nad has been researched along with 4-dimethylaminocinnamaldehyde in 10 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 7 (70.00) | 18.7374 |
| 1990's | 3 (30.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Abriola, DP; Blatter, EE; Pietruszko, R | 1 |
| Guerin, MC; Torreilles, J | 1 |
| Andersson, P; Kvassman, J; Oldén, B; Pettersson, G | 1 |
| Dahl, KH; Dunn, MF | 2 |
| Cedergren-Zeppezauer, E; Eklund, H; Samama, JP | 1 |
| Dunn, MF; Morris, RG; Saliman, G | 1 |
| Andersson, P; Kvassman, J; Lindström, A; Oldén, B; Pettersson, G | 1 |
| Bosron, WF; Dunn, MF; Stone, CL | 1 |
| Anderson, BM; Leskovac, V; Stancić, B; Trivić, S; Zeremski, J | 1 |
10 other study(ies) available for nad and 4-dimethylaminocinnamaldehyde
| Article | Year |
|---|---|
Aldehyde dehydrogenase. Covalent intermediate in aldehyde dehydrogenation and ester hydrolysis.
Topics: Alcohol Dehydrogenase; Aldehydes; Amino Acid Sequence; Catalysis; Chloral Hydrate; Chromatography, Liquid; Cinnamates; Esters; Humans; Hydrolysis; Imidazoles; Isoenzymes; Kinetics; Molecular Sequence Data; NAD; Nitrophenols; Substrate Specificity | 1992 |
Influence of coenzyme structure on the transient chemical intermediate formed during horse-liver alcohol-dehydrogenase-catalyzed reduction of aromatic aldehydes.
Topics: Alcohol Dehydrogenase; Alcohol Oxidoreductases; Aldehydes; Benzaldehydes; Chemical Phenomena; Chemistry; Cinnamates; Coenzymes; NAD; NADP; Spectrophotometry; Structure-Activity Relationship; Sulfites | 1986 |
Catalytic significance of binary enzyme-aldehyde complexes in the liver alcohol dehydrogenase reaction.
Topics: Alcohol Dehydrogenase; Alcohol Oxidoreductases; Aldehydes; Animals; Catalysis; Cinnamates; Horses; Kinetics; Liver; Macromolecular Substances; Models, Chemical; NAD; Oxidation-Reduction; Photometry; Protein Binding; Spectrometry, Fluorescence; Substrate Specificity | 1984 |
Reaction of 4-trans-(N,N-dimethylamino)cinnamaldehyde with the liver alcohol dehydrogenase-oxidized nicotinamide adenine dinucleotide complex.
Topics: Alcohol Dehydrogenase; Alcohol Oxidoreductases; Animals; Cinnamates; Horses; Hydrogen-Ion Concentration; Indicators and Reagents; Kinetics; Liver; NAD; Oxidation-Reduction; Protein Binding; Spectrophotometry | 1984 |
Carboxymethylated liver alcohol dehydrogenase: kinetic and thermodynamic characterization of reactions with substrates and inhibitors.
Topics: Alcohol Dehydrogenase; Alcohol Oxidoreductases; Animals; Benzaldehydes; Cinnamates; Horses; In Vitro Techniques; Kinetics; Liver; Methylation; NAD; Pyrazoles; Substrate Specificity; Thermodynamics | 1984 |
Crystal structure determinations of coenzyme analogue and substrate complexes of liver alcohol dehydrogenase: binding of 1,4,5,6-tetrahydronicotinamide adenine dinucleotide and trans-4-(N,N-dimethylamino)cinnamaldehyde to the enzyme.
Topics: Alcohol Dehydrogenase; Alcohol Oxidoreductases; Animals; Binding Sites; Cinnamates; Horses; Liver; Macromolecular Substances; Models, Molecular; NAD; Protein Conformation; X-Ray Diffraction | 1982 |
Evidence that hydride transfer precedes proton transfer in the liver alcohol dehydrogenase catalyzed reduction of trans-4-(N,N-dimethylamino)cinnamaldehyde.
Topics: Alcohol Oxidoreductases; Aldehydes; Animals; Cinnamates; Horses; Kinetics; Liver; Mathematics; NAD; Oxidation-Reduction | 1980 |
Effect of NADH on the pKa of zinc-bound water in liver alcohol dehydrogenase.
Topics: Alcohol Oxidoreductases; Aldehydes; Animals; Binding Sites; Cinnamates; Horses; Hydrogen-Ion Concentration; In Vitro Techniques; Kinetics; Ligands; Liver; NAD; Water; Zinc | 1981 |
Amino acid substitutions at position 47 of human beta 1 beta 1 and beta 2 beta 2 alcohol dehydrogenases affect hydride transfer and coenzyme dissociation rate constants.
Topics: Alcohol Dehydrogenase; Amino Acid Sequence; Animals; Arginine; Binding Sites; Chromatography, DEAE-Cellulose; Cinnamates; Enzyme Stability; Horses; Humans; Indicators and Reagents; Isomerism; Kinetics; Liver; Macromolecular Substances; Models, Theoretical; Mutagenesis, Site-Directed; NAD; Time Factors | 1993 |
Novel substrates of yeast alcohol dehydrogenase-3. 4-dimethylamino-cinnamaldehyde and chloroacetaldehyde.
Topics: Acetaldehyde; Alcohol Dehydrogenase; Cinnamates; Hydrogen-Ion Concentration; Kinetics; NAD; Polymers; Schiff Bases; Spectrophotometry; Substrate Specificity | 1997 |