nad has been researched along with propionaldehyde in 26 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 8 (30.77) | 18.7374 |
| 1990's | 8 (30.77) | 18.2507 |
| 2000's | 3 (11.54) | 29.6817 |
| 2010's | 6 (23.08) | 24.3611 |
| 2020's | 1 (3.85) | 2.80 |
| Authors | Studies |
|---|---|
| Blackwell, LF; Buckley, PD; Hill, JP; Kingston, RL; Sime, RM | 1 |
| Abriola, DP; Blatter, EE; Pietruszko, R | 1 |
| Blackwell, LF; Buckley, PD; Hill, JP; Motion, RL | 2 |
| Marselos, M; Vasiliou, V | 1 |
| Marselos, M; Michalopoulos, G; Strom, SC | 1 |
| Blackwell, LF; Buckley, PD; Hardman, MJ; MacGibbon, AK; Motion, RL | 1 |
| Bennett, AF; Blackwell, LF; Buckley, PD; Deady, LW | 1 |
| Bennett, AF; Blackwell, LF; Buckley, PD | 2 |
| Blackwell, LF; Buckley, PD; Motion, RL | 1 |
| Bennett, AF; Blackwell, LF; Buckley, PD; Crow, KE; Deady, LW | 1 |
| Dickinson, FM; Hart, GJ | 1 |
| Bennett, AF; Blackwell, LF; Buckley, PD; Hill, JP; Motion, RL | 1 |
| Anderson, BM; Leskovac, V; Stancić, B; Trivić, S; Zeremski, J | 1 |
| Hwang, S; Kim, CK; Kim, SJ; Kim, Y; Kim, YC | 1 |
| Allali-Hassani, A; Weiner, H | 1 |
| Barber, AR; Pamment, NB; Vriesekoop, F | 1 |
| Deerfield, DW; Hempel, J; Wymore, T | 1 |
| Baek, JO; Heo, SY; Hong, WK; Kim, CH; Kim, DH; Luo, LH; Oh, BR; Seo, JW | 1 |
| Huang, HC; Huang, ST; Lin, CM; Lin, HY; Wang, KL | 1 |
| Branlant, G; Stines-Chaumeil, C; Talfournier, F | 1 |
| Asiimwe, T; Kothe, E; Krause, K; Schlunk, I | 1 |
| Hatti-Kaul, R; Linares-Pastén, JA; Sabet-Azad, R; Sardari, RR; Torkelson, L | 1 |
| Bobik, TA; Chowdhury, C | 1 |
| Chowdhury, NP; Moon, J; Müller, V | 1 |
26 other study(ies) available for nad and propionaldehyde
| Article | Year |
|---|---|
Activation of aldehyde dehydrogenase at physiological temperatures.
Topics: Aldehyde Dehydrogenase; Aldehydes; Animals; Body Temperature; Cytosol; Enzyme Activation; Liver; NAD; Sheep | 1992 |
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 |
Steady-state and pre-steady-state kinetics of propionaldehyde oxidation by sheep liver cytosolic aldehyde dehydrogenase at pH 5.2. Evidence that the release of NADH remains rate-limiting in the enzyme mechanism at acid pH values.
Topics: Aldehyde Dehydrogenase; Aldehydes; Animals; Cytosol; Hydrogen-Ion Concentration; In Vitro Techniques; Kinetics; Liver; NAD; Osmolar Concentration; Sheep; Spectrometry, Fluorescence | 1991 |
Effect of various chemicals on the aldehyde dehydrogenase activity of the rat liver cytosol.
Topics: Aldehyde Dehydrogenase; Aldehydes; Amines; Animals; Benzaldehydes; Carcinogens; Cytosol; Liver; NAD; NADP; Nitrosamines; Oxidation-Reduction; Polycyclic Compounds; Rats; Rats, Inbred Strains; Structure-Activity Relationship | 1991 |
Effect of phenobarbital and 3-methylcholanthrene on aldehyde dehydrogenase activity in cultures of HepG2 cells and normal human hepatocytes.
Topics: Aldehyde Dehydrogenase; Aldehydes; Benzaldehydes; Carcinoma, Hepatocellular; Cells, Cultured; Liver; Liver Neoplasms; Methylcholanthrene; NAD; Neoplasm Proteins; Phenobarbital; Substrate Specificity | 1987 |
Evidence that the slow conformation change controlling NADH release from the enzyme is rate-limiting during the oxidation of propionaldehyde by aldehyde dehydrogenase.
Topics: Aldehyde Dehydrogenase; Aldehydes; Binding Sites; Catalysis; Hydrogen-Ion Concentration; Kinetics; Macromolecular Substances; NAD; Oxidation-Reduction; Protein Conformation | 1987 |
Kinetics of inhibition and hysteresis of sheep liver cytoplasmic aldehyde dehydrogenase with glyoxylic acid: further evidence relating to the two-site model for aldehyde oxidation.
Topics: Aldehyde Dehydrogenase; Aldehydes; Animals; Binding Sites; Cytoplasm; Glyoxylates; Hydrogen-Ion Concentration; Kinetics; Liver; Models, Chemical; NAD; Oxidation-Reduction; Sheep; Spectrometry, Fluorescence | 1985 |
Proton release during the pre-steady-state oxidation of aldehydes by aldehyde dehydrogenase. Evidence for a rate-limiting conformational change.
Topics: Acetaldehyde; Aldehyde Dehydrogenase; Aldehyde Oxidoreductases; Aldehydes; Benzaldehydes; Hydrogen-Ion Concentration; Kinetics; NAD; Oxidation-Reduction; Protein Conformation; Protons; Spectrophotometry | 1982 |
Activating effect of p-(chloromercuri)benzoate on the cytoplasmic aldehyde dehydrogenase from sheep liver.
Topics: Aldehyde Dehydrogenase; Aldehydes; Animals; Chloromercuribenzoates; Cytoplasm; Enzyme Activation; In Vitro Techniques; Kinetics; Liver; NAD; p-Chloromercuribenzoic Acid; Sheep | 1984 |
Relationship between the mechanisms of the esterase and dehydrogenase activities of the cytoplasmic aldehyde dehydrogenase from sheep liver. An alternative view.
Topics: Aldehyde Dehydrogenase; Aldehyde Oxidoreductases; Aldehydes; Animals; Binding, Competitive; Chloral Hydrate; Esterases; Kinetics; Ligands; Liver; NAD; Sheep | 1983 |
A two-site model for the esterase and dehydrogenase activities of sheep liver aldehyde dehydrogenase.
Topics: Aldehyde Dehydrogenase; Aldehyde Oxidoreductases; Aldehydes; Animals; Esterases; Glyoxylates; Hydrogen-Ion Concentration; Liver; NAD; Sheep; Substrate Specificity | 1983 |
Kinetic properties of highly purified preparations of sheep liver cytoplasmic aldehyde dehydrogenase.
Topics: Aldehyde Dehydrogenase; Aldehyde Oxidoreductases; Aldehydes; Animals; Cytoplasm; Kinetics; Liver; NAD; Oxidation-Reduction; Sheep; Spectrometry, Fluorescence; Spectrophotometry | 1982 |
The effect of p-(chloromercuri)benzoate modification of cytosolic aldehyde dehydrogenase from sheep liver. Evidence for a second aldehyde binding site.
Topics: Aldehyde Dehydrogenase; Aldehydes; Animals; Chloromercuribenzoates; Enzyme Activation; Fluorescence; Liver; Molecular Weight; NAD; p-Chloromercuribenzoic Acid; Protein Conformation; Sheep | 1994 |
Is the single site binding model for aldehyde dehydrogenase an oversimplification? The one-site, two-site debate revisited.
Topics: Aldehyde Dehydrogenase; Aldehydes; Animals; Binding Sites; Chloromercuribenzoates; Cytosol; Disulfiram; Fluorescence; In Vitro Techniques; Kinetics; Liver; Models, Chemical; NAD; Protons; Sheep | 1993 |
Influence of Tris(hydroxymethyl)aminomethane on kinetic mechanism of yeast alcohol dehydrogenase.
Topics: 1-Propanol; Acetaldehyde; Acridines; Alcohol Dehydrogenase; Aldehydes; Buffers; Enzyme Inhibitors; Kinetics; NAD; Oxidation-Reduction; Phosphates; Potassium Compounds; Saccharomyces cerevisiae; Tromethamine | 1998 |
The phnIJ genes encoding acetaldehyde dehydrogenase (acylating) and 4-hydroxy-2-oxovalerate aldolase in Pseudomonas sp. DJ77 and their evolutionary implications.
Topics: Acetaldehyde; Aldehyde Oxidoreductases; Aldehydes; Amino Acid Sequence; Base Sequence; Blotting, Southern; Cloning, Molecular; Coenzyme A; Evolution, Molecular; Genes, Bacterial; Molecular Sequence Data; NAD; Open Reading Frames; Operon; Oxo-Acid-Lyases; Phenanthrenes; Phylogeny; Pseudomonas; Recombinant Proteins; Sequence Homology, Amino Acid | 1999 |
Interaction of human aldehyde dehydrogenase with aromatic substrates and ligands.
Topics: Aldehyde Dehydrogenase; Aldehyde Dehydrogenase 1 Family; Aldehydes; Benzaldehydes; Binding Sites; Catalytic Domain; Chloramphenicol; Chromatography, Affinity; Enzyme Activation; Enzyme Inhibitors; Humans; In Vitro Techniques; Isoenzymes; Kinetics; Ligands; NAD; Retinal Dehydrogenase; Substrate Specificity | 2001 |
Acetaldehyde mediates growth stimulation of ethanol-stressed Saccharomyces cerevisiae: evidence of a redox-driven mechanism.
Topics: Acetaldehyde; Aldehydes; Electrons; Ethanol; Glucose; NAD; Oxidation-Reduction; Saccharomyces cerevisiae; Time Factors | 2007 |
Mechanistic implications of the cysteine-nicotinamide adduct in aldehyde dehydrogenase based on quantum mechanical/molecular mechanical simulations.
Topics: Aldehyde Dehydrogenase; Aldehyde Dehydrogenase, Mitochondrial; Aldehydes; Computer Simulation; Cysteine; Humans; NAD; Niacinamide; Protein Conformation; Protons; Quantum Theory | 2007 |
Identification and characterization of the propanediol utilization protein PduP of Lactobacillus reuteri for 3-hydroxypropionic acid production from glycerol.
Topics: Aldehydes; Bacterial Proteins; Cloning, Molecular; Coenzymes; Enzymes; Gene Expression; Glycerol; Kinetics; Klebsiella pneumoniae; Lactic Acid; Limosilactobacillus reuteri; NAD; NADP; Recombinant Proteins; Substrate Specificity | 2011 |
Development of a sensitive long-wavelength fluorogenic probe for nitroreductase: a new fluorimetric indictor for analyte determination by dehydrogenase-coupled biosensors.
Topics: 3-Hydroxybutyric Acid; Aldehyde Dehydrogenase; Aldehydes; Biosensing Techniques; Fluorescence; Fluorescent Dyes; Fluorometry; Hydroxybutyrate Dehydrogenase; NAD; Nitro Compounds; Nitroreductases | 2011 |
Methylmalonate-semialdehyde dehydrogenase from Bacillus subtilis: substrate specificity and coenzyme A binding.
Topics: Aldehydes; Amino Acid Sequence; Amino Acid Substitution; Animals; Bacillus subtilis; Biocatalysis; Coenzyme A; Enzyme Stability; Esterification; Humans; Kinetics; Methylmalonate-Semialdehyde Dehydrogenase (Acylating); Methylmalonic Acid; Molecular Sequence Data; Mutation; NAD; Protein Binding; Rats; Substrate Specificity | 2011 |
Modulation of ethanol stress tolerance by aldehyde dehydrogenase in the mycorrhizal fungus Tricholoma vaccinum.
Topics: Aldehyde Dehydrogenase; Aldehydes; Amino Acid Motifs; Amino Acid Sequence; Base Sequence; Ethanol; Evolution, Molecular; Fungal Proteins; Gene Expression Regulation, Fungal; Kinetics; Molecular Sequence Data; Mycelium; Mycorrhizae; NAD; NADP; Phylogeny; Recombinant Fusion Proteins; Stress, Physiological; Substrate Specificity; Tricholoma; Up-Regulation | 2012 |
Coenzyme A-acylating propionaldehyde dehydrogenase (PduP) from Lactobacillus reuteri: kinetic characterization and molecular modeling.
Topics: Aldehyde Dehydrogenase; Aldehyde Oxidoreductases; Aldehydes; Amino Acid Sequence; Bacterial Proteins; Binding Sites; Cloning, Molecular; Coenzyme A; Computer Simulation; Genes, Bacterial; Kinetics; Limosilactobacillus reuteri; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; NAD; Protein Conformation; Recombinant Proteins; Sequence Homology, Amino Acid | 2013 |
Engineering the PduT shell protein to modify the permeability of the 1,2-propanediol microcompartment of
Topics: Aldehydes; Bacterial Proteins; Culture Media; Models, Biological; Models, Molecular; Mutagenesis, Site-Directed; Mutation; NAD; Organelles; Permeability; Propylene Glycol; Salmonella | 2019 |
Adh4, an alcohol dehydrogenase controls alcohol formation within bacterial microcompartments in the acetogenic bacterium Acetobacterium woodii.
Topics: 1-Propanol; Acetaldehyde; Acetates; Acetobacterium; Alcohol Dehydrogenase; Aldehydes; Bacterial Proteins; Carbon Dioxide; Ethanol; Genome, Bacterial; NAD; Oxidation-Reduction | 2021 |