n-(n-(3-carboxyoxirane-2-carbonyl)leucyl)isoamylamine has been researched along with maduramicin in 1 studies
Studies (n-(n-(3-carboxyoxirane-2-carbonyl)leucyl)isoamylamine) | Trials (n-(n-(3-carboxyoxirane-2-carbonyl)leucyl)isoamylamine) | Recent Studies (post-2010) (n-(n-(3-carboxyoxirane-2-carbonyl)leucyl)isoamylamine) | Studies (maduramicin) | Trials (maduramicin) | Recent Studies (post-2010) (maduramicin) |
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79 | 1 | 16 | 83 | 2 | 33 |
Protein | Taxonomy | n-(n-(3-carboxyoxirane-2-carbonyl)leucyl)isoamylamine (IC50) | maduramicin (IC50) |
---|---|---|---|
5-hydroxytryptamine receptor 4 | Cavia porcellus (domestic guinea pig) | 0.034 | |
Alpha-2A adrenergic receptor | Homo sapiens (human) | 0.18 | |
Cytochrome P450 2D6 | Homo sapiens (human) | 1 | |
D(2) dopamine receptor | Homo sapiens (human) | 0.702 | |
Alpha-2B adrenergic receptor | Homo sapiens (human) | 0.027 | |
Alpha-2C adrenergic receptor | Homo sapiens (human) | 1.61 | |
5-hydroxytryptamine receptor 1A | Rattus norvegicus (Norway rat) | 0.0078 | |
D(1A) dopamine receptor | Homo sapiens (human) | 2.908 | |
Alpha-1D adrenergic receptor | Homo sapiens (human) | 1.128 | |
5-hydroxytryptamine receptor 2A | Homo sapiens (human) | 0.0087 | |
5-hydroxytryptamine receptor 2C | Homo sapiens (human) | 0.034 | |
5-hydroxytryptamine receptor 1B | Rattus norvegicus (Norway rat) | 0.0078 | |
D(3) dopamine receptor | Homo sapiens (human) | 0.027 | |
5-hydroxytryptamine receptor 2B | Homo sapiens (human) | 0.033 | |
5-hydroxytryptamine receptor 6 | Homo sapiens (human) | 0.0017 |
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 |
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Batista-Gonzalez, A; Brunhofer, G; Fallarero, A; Gopi Mohan, C; Karlsson, D; Shinde, P; Vuorela, P | 1 |
1 other study(ies) available for n-(n-(3-carboxyoxirane-2-carbonyl)leucyl)isoamylamine and maduramicin
Article | Year |
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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 |