9-amino-6-chloro-2-methoxyacridine has been researched along with carbonyl cyanide m-chlorophenyl hydrazone in 3 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 1 (33.33) | 18.7374 |
1990's | 1 (33.33) | 18.2507 |
2000's | 1 (33.33) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Carlenor, E; Eytan, GD; Rydström, J | 1 |
Enander, K; Persson, B; Rydström, J; Tang, HL | 1 |
Kanazawa, H; Mitsui, K; Nakamura, N; Ohgaki, R | 1 |
3 other study(ies) available for 9-amino-6-chloro-2-methoxyacridine and carbonyl cyanide m-chlorophenyl hydrazone
Article | Year |
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Energy-linked transhydrogenase. Effects of valinomycin and nigericin on the ATP-driven transhydrogenase reaction catalyzed by reconstituted transhydrogenase-ATPase vesicles.
Topics: Adenosine Triphosphatases; Adenosine Triphosphate; Aminoacridines; Animals; Anti-Bacterial Agents; Carbonyl Cyanide m-Chlorophenyl Hydrazone; Cattle; Fluorescent Dyes; Kinetics; Liposomes; Membrane Potentials; Mitochondria, Heart; Nigericin; Spectrometry, Fluorescence; Valinomycin | 1990 |
Energy-linked nicotinamide nucleotide transhydrogenase. Properties of proton-translocating mitochondrial transhydrogenase from beef heart purified by fast protein liquid chromatography.
Topics: Aminacrine; Amino Acids; Aminoacridines; Animals; Carbonyl Cyanide m-Chlorophenyl Hydrazone; Cattle; Dicyclohexylcarbodiimide; Energy Metabolism; Fluorescent Dyes; Kinetics; Liposomes; Mitochondria; Mitochondria, Heart; NADH, NADPH Oxidoreductases; NADP Transhydrogenases; Proton-Translocating ATPases; Submitochondrial Particles | 1984 |
Characterization of the ion transport activity of the budding yeast Na+/H+ antiporter, Nha1p, using isolated secretory vesicles.
Topics: Aminoacridines; Carbonyl Cyanide m-Chlorophenyl Hydrazone; Catalysis; Cation Transport Proteins; Cations; Cell Membrane; Electrophoresis, Polyacrylamide Gel; Green Fluorescent Proteins; Hydrogen-Ion Concentration; Immunoblotting; Ions; Kinetics; Membrane Proteins; Microscopy, Fluorescence; Mutation; Open Reading Frames; Plasmids; Protein Structure, Tertiary; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Salts; Sodium; Sodium-Hydrogen Exchangers; Substrate Specificity; Temperature | 2005 |