Associated Papers
Biotransformation, Using Recombinant CYP450-Expressing Baker's Yeast Cells, Identifies a Novel CYP2D6.10A122V Variant Which Is a Superior Metabolizer of Codeine to Morphine Than the Wild-Type Enzyme.
Williams IS et al.
Acs Omega, 2018
Molecular dynamics of CYP2D6 polymorphisms in the absence and presence of a mechanism-based inactivator reveals changes in local flexibility and dominant substrate access channels.
de Waal PW et al.
Plos One, 2014
Crystal structure of human cytochrome P450 2D6 with prinomastat bound.
Wang A et al.
The Journal of Biological Chemistry, 2012
Roles of phenylalanine at position 120 and glutamic acid at position 222 in the oxidation of chiral substrates by cytochrome P450 2D6.
Masuda K et al.
Chirality, 2006
The relationship between the pharmacology of antiepileptic drugs and human gene variation: an overview.
Ferraro TN et al.
Epilepsy & Behavior : E&b, 2005
Essential requirements for substrate binding affinity and selectivity toward human CYP2 family enzymes.
Lewis DF
Archives of Biochemistry and Biophysics, 2003
Molecular modelling of cytochrome P4502D6 (CYP2D6) based on an alignment with CYP102: structural studies on specific CYP2D6 substrate metabolism.
Lewis DF et al.
Xenobiotica; the Fate of Foreign Compounds in Biological Systems, 1997
Comparison of substrate metabolism by wild type CYP2D6 protein and a variant containing methionine, not valine, at position 374.
Crespi CL et al.
Pharmacogenetics, 1995
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