The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.
NAD+/NADH and skeletal muscle mitochondrial adaptations to exercise
Open accessAbstract
The pyridine nucleotides, NAD+and NADH, are coenzymes that provide oxidoreductive power for the generation of ATP by mitochondria. In skeletal muscle, exercise perturbs the levels of NAD+, NADH, and consequently, the NAD+/NADH ratio, and initial research in this area focused on the contribution of redox control to ATP production. More recently, numerous signaling pathways that are sensitive to perturbations in NAD+(H) have come to the fore, as has an appreciation for the potential importance of compartmentation of NAD+(H) metabolism and its subsequent effects on various signaling pathways. These pathways, which include the sirtuin (SIRT) proteins SIRT1 and SIRT3, the poly(ADP-ribose) polymerase (PARP) proteins PARP1 and PARP2, and COOH-terminal binding protein (CtBP), are of particular interest because they potentially link changes in cellular redox state to both immediate, metabolic-related changes and transcriptional adaptations to exercise. In this review, we discuss what is known, and not known, about the contribution of NAD+(H) metabolism and these aforementioned proteins to mitochondrial adaptations to acute and chronic endurance exercise.
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1 retracted
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RetractedAMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity
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Cited by
Allen, D. G., Whitehead, N. P., & Froehner, S. C. (2016) · Physiological Reviews · doi:10.1152/physrev.00007.2015 · Cited by 426
Protective effects of sirtuins in cardiovascular diseases: from bench to bedside
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Egan, B., & Sharples, A. P. (2023) · Physiological Reviews · doi:10.1152/physrev.00054.2021 · Cited by 278
Mitohormesis in exercise training
Merry, T. L., & Ristow, M. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.11.032 · Cited by 176
Perry, C. G. R., & Hawley, J. A. (2018) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a029686 · Cited by 130
Metadata
- Authors
- White, A. T., & Schenk, S.
- Venue
- American Journal of Physiology-Endocrinology and Metabolism
- Publisher
- American Physiological Society
- Published
- 2012-08-01
- Volume
- 303
- Issue
- 3
- Pages
- E308-E321
- ISSN
- 0193-1849 (ISSN-L)
- 1522-1555
- OpenAlex
- W2171342857
- Cited by
- 193
- References
- 32
- FWCI
- 5.17
- Type
- journal article
- Language
- en
- Open access
- green
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