Substrate-dependent modulation of CYP3A4 catalytic activity: analysis of 27 test compounds with four fluorometric substrates.

@article{Stresser2000SubstratedependentMO,
  title={Substrate-dependent modulation of CYP3A4 catalytic activity: analysis of 27 test compounds with four fluorometric substrates.},
  author={David M. Stresser and Andrew P. Blanchard and Stephanie D Turner and John C. L. Erve and Andre A Dandeneau and Vaughn P Miller and Charles L. Crespi},
  journal={Drug metabolism and disposition: the biological fate of chemicals},
  year={2000},
  volume={28 12},
  pages={1440-8}
}
Inhibition of cytochrome P450 catalytic activity is a principal mechanism for pharmacokinetic drug-drug interactions. Rapid, in vitro testing for cytochrome P450 inhibition potential is part of the current paradigm for identifying drug candidates likely to give such interactions. We have explored the extent that qualitative and quantitative inhibition parameters are dependent on the cytochrome P450 (CYP) 3A4 probe substrate. Inhibition potential (e.g., IC(50) values from 8-point inhibition… CONTINUE READING
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Drug Metab Dispos25:840–844

  • N Tremblay, RL Lackman, JY Gauthier, JM Silva, J Marois
  • 1999

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