V
Vladimir Mishin
Researcher at Rutgers University
Publications - 37
Citations - 1285
Vladimir Mishin is an academic researcher from Rutgers University. The author has contributed to research in topics: Cytochrome P450 reductase & Reductase. The author has an hindex of 19, co-authored 35 publications receiving 1113 citations.
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Journal ArticleDOI
Piperine enhances the bioavailability of the tea polyphenol (-)-epigallocatechin-3-gallate in mice
TL;DR: It is reported that cotreatment with a second dietary component, piperine (from black pepper), enhanced the bioavailability of EGCG in mice and demonstrated the modulation of the E GCG bioavailablity by a second Dietary component and illustrates a mechanism for interactions between dietary chemicals.
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Characterization of the Oxidase Activity in Mammalian Catalase
Anna M. Vetrano,Diane E. Heck,Thomas M. Mariano,Vladimir Mishin,Debra L. Laskin,Jeffrey D. Laskin +5 more
TL;DR: A novel function for catalase is described potentially important in metabolism of endogenous substrates and in the action of carcinogens and chemopreventative agents.
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Application of the Amplex Red/Horseradish Peroxidase Assay to Measure Hydrogen Peroxide Generation by Recombinant Microsomal Enzymes
TL;DR: It is demonstrated that cytochrome P450s are a major source of hydrogen peroxide in the recombinant cyto Chrome P450 monooxygenase system, and substrate binding is not required for the cy tochrome P 450s to generate reactive oxygen species.
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Redox cycling and increased oxygen utilization contribute to diquat-induced oxidative stress and cytotoxicity in Chinese hamster ovary cells overexpressing NADPH-cytochrome P450 reductase.
Karma C. Fussell,Ronald G. Udasin,Joshua P. Gray,Vladimir Mishin,Peter K. Smith,Diane E. Heck,Jeffrey D. Laskin +6 more
TL;DR: Diquat redox cycling in CHO cells was associated with marked increases in protein carbonyl formation, a marker of protein oxidation, as well as cellular oxygen consumption, measured using oxygen microsensors; greater activity was detected in CHO-OR cells than in CHO
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Paraquat Increases Cyanide-insensitive Respiration in Murine Lung Epithelial Cells by Activating an NAD(P)H:Paraquat Oxidoreductase: IDENTIFICATION OF THE ENZYME AS THIOREDOXIN REDUCTASE
Joshua P. Gray,Diane E. Heck,Vladimir Mishin,Peter K. Smith,Jun-Yan Hong,Mona Thiruchelvam,Deborah A. Cory-Slechta,Debra L. Laskin,Jeffrey D. Laskin +8 more
TL;DR: It is discovered that lung epithelial cells possess a distinct cytoplasmic diphenyleneiodonium-sensitive NAD(P)H:paraquat oxidoreductase, which utilizes oxygen, requires NADH or NADPH, and readily generates the reduced paraquat radical.