bufuralol has been researched along with 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine 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 |
|---|---|
| Bargetzi, MJ; Fonne-Pfister, R; Meyer, UA | 1 |
| Gilham, DE; Lian, LY; Modi, S; Primrose, WU; Roberts, GC; Sutcliffe, MJ; Wolf, CR | 1 |
| Cai, H; Guengerich, FP; Hanna, IH; Kim, MS; Krauser, JA | 1 |
3 other study(ies) available for bufuralol and 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine
| Article | Year |
|---|---|
MPTP, the neurotoxin inducing Parkinson's disease, is a potent competitive inhibitor of human and rat cytochrome P450 isozymes (P450bufI, P450db1) catalyzing debrisoquine 4-hydroxylation.
Topics: 1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine; Animals; Antibodies, Monoclonal; Brain; Cytochrome P-450 CYP2D6; Cytochrome P-450 Enzyme Inhibitors; Ethanolamines; Humans; Microsomes; Microsomes, Liver; Mixed Function Oxygenases; Parkinson Disease; Pyridines; Rats | 1987 |
1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine as a substrate of cytochrome P450 2D6: allosteric effects of NADPH-cytochrome P450 reductase.
Topics: 1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine; Allosteric Regulation; Binding Sites; Codeine; Cytochrome P-450 CYP2D6; Ethanolamines; Humans; Models, Molecular; NADH, NADPH Oxidoreductases; NADPH-Ferrihemoprotein Reductase; Structure-Activity Relationship; Substrate Specificity | 1997 |
Diversity in mechanisms of substrate oxidation by cytochrome P450 2D6. Lack of an allosteric role of NADPH-cytochrome P450 reductase in catalytic regioselectivity.
Topics: 1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine; Adrenergic beta-Agonists; Adrenergic beta-Antagonists; Allosteric Regulation; Cytochrome P-450 CYP1A2; Cytochrome P-450 CYP2D6; Cytochrome P-450 CYP3A; Cytochrome P-450 Enzyme System; Dopamine Agents; Ethanolamines; Metoprolol; Mixed Function Oxygenases; Models, Chemical; Molecular Conformation; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction | 2001 |