Title : Characterization of cytochrome P450 (CYP) 2D6 drugs as substrates of human organic cation transporters and multidrug and toxin extrusion proteins.

Pub. Date : 2021 Mar

PMID : 33434947






3 Functional Relationships(s)
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1 Since CYP2D6 prototypic substrates are positively charged, the aim of this study was to evaluate the organic cation membrane transporters (OCTs) and multidrug and toxin extrusion proteins (MATEs) as potential contributors to the variability of CYP2D6 hydroxylation of the CYP2D6 drugs debrisoquine, dextromethorphan, diphenhydramine, perhexiline and sparteine. Dextromethorphan cytochrome P450 family 2 subfamily D member 6 Homo sapiens
2 Since CYP2D6 prototypic substrates are positively charged, the aim of this study was to evaluate the organic cation membrane transporters (OCTs) and multidrug and toxin extrusion proteins (MATEs) as potential contributors to the variability of CYP2D6 hydroxylation of the CYP2D6 drugs debrisoquine, dextromethorphan, diphenhydramine, perhexiline and sparteine. Dextromethorphan cytochrome P450 family 2 subfamily D member 6 Homo sapiens
3 Since CYP2D6 prototypic substrates are positively charged, the aim of this study was to evaluate the organic cation membrane transporters (OCTs) and multidrug and toxin extrusion proteins (MATEs) as potential contributors to the variability of CYP2D6 hydroxylation of the CYP2D6 drugs debrisoquine, dextromethorphan, diphenhydramine, perhexiline and sparteine. Dextromethorphan cytochrome P450 family 2 subfamily D member 6 Homo sapiens