Associated Papers
Pharmacophore, QSAR, and binding mode studies of substrates of human cytochrome P450 2D6 (CYP2D6) using molecular docking and virtual mutations and an application to chinese herbal medicine screening.
Mo SL et al.
Current Pharmaceutical Biotechnology, 2012
Ligand- and protein-based modeling studies of the inhibitors of human cytochrome P450 2D6 and a virtual screening for potential inhibitors from the Chinese herbal medicine, Scutellaria baicalensis (Huangqin,Baikal Skullcap).
Mo SL et al.
Combinatorial Chemistry & High Throughput Screening, 2012
New insights into the structural characteristics and functional relevance of the human cytochrome P450 2D6 enzyme.
Wang B et al.
Drug Metabolism Reviews, 2009
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
Functional analysis of CYP2D6.31 variant: homology modeling suggests possible disruption of redox partner interaction by Arg440His substitution.
Allorge D et al.
Proteins, 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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