hydrogen cyanide has been researched along with azides in 9 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 1 (11.11) | 18.7374 |
1990's | 2 (22.22) | 18.2507 |
2000's | 2 (22.22) | 29.6817 |
2010's | 4 (44.44) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Cincinelli, A; Martellini, T; Supuran, CT; Vullo, D | 1 |
AlOthman, Z; Capasso, C; Carginale, V; De Luca, V; Dedeoglu, N; Del Prete, S; Ferraroni, M; Osman, SM; Supuran, CT; Vullo, D | 1 |
AlOthman, Z; Capasso, C; Carginale, V; De Luca, V; Del Prete, S; di Fonzo, P; Osman, SM; Supuran, CT; Vullo, D | 1 |
Albery, WJ; Cass, AE; Mangold, BP; Shu, ZX | 1 |
Hardy, RW; Knight, E | 1 |
Dou, Y; Ikeda-Saito, M; Olson, JS; Wilkinson, AJ | 1 |
Dilworth, MJ; Fisher, K; Newton, WE | 1 |
Searcy, DG | 1 |
Bennett, CJ; Kaiser, RI; Kim, YS; Quinto-Hernandez, A; Wodtke, AM | 1 |
9 other study(ies) available for hydrogen cyanide and azides
Article | Year |
---|---|
Anion and sulfonamide inhibition studies of an α-carbonic anhydrase from the Antarctic hemoglobinless fish Chionodraco hamatus.
Topics: Animals; Anions; Antarctic Regions; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Enzyme Activation; Fishes; Molecular Structure; Sulfonamides | 2015 |
Anion inhibition studies of the β-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae.
Topics: Anions; Arsenicals; Boronic Acids; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Dose-Response Relationship, Drug; Models, Molecular; Structure-Activity Relationship; Sulfonamides; Sulfonic Acids; Vibrio cholerae | 2016 |
Anion inhibition profiles of α-, β- and γ-carbonic anhydrases from the pathogenic bacterium Vibrio cholerae.
Topics: Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Enzyme Stability; Hot Temperature; Humans; Kinetics; Vibrio cholerae | 2016 |
Inhibited enzyme electrodes. Part 3. A sensor for low levels of H2S and HCN.
Topics: Azides; Biosensing Techniques; Electron Transport Complex IV; Hydrogen Cyanide; Hydrogen Sulfide; Kinetics | 1990 |
ATP-dependent reduction of azide and HCN by N2-fixing enzymes of Azotobacter vinelandii and Clostridium pasteurianum.
Topics: Adenosine Triphosphate; Amines; Azides; Azotobacter; Bacteriological Techniques; Carbon Isotopes; Centrifugation; Chromatography; Chromatography, Gas; Clostridium; Enzymes; Hydrogen Cyanide; Kinetics; Nitrogen Fixation; Oxidoreductases | 1967 |
Mechanism of hydrogen cyanide binding to myoglobin.
Topics: Amino Acids; Animals; Azides; Binding Sites; Binding, Competitive; Humans; Hydrogen Cyanide; Kinetics; Models, Chemical; Mutagenesis, Site-Directed; Myoglobin; Protein Binding; Recombinant Proteins; Swine; Whales | 1996 |
Azotobacter vinelandii vanadium nitrogenase: formaldehyde is a product of catalyzed HCN reduction, and excess ammonia arises directly from catalyzed azide reduction.
Topics: Ammonia; Azides; Azotobacter vinelandii; Carbon Monoxide; Catalysis; Formaldehyde; Hydrogen Cyanide; Nitrogenase; Oxidation-Reduction | 2006 |
Rapid hydrogen sulfide consumption by Tetrahymena pyriformis and its implications for the origin of mitochondria.
Topics: Animals; Azides; Biological Evolution; Cell Fractionation; Chemical Precipitation; Hydrogen Cyanide; Hydrogen Sulfide; Mitochondria; Oxygen Consumption; Quinone Reductases; Silver Compounds; Silver Nitrate; Symbiosis; Tetrahymena pyriformis | 2006 |
On the interaction of methyl azide (CH3N3) ices with ionizing radiation: formation of methanimine (CH2NH), hydrogen cyanide (HCN), and hydrogen isocyanide (HNC).
Topics: Azides; Cyanates; Hydrogen Cyanide; Imines; Radiation, Ionizing; Spectrophotometry, Infrared | 2011 |