hyoscyamine has been researched along with vinblastine sulfate in 1 studies
| Studies (hyoscyamine) | Trials (hyoscyamine) | Recent Studies (post-2010) (hyoscyamine) | Studies (vinblastine sulfate) | Trials (vinblastine sulfate) | Recent Studies (post-2010) (vinblastine sulfate) |
|---|---|---|---|---|---|
| 99 | 1 | 55 | 41 | 0 | 17 |
| Protein | Taxonomy | hyoscyamine (IC50) | vinblastine sulfate (IC50) |
|---|---|---|---|
| Tubulin alpha-1A chain | Sus scrofa (pig) | 0.13 | |
| Tubulin beta chain | Sus scrofa (pig) | 0.13 | |
| Tubulin beta-4A chain | Homo sapiens (human) | 0.13 | |
| Tubulin beta chain | Homo sapiens (human) | 0.13 | |
| Tubulin alpha-3C chain | Homo sapiens (human) | 0.13 | |
| Tubulin alpha-1B chain | Homo sapiens (human) | 0.13 | |
| Tubulin alpha-4A chain | Homo sapiens (human) | 0.13 | |
| Tubulin beta-4B chain | Homo sapiens (human) | 0.13 | |
| Tubulin beta-3 chain | Homo sapiens (human) | 0.13 | |
| Tubulin beta-2A chain | Homo sapiens (human) | 0.13 | |
| Tubulin beta-8 chain | Homo sapiens (human) | 0.13 | |
| Tubulin alpha-3E chain | Homo sapiens (human) | 0.13 | |
| Tubulin alpha-1A chain | Homo sapiens (human) | 0.13 | |
| Tubulin alpha-1C chain | Homo sapiens (human) | 0.13 | |
| Tubulin beta-6 chain | Homo sapiens (human) | 0.13 | |
| Tubulin beta-2B chain | Homo sapiens (human) | 0.13 | |
| Tubulin beta-1 chain | Homo sapiens (human) | 0.13 |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 1 (100.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Batista-Gonzalez, A; Brunhofer, G; Fallarero, A; Gopi Mohan, C; Karlsson, D; Shinde, P; Vuorela, P | 1 |
1 other study(ies) available for hyoscyamine and vinblastine sulfate
| Article | Year |
|---|---|
Exploration of natural compounds as sources of new bifunctional scaffolds targeting cholinesterases and beta amyloid aggregation: the case of chelerythrine.
Topics: Acetylcholinesterase; Amyloid beta-Peptides; Benzophenanthridines; Binding Sites; Butyrylcholinesterase; Catalytic Domain; Cholinesterase Inhibitors; Humans; Isoquinolines; Kinetics; Molecular Docking Simulation; Structure-Activity Relationship | 2012 |