sodium azide has been researched along with glycine in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 2 (50.00) | 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 |
|---|---|
| Eads, C; Gan, LS; Niederer, T; Thakker, D | 1 |
| Ciaramella, M; Moracci, M; Perugino, G; Rossi, M; Trincone, A | 1 |
| Fritz, G; Glatter, O; Hammel, M; Jerlich, A; Kharrazi, H; Schaur, RJ; Tschabuschnig, S | 1 |
| Allison, WS; Bandyopadhyay, S; Huynh, HG; Ren, H; Valder, CR | 1 |
4 other study(ies) available for sodium azide and glycine
| Article | Year |
|---|---|
Evidence for predominantly paracellular transport of thyrotropin-releasing hormone across CACO-2 cell monolayers.
Topics: 2,4-Dinitrophenol; Adenocarcinoma; Amiloride; Azides; Biological Transport; Cell Line; Cell Membrane; Colonic Neoplasms; Dinitrophenols; Dipeptides; Edetic Acid; Epithelium; Glycine; Humans; Intestines; Kinetics; Ouabain; Sodium Azide; Thyrotropin-Releasing Hormone; Tritium; Tumor Cells, Cultured | 1993 |
Restoration of the activity of active-site mutants of the hyperthermophilic beta-glycosidase from Sulfolobus solfataricus: dependence of the mechanism on the action of external nucleophiles.
Topics: Binding Sites; Catalytic Domain; Enzyme Activation; Formates; Glucosidases; Glucosides; Glutamic Acid; Glutamine; Glycine; Hot Temperature; Kinetics; Mutagenesis, Site-Directed; Sodium Azide; Sulfolobus | 1998 |
Comparison of HOCl traps with myeloperoxidase inhibitors in prevention of low density lipoprotein oxidation.
Topics: Arteriosclerosis; Dose-Response Relationship, Drug; Enzyme Inhibitors; Fluorescence; Glycine; Humans; Hydroxamic Acids; Hydroxybenzoates; Hypochlorous Acid; Lipoproteins, LDL; Methionine; Neutrophils; Peroxidase; Potassium Cyanide; Salicylamides; Sodium Azide; Taurine; Tryptophan | 2000 |
The beta G156C substitution in the F1-ATPase from the thermophilic Bacillus PS3 affects catalytic site cooperativity by destabilizing the closed conformation of the catalytic site.
Topics: Adenosine Triphosphate; Amino Acid Substitution; Bacillus; Binding Sites; Catalysis; Catalytic Domain; Cysteine; Dimethylamines; Enzyme Stability; Glutamic Acid; Glycine; Hydrolysis; Magnesium; Mutagenesis, Site-Directed; Protein Conformation; Proton-Translocating ATPases; Sodium Azide; Tryptophan; Tyrosine; Valine | 2002 |