Identification of Tazarotenic Acid as the First Xenobiotic Substrate of Human Retinoic Acid Hydroxylase CYP26A1 and CYP26B1

@article{Foti2016IdentificationOT,
  title={Identification of Tazarotenic Acid as the First Xenobiotic Substrate of Human Retinoic Acid Hydroxylase CYP26A1 and CYP26B1},
  author={R. Foti and N. Isoherranen and Alex Zelter and L. Dickmann and Brian R Buttrick and P. Diaz and D. Douguet},
  journal={The Journal of Pharmacology and Experimental Therapeutics},
  year={2016},
  volume={357},
  pages={281 - 292}
}
  • R. Foti, N. Isoherranen, +4 authors D. Douguet
  • Published 2016
  • Biology, Medicine
  • The Journal of Pharmacology and Experimental Therapeutics
  • Cytochrome P450 (CYP) 26A1 and 26B1 are heme-containing enzymes responsible for metabolizing all-trans retinoic acid (at-RA). No crystal structures have been solved, and therefore homology models that provide structural information are extremely valuable for the development of inhibitors of cytochrome P450 family 26 (CYP26). The objectives of this study were to use homology models of CYP26A1 and CYP26B1 to characterize substrate binding characteristics, to compare structural aspects of their… CONTINUE READING
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