M
Michael E. Burczynski
Researcher at University of Pennsylvania
Publications - 15
Citations - 2002
Michael E. Burczynski is an academic researcher from University of Pennsylvania. The author has contributed to research in topics: Reductase & Aldo-keto reductase. The author has an hindex of 10, co-authored 15 publications receiving 1923 citations.
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Journal ArticleDOI
Human 3alpha-hydroxysteroid dehydrogenase isoforms (AKR1C1-AKR1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones.
Trevor M. Penning,Michael E. Burczynski,Joseph M. Jez,Chien Fu Hung,Hseuh-Kung Lin,Haiching Ma,Margaret Moore,Nisha T. Palackal,Kapila Ratnam +8 more
TL;DR: The kinetic parameters, steroid substrate specificity and identities of reaction products were determined for four homogeneous recombinant human 3alpha-hydroxysteroid dehydrogenase (3alpha-HSD) isoforms of the aldo-keto reductase (AKR) superfamily and the functional plasticity of these isoforms highlights their ability to modulate the levels of active androgens, oestrogens and progestins.
Journal ArticleDOI
Dihydrodiol dehydrogenases and polycyclic aromatic hydrocarbon activation: generation of reactive and redox active o-quinones.
Trevor M. Penning,Michael E. Burczynski,Chien Fu Hung,Kirsten D. McCoull,Nisha T. Palackal,Laurie Tsuruda +5 more
Journal Article
Isoform-specific Induction of a Human Aldo-Keto Reductase by Polycyclic Aromatic Hydrocarbons (PAHs), Electrophiles, and Oxidative Stress: Implications for the Alternative Pathway of PAH Activation Catalyzed by Human Dihydrodiol Dehydrogenase
TL;DR: Data suggest that, in contrast to the CYPs, induction of AKR1C member(s) by PAHs and other bifunctional inducers is mediated indirectly via an antioxidant response element rather than a xenobiotic response element.
Journal ArticleDOI
The Reactive Oxygen Species- and Michael Acceptor-inducible Human Aldo-Keto Reductase AKR1C1 Reduces the α,β-Unsaturated Aldehyde 4-Hydroxy-2-nonenal to 1,4-Dihydroxy-2-nonene *
TL;DR: HNE induces its own metabolism via AKR1C1, and this enzyme may play a hitherto unrecognized role in a response mounted to counter oxidative stress.
Journal Article
Genotoxic polycyclic aromatic hydrocarbon ortho-quinones generated by aldo-keto reductases induce CYP1A1 via nuclear translocation of the aryl hydrocarbon receptor
TL;DR: The AhR provides the only known mechanism by which genotoxic PAH o-quinones generated in the cytosol can be targeted to the nucleus with specificity and is shown to be a potent and rapid inducer of CYP1A1.