chlorates has been researched along with flavin-adenine dinucleotide in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 3 (75.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 1 (25.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Barea, JL; Cárdenas, J | 1 |
| Coddington, A; McDonald, DW | 1 |
| Barrett, EL; Kwan, HS | 1 |
| Bhakuni, V; Misra, SK | 1 |
4 other study(ies) available for chlorates and flavin-adenine dinucleotide
| Article | Year |
|---|---|
The nitrate-reducing enzyme system of Chlamydomonas reinhardii.
Topics: Azides; Cell-Free System; Chlamydomonas; Chlorates; Cyanides; Dihydrolipoamide Dehydrogenase; Dithionite; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Hot Temperature; Hydroxymercuribenzoates; Kinetics; Molecular Weight; NAD; NADH, NADPH Oxidoreductases; NADP; Nitrate Reductases; Nitrite Reductases; Oxidation-Reduction; Phenanthrolines; Viologens | 1975 |
Properties of the assimilatory nitrate reductase from Aspergillus nidulans.
Topics: Aspergillus nidulans; Benzyl Compounds; Binding Sites; Centrifugation, Density Gradient; Chemical Precipitation; Chlorates; Chromatography, DEAE-Cellulose; Chromatography, Gel; Coloring Agents; Cytochrome c Group; Cytochrome Reductases; Electron Transport; Flavin-Adenine Dinucleotide; Hemeproteins; Hot Temperature; Hydrogen-Ion Concentration; Kinetics; Molecular Weight; Molybdenum; NADP; Nitrate Reductases; Oxidation-Reduction; Pyridinium Compounds; Spectrophotometry; Ultracentrifugation | 1974 |
Purification and properties of trimethylamine oxide reductase from Salmonella typhimurium.
Topics: Chlorates; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Isoelectric Point; Kinetics; Molecular Weight; NADH, NADPH Oxidoreductases; Oxidoreductases Acting on CH-NH Group Donors; Salmonella typhimurium | 1983 |
Unique holoenzyme dimers of the tetrameric enzyme Escherichia coli methylenetetrahydrofolate reductase: characterization of structural features associated with modulation of the enzyme's function.
Topics: Bacterial Proteins; Chlorates; Circular Dichroism; Cross-Linking Reagents; Dimerization; Enzyme Stability; Escherichia coli; Flavin-Adenine Dinucleotide; Glutaral; Holoenzymes; Hot Temperature; Humans; Methylenetetrahydrofolate Reductase (NADPH2); Mutation; Oxidoreductases Acting on CH-NH Group Donors; Plasmids; Protein Conformation; Protein Denaturation; Protein Folding; Spectrometry, Fluorescence; Structure-Activity Relationship; Urea | 2003 |