3-acetylpyridine adenine dinucleotide has been researched along with hydrogen in 4 studies
| Studies (3-acetylpyridine adenine dinucleotide) | Trials (3-acetylpyridine adenine dinucleotide) | Recent Studies (post-2010) (3-acetylpyridine adenine dinucleotide) | Studies (hydrogen) | Trials (hydrogen) | Recent Studies (post-2010) (hydrogen) |
|---|---|---|---|---|---|
| 68 | 0 | 2 | 28,781 | 399 | 11,492 |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 2 (50.00) | 18.2507 |
| 2000's | 1 (25.00) | 29.6817 |
| 2010's | 1 (25.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Bragg, PD; Glavas, NA | 1 |
| Bizouarn, T; Diggle, C; Grimley, R; Jackson, JB; Thomas, CM | 1 |
| Hirst, J; Yakovlev, G | 1 |
| Birrell, JA; Hirst, J | 1 |
4 other study(ies) available for 3-acetylpyridine adenine dinucleotide and hydrogen
| Article | Year |
|---|---|
The mechanism of hydride transfer between NADH and 3-acetylpyridine adenine dinucleotide by the pyridine nucleotide transhydrogenase of Escherichia coli.
Topics: Amino Acid Sequence; Escherichia coli; Hydrogen; Hydrogen-Ion Concentration; Molecular Sequence Data; NAD; NADP; NADP Transhydrogenases; Trypsin | 1995 |
Mutations at tyrosine-235 in the mobile loop region of domain I protein of transhydrogenase from Rhodospirillum rubrum strongly inhibit hydride transfer.
Topics: Hydrogen; Mutation; NAD; NADP; NADP Transhydrogenases; Oxidation-Reduction; Protein Binding; Recombinant Proteins; Rhodospirillum rubrum; Tyrosine | 1997 |
Transhydrogenation reactions catalyzed by mitochondrial NADH-ubiquinone oxidoreductase (Complex I).
Topics: Animals; Cattle; Electron Transport Complex I; Hydrogen; Mitochondria, Heart; NAD; NADP | 2007 |
Investigation of NADH binding, hydride transfer, and NAD(+) dissociation during NADH oxidation by mitochondrial complex I using modified nicotinamide nucleotides.
Topics: Adenosine; Adenosine Diphosphate; Adenosine Diphosphate Ribose; Adenosine Monophosphate; Animals; Binding, Competitive; Cattle; Coenzymes; Electron Transport Complex I; Flavins; Hydrogen; Kinetics; Mitochondria, Heart; Models, Molecular; NAD; Nicotinamide Mononucleotide; Oxidation-Reduction; Protein Binding | 2013 |