; Supuran, CT; Turan, Y; Turkoglu, S1
Joseph, P; Köhler, S; Minakuchi, T; Montero, JL; Nishimori, I; Ouahrani-Bettache, S; Scozzafava, A; Supuran, CT; Vullo, D; Winum, JY1
Jackson, DJ; Ohradanova, A; Pastorek, J; Pastorekova, S; Supuran, CT; Vullo, D; Wörheide, G1
Alper, M; Arslan, O; Işık, S; Kockar, F; Maresca, A; Ozensoy, O; Sinan, S; Supuran, CT; Turkoglu, S1
Hewitson, KS; Mastrolorenzo, A; Scozzafava, A; Supuran, CT; Vullo, D1
Capasso, C; Carginale, V; Luca, VD; Rossi, M; Scozzafava, A; Supuran, CT; Vullo, D1
Capasso, C; Carginale, V; De Luca, V; Del Prete, S; Isik, S; Scozzafava, A; Supuran, CT; Vullo, D1
Capaci Rodrigues, G; Capasso, C; Pan, P; Parkkila, S; Scozzafava, A; Supuran, CT; Tolvanen, ME; Vermelho, AB1
Capasso, C; Leewattanapasuk, W; Mastrolorenzo, A; Mühlschlegel, FA; Supuran, CT; Vullo, D1
Capasso, C; Corte-Real, S; Pan, P; Parkkila, S; Rodrigues, Ide A; Salonen, T; Supuran, CT; Syrjänen, L; Vermelho, AB; Vullo, D1
Alothman, Z; Capasso, C; De Luca, V; Del Prete, S; Osman, SM; Scozzafava, A; Supuran, CT; Vullo, D2
Capasso, C; Minakuchi, T; Nishimori, I; Scozzafava, A; Supuran, CT; Vullo, D1
AlOthman, Z; Capasso, C; Osman, SM; Prete, SD; Scozzafava, A; Supuran, CT; Vullo, D1
Andrews, KT; Capasso, C; Del Prete, S; Fisher, GM; Poulsen, SA; Supuran, CT; Vullo, D1
Capasso, C; Carginale, V; De Luca, V; Del Prete, S; Scozzafava, A; Supuran, CT; Vullo, D2
Kuuslahti, M; Parkkila, S; Supuran, CT; Syrjänen, L; Tolvanen, M; Vullo, D1
Capasso, C; Dedeoglu, N; DeLuca, V; Isik, S; Kockar, F; Supuran, CT; Yildirim, H1
Bhatt, A; Mahon, BP; McKenna, R; Supuran, CT; Vullo, D1
AlOthman, Z; Capasso, C; Carginale, V; De Luca, V; Del Prete, S; Osman, SM; Scozzafava, A; Supuran, CT; Vullo, D1
AlOthman, Z; Capasso, C; Carginale, V; De Luca, V; Del Prete, S; Ferraroni, M; Osman, SM; Supuran, CT; Vullo, D1
Aşık, A; Beldüz, AO; Çanakçı, S; Çolak, DN; Eminoğlu, A; Supuran, CT; Vullo, D1
AlOthman, Z; Capasso, C; Carginale, V; De Luca, V; Del Prete, S; Osman, SM; Supuran, CT; Vullo, D2

Other Studies

52 other study(ies) available for 5-amino-1,3,4-thiadiazole-2-sulfonamide and ethoxzolamide

ArticleYear
Carbonic anhydrase inhibitors. Synthesis of water-soluble, topically effective, intraocular pressure-lowering aromatic/heterocyclic sulfonamides containing cationic or anionic moieties: is the tail more important than the ring?
    Journal of medicinal chemistry, 1999, Jul-15, Volume: 42, Issue:14

    Topics: Administration, Topical; Animals; Aqueous Humor; Benzene Derivatives; Carbonic Anhydrase Inhibitors; Cattle; Eye; Humans; Intraocular Pressure; Isoenzymes; Male; Ophthalmic Solutions; Pyridines; Rabbits; Solubility; Structure-Activity Relationship; Sulfonamides; Thiadiazoles; Tissue Distribution

1999
Carbonic anhydrase inhibitors. A general approach for the preparation of water-soluble sulfonamides incorporating polyamino-polycarboxylate tails and of their metal complexes possessing long-lasting, topical intraocular pressure-lowering properties.
    Journal of medicinal chemistry, 2002, Mar-28, Volume: 45, Issue:7

    Topics: Animals; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Chelating Agents; Chloroform; Chromatography, High Pressure Liquid; Cornea; DNA, Complementary; Edetic Acid; Enzyme Inhibitors; Escherichia coli; Glaucoma; Humans; Hydrogen-Ion Concentration; Imino Acids; Kinetics; Male; Models, Chemical; Nitrilotriacetic Acid; Pentetic Acid; Pressure; Rabbits; Sulfonamides; Temperature; Time Factors; Ultraviolet Rays; Water

2002
Carbonic anhydrase inhibitors: inhibition of the tumor-associated isozyme IX with aromatic and heterocyclic sulfonamides.
    Bioorganic & medicinal chemistry letters, 2003, Mar-24, Volume: 13, Issue:6

    Topics: Animals; Antigens, Neoplasm; Carbonic Anhydrase Inhibitors; Carbonic Anhydrase IX; Carbonic Anhydrases; Cattle; Heterocyclic Compounds; Humans; Hydrocarbons, Aromatic; Isoenzymes; Kinetics; Neoplasm Proteins; Neoplasms; Structure-Activity Relationship; Sulfonamides

2003
Carbonic anhydrase inhibitors. Inhibition of tumor-associated isozyme IX by halogenosulfanilamide and halogenophenylaminobenzolamide derivatives.
    Journal of medicinal chemistry, 2003, May-22, Volume: 46, Issue:11

    Topics: Antigens, Neoplasm; Antineoplastic Agents; Benzene Derivatives; Bromine; Carbonic Anhydrase I; Carbonic Anhydrase II; Carbonic Anhydrase IV; Carbonic Anhydrase IX; Carbonic Anhydrases; Chlorine; Enzyme Inhibitors; Humans; Iodine; Neoplasm Proteins; Structure-Activity Relationship; Sulfanilamides; Sulfonamides

2003
Carbonic anhydrase inhibitors: the first QSAR study on inhibition of tumor-associated isoenzyme IX with aromatic and heterocyclic sulfonamides.
    Bioorganic & medicinal chemistry letters, 2004, Jun-21, Volume: 14, Issue:12

    Topics: Antigens, Neoplasm; Carbonic Anhydrase Inhibitors; Carbonic Anhydrase IX; Carbonic Anhydrases; Isoenzymes; Quantitative Structure-Activity Relationship; Sulfonamides

2004
Carbonic anhydrase inhibitors. Novel sulfanilamide/acetazolamide derivatives obtained by the tail approach and their interaction with the cytosolic isozymes I and II, and the tumor-associated isozyme IX.
    Bioorganic & medicinal chemistry letters, 2005, Jan-17, Volume: 15, Issue:2

    Topics: Acetazolamide; Amines; Biomarkers, Tumor; Carbonic Anhydrase Inhibitors; Catalysis; Cytosol; Heterocyclic Compounds; Humans; Isoenzymes; Morpholines; Piperazine; Piperazines; Piperidines; Structure-Activity Relationship; Sulfanilamide; Sulfanilamides

2005
Carbonic anhydrase inhibitors. Inhibition of the transmembrane isozyme XII with sulfonamides-a new target for the design of antitumor and antiglaucoma drugs?
    Bioorganic & medicinal chemistry letters, 2005, Feb-15, Volume: 15, Issue:4

    Topics: Antineoplastic Agents; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Drug Design; Glaucoma; Humans; Isoenzymes; Structure-Activity Relationship; Sulfonamides

2005
Carbonic anhydrase inhibitors. Inhibition of the human cytosolic isozyme VII with aromatic and heterocyclic sulfonamides.
    Bioorganic & medicinal chemistry letters, 2005, Feb-15, Volume: 15, Issue:4

    Topics: Anticonvulsants; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Heterocyclic Compounds; Humans; Hydrocarbons, Aromatic; Isoenzymes; Protein Subunits; Structure-Activity Relationship; Sulfonamides

2005
Carbonic anhydrase inhibitors. Inhibition of the membrane-bound human and bovine isozymes IV with sulfonamides.
    Bioorganic & medicinal chemistry letters, 2005, Feb-15, Volume: 15, Issue:4

    Topics: Animals; Carbonic Anhydrase Inhibitors; Carbonic Anhydrase IV; Cattle; Dose-Response Relationship, Drug; Humans; Isoenzymes; Kinetics; Membrane Proteins; Structure-Activity Relationship; Sulfonamides; Sulfonic Acids

2005
Carbonic anhydrase inhibitors: inhibition of the transmembrane isozyme XIV with sulfonamides.
    Bioorganic & medicinal chemistry letters, 2005, Sep-01, Volume: 15, Issue:17

    Topics: Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Fructose; Humans; Kinetics; Membrane Proteins; Protein Binding; Structure-Activity Relationship; Sulfonamides; Topiramate

2005
Carbonic anhydrase inhibitors. The mitochondrial isozyme VB as a new target for sulfonamide and sulfamate inhibitors.
    Journal of medicinal chemistry, 2005, Dec-01, Volume: 48, Issue:24

    Topics: Amino Acid Sequence; Carbonic Anhydrase Inhibitors; Carbonic Anhydrase V; Catalysis; Cloning, Molecular; Humans; Isoenzymes; Kinetics; Mitochondria; Molecular Sequence Data; Structure-Activity Relationship; Sulfonamides; Sulfonic Acids

2005
Carbonic anhydrase inhibitors: cloning and sulfonamide inhibition studies of a carboxyterminal truncated alpha-carbonic anhydrase from Helicobacter pylori.
    Bioorganic & medicinal chemistry letters, 2006, Apr-15, Volume: 16, Issue:8

    Topics: Benzenesulfonamides; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Cloning, Molecular; Helicobacter pylori; Humans; Hydrogen-Ion Concentration; Structure-Activity Relationship; Sulfonamides

2006
Carbonic anhydrase inhibitors: DNA cloning and inhibition studies of the alpha-carbonic anhydrase from Helicobacter pylori, a new target for developing sulfonamide and sulfamate gastric drugs.
    Journal of medicinal chemistry, 2006, Mar-23, Volume: 49, Issue:6

    Topics: Amino Acid Sequence; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Cloning, Molecular; DNA, Bacterial; Gastric Mucosa; Gastritis; Helicobacter pylori; Humans; Molecular Sequence Data; Polymorphism, Genetic; Stomach Neoplasms; Stomach Ulcer; Sulfonamides; Sulfonic Acids

2006
Carbonic anhydrase inhibitors. DNA cloning, characterization, and inhibition studies of the human secretory isoform VI, a new target for sulfonamide and sulfamate inhibitors.
    Journal of medicinal chemistry, 2007, Jan-25, Volume: 50, Issue:2

    Topics: Amino Acid Sequence; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Catalysis; Cloning, Molecular; DNA; Humans; Isoenzymes; Molecular Sequence Data; Protein Subunits; Sequence Homology, Amino Acid; Structure-Activity Relationship; Sulfonamides; Sulfonic Acids

2007
Carbonic anhydrase inhibitors: the beta-carbonic anhydrase from Helicobacter pylori is a new target for sulfonamide and sulfamate inhibitors.
    Bioorganic & medicinal chemistry letters, 2007, Jul-01, Volume: 17, Issue:13

    Topics: Amino Acid Sequence; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Chemistry, Pharmaceutical; Cloning, Molecular; Drug Design; Enzyme Inhibitors; Helicobacter pylori; Humans; Molecular Sequence Data; Recombinant Proteins; Sequence Homology, Amino Acid; Stomach Neoplasms; Stomach Ulcer; Sulfonamides

2007
Carbonic anhydrase inhibitors: cloning, characterization, and inhibition studies of the cytosolic isozyme III with sulfonamides.
    Bioorganic & medicinal chemistry, 2007, Dec-01, Volume: 15, Issue:23

    Topics: Amino Acid Sequence; Carbonic Anhydrase III; Carbonic Anhydrase Inhibitors; Cloning, Molecular; Cytosol; Enzyme Activation; Humans; Isoenzymes; Kinetics; Molecular Sequence Data; Recombinant Proteins; Structure-Activity Relationship; Sulfonamides; Sulfonic Acids

2007
Carbonic anhydrase inhibitors: inhibition of the beta-class enzyme from the yeast Saccharomyces cerevisiae with sulfonamides and sulfamates.
    Bioorganic & medicinal chemistry, 2009, Feb-01, Volume: 17, Issue:3

    Topics: Amino Acid Sequence; Antifungal Agents; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Kinetics; Molecular Sequence Data; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Sequence Alignment; Sequence Homology, Amino Acid; Sulfonamides; Sulfonic Acids

2009
Cloning, expression, post-translational modifications and inhibition studies on the latest mammalian carbonic anhydrase isoform, CA XV.
    Journal of medicinal chemistry, 2009, Feb-12, Volume: 52, Issue:3

    Topics: Animals; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Cloning, Molecular; Isoenzymes; Kidney; Mice; Protein Processing, Post-Translational

2009
A QSAR study on relationship between structure of sulfonamides and their carbonic anhydrase inhibitory activity using the eigenvalue (EVA) method.
    European journal of medicinal chemistry, 2009, Volume: 44, Issue:9

    Topics: Artificial Intelligence; Carbonic Anhydrase II; Computer Simulation; Isoenzymes; Models, Chemical; Quantitative Structure-Activity Relationship; Sulfonamides

2009
Molecular cloning, characterization, and inhibition studies of the Rv1284 beta-carbonic anhydrase from Mycobacterium tuberculosis with sulfonamides and a sulfamate.
    Journal of medicinal chemistry, 2009, Apr-23, Volume: 52, Issue:8

    Topics: Amino Acid Sequence; Anti-Bacterial Agents; Base Sequence; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Catalysis; Cloning, Molecular; Drug Resistance, Multiple, Bacterial; Humans; Molecular Sequence Data; Mycobacterium tuberculosis; Recombinant Proteins; Structure-Activity Relationship; Sulfonamides; Sulfonic Acids

2009
Carbonic anhydrase inhibitors. Cloning, characterization, and inhibition studies of a new beta-carbonic anhydrase from Mycobacterium tuberculosis.
    Journal of medicinal chemistry, 2009, May-14, Volume: 52, Issue:9

    Topics: Amino Acid Sequence; Biocatalysis; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Cloning, Molecular; Molecular Sequence Data; Mycobacterium tuberculosis; Sulfonamides; Sulfonic Acids

2009
Carbonic anhydrase inhibitors. Inhibition and homology modeling studies of the fungal beta-carbonic anhydrase from Candida albicans with sulfonamides.
    Bioorganic & medicinal chemistry, 2009, Jul-01, Volume: 17, Issue:13

    Topics: Amino Acid Sequence; Antifungal Agents; Bacterial Proteins; Candida albicans; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Cryptococcus neoformans; Helicobacter pylori; Humans; Models, Molecular; Molecular Sequence Data; Protein Binding; Protein Conformation; Sequence Alignment; Structure-Activity Relationship; Sulfonamides

2009
Carbonic anhydrase inhibitors. Inhibition studies of a coral secretory isoform by sulfonamides.
    Bioorganic & medicinal chemistry, 2009, Jul-15, Volume: 17, Issue:14

    Topics: Amino Acid Sequence; Animals; Anthozoa; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Humans; Molecular Sequence Data; Molecular Structure; Recombinant Proteins; Sequence Alignment; Sulfonamides

2009
Carbonic anhydrase inhibitors. Characterization and inhibition studies of the most active beta-carbonic anhydrase from Mycobacterium tuberculosis, Rv3588c.
    Bioorganic & medicinal chemistry letters, 2009, Dec-01, Volume: 19, Issue:23

    Topics: Amino Acid Sequence; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Catalytic Domain; Drug Design; Models, Molecular; Molecular Sequence Data; Molecular Structure; Mycobacterium tuberculosis; Structure-Activity Relationship

2009
Cloning, characterization, and inhibition studies of a beta-carbonic anhydrase from Brucella suis.
    Journal of medicinal chemistry, 2010, Mar-11, Volume: 53, Issue:5

    Topics: Amino Acid Sequence; Animals; Base Sequence; Brucella suis; Brucellosis; Carbonic Anhydrases; Cloning, Molecular; DNA, Bacterial; Humans; Kinetics; Molecular Sequence Data; Phylogeny; Polymerase Chain Reaction; Sequence Alignment; Sequence Analysis, DNA; Structure-Activity Relationship; Sulfonamides

2010
Mutation of Phe91 to Asn in human carbonic anhydrase I unexpectedly enhanced both catalytic activity and affinity for sulfonamide inhibitors.
    Bioorganic & medicinal chemistry, 2010, Aug-01, Volume: 18, Issue:15

    Topics: Amino Acid Sequence; Amino Acid Substitution; Asparagine; Binding Sites; Carbonic Anhydrase I; Carbonic Anhydrase II; Carbonic Anhydrase Inhibitors; Cell Line, Tumor; Computer Simulation; Humans; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Phenylalanine; Sulfonamides

2010
Carbonic anhydrase inhibitors. Inhibition studies with anions and sulfonamides of a new cytosolic enzyme from the scleractinian coral Stylophora pistillata.
    Bioorganic & medicinal chemistry letters, 2011, Jan-15, Volume: 21, Issue:2

    Topics: Animals; Anions; Anthozoa; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Humans; Structure-Activity Relationship; Sulfonamides

2011
A new β-carbonic anhydrase from Brucella suis, its cloning, characterization, and inhibition with sulfonamides and sulfamates, leading to impaired pathogen growth.
    Bioorganic & medicinal chemistry, 2011, Feb-01, Volume: 19, Issue:3

    Topics: Anti-Bacterial Agents; Brucella suis; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Cloning, Molecular; Drug Design; Drug Discovery; Inhibitory Concentration 50; Kinetics; Sulfonamides; Sulfonic Acids

2011
Inhibition studies of the β-carbonic anhydrases from the bacterial pathogen Salmonella enterica serovar Typhimurium with sulfonamides and sulfamates.
    Bioorganic & medicinal chemistry, 2011, Aug-15, Volume: 19, Issue:16

    Topics: Anti-Bacterial Agents; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Salmonella Infections; Salmonella typhimurium; Structure-Activity Relationship; Sulfonamides; Sulfonic Acids

2011
Cloning, characterization and sulfonamide inhibition studies of an α-carbonic anhydrase from the living fossil sponge Astrosclera willeyana.
    Bioorganic & medicinal chemistry, 2012, Feb-15, Volume: 20, Issue:4

    Topics: Amino Acid Sequence; Animals; Carbonic Anhydrases; Cloning, Molecular; Fossils; Humans; Molecular Sequence Data; Porifera; Protein Binding; Sequence Alignment; Sulfonamides; Sulfonic Acids

2012
Mutation of active site residues Asn67 to Ile, Gln92 to Val and Leu204 to Ser in human carbonic anhydrase II: influences on the catalytic activity and affinity for inhibitors.
    Bioorganic & medicinal chemistry, 2012, Apr-01, Volume: 20, Issue:7

    Topics: Amino Acid Sequence; Amino Acid Substitution; Carbonic Anhydrase II; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Catalytic Domain; Humans; Molecular Sequence Data; Mutagenesis, Site-Directed; Sulfonamides

2012
Molecular cloning, characterization, and inhibition studies of a β-carbonic anhydrase from Malassezia globosa, a potential antidandruff target.
    Journal of medicinal chemistry, 2012, Apr-12, Volume: 55, Issue:7

    Topics: Amino Acid Sequence; Animals; Antifungal Agents; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Cloning, Molecular; Dermatomycoses; Fungal Proteins; Humans; Isoenzymes; Malassezia; Mice; Microbial Sensitivity Tests; Models, Molecular; Molecular Sequence Data; Recombinant Fusion Proteins; Scalp Dermatoses; Structure-Activity Relationship; Sulfonamides; Sulfonic Acids

2012
The alpha-carbonic anhydrase from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1 is highly susceptible to inhibition by sulfonamides.
    Bioorganic & medicinal chemistry, 2013, Mar-15, Volume: 21, Issue:6

    Topics: Amino Acid Sequence; Bacteria; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Humans; Kinetics; Molecular Sequence Data; Phylogeny; Protein Binding; Recombinant Proteins; Sequence Alignment; Sulfonamides

2013
DNA cloning, characterization, and inhibition studies of an α-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae.
    Journal of medicinal chemistry, 2012, Dec-13, Volume: 55, Issue:23

    Topics: Amino Acid Sequence; Biocatalysis; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Cloning, Molecular; DNA; Electrophoresis, Polyacrylamide Gel; Molecular Sequence Data; Phylogeny; Sequence Homology, Amino Acid; Vibrio cholerae

2012
Cloning, characterization, and sulfonamide and thiol inhibition studies of an α-carbonic anhydrase from Trypanosoma cruzi, the causative agent of Chagas disease.
    Journal of medicinal chemistry, 2013, Feb-28, Volume: 56, Issue:4

    Topics: Amino Acid Sequence; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Chagas Disease; Cloning, Molecular; Humans; Molecular Sequence Data; Phylogeny; Protozoan Proteins; Structure-Activity Relationship; Sulfhydryl Compounds; Sulfonamides; Thiadiazoles; Trypanocidal Agents; Trypanosoma cruzi

2013
Carbonic anhydrase inhibitors: inhibition of the β-class enzyme from the pathogenic yeast Candida glabrata with sulfonamides, sulfamates and sulfamides.
    Bioorganic & medicinal chemistry letters, 2013, May-01, Volume: 23, Issue:9

    Topics: Acetazolamide; Amino Acid Sequence; Antifungal Agents; Candida glabrata; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Humans; Kinetics; Molecular Sequence Data; Phylogeny; Protein Binding; Sequence Alignment; Structure-Activity Relationship; Sulfonamides; Sulfonic Acids

2013
Cloning, characterization, and inhibition studies of a β-carbonic anhydrase from Leishmania donovani chagasi, the protozoan parasite responsible for leishmaniasis.
    Journal of medicinal chemistry, 2013, Sep-26, Volume: 56, Issue:18

    Topics: Amino Acid Sequence; Antiprotozoal Agents; Biocatalysis; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Cloning, Molecular; Leishmania infantum; Leishmaniasis; Molecular Sequence Data

2013
Sulfonamide inhibition studies of the δ-carbonic anhydrase from the diatom Thalassiosira weissflogii.
    Bioorganic & medicinal chemistry letters, 2014, Jan-01, Volume: 24, Issue:1

    Topics: Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Diatoms; Dose-Response Relationship, Drug; Molecular Structure; Structure-Activity Relationship; Sulfonamides

2014
Sulfonamide inhibition studies of the γ-carbonic anhydrase from the oral pathogen Porphyromonas gingivalis.
    Bioorganic & medicinal chemistry letters, 2014, Jan-01, Volume: 24, Issue:1

    Topics: Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Dose-Response Relationship, Drug; Humans; Molecular Structure; Porphyromonas gingivalis; Structure-Activity Relationship; Sulfonamides

2014
Sulfonamide inhibition studies of two β-carbonic anhydrases from the bacterial pathogen Legionella pneumophila.
    Bioorganic & medicinal chemistry, 2014, Jun-01, Volume: 22, Issue:11

    Topics: Amino Acid Sequence; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Dose-Response Relationship, Drug; Legionella pneumophila; Molecular Sequence Data; Molecular Structure; Sequence Alignment; Structure-Activity Relationship; Sulfonamides

2014
Sulfonamide inhibition study of the carbonic anhydrases from the bacterial pathogen Porphyromonas gingivalis: the β-class (PgiCAb) versus the γ-class (PgiCA) enzymes.
    Bioorganic & medicinal chemistry, 2014, Sep-01, Volume: 22, Issue:17

    Topics: Amino Acid Sequence; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Dose-Response Relationship, Drug; Humans; Molecular Sequence Data; Molecular Structure; Phylogeny; Porphyromonas gingivalis; Structure-Activity Relationship; Sulfonamides

2014
Sulfonamide inhibition studies of the η-class carbonic anhydrase from the malaria pathogen Plasmodium falciparum.
    Bioorganic & medicinal chemistry, 2015, Feb-01, Volume: 23, Issue:3

    Topics: Antimalarials; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Plasmodium falciparum; Structure-Activity Relationship; Sulfonamides

2015
Sulfonamide inhibition studies of the γ-carbonic anhydrase from the Antarctic cyanobacterium Nostoc commune.
    Bioorganic & medicinal chemistry, 2015, Apr-15, Volume: 23, Issue:8

    Topics: Amino Acid Sequence; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Molecular Sequence Data; Nostoc commune; Sequence Alignment; Sulfanilamide; Sulfanilamides; Sulfonamides; Thiazines; Thiophenes

2015
The β-carbonic anhydrase from the malaria mosquito Anopheles gambiae is highly inhibited by sulfonamides.
    Bioorganic & medicinal chemistry, 2015, May-15, Volume: 23, Issue:10

    Topics: Amino Acid Sequence; Animals; Anopheles; Baculoviridae; Bicarbonates; Carbon Dioxide; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Cloning, Molecular; Gene Expression; High-Throughput Screening Assays; Insect Proteins; Insecticides; Kinetics; Molecular Sequence Data; Phylogeny; Protons; Recombinant Proteins; Sequence Alignment; Sf9 Cells; Spodoptera; Sulfanilamides

2015
Sulfonamide inhibition study of the β-class carbonic anhydrase from the caries producing pathogen Streptococcus mutans.
    Bioorganic & medicinal chemistry letters, 2015, Jun-01, Volume: 25, Issue:11

    Topics: Amino Acid Sequence; Anti-Bacterial Agents; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Gene Expression Regulation, Bacterial; Gene Expression Regulation, Enzymologic; Molecular Sequence Data; Molecular Structure; Phylogeny; Streptococcus mutans; Sulfonamides

2015
Sulfonamide inhibition studies of the γ-carbonic anhydrase from the Antarctic bacterium Pseudoalteromonas haloplanktis.
    Bioorganic & medicinal chemistry letters, 2015, Sep-01, Volume: 25, Issue:17

    Topics: Acclimatization; Amino Acid Sequence; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Cold Temperature; Humans; Molecular Sequence Data; Phylogeny; Pseudoalteromonas; Sequence Alignment; Sulfonamides

2015
Sulfonamide inhibition studies of the α-carbonic anhydrase from the gammaproteobacterium Thiomicrospira crunogena XCL-2, TcruCA.
    Bioorganic & medicinal chemistry letters, 2016, Jan-15, Volume: 26, Issue:2

    Topics: Anti-Bacterial Agents; Carbon Dioxide; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Gammaproteobacteria; Molecular Docking Simulation; Sulfonamides

2016
Sulfonamide inhibition studies of the γ-carbonic anhydrase from the Antarctic bacterium Colwellia psychrerythraea.
    Bioorganic & medicinal chemistry letters, 2016, Feb-15, Volume: 26, Issue:4

    Topics: Alteromonadaceae; Anti-Bacterial Agents; Bacterial Proteins; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Humans; Kinetics; Phylogeny; Protein Binding; Sulfanilamide; Sulfanilamides

2016
Sulfonamide inhibition studies of the β-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae.
    Bioorganic & medicinal chemistry, 2016, Mar-01, Volume: 24, Issue:5

    Topics: Amino Acid Sequence; Base Sequence; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Cholera; Crystallography, X-Ray; Humans; Models, Molecular; Molecular Sequence Data; Sulfonamides; Vibrio cholerae

2016
Sulfonamide inhibition studies of the β-carbonic anhydrase from the newly discovered bacterium Enterobacter sp. B13.
    Bioorganic & medicinal chemistry letters, 2016, Apr-01, Volume: 26, Issue:7

    Topics: Acetazolamide; Benzenesulfonamides; Carbonic Anhydrase I; Carbonic Anhydrase Inhibitors; Enterobacter; Enterobacteriaceae Infections; Humans; Methazolamide; Structure-Activity Relationship; Sulfonamides

2016
Comparison of the sulfonamide inhibition profiles of the α-, β- and γ-carbonic anhydrases from the pathogenic bacterium Vibrio cholerae.
    Bioorganic & medicinal chemistry letters, 2016, Apr-15, Volume: 26, Issue:8

    Topics: Amino Acid Sequence; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Dose-Response Relationship, Drug; Humans; Molecular Structure; Structure-Activity Relationship; Sulfonamides; Vibrio cholerae

2016
Cloning, expression, purification and sulfonamide inhibition profile of the complete domain of the η-carbonic anhydrase from Plasmodium falciparum.
    Bioorganic & medicinal chemistry letters, 2016, 09-01, Volume: 26, Issue:17

    Topics: Amino Acid Sequence; Carbonic Anhydrase I; Carbonic Anhydrase II; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Cloning, Molecular; Humans; Kinetics; Molecular Sequence Data; Plasmodium falciparum; Protein Isoforms; Protein Structure, Tertiary; Recombinant Proteins; Sequence Alignment; Structure-Activity Relationship; Sulfonamides

2016