Investigation by site-directed mutagenesis of the role of cytochrome P450 2B4 non-active site residues in protein-ligand interactions based on crystal structures of the ligand-bound enzyme

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• Investigation of the Role of Cytochrome P450 2B4 Active Site Residues in Substrate Metabolism Based on Crystal Structures of the Ligand-bound Enzyme
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  Cyhoeddwyd: (2006)
• Structural and Biophysical Characterization of Human Cytochromes P450 2B6 and 2A6 Bound to Volatile Hydrocarbons: Analysis and Comparison
  gan: Shah, Manish B., et al.
  Cyhoeddwyd: (2015)
• Conformational Adaptation of Human Cytochrome P450 2B6 and Rabbit Cytochrome P450 2B4 Revealed Upon Binding Multiple Amlodipine Molecules()
  gan: Shah, Manish B., et al.
  Cyhoeddwyd: (2012)
• X-ray Crystal Structure of the Cytochrome P450 2B4 Active Site Mutant F297A in Complex with Clopidogrel: Insights into Compensatory Rearrangements of the Binding Pocket()
  gan: Shah, Manish B., et al.
  Cyhoeddwyd: (2013)
• Crystal structures of cytochrome P450 2B4 in complex with the inhibitor 1-biphenyl-4-methyl-1H–imidazole: ligand induced structural response through α-helical repositioning
  gan: Gay, Sean C., et al.
  Cyhoeddwyd: (2009)