Nisha T. Palackal, Ph.D.

Affiliations: 
2002 University of Pennsylvania, Philadelphia, PA, United States 
Area:
Biochemistry, Pathology
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"Nisha Palackal"
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Trevor M. Penning grad student 2002 Penn
 (Role of human aldo -keto reductases in PAH activation.)
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Publications

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Shultz CA, Palackal NT, Mangal D, et al. (2008) Fjord-region benzo[g]chrysene-11,12-dihydrodiol and benzo[c]phenanthrene-3,4-dihydrodiol as substrates for rat liver dihydrodiol dehydrogenase (AKR1C9): structural basis for stereochemical preference. Chemical Research in Toxicology. 21: 668-77
Palackal NT, Lee SH, Harvey RG, et al. (2002) 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. The Journal of Biological Chemistry. 277: 24799-808
Palackal NT, Lee SH, Harvey RG, et al. (2002) Human AKR1C isoforms oxidize the potent proximate carcinogen 7,12-DMBA-3,4-diol in the human lung A549 carcinoma cell line Polycyclic Aromatic Compounds. 22: 801-810
Penning TM, Palackal NT, Blair IA, et al. (2002) The aldo-keto reductases and polycyclic aromatic hydrocarbon activation Polycyclic Aromatic Compounds. 22: 791-800
Palackal NT, Burczynski ME, Harvey RG, et al. (2001) The ubiquitous aldehyde reductase (AKR1A1) oxidizes proximate carcinogen trans-dihydrodiols to o-quinones: potential role in polycyclic aromatic hydrocarbon activation. Biochemistry. 40: 10901-10
Jin Y, Stayrook SE, Albert RH, et al. (2001) Crystal structure of human type III 3alpha-hydroxysteroid dehydrogenase/bile acid binding protein complexed with NADP(+) and ursodeoxycholate. Biochemistry. 40: 10161-8
Palackal NT, Burczynski ME, Harvey RG, et al. (2001) Metabolic activation of polycyclic aromatic hydrocarbon trans-dihydrodiols by ubiquitously expressed aldehyde reductase (AKR1A1). Chemico-Biological Interactions. 130: 815-24
Penning TM, Burczynski ME, Jez JM, et al. (2001) Structure-function aspects and inhibitor design of type 5 17beta-hydroxysteroid dehydrogenase (AKR1C3). Molecular and Cellular Endocrinology. 171: 137-49
Burczynski ME, Sridhar GR, Palackal NT, et al. (2001) The reactive oxygen species--and Michael acceptor-inducible human aldo-keto reductase AKR1C1 reduces the alpha,beta-unsaturated aldehyde 4-hydroxy-2-nonenal to 1,4-dihydroxy-2-nonene. The Journal of Biological Chemistry. 276: 2890-7
Penning TM, Burczynski ME, Jez JM, et al. (2000) 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. The Biochemical Journal. 351: 67-77
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