Author pages are created from data sourced from our academic publisher partnerships and public sources.
- Publications
- Influence
Structure of a cytochrome P450-redox partner electron-transfer complex.
- I. Sevrioukova, H. Li, H. Zhang, J. Peterson, T. Poulos
- Chemistry, Medicine
- Proceedings of the National Academy of Sciences…
- 2 March 1999
The crystal structure of the complex between the heme- and FMN-binding domains of bacterial cytochrome P450BM-3, a prototype for the complex between eukaryotic microsomal P450s and P450 reductase,… Expand
Severe X-linked mitochondrial encephalomyopathy associated with a mutation in apoptosis-inducing factor.
- D. Ghezzi, I. Sevrioukova, +7 authors M. Zeviani
- Biology, Medicine
- American journal of human genetics
- 9 April 2010
We investigated two male infant patients who were given a diagnosis of progressive mitochondrial encephalomyopathy on the basis of clinical, biochemical, and morphological features. These patients… Expand
Apoptosis-inducing factor: structure, function, and redox regulation.
- I. Sevrioukova
- Biology, Medicine
- Antioxidants & redox signaling
- 15 June 2011
Apoptosis-inducing factor (AIF) is a flavin adenine dinucleotide-containing, NADH-dependent oxidoreductase residing in the mitochondrial intermembrane space whose specific enzymatic activity remains… Expand
Structure and mechanism of the complex between cytochrome P4503A4 and ritonavir
- I. Sevrioukova, T. Poulos
- Chemistry, Medicine
- Proceedings of the National Academy of Sciences
- 11 October 2010
Ritonavir is a HIV protease inhibitor routinely prescribed to HIV patients that also potently inactivates cytochrome P4503A4 (CYP3A4), the major human drug-metabolizing enzyme. By inhibiting CYP3A4,… Expand
Understanding the mechanism of cytochrome P450 3A4: recent advances and remaining problems.
- I. Sevrioukova, T. Poulos
- Chemistry, Medicine
- Dalton transactions
- 5 February 2013
Cytochromes P450 (CYPs) represent a diverse group of heme-thiolate proteins found in almost all organisms. CYPs share a common protein fold but differ in substrate selectivity and catalyze a wide… Expand
Cowchock syndrome is associated with a mutation in apoptosis-inducing factor.
- C. Rinaldi, C. Grunseich, +11 authors K. Fischbeck
- Biology, Medicine
- American journal of human genetics
- 7 December 2012
Cowchock syndrome (CMTX4) is a slowly progressive X-linked recessive disorder with axonal neuropathy, deafness, and cognitive impairment. The disease locus was previously mapped to an 11 cM region at… Expand
Photoreduction of the active site of the metalloprotein putidaredoxin by synchrotron radiation.
- M. Corbett, M. Latimer, T. Poulos, I. Sevrioukova, K. Hodgson, B. Hedman
- Chemistry, Medicine
- Acta crystallographica. Section D, Biological…
- 1 September 2007
X-ray damage to protein crystals is often assessed on the basis of the degradation of diffraction intensity, yet this measure is not sensitive to the rapid changes that occur at photosensitive groups… Expand
Structural and Mechanistic Insights into the Interaction of Cytochrome P4503A4 with Bromoergocryptine, a Type I Ligand*
- I. Sevrioukova, T. Poulos
- Chemistry, Medicine
- The Journal of Biological Chemistry
- 7 December 2011
Background: Human CYP3A4 metabolizes the majority of administered drugs including bromoergocryptine (BEC), a dopamine receptor agonist. Results: Crystallographic and experimental data suggest the… Expand
Redox-dependent Changes in Molecular Properties of Mitochondrial Apoptosis-inducing Factor*
- I. Y. Churbanova, I. Sevrioukova
- Biology, Medicine
- Journal of Biological Chemistry
- 29 February 2008
Mitochondrial apoptosis-inducing factor (AIF) is a central player in the caspase-independent cell death pathway whose normal physiological function remains unclear. Our study showed that naturally… Expand
Equilibrium and transient state spectrophotometric studies of the mechanism of reduction of the flavoprotein domain of P450BM-3.
- I. Sevrioukova, C. Shaffer, D. Ballou, J. Peterson
- Chemistry, Medicine
- Biochemistry
- 4 June 1996
The flavoprotein domain of P450BM-3 (BMR), which is functionally analogous to eukaryotic NADPH-P450 oxidoreductases, contains both FAD and FMN. When BMR is titrated with NADPH or sodium dithionite… Expand