Pyruvate dehydrogenase complex and nicotinamide nucleotide transhydrogenase constitute an energy-consuming redox circuit
Authors: Kelsey H, Fisher-Wellman; Chien-Te, Lin; Terence E, Ryan; Lauren R, Reese; Laura A A, Gilliam; Brook L, Cathey; Daniel S, Lark; +3 Authors
Kelsey H, Fisher-Wellman; Chien-Te, Lin; Terence E, Ryan; Lauren R, Reese; Laura A A, Gilliam; Brook L, Cathey; Daniel S, Lark; Cody D, Smith; Deborah M, Muoio; P Darrell, Neufer;
Pyruvate dehydrogenase complex and nicotinamide nucleotide transhydrogenase constitute an energy-consuming redox circuit
Abstract
Mitochondria generate and maintain a redox or “electrical” charge that is distributed throughout cells. The current work identifies a redox mechanism by which energy balance is continuously sensed and coupled to compensatory changes in energy expenditure.
Related Organizations
- Duke University United States
- East Carolina University United States
Keywords
Membrane Potential, Mitochondrial, Pyruvate Dehydrogenase Complex, Hydrogen Peroxide, NADP Transhydrogenase, AB-Specific, Mitochondria, Muscle, Mitochondrial Proteins, Mice, Animals, Enzyme Inhibitors, Oxidation-Reduction, NADP
Membrane Potential, Mitochondrial, Pyruvate Dehydrogenase Complex, Hydrogen Peroxide, NADP Transhydrogenase, AB-Specific, Mitochondria, Muscle, Mitochondrial Proteins, Mice, Animals, Enzyme Inhibitors, Oxidation-Reduction, NADP
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citations
Citations provided by BIP!
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
popularity
Popularity provided by BIP!
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
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