sodium and acetazolamide

sodium has been researched along with acetazolamide in 7 studies

*Acetazolamide: One of the CARBONIC ANHYDRASE INHIBITORS that is sometimes effective against absence seizures. It is sometimes useful also as an adjunct in the treatment of tonic-clonic, myoclonic, and atonic seizures, particularly in women whose seizures occur or are exacerbated at specific times in the menstrual cycle. However, its usefulness is transient often because of rapid development of tolerance. Its antiepileptic effect may be due to its inhibitory effect on brain carbonic anhydrase, which leads to an increased transneuronal chloride gradient, increased chloride current, and increased inhibition. (From Smith and Reynard, Textbook of Pharmacology, 1991, p337) [MeSH]

*Acetazolamide: One of the CARBONIC ANHYDRASE INHIBITORS that is sometimes effective against absence seizures. It is sometimes useful also as an adjunct in the treatment of tonic-clonic, myoclonic, and atonic seizures, particularly in women whose seizures occur or are exacerbated at specific times in the menstrual cycle. However, its usefulness is transient often because of rapid development of tolerance. Its antiepileptic effect may be due to its inhibitory effect on brain carbonic anhydrase, which leads to an increased transneuronal chloride gradient, increased chloride current, and increased inhibition. (From Smith and Reynard, Textbook of Pharmacology, 1991, p337) [MeSH]

Research

Studies (7)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's0 (0.00)29.6817
2010's7 (100.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Capasso, C; Carginale, V; De Luca, V; Rossi, M; Scozzafava, A; Supuran, CT; Vullo, D1
Capasso, C; Dathan, NA; De Simone, G; Ludwig, M; Monti, SM; Scozzafava, A; Supuran, CT; Vullo, D1
Capasso, C; Carginale, V; De Luca, V; Del Prete, S; Scozzafava, A; Supuran, CT; Vullo, D1
Capasso, C; Ferry, JG; Sai Kumar, RS; Scozzafava, A; Supuran, CT; Vullo, D1
AlOthman, Z; Capasso, C; Minakuchi, T; Nishimori, I; Osman, SM; Scozzafava, A; Supuran, CT; Vullo, D1
AlOthman, Z; Capasso, C; Carginale, V; De Luca, V; Del Prete, S; Osman, SM; Supuran, CT; Vullo, D1
AlOthman, Z; Capasso, C; Carginale, V; De Luca, V; Del Prete, S; di Fonzo, P; Osman, SM; Supuran, CT; Vullo, D1

Other Studies

7 other study(ies) available for sodium and acetazolamide

ArticleYear
Anion inhibition studies of the fastest carbonic anhydrase (CA) known, the extremo-CA from the bacterium Sulfurihydrogenibium azorense.
    Bioorganic & medicinal chemistry letters, 2012, Dec-01, Volume: 22, Issue:23

    Topics: Amino Acid Sequence; Anions; Bacteria; Carbon Dioxide; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Catalysis; Kinetics; Molecular Sequence Data; Phylogeny; Protein Binding; Sequence Alignment; Temperature

2012
Kinetic and anion inhibition studies of a β-carbonic anhydrase (FbiCA 1) from the C4 plant Flaveria bidentis.
    Bioorganic & medicinal chemistry letters, 2013, Mar-15, Volume: 23, Issue:6

    Topics: Amino Acid Sequence; Anions; Carbon Dioxide; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Flaveria; Humans; Kinetics; Molecular Sequence Data; Phylogeny; Protein Isoforms; Recombinant Proteins

2013
A highly catalytically active γ-carbonic anhydrase from the pathogenic anaerobe Porphyromonas gingivalis and its inhibition profile with anions and small molecules.
    Bioorganic & medicinal chemistry letters, 2013, Jul-15, Volume: 23, Issue:14

    Topics: Amino Acid Sequence; Anions; Biocatalysis; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Humans; Kinetics; Molecular Sequence Data; Phylogeny; Porphyromonas gingivalis; Protein Isoforms; Sequence Alignment

2013
Anion inhibition studies of a β-carbonic anhydrase from Clostridium perfringens.
    Bioorganic & medicinal chemistry letters, 2013, Dec-15, Volume: 23, Issue:24

    Topics: Amino Acid Sequence; Animals; Anions; Bacterial Proteins; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Clostridium perfringens; Enzyme Activation; Humans; Kinetics; Molecular Sequence Data; Phylogeny; Protein Binding; Sequence Alignment

2013
Anion inhibition studies of two new β-carbonic anhydrases from the bacterial pathogen Legionella pneumophila.
    Bioorganic & medicinal chemistry letters, 2014, Feb-15, Volume: 24, Issue:4

    Topics: Anions; Carbonic Anhydrases; Dose-Response Relationship, Drug; Enzyme Inhibitors; Legionella pneumophila; Molecular Conformation; Structure-Activity Relationship

2014
Cloning, characterization and anion inhibition studies of a γ-carbonic anhydrase from the Antarctic bacterium Colwellia psychrerythraea.
    Bioorganic & medicinal chemistry, 2016, Feb-15, Volume: 24, Issue:4

    Topics: Acetazolamide; Alteromonadaceae; Amino Acid Sequence; Anions; Antarctic Regions; Bacterial Proteins; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Cloning, Molecular; Enzyme Assays; Escherichia coli; Gene Expression; Kinetics; Molecular Sequence Data; Open Reading Frames; Phylogeny; Sequence Alignment

2016
Anion inhibition profiles of the complete domain of the η-carbonic anhydrase from Plasmodium falciparum.
    Bioorganic & medicinal chemistry, 2016, 09-15, Volume: 24, Issue:18

    Topics: Animals; Antimalarials; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Kinetics; Plasmodium falciparum

2016