nad has been researched along with n-cyclohexylformamide in 3 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 2 (66.67) | 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 |
|---|---|
| Plapp, BV; Ramaswamy, S; Scholze, M | 1 |
| Berst, KB; Callender, R; Deng, H; Plapp, BV; Schindler, JF | 1 |
| Höög, JO; Sandalova, T; Schneider, G; Svensson, S | 1 |
3 other study(ies) available for nad and n-cyclohexylformamide
| Article | Year |
|---|---|
Binding of formamides to liver alcohol dehydrogenase.
Topics: Alcohol Dehydrogenase; Animals; Binding Sites; Crystallography, X-Ray; Enzyme Inhibitors; Formamides; Horses; Isoenzymes; Kinetics; Liver; Models, Chemical; Models, Molecular; Molecular Sequence Data; NAD; Piperidines; Protein Conformation; Structure-Activity Relationship | 1997 |
A Raman spectroscopic characterization of bonding in the complex of horse liver alcohol dehydrogenase with NADH and N-cyclohexylformamide.
Topics: Alcohol Dehydrogenase; Animals; Formamides; Horses; Hydrogen Bonding; Kinetics; Liver; Macromolecular Substances; Magnetic Resonance Spectroscopy; Mathematical Computing; Models, Chemical; NAD; Protein Binding; Spectrum Analysis, Raman; Thermodynamics | 1998 |
Crystal structures of mouse class II alcohol dehydrogenase reveal determinants of substrate specificity and catalytic efficiency.
Topics: Alcohol Dehydrogenase; Amino Acid Substitution; Animals; Apoenzymes; Binding Sites; Catalysis; Crystallography, X-Ray; Dimerization; Formamides; Holoenzymes; Hydrogen; Hydrogen Bonding; Lauric Acids; Mice; Models, Molecular; Mutation; NAD; Protein Structure, Secondary; Protein Structure, Tertiary; Static Electricity; Substrate Specificity | 2000 |