Associated Papers
Pharmacokinetic recall study of Estonian Biobank participants with novel genetic variants in CYP2C19 and CYP2D6.
Krebs K et al.
Npj Genomic Medicine, 2026
The genetic landscape of major drug metabolizing cytochrome P450 genes-an updated analysis of population-scale sequencing data.
Zhou Y et al.
The Pharmacogenomics Journal, 2022
36068297 (PubMed )
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New insights into the structural characteristics and functional relevance of the human cytochrome P450 2D6 enzyme.
Wang B et al.
Drug Metabolism Reviews, 2009
Insights into drug metabolism by cytochromes P450 from modelling studies of CYP2D6-drug interactions.
Maréchal JD et al.
British Journal of Pharmacology, 2008
Topological role of cytochrome P450 2D6 active site residues.
van Waterschoot RA et al.
Archives of Biochemistry and Biophysics, 2006
Why is quinidine an inhibitor of cytochrome P450 2D6? The role of key active-site residues in quinidine binding.
McLaughlin LA et al.
The Journal of Biological Chemistry, 2005
Progress in cytochrome P450 active site modeling.
Kemp CA et al.
Archives of Biochemistry and Biophysics, 2005
Role of glutamic acid 216 in cytochrome P450 2D6 substrate binding and catalysis.
Guengerich FP et al.
Biochemistry, 2003
Residues glutamate 216 and aspartate 301 are key determinants of substrate specificity and product regioselectivity in cytochrome P450 2D6.
Paine MJ et al.
The Journal of Biological Chemistry, 2003
Evidence that aspartic acid 301 is a critical substrate-contact residue in the active site of cytochrome P450 2D6.
Ellis SW et al.
The Journal of Biological Chemistry, 1995
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