nad has been researched along with s-hydroxymethylglutathione in 4 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 2 (50.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 2 (50.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Creighton, DJ; Pourmotabbed, T | 1 |
Mannervik, B; Uotila, L | 1 |
Bosron, WF; Hurley, TD; Pindel, EV; Ray, BD; Sanghani, PC; Stone, CL | 1 |
Bosron, WF; Hurley, TD; Sanghani, PC | 1 |
4 other study(ies) available for nad and s-hydroxymethylglutathione
Article | Year |
---|---|
Substrate specificity of bovine liver formaldehyde dehydrogenase.
Topics: Acylation; Aldehyde Oxidoreductases; Animals; Cattle; Glutathione; Liver; Molecular Weight; NAD; Pyruvaldehyde; Substrate Specificity | 1986 |
Product inhibition studies of human liver formaldehyde dehydrogenase.
Topics: Aldehyde Oxidoreductases; Glutathione; Humans; In Vitro Techniques; Liver; Models, Chemical; NAD | 1980 |
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. Structural changes associated with ternary complex formation.
Topics: Aldehyde Oxidoreductases; Binding Sites; Catalytic Domain; Dimerization; Glutathione; Humans; Macromolecular Substances; NAD; Protein Conformation; Protein Subunits; Protons; Structure-Activity Relationship; Substrate Specificity; Zinc | 2002 |