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Nisha T. Palackal
Researcher at University of Pennsylvania
Publications - 13
Citations - 1751
Nisha T. Palackal 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 8, co-authored 12 publications receiving 1675 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.
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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
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Activation of polycyclic aromatic hydrocarbon trans-dihydrodiol proximate carcinogens by human aldo-keto reductase (AKR1C) enzymes and their functional overexpression in human lung carcinoma (A549) cells.
TL;DR: The ability to measure DMBA-3,4-dione formation in A549 cells implicates the AKR pathway in the metabolic activation of PAH in human lung, and shows that four homogeneous human recombinant aldo-keto reductases (AKR1C1–AKR 1C4) are regioselective and oxidize only the relevant non-K regiontrans-dihydrodiols.
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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.
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The ubiquitous aldehyde reductase (AKR1A1) oxidizes proximate carcinogen trans-dihydrodiols to o-quinones: potential role in polycyclic aromatic hydrocarbon activation.
TL;DR: The ability of this general metabolic enzyme to divert trans-dihydrodiols to o-quinones suggests that this pathway of PAH activation may be widespread in human tissues.