nad has been researched along with 3-chloroacetylpyridine-adenine dinucleotide in 9 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 7 (77.78) | 18.7374 |
| 1990's | 1 (11.11) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 1 (11.11) | 2.80 |
| Authors | Studies |
|---|---|
| Albrecht, AM; Biellmann, JF; Branlant, G; Eiler-Samama, B; Svircevic, J; Tritsch, D | 1 |
| Biellmann, JF; Foucaud, B | 3 |
| Biellmann, JF; Branlant, G; Eiler, B; Tritsch, D; Wallen, L | 1 |
| Biellmann, JF; Branlant, G; Eiler, B; Wallen, L | 1 |
| Flynn, CT; Shadur, CA | 1 |
| el Kebbaj, MS; Latruffe, N | 1 |
| de Borst, GJ; Spierings, J; Teraa, M; van Rhijn-Brouwer, FCC; Verhaar, MC; Wijnand, JGJ | 1 |
9 other study(ies) available for nad and 3-chloroacetylpyridine-adenine dinucleotide
| Article | Year |
|---|---|
4-Chloroacetylpyridine adenine dinucleotide. A highly reactive and chromophoric affinity label of glyceraldehyde-3-phosphate dehydrogenase from sturgeon.
Topics: Affinity Labels; Animals; Binding Sites; Fishes; Geobacillus stearothermophilus; Glyceraldehyde-3-Phosphate Dehydrogenases; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Molecular Conformation; Muscles; NAD; Peptide Mapping; Protein Conformation; Spectrophotometry | 1989 |
Properties of horse liver alcohol dehydrogenase modified by the affinity label 3-chloroacetylpyridine-adenine dinucleotide.
Topics: Affinity Labels; Alcohol Dehydrogenase; Alcohol Oxidoreductases; Animals; Horses; Liver; NAD; Protein Conformation; Spectrophotometry | 1983 |
Inactivation of yeast alcohol dehydrogenase by a reactive coenzyme analogue: 3-chloroacetyl pyridine adenine dinucleotide.
Topics: Affinity Labels; Alcohol Dehydrogenase; Alcohol Oxidoreductases; Alkylation; Coenzymes; Hydrogen-Ion Concentration; Kinetics; NAD; Saccharomyces cerevisiae; Substrate Specificity | 1982 |
Affinity labeling of horse-liver alcohol dehydrogenase by 3-chloroacetylpyridine--adenine dinucleotide.
Topics: Affinity Labels; Alcohol Dehydrogenase; Alcohol Oxidoreductases; Animals; Horses; Hydrogen-Ion Concentration; Kinetics; Liver; NAD; Structure-Activity Relationship | 1981 |
Properties of the charge-transfer transition observed in glyceraldehyde-3-phosphate dehydrogenase from sturgeon muscle alkylated by 3-chloroacetylpyridine--adenine dinucleotide. Characterisation of the modified amino acid.
Topics: Affinity Labels; Alkylation; Amino Acids; Animals; Chemical Phenomena; Chemistry; Cysteine; Energy Transfer; Fishes; Glyceraldehyde-3-Phosphate Dehydrogenases; Muscles; NAD; Spectrophotometry, Ultraviolet; Sulfhydryl Reagents | 1982 |
Affinity labeling of glyceraldehyde-3-phosphate dehydrogenase from sturgeon and Bacillus stearothermophilus by 3-chloroacetylpyridine--adenine dinucleotide. Kinetic studies.
Topics: Affinity Labels; Animals; Binding Sites; Fishes; Geobacillus stearothermophilus; Glyceraldehyde-3-Phosphate Dehydrogenases; Hydrogen-Ion Concentration; Kinetics; NAD | 1982 |
A comparison of continuous ambulatory peritoneal dialysis in diabetic and nondiabetic patients.
Topics: Adolescent; Adult; Aged; Blood Glucose; Child; Diabetic Nephropathies; Humans; Kidney Failure, Chronic; Lipids; Middle Aged; NAD; Peritoneal Dialysis, Continuous Ambulatory; Peritonitis | 1981 |
Alkylation at the active site of the D-3-hydroxybutyrate dehydrogenase (BDH), a membrane phospholipid-dependent enzyme, by 3-chloroacetyl pyridine adenine dinucleotide (3-CAPAD).
Topics: Affinity Labels; Alkylation; Animals; Binding Sites; Cysteine; Hydroxybutyrate Dehydrogenase; Linear Models; Membrane Lipids; Mitochondria, Liver; Molecular Structure; NAD; Phospholipids; Rats | 1997 |
Nailfold Capillaroscopy in Patients with Peripheral Artery Disease of the Lower Limb (CAPAD study).
Topics: Humans; Lower Extremity; Microscopic Angioscopy; NAD; Peripheral Arterial Disease | 2022 |