thiorphan has been researched along with arginine in 3 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 1 (33.33) | 18.7374 |
| 1990's | 1 (33.33) | 18.2507 |
| 2000's | 1 (33.33) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Bellows, DS; Clarke, ID; Diamandis, P; Dirks, PB; Graham, J; Jamieson, LG; Ling, EK; Sacher, AG; Tyers, M; Ward, RJ; Wildenhain, J | 1 |
| Dasarathy, Y; Fanburg, BL; Lanzillo, JJ | 1 |
| Antonczak, S; Beaumont, A; Fournié-Zaluski, MC; Marie-Claire, C; O'Donohue, M; Roques, BP; Ruffet, E | 1 |
3 other study(ies) available for thiorphan and arginine
| Article | Year |
|---|---|
Chemical genetics reveals a complex functional ground state of neural stem cells.
Topics: Animals; Cell Survival; Cells, Cultured; Mice; Molecular Structure; Neoplasms; Neurons; Pharmaceutical Preparations; Sensitivity and Specificity; Stem Cells | 2007 |
Detection of essential arginine in bacterial peptidyl dipeptidase-4: arginine is not the anion binding site.
Topics: Anions; Arginine; Binding Sites; Chlorides; Diacetyl; Endopeptidases; Hydrolysis; Kinetics; Phenylglyoxal; Phosphates; Protease Inhibitors; Pseudomonas; Substrate Specificity; Thiorphan | 1989 |
Evidence by site-directed mutagenesis that arginine 203 of thermolysin and arginine 717 of neprilysin (neutral endopeptidase) play equivalent critical roles in substrate hydrolysis and inhibitor binding.
Topics: Amino Acid Sequence; Arginine; Bacillus subtilis; Binding, Competitive; DNA, Complementary; Glycopeptides; Hydrolysis; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Neprilysin; Protease Inhibitors; Recombinant Proteins; Substrate Specificity; Thermolysin; Thiorphan | 1997 |