4-(2-aminoethyl)benzenesulfonamide has been researched along with acetazolamide in 66 studies
Studies (4-(2-aminoethyl)benzenesulfonamide) | Trials (4-(2-aminoethyl)benzenesulfonamide) | Recent Studies (post-2010) (4-(2-aminoethyl)benzenesulfonamide) | Studies (acetazolamide) | Trials (acetazolamide) | Recent Studies (post-2010) (acetazolamide) |
---|---|---|---|---|---|
91 | 0 | 37 | 7,604 | 495 | 1,521 |
Protein | Taxonomy | 4-(2-aminoethyl)benzenesulfonamide (IC50) | acetazolamide (IC50) |
---|---|---|---|
Chain A, Class Iii Chitinase Chia1 | Aspergillus fumigatus A1163 | 164 | |
Carbonic anhydrase 12 | Homo sapiens (human) | 0.3178 | |
Renin | Homo sapiens (human) | 8.2 | |
Carbonic anhydrase 1 | Homo sapiens (human) | 2.3173 | |
Carbonic anhydrase 2 | Homo sapiens (human) | 1.2619 | |
Carbonic anhydrase 2 | Bos taurus (cattle) | 0.7 | |
Carbonic anhydrase 3 | Homo sapiens (human) | 1.95 | |
Cathepsin B | Bos taurus (cattle) | 0.02 | |
Steryl-sulfatase | Homo sapiens (human) | 0.025 | |
Carbonic anhydrase 4 | Homo sapiens (human) | 0.1216 | |
Carbonic anhydrase 6 | Homo sapiens (human) | 0.2925 | |
Carbonic anhydrase 5A, mitochondrial | Homo sapiens (human) | 0.1763 | |
Carbonic anhydrase 7 | Homo sapiens (human) | 1.1737 | |
Carbonic anhydrase 9 | Homo sapiens (human) | 0.464 | |
Renin | Macaca mulatta (Rhesus monkey) | 8.2 | |
Carbonic anhydrase 13 | Homo sapiens (human) | 0.23 | |
Carbonic anhydrase 4 | Bos taurus (cattle) | 0.07 | |
Carbonic anhydrase 13 | Mus musculus (house mouse) | 0.77 | |
Carbonic anhydrase 14 | Homo sapiens (human) | 0.183 | |
Carbonic anhydrase 5B, mitochondrial | Homo sapiens (human) | 0.23 |
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 2 (3.03) | 18.2507 |
2000's | 31 (46.97) | 29.6817 |
2010's | 33 (50.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Briganti, F; Menabuoni, L; Mincione, F; Mincione, G; Scozzafava, A; Supuran, CT | 2 |
Briganti, F; Ilies, MA; Scozzafava, A; Supuran, CT | 1 |
Menabuoni, L; Mincione, F; Mincione, G; Scozzafava, A; Supuran, CT | 1 |
Menabuoni, L; Mincione, F; Scozzafava, A; Supuran, CT | 1 |
Franchi, M; Gallori, E; Pastorek, J; Pastorekova, S; Scozzafava, A; Supuran, CT; Vullo, D | 1 |
Antel, J; Franchi, M; Gallori, E; Scozzafava, A; Supuran, CT; Vullo, D | 1 |
Jaiswal, M; Khadikar, PV; Scozzafava, A; Supuran, CT | 1 |
Casini, A; Lehtonen, JM; Parkkila, S; Scozzafava, A; Supuran, CT; Vullo, D | 1 |
Fasolis, G; Garaj, V; Innocenti, A; Montero, JL; Puccetti, L; Scozzafava, A; Supuran, CT; Vullo, D; Winum, JY | 1 |
Casini, A; Ferry, JG; Innocenti, A; Scozzafava, A; Supuran, CT; Zimmerman, S | 1 |
Innocenti, A; Nishimori, I; Pastorek, J; Pastoreková, S; Scozzafava, A; Supuran, CT; Vullo, D | 1 |
Innocenti, A; Kaila, K; Ranki, H; Rivera, C; Scozzafava, A; Supuran, CT; Voipio, J; Vullo, D | 1 |
Antel, J; Firnges, MA; Innocenti, A; Scozzafava, A; Supuran, CT; Wurl, M | 1 |
Cecchi, A; Fasolis, G; Gamberi, A; Montero, JL; Puccetti, L; Scozzafava, A; Supuran, CT; Winum, JY | 1 |
Cecchi, A; Hulikova, A; Montero, JL; Pastorek, J; Pastoreková, S; Scozzafava, A; Supuran, CT; Winum, JY | 1 |
Innocenti, A; Mastrolorenzo, A; Nishimori, I; Scozzafava, A; Supuran, CT; Vullo, D | 2 |
Minakuchi, T; Morimoto, K; Nishimori, I; Onishi, S; Scozzafava, A; Supuran, CT; Vullo, D | 1 |
Minakuchi, T; Morimoto, K; Nishimori, I; Onishi, S; Sano, S; Scozzafava, A; Supuran, CT; Takeuchi, H; Vullo, D | 1 |
Minakuchi, T; Nishimori, I; Onishi, S; Scozzafava, A; Supuran, CT; Vullo, D | 1 |
Kohsaki, T; Minakuchi, T; Nishimori, I; Onishi, S; Scozzafava, A; Supuran, CT; Takeuchi, H; Vullo, D | 1 |
Cecchi, A; Minakuchi, T; Nishimori, I; Onishi, S; Scozzafava, A; Supuran, CT; Vullo, D | 1 |
Cecchi, A; Dogné, JM; Frederick, R; Ledecq, M; Masereel, B; Supuran, CT; Thiry, A; Wouters, J | 1 |
Arslan, O; Aydin, M; Guler, OO; Innocenti, A; Isik, S; Kockar, F; Scozzafava, A; Supuran, CT | 1 |
Hilvo, M; Innocenti, A; Kulomaa, MS; Parkkila, S; Salzano, AM; Scaloni, A; Scozzafava, A; Supuran, CT | 1 |
Eroğlu, E; Oltulu, O; Yaşar, MM | 1 |
Minakuchi, T; Nishimori, I; Scozzafava, A; Supuran, CT; Vullo, D | 2 |
Innocenti, A; Minakuchi, T; Nishimori, I; Scozzafava, A; Supuran, CT; Vullo, D | 1 |
Hall, RA; Innocenti, A; Mühlschlegel, FA; Schlicker, C; Scozzafava, A; Steegborn, C; Supuran, CT | 1 |
Bertucci, A; Innocenti, A; Scozzafava, A; Supuran, CT; Tambutté, S; Zoccola, D | 2 |
Carta, F; Maresca, A; Scozzafava, A; Supuran, CT; Vullo, D | 1 |
Carta, F; Covarrubias, AS; Jones, TA; Maresca, A; Mowbray, SL; Supuran, CT | 1 |
Joseph, P; Köhler, S; Minakuchi, T; Montero, JL; Nishimori, I; Ouahrani-Bettache, S; Scozzafava, A; Supuran, CT; Turtaut, F; Vullo, D; Winum, JY | 1 |
Bornaghi, LF; Charman, SA; Innocenti, A; Lopez, M; Poulsen, SA; Supuran, CT; Vullo, D | 1 |
Arslan, O; Aydin, M; Güler, OO; Işik, S; Kockar, F; Maresca, A; Sinan, S; Supuran, CT; Turan, Y; Turkoglu, S | 1 |
Joseph, P; Köhler, S; Minakuchi, T; Montero, JL; Nishimori, I; Ouahrani-Bettache, S; Scozzafava, A; Supuran, CT; Vullo, D; Winum, JY | 1 |
Jackson, DJ; Ohradanova, A; Pastorek, J; Pastorekova, S; Supuran, CT; Vullo, D; Wörheide, G | 1 |
Bornaghi, LF; Innocenti, A; Lopez, M; Moeker, J; Poulsen, SA; Rossit, S; Supuran, CT; Teruya, K; Wilkinson, BL | 1 |
Alper, M; Arslan, O; Işık, S; Kockar, F; Maresca, A; Ozensoy, O; Sinan, S; Supuran, CT; Turkoglu, S | 1 |
Hewitson, KS; Mastrolorenzo, A; Scozzafava, A; Supuran, CT; Vullo, D | 1 |
Capasso, C; Carginale, V; Luca, VD; Rossi, M; Scozzafava, A; Supuran, CT; Vullo, D | 1 |
Capasso, C; Carginale, V; De Luca, V; Del Prete, S; Isik, S; Scozzafava, A; Supuran, CT; Vullo, D | 1 |
Capaci Rodrigues, G; Capasso, C; Pan, P; Parkkila, S; Scozzafava, A; Supuran, CT; Tolvanen, ME; Vermelho, AB | 1 |
Capasso, C; Leewattanapasuk, W; Mastrolorenzo, A; Mühlschlegel, FA; Supuran, CT; Vullo, D | 1 |
Capasso, C; Corte-Real, S; Pan, P; Parkkila, S; Rodrigues, Ide A; Salonen, T; Supuran, CT; Syrjänen, L; Vermelho, AB; Vullo, D | 1 |
Alothman, Z; Capasso, C; De Luca, V; Del Prete, S; Osman, SM; Scozzafava, A; Supuran, CT; Vullo, D | 2 |
Barboiu, M; Cristian, A; Nasr, G; Supuran, CT; Vullo, D; Winum, JY | 1 |
Capasso, C; Minakuchi, T; Nishimori, I; Scozzafava, A; Supuran, CT; Vullo, D | 1 |
AlOthman, Z; Capasso, C; Osman, SM; Prete, SD; Scozzafava, A; Supuran, CT; Vullo, D | 1 |
Andrews, KT; Capasso, C; Del Prete, S; Fisher, GM; Poulsen, SA; Supuran, CT; Vullo, D | 1 |
Capasso, C; Carginale, V; De Luca, V; Del Prete, S; Scozzafava, A; Supuran, CT; Vullo, D | 2 |
Kuuslahti, M; Parkkila, S; Supuran, CT; Syrjänen, L; Tolvanen, M; Vullo, D | 1 |
Capasso, C; Dedeoglu, N; DeLuca, V; Isik, S; Kockar, F; Supuran, CT; Yildirim, H | 1 |
Bhatt, A; Mahon, BP; McKenna, R; Supuran, CT; Vullo, D | 1 |
AlOthman, Z; Capasso, C; Carginale, V; De Luca, V; Del Prete, S; Osman, SM; Scozzafava, A; Supuran, CT; Vullo, D | 1 |
AlOthman, Z; Capasso, C; Carginale, V; De Luca, V; Del Prete, S; Ferraroni, M; Osman, SM; Supuran, CT; Vullo, D | 1 |
Aşık, A; Beldüz, AO; Çanakçı, S; Çolak, DN; Eminoğlu, A; Supuran, CT; Vullo, D | 1 |
AlOthman, Z; Capasso, C; Carginale, V; De Luca, V; Del Prete, S; Osman, SM; Supuran, CT; Vullo, D | 2 |
Ahmed, HY; Al-Ansary, GH; Altoukhy, A; Bua, S; Eldehna, WM; Ghabbour, H; Gratteri, P; Nocentini, A; Supuran, CT | 1 |
Bua, S; Kopecka, J; Mujumdar, P; Poulsen, SA; Riganti, C; Supuran, CT | 1 |
66 other study(ies) available for 4-(2-aminoethyl)benzenesulfonamide and acetazolamide
Article | Year |
---|---|
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?
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: synthesis of water-soluble, aminoacyl/dipeptidyl sulfonamides possessing long-lasting intraocular pressure-lowering properties via the topical route.
Topics: Administration, Topical; Animals; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Cell Membrane Permeability; Cornea; Delayed-Action Preparations; Dipeptides; Disease Models, Animal; Glaucoma; Humans; Intraocular Pressure; Isoenzymes; Models, Molecular; Rabbits; Solubility; Sulfonamides; Time Factors | 1999 |
Carbonic anhydrase inhibitors: synthesis of membrane-impermeant low molecular weight sulfonamides possessing in vivo selectivity for the membrane-bound versus cytosolic isozymes.
Topics: Animals; Carbonic Anhydrase Inhibitors; Cattle; Cell Membrane Permeability; Cytosol; Erythrocyte Membrane; Humans; Isoenzymes; Magnetic Resonance Spectroscopy; Male; Rats; Rats, Wistar; Spectrophotometry, Ultraviolet; Sulfonamides | 2000 |
Carbonic anhydrase inhibitors: synthesis of sulfonamides incorporating dtpa tails and of their zinc complexes with powerful topical antiglaucoma properties.
Topics: Administration, Topical; Animals; Carbonic Anhydrase Inhibitors; Glaucoma; Intraocular Pressure; Pentetic Acid; Quantitative Structure-Activity Relationship; Rabbits; Sulfonamides; Zinc | 2001 |
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.
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.
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 mitochondrial isozyme V with aromatic and heterocyclic sulfonamides.
Topics: Animals; Benzene Derivatives; Carbonic Anhydrase Inhibitors; Carbonic Anhydrase V; Coumarins; Mice; Mitochondria; Structure-Activity Relationship; Sulfonamides; Thiadiazoles | 2004 |
Carbonic anhydrase inhibitors: the first QSAR study on inhibition of tumor-associated isoenzyme IX with aromatic and heterocyclic sulfonamides.
Topics: Antigens, Neoplasm; Carbonic Anhydrase Inhibitors; Carbonic Anhydrase IX; Carbonic Anhydrases; Isoenzymes; Quantitative Structure-Activity Relationship; Sulfonamides | 2004 |
Carbonic anhydrase inhibitors. Inhibition of cytosolic isozyme XIII with aromatic and heterocyclic sulfonamides: a novel target for the drug design.
Topics: Amino Acid Sequence; Animals; Carbonic Anhydrase Inhibitors; Cytosol; Drug Design; Humans; Hydrogen-Ion Concentration; Isoenzymes; Kinetics; Molecular Sequence Data; Neoplasms; Rats; Structure-Activity Relationship; Sulfonamides | 2004 |
Carbonic anhydrase inhibitors: synthesis and inhibition of cytosolic/tumor-associated carbonic anhydrase isozymes I, II, and IX with sulfonamides incorporating 1,2,4-triazine moieties.
Topics: Antigens, Neoplasm; Antineoplastic Agents; Carbonic Anhydrase I; Carbonic Anhydrase II; Carbonic Anhydrase Inhibitors; Carbonic Anhydrase IX; Carbonic Anhydrases; Cytosol; Enzyme Inhibitors; Humans; Isoenzymes; Structure-Activity Relationship; Sulfonamides; Triazines | 2004 |
Carbonic anhydrase inhibitors. Inhibition of the prokariotic beta and gamma-class enzymes from Archaea with sulfonamides.
Topics: Archaea; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Humans; Isoenzymes; Molecular Structure; Structure-Activity Relationship; Sulfonamides | 2004 |
Carbonic anhydrase inhibitors. Inhibition of the transmembrane isozyme XII with sulfonamides-a new target for the design of antitumor and antiglaucoma drugs?
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.
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.
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: synthesis and inhibition of cytosolic/tumor-associated carbonic anhydrase isozymes I, II, and IX with sulfonamides incorporating thioureido-sulfanilyl scaffolds.
Topics: Antigens, Neoplasm; Carbonic Anhydrase I; Carbonic Anhydrase II; Carbonic Anhydrase Inhibitors; Carbonic Anhydrase IX; Carbonic Anhydrases; Catalytic Domain; Cytosol; Humans; Kinetics; Neoplasms; Structure-Activity Relationship; Sulfonamides; Urea | 2005 |
Carbonic anhydrase inhibitors. Design of fluorescent sulfonamides as probes of tumor-associated carbonic anhydrase IX that inhibit isozyme IX-mediated acidification of hypoxic tumors.
Topics: Animals; Antigens, Neoplasm; Carbonic Anhydrase Inhibitors; Carbonic Anhydrase IX; Carbonic Anhydrases; Catalytic Domain; Cell Hypoxia; Cell Line; Cell Membrane Permeability; Dogs; Erythrocyte Membrane; Extracellular Fluid; Fluorescent Dyes; Humans; Hydrogen-Ion Concentration; In Vitro Techniques; Isoenzymes; Mutation; Sequence Deletion; Sulfonamides | 2005 |
Carbonic anhydrase inhibitors: inhibition of the transmembrane isozyme XIV with sulfonamides.
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.
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.
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.
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.
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.
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.
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 |
Ligand-based and structure-based virtual screening to identify carbonic anhydrase IX inhibitors.
Topics: Antigens, Neoplasm; Carbonic Anhydrase Inhibitors; Carbonic Anhydrase IX; Carbonic Anhydrases; Computer Simulation; Drug Discovery; Drug Evaluation, Preclinical; Humans; Ligands; Protein Binding; Structure-Activity Relationship | 2009 |
Carbonic anhydrase inhibitors: inhibition of the beta-class enzyme from the yeast Saccharomyces cerevisiae with sulfonamides and sulfamates.
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.
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.
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.
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.
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.
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.
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. Inhibition of the Rv1284 and Rv3273 beta-carbonic anhydrases from Mycobacterium tuberculosis with diazenylbenzenesulfonamides.
Topics: Anti-Bacterial Agents; Benzenesulfonamides; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Humans; Mycobacterium tuberculosis; Recombinant Proteins; Structure-Activity Relationship; Sulfonamides | 2009 |
Carbonic anhydrase inhibitors. Characterization and inhibition studies of the most active beta-carbonic anhydrase from Mycobacterium tuberculosis, Rv3588c.
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.
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 |
Sulfonamide linked neoglycoconjugates--a new class of inhibitors for cancer-associated carbonic anhydrases.
Topics: Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Cell Membrane Permeability; Glycoconjugates; Humans; Isoenzymes; Neoplasms; 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.
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.
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.
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.
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.
Topics: Amino Acid Sequence; Animals; Carbonic Anhydrases; Cloning, Molecular; Fossils; Humans; Molecular Sequence Data; Porifera; Protein Binding; Sequence Alignment; Sulfonamides; Sulfonic Acids | 2012 |
Design and synthesis of thiourea compounds that inhibit transmembrane anchored carbonic anhydrases.
Topics: Carbohydrates; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Drug Design; Glycoconjugates; Humans; Protein Isoforms; Solubility; Sulfonamides; Thiourea | 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.
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.
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.
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.
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.
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.
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.
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.
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.
Topics: Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Dose-Response Relationship, Drug; Humans; Molecular Structure; Porphyromonas gingivalis; Structure-Activity Relationship; Sulfonamides | 2014 |
Carbonic anhydrase inhibitors. Inhibition of human cytosolic isoforms I and II with (reduced) Schiff's bases incorporating sulfonamide, carboxylate and carboxymethyl moieties.
Topics: Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Carboxylic Acids; Dose-Response Relationship, Drug; Humans; Isoenzymes; Molecular Structure; Schiff Bases; Structure-Activity Relationship; Sulfonamides | 2014 |
Sulfonamide inhibition studies of two β-carbonic anhydrases from the bacterial pathogen Legionella pneumophila.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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 |
Novel indolin-2-one-based sulfonamides as carbonic anhydrase inhibitors: Synthesis, in vitro biological evaluation against carbonic anhydrases isoforms I, II, IV and VII and molecular docking studies.
Topics: Carbonic Anhydrase I; Carbonic Anhydrase II; Carbonic Anhydrase Inhibitors; Carbonic Anhydrase IV; Carbonic Anhydrases; Catalytic Domain; Chemistry Techniques, Synthetic; Drug Design; Humans; Indoles; Isoenzymes; Molecular Docking Simulation; Structure-Activity Relationship; Sulfonamides | 2017 |
Carbonic Anhydrase XII Inhibitors Overcome Temozolomide Resistance in Glioblastoma.
Topics: Animals; Antineoplastic Agents; Brain Neoplasms; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Cell Survival; Drug Design; Drug Resistance, Neoplasm; Female; Glioblastoma; Humans; Mice; Mice, Nude; Protein Isoforms; Structure-Activity Relationship; Temozolomide; Transplantation, Heterologous; Tumor Cells, Cultured | 2019 |