Irina F Sevrioukova


Affiliation: University of California
Country: USA


  1. Sevrioukova I, Poulos T. Pyridine-substituted desoxyritonavir is a more potent inhibitor of cytochrome P450 3A4 than ritonavir. J Med Chem. 2013;56:3733-41 pubmed publisher
    ..Additionally, Ser119 was identified as a key residue assisting binding of ritonavir-like inhibitors, which emphasizes the importance of polar interactions in the CYP3A4-ligand association. ..
  2. Sevrioukova I, Poulos T, Churbanova I. Crystal structure of the putidaredoxin reductase x putidaredoxin electron transfer complex. J Biol Chem. 2010;285:13616-20 pubmed publisher
  3. Sevrioukova I, Poulos T. Ritonavir analogues as a probe for deciphering the cytochrome P450 3A4 inhibitory mechanism. Curr Top Med Chem. 2014;14:1348-55 pubmed
  4. Sevrioukova I, Poulos T. Structure and mechanism of the complex between cytochrome P4503A4 and ritonavir. Proc Natl Acad Sci U S A. 2010;107:18422-7 pubmed publisher
  5. Sevrioukova I, Poulos T. Current Approaches for Investigating and Predicting Cytochrome P450 3A4-Ligand Interactions. Adv Exp Med Biol. 2015;851:83-105 pubmed publisher
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    Sevrioukova I, Hazzard J, Tollin G, Poulos T. Laser flash induced electron transfer in P450cam monooxygenase: putidaredoxin reductase-putidaredoxin interaction. Biochemistry. 2001;40:10592-600 pubmed
    ..Transient kinetics as a function of ionic strength suggest that, in contrast to the Pdx-P450cam redox couple where complex formation is predominantly electrostatic, the Pdx-Pdr association is driven by nonelectrostatic interactions. ..
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    Sevrioukova I, Garcia C, Li H, Bhaskar B, Poulos T. Crystal structure of putidaredoxin, the [2Fe-2S] component of the P450cam monooxygenase system from Pseudomonas putida. J Mol Biol. 2003;333:377-92 pubmed
    ..Therefore, Trp106, previously shown to be important in the Pdr-to-Pdx and Pdx-to-P450cam electron transfer reactions is in a position to regulate and/or mediate electron transfer to or from the [2Fe-2S] center of Pdx. ..
  8. Sevrioukova I. Apoptosis-inducing factor: structure, function, and redox regulation. Antioxid Redox Signal. 2011;14:2545-79 pubmed publisher
  9. Sevrioukova I, Poulos T. Interaction of human cytochrome P4503A4 with ritonavir analogs. Arch Biochem Biophys. 2012;520:108-16 pubmed publisher

More Information


  1. Sevrioukova I. Structure/Function Relations in AIFM1 Variants Associated with Neurodegenerative Disorders. J Mol Biol. 2016;428:3650-65 pubmed publisher
  2. Sevrioukova I, Poulos T. Structural basis for regiospecific midazolam oxidation by human cytochrome P450 3A4. Proc Natl Acad Sci U S A. 2017;114:486-491 pubmed publisher
  3. Sevrioukova I. Redox-linked conformational dynamics in apoptosis-inducing factor. J Mol Biol. 2009;390:924-38 pubmed publisher
    ..Structural findings agree with biochemical data and support the hypothesis that both normal and apoptogenic functions of AIF are controlled by NADH. ..
  4. Sevrioukova I, Poulos T. Dissecting cytochrome P450 3A4-ligand interactions using ritonavir analogues. Biochemistry. 2013;52:4474-81 pubmed publisher
    ..Overall, however, the end group contributes less to the ligand association process, which, in contrast, is greatly facilitated by the polar interactions mediated by the active site Ser119. ..