nad has been researched along with 12-hydroxydodecanoic acid in 5 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 2 (40.00) | 18.2507 |
| 2000's | 3 (60.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Gotoh, Y; Minakami, S; Sumimoto, H | 1 |
| Belka, GK; Du Bois, GC; Jensen, DE | 1 |
| Höög, JO; Sandalova, T; Schneider, G; Svensson, S | 1 |
| Bosron, WF; Hurley, TD; Pindel, EV; Ray, BD; Sanghani, PC; Stone, CL | 1 |
| Bosron, WF; Hurley, TD; Robinson, H; Sanghani, PC | 1 |
5 other study(ies) available for nad and 12-hydroxydodecanoic acid
| Article | Year |
|---|---|
Formation of 20-oxoleukotriene B4 by an alcohol dehydrogenase isolated from human neutrophils.
Topics: 12-Hydroxy-5,8,10,14-eicosatetraenoic Acid; Alcohol Dehydrogenase; Chromatography, High Pressure Liquid; Gas Chromatography-Mass Spectrometry; Humans; Hydrogen-Ion Concentration; Hydroxyeicosatetraenoic Acids; Kinetics; Lauric Acids; Leukotriene B4; NAD; NADP; Neutrophils; Palmitic Acids; Spectrophotometry, Ultraviolet | 1990 |
S-Nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III isoenzyme.
Topics: Alcohol Dehydrogenase; Amino Acid Sequence; Animals; Cytosol; Glutathione; Isoenzymes; Kinetics; Lauric Acids; Liver; Molecular Sequence Data; NAD; Nitroso Compounds; Octanols; Rats; S-Nitrosoglutathione; Substrate Specificity | 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 |
Kinetic mechanism of human glutathione-dependent formaldehyde dehydrogenase.
Topics: Aldehyde Oxidoreductases; Binding, Competitive; Carbon Isotopes; Fatty Acids, Unsaturated; Glutathione; Humans; Kinetics; Lauric Acids; NAD; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Protein Binding; Spectrophotometry, Ultraviolet; Substrate Specificity | 2000 |
Human glutathione-dependent formaldehyde dehydrogenase. Structures of apo, binary, and inhibitory ternary complexes.
Topics: Aldehyde Oxidoreductases; Apoenzymes; Binding Sites; Computer Simulation; Crystallography, X-Ray; Dimerization; Enzyme Inhibitors; Humans; Kinetics; Lauric Acids; Macromolecular Substances; Models, Molecular; NAD; Protein Conformation; Structure-Activity Relationship; Substrate Specificity; Zinc | 2002 |