harmalol hydrochloride has been researched along with oleanolic acid in 1 studies
| Studies (harmalol hydrochloride) | Trials (harmalol hydrochloride) | Recent Studies (post-2010) (harmalol hydrochloride) | Studies (oleanolic acid) | Trials (oleanolic acid) | Recent Studies (post-2010) (oleanolic acid) |
|---|---|---|---|---|---|
| 7 | 0 | 4 | 4,169 | 31 | 2,404 |
| Protein | Taxonomy | harmalol hydrochloride (IC50) | oleanolic acid (IC50) |
|---|---|---|---|
| Aldo-keto reductase family 1 member B10 | Homo sapiens (human) | 2.045 | |
| Phospholipase A2 | Homo sapiens (human) | 3 | |
| DNA polymerase beta | Homo sapiens (human) | 6.8667 | |
| DNA polymerase beta | Rattus norvegicus (Norway rat) | 5.6 | |
| Receptor-type tyrosine-protein phosphatase C | Homo sapiens (human) | 1 | |
| Receptor-type tyrosine-protein phosphatase F | Homo sapiens (human) | 3.065 | |
| Tissue factor | Homo sapiens (human) | 0.005 | |
| Tyrosine-protein phosphatase non-receptor type 2 | Homo sapiens (human) | 4.38 | |
| Tyrosine-protein phosphatase non-receptor type 1 | Homo sapiens (human) | 2.8444 | |
| Liver carboxylesterase 1 | Homo sapiens (human) | 0.1 | |
| Tyrosine-protein phosphatase non-receptor type 6 | Homo sapiens (human) | 3.065 | |
| M-phase inducer phosphatase 2 | Homo sapiens (human) | 0.98 | |
| Dual specificity protein phosphatase 3 | Homo sapiens (human) | 5.4 | |
| Transcription factor p65 | Homo sapiens (human) | 2.4 | |
| Tyrosine-protein phosphatase non-receptor type 11 | Homo sapiens (human) | 3.065 | |
| Protease | Human immunodeficiency virus 1 | 8 |
| 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 harmalol hydrochloride and oleanolic acid
| 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 |