L
Lucy A. Hunsaker
Researcher at University of New Mexico
Publications - 54
Citations - 3788
Lucy A. Hunsaker is an academic researcher from University of New Mexico. The author has contributed to research in topics: Aldose reductase & Aldehyde Reductase. The author has an hindex of 32, co-authored 54 publications receiving 3619 citations. Previous affiliations of Lucy A. Hunsaker include Rutgers University.
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Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic complications.
TL;DR: A new integrative model of diabetic complications is proposed that combines the aldose reductase/polyol pathway theory and the nonenzymatic glycation theory except that emphasis is placed both on methylglyoxal/acetol metabolism and on glucose metabolism.
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Anti-oxidant activities of curcumin and related enones.
TL;DR: The natural product curcumin, obtained from the spice turmeric, exhibits numerous biological activities including anti-cancer, anti-inflammatory, and anti-angiogenesis activities; some of these biological activities may derive from its anti-oxidant properties.
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Methylglyoxal metabolism and diabetic complications: roles of aldose reductase, glyoxalase-I, betaine aldehyde dehydrogenase and 2-oxoaldehyde dehydrogenase.
TL;DR: The 2-oxoaldehyde methylglyoxal (MeG) is the precursor to a number of the known advanced glycation endproducts (AGE) implicated in the development of diabetic complications, and rates of production of MeG depend upon physiological conditions such as hyperglycemia and ketoacidosis.
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Substrate specificity of human aldose reductase: identification of 4-hydroxynonenal as an endogenous substrate.
David L. bander Jagt,Natasha S. Kolb,Timothy J. bander Jagt,Joachim Chino,Francella J. Martinez,Lucy A. Hunsaker,Robert E. Royer +6 more
TL;DR: Analysis of the binding of NADPH by fluorescence quenching techniques indicates that aldose reductase exhibits higher affinity for NADPH than NADP, suggesting that this enzyme is normally primed for reductive metabolism.
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Inactivation of glutathione reductase by 4-hydroxynonenal and other endogenous aldehydes
David L. Vander Jagt,Lucy A. Hunsaker,Timothy J. Van der Jagt,Manuel S. Gomez,Donna M. Gonzales,Lorraine M. Deck,Robert E. Royer +6 more
TL;DR: The ability of 4-hydroxynonenal at low concentrations to inactivate glutathione reductase, a central antioxidant enzyme, suggests that oxidative degradation of unsaturated lipids may initiate a positive feedback loop that enhances the potential for oxidative damage.