deguelin has been researched along with orlistat in 1 studies
Studies (deguelin) | Trials (deguelin) | Recent Studies (post-2010) (deguelin) | Studies (orlistat) | Trials (orlistat) | Recent Studies (post-2010) (orlistat) |
---|---|---|---|---|---|
182 | 0 | 115 | 1,432 | 274 | 539 |
Protein | Taxonomy | deguelin (IC50) | orlistat (IC50) |
---|---|---|---|
Phosphatidylserine lipase ABHD16A | Homo sapiens (human) | 0.1 | |
Pancreatic triacylglycerol lipase | Sus scrofa (pig) | 0.4214 | |
Lipoprotein lipase | Homo sapiens (human) | 0.066 | |
Cytochrome P450 3A4 | Homo sapiens (human) | 0.42 | |
Hepatic triacylglycerol lipase | Homo sapiens (human) | 0.003 | |
Pancreatic triacylglycerol lipase | Homo sapiens (human) | 0.3253 | |
Translocator protein | Rattus norvegicus (Norway rat) | 1 | |
Cytochrome P450 2C19 | Homo sapiens (human) | 0.42 | |
Kappa-type opioid receptor | Mus musculus (house mouse) | 0.1903 | |
Fatty acid synthase | Homo sapiens (human) | 2.99 | |
Fatty-acid amide hydrolase 1 | Rattus norvegicus (Norway rat) | 0.01 | |
Platelet-activating factor acetylhydrolase | Homo sapiens (human) | 0.05 | |
Diacylglycerol lipase-alpha | Mus musculus (house mouse) | 0.02 | |
Lysophosphatidylserine lipase ABHD12 | Homo sapiens (human) | 0.1682 | |
Diacylglycerol lipase-beta | Homo sapiens (human) | 0.24 | |
Monoacylglycerol lipase ABHD6 | Homo sapiens (human) | 0.03 | |
Acyl-protein thioesterase 2 | Rattus norvegicus (Norway rat) | 0.17 | |
Diacylglycerol lipase-alpha | Homo sapiens (human) | 0.2677 | |
Endothelial lipase | Homo sapiens (human) | 0.006 |
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 deguelin and orlistat
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 |