Role of PGC-1α Signaling in Skeletal Muscle Health and Disease
Open accessAbstract
This paper reviews the current understanding of the molecular basis of the peroxisome proliferator-activated receptor-γ coactivator-1α (PGC-1α)-mediated pathway and discusses the role of PGC-1α in skeletal muscle atrophy caused by immobilization. PGC-1α is the master transcription regulator that stimulates mitochondrial biogenesis, by upregulating nuclear respiratory factors (NRF-1, 2) and mitochondrial transcription factor A (Tfam), which leads to increased mitochondrial DNA replication and gene transcription. PGC-1α also regulates cellular oxidant-antioxidant homeostasis by stimulating the gene expression of superoxide dismutase-2 (SOD2), catalase, glutathione peroxidase 1 (GPx1), and uncoupling protein (UCP). Recent reports from muscle-specific PGC-1α overexpression underline the importance of PGC-1α in atrophied skeletal muscle, demonstrate enhancement of the PGC-1α mitochondrial biogenic pathway, and reduced oxidative damage. Thus, PGC-1α appears to play a protective role against atrophy-linked skeletal muscle deterioration.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Through deacetylation, AMPK upregulates PGC-1α via the SIRT1 signaling pathway, which modulates FoxO transcriptional activity by repressing atrogin-1 and MuRF1, preventing proteasome-mediated muscle protein degradation while enhancing mitochondrial biogenesis, antioxidant defense, and metabolic resilience.
“Through deacetylation, AMPK upregulates the expression of PGC-1α via the SIRT1 signaling pathway which in turn modulates FoxO transcriptional activity by repressing the expression of key atrogenes such as atrogin-1 and muscle RING-finger protein-1 (MuRF1), thereby preventing proteasome-mediated muscle protein degradation while simultaneously enhancing mitochondrial biogenesis, antioxidant defense,”
From Exercise-Induced Muscle–Fat Crosstalk: Molecular Mediators and Their Pharmacological Modulation for the Maintenance of Metabolic Flexibility in Aging (2025) · cites this paper as [103]
Split into 2 atoms — 0 confirmed, 2 partially supported, 0 disputed, 0 misattributed, 0 unverifiable. Expand the claim to see per-atom verdicts.
Experimental — accuracy not yet measuredPPARGC1A inhibits the expression of multiple pro-inflammatory mediators, including TNF-α and IL-6, and regulates antioxidant defense mechanisms.
“In addition, PPARGC1A inhibits the expression of multiple pro‐inflammatory mediators, including TNF‐α and IL‐6, and regulates antioxidant defense mechanisms (Kang & Li Ji, 2012), both of which in turn can activate autophagy.”
From Autophagy gene expression in skeletal muscle of older individuals is associated with physical performance, muscle volume and mitochondrial function in the study of muscle, mobility and aging ( <scp>SOMMA</scp> ) (2024) · cites this paper as Kang & Li Ji, 2012
ApN may also induce Ca2+ influx, thereby activating CaMKKβ, which leads to increased expression of PGC-1α.
“ApN may also induce Ca2+ influx, thereby activating CaMKKβ, which leads to increased expression of peroxisome proliferator-activated receptor γ coactivator-1α (PGC-1α), a key player in mitochondrial function and biogenesis [42,43].”
From Adiponectin and Its Mimics on Skeletal Muscle: Insulin Sensitizers, Fat Burners, Exercise Mimickers, Muscling Pills … or Everything Together? (2020) · cites this paper as [43]
Activation of PGC-1α enhances the expression of several oxidative-stress detoxification enzymes and molecules involved in fatty-acid oxidation.
“Second, activation of PGC-1α enhances the expression of several oxidative-stress detoxification enzymes and molecules involved in fatty-acid oxidation [43,51].”
From Adiponectin and Its Mimics on Skeletal Muscle: Insulin Sensitizers, Fat Burners, Exercise Mimickers, Muscling Pills … or Everything Together? (2020) · cites this paper as [43]
PGC-1α is a regulator of cellular oxidant-antioxidant homeostasis by stimulating gene expression of several antioxidant enzymes such as superoxide dismutase-2, catalase, and glutathione peroxidase.
“Eventually, as mentioned earlier, PGC-1α is also a regulator of cellular oxidant–antioxidant homeostasis by stimulating gene expression of several antioxidant enzymes such as superoxide dismutase-2, catalase, and glutathione peroxidase [43].”
From Adiponectin and Its Mimics on Skeletal Muscle: Insulin Sensitizers, Fat Burners, Exercise Mimickers, Muscling Pills … or Everything Together? (2020) · cites this paper as [43]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
1 retracted
Wenz, T., Rossi, S. G., Rotundo, R. L., Spiegelman, B. M., & Moraes, C. T. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911570106 · Cited by 600 · see citing works
RetractedMootha, V. K., Lindgren, C. M., Eriksson, K.-F., Subramanian, A., Sihag, S., Lehar, J., Puigserver, P., Carlsson, E., Ridderstråle, M., Laurila, E., et al. (2003) · Nature Genetics · doi:10.1038/ng1180 · Cited by 10,197 · see citing works
THE NF-κB AND IκB PROTEINS: New Discoveries and Insights
Baldwin, A. S. (1996) · Annual Review of Immunology · doi:10.1146/annurev.immunol.14.1.649 · Cited by 5,882 · see citing works
Inflammation, stress, and diabetes
Wellen, K. E., & Hotamisligil, G. S. (2005) · Journal of Clinical Investigation · doi:10.1172/jci25102 · Cited by 4,143 · see citing works
Wu, Z., Puigserver, P., Andersson, U., Zhang, C., Adelmant, G., Mootha, V., Troy, A., Cinti, S., Lowell, B., Scarpulla, R. C., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80611-x · Cited by 4,139 · see citing works
A Cold-Inducible Coactivator of Nuclear Receptors Linked to Adaptive Thermogenesis
Puigserver, P., Wu, Z., Park, C. W., Graves, R., Wright, M., & Spiegelman, B. M. (1998) · Cell · doi:10.1016/s0092-8674(00)81410-5 · Cited by 3,864 · see citing works
Transcriptional co-activator PGC-1α drives the formation of slow-twitch muscle fibres
Lin, J., Wu, H., Tarr, P. T., Zhang, C.-Y., Wu, Z., Boss, O., Michael, L. F., Puigserver, P., Isotani, E., Olson, E. N., et al. (2002) · Nature · doi:10.1038/nature00904 · Cited by 2,546 · see citing works
St-Pierre, J., Drori, S., Uldry, M., Silvaggi, J. M., Rhee, J., Jäger, S., Handschin, C., Zheng, K., Lin, J., Yang, W., et al. (2006) · Cell · doi:10.1016/j.cell.2006.09.024 · Cited by 2,233 · see citing works
Metabolic control through the PGC-1 family of transcription coactivators
Lin, J., Handschin, C., & Spiegelman, B. M. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.05.004 · Cited by 2,130 · see citing works
Puigserver, P., & Spiegelman, B. M. (2003) · Endocrine Reviews · doi:10.1210/er.2002-0012 · Cited by 2,076 · see citing works
Adaptations of skeletal muscle to endurance exercise and their metabolic consequences
Holloszy, J. O., & Coyle, E. F. (1984) · Journal of Applied Physiology · doi:10.1152/jappl.1984.56.4.831 · Cited by 1,985 · see citing works
Transcriptional paradigms in mammalian mitochondrial biogenesis and function
Scarpulla, R. C. (2008) · Physiological Reviews · doi:10.1152/physrev.00025.2007 · Cited by 1,666 · see citing works
Biochemical Adaptations in Muscle
Holloszy, J. O. (1967) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)96046-1 · Cited by 1,517 · see citing works
PGC-1 coactivators: inducible regulators of energy metabolism in health and disease
Finck, B. N. (2006) · Journal of Clinical Investigation · doi:10.1172/jci27794 · Cited by 1,427 · see citing works
Peroxisome proliferator–activated receptor γ coactivator-1 promotes cardiac mitochondrial biogenesis
Lehman, J. J., Barger, P. M., Kovacs, A., Saffitz, J. E., Medeiros, D. M., & Kelly, D. P. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10268 · Cited by 1,285 · see citing works
Transcriptional regulatory circuits controlling mitochondrial biogenesis and function
Kelly, D. P., & Scarpulla, R. C. (2004) · Genes & Development · doi:10.1101/gad.1177604 · Cited by 1,243 · see citing works
The role of exercise and PGC1α in inflammation and chronic disease
Handschin, C., & Spiegelman, B. M. (2008) · Nature · doi:10.1038/nature07206 · Cited by 1,083 · see citing works
Adaptations of skeletal muscle to exercise: rapid increase in the transcriptional coactivator PGC-1
Baar, K., Wende, A. R., Jones, T. E., Marison, M., Nolte, L. A., Chen, M., Kelly, D. P., & Holloszy, J. O. (2002) · The FASEB Journal · doi:10.1096/fj.02-0367com · Cited by 1,020 · see citing works
Sandri, M., Lin, J., Handschin, C., Yang, W., Arany, Z. P., Lecker, S. H., Goldberg, A. L., & Spiegelman, B. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607795103 · Cited by 974 · see citing works
Cytokine Stimulation of Energy Expenditure through p38 MAP Kinase Activation of PPARγ Coactivator-1
Puigserver, P., Rhee, J., Lin, J., Wu, Z., Yoon, J. C., Zhang, C.-Y., Krauss, S., Mootha, V. K., Lowell, B. B., & Spiegelman, B. M. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00390-2 · Cited by 732 · see citing works
Kong, X., Wang, R., Xue, Y., Liu, X., Zhang, H., Chen, Y., Fang, F., & Chang, Y. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011707 · Cited by 718 · see citing works
Akimoto, T., Pohnert, S. C., Li, P., Zhang, M., Gumbs, C., Rosenberg, P. B., Williams, R. S., & Yan, Z. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m408862200 · Cited by 714 · see citing works
Shi, T., Wang, F., Stieren, E., & Tong, Q. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414670200 · Cited by 712 · see citing works
Michael, L. F., Wu, Z., Cheatham, R. B., Puigserver, P., Adelmant, G., Lehman, J. J., Kelly, D. P., & Spiegelman, B. M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.061035098 · Cited by 663 · see citing works
Schreiber, S., Emter, R., Hock, M. B., Knutti, D., Cardenas, J., Podvinec, M., Oakeley, E. J., & Kralli, A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308686101 · Cited by 657 · see citing works
Handschin, C., Chin, S., Li, P., Liu, F., Maratos-Flier, E., LeBrasseur, N. K., Yan, Z., & Spiegelman, B. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704817200 · Cited by 611 · see citing works
Cao, W., Daniel, K. W., Robidoux, J., Puigserver, P., Medvedev, A. V., Bai, X., Floering, L. M., Spiegelman, B. M., & Collins, S. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.7.3057-3067.2004 · Cited by 605 · see citing works
PGC-1α regulates the mitochondrial antioxidant defense system in vascular endothelial cells
VALLE, I., ALVAREZBARRIENTOS, A., ARZA, E., LAMAS, S., & MONSALVE, M. (2005) · Cardiovascular Research · doi:10.1016/j.cardiores.2005.01.026 · Cited by 556 · see citing works
St‐Pierre, J., Lin, J. D., Krauss, S., Tarr, P. T., Yang, R., Newgard, C. B., & Spiegelman, B. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301850200 · Cited by 543 · see citing works
Russell, L. K., Mansfield, C. M., Lehman, J. J., Kovacs, A., Courtois, M., Saffitz, J. E., Medeiros, D. M., Valencik, M. L., McDonald, J. A., & Kelly, D. P. (2004) · Circulation Research · doi:10.1161/01.res.0000117088.36577.eb · Cited by 402 · see citing works
What do we really know about the ubiquitin-proteasome pathway in muscle atrophy?
Jagoe, R. T., & Goldberg, A. L. (2001) · Current Opinion in Clinical Nutrition and Metabolic Care · doi:10.1097/00075197-200105000-00003 · Cited by 399 · see citing works
Intracellular signaling during skeletal muscle atrophy
Kandarian, S. C., & Jackman, R. W. (2005) · Muscle & Nerve · doi:10.1002/mus.20442 · Cited by 393 · see citing works
Bellizzi, D., Rose, G., Cavalcante, P., Covello, G., Dato, S., De Rango, F., Greco, V., Maggiolini, M., Feraco, E., Mari, V., et al. (2005) · Genomics · doi:10.1016/j.ygeno.2004.11.003 · Cited by 367 · see citing works
PGC-1α regulates the neuromuscular junction program and ameliorates Duchenne muscular dystrophyPreprint
Handschin, C., Kobayashi, Y. M., Chin, S., Seale, P., Campbell, K. P., & Spiegelman, B. M. (2007) · Genes & Development · doi:10.1101/gad.1525107 · Cited by 355 · see citing works
Resistance Exercise Reverses Aging in Human Skeletal Muscle
Melov, S., Tarnopolsky, M. A., Beckman, K. B., Felkey, K., & Hubbard, A. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000465 · Cited by 348 · see citing works
Li, Y.-P., Chen, Y., Li, A. S., & Reid, M. B. (2003) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00129.2003 · Cited by 313 · see citing works
PGC-1α and PGC-1Β Regulate Mitochondrial Density in Neurons
Warȩski, P., Vaarmann, A., Choubey, V., Safiulina, D., Liiv, J., Kuum, M., & Kaasik, A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.018911 · Cited by 294 · see citing works
PGC-1, a versatile coactivator
Knutti, D., & Kralli, A. (2001) · Trends in Endocrinology and Metabolism · doi:10.1016/s1043-2760(01)00457-x · Cited by 294 · see citing works
Modulation of skeletal muscle antioxidant defense by exercise: Role of redox signaling
Ji, L. L. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.02.031 · Cited by 291 · see citing works
The muscle-specific ubiquitin ligase atrogin-1/MAFbx mediates statin-induced muscle toxicity
Hanai, J., Cao, P., Tanksale, P., Imamura, S., Koshimizu, E., Zhao, J., Kishi, S., Yamashita, M., Phillips, P. S., Sukhatme, V. P., et al. (2007) · Journal of Clinical Investigation · doi:10.1172/jci32741 · Cited by 281 · see citing works
Plasticity of skeletal muscle mitochondria: structure and function.
HOPPELER, H., & FL??CK, M. (2003) · Medicine & Science in Sports & Exercise · doi:10.1097/00005768-200301000-00016 · Cited by 267 · see citing works
Geng, T., Li, P., Okutsu, M., Yin, X., Kwek, J., Zhang, M., & Yan, Z. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00481.2009 · Cited by 263 · see citing works
Role of nuclear factor κB in cardiovascular health and disease
der Heiden, K. V., Cuhlmann, S., Luong, L. A., Zakkar, M., & Evans, P. C. (2010) · Clinical Science · doi:10.1042/cs20090557 · Cited by 236 · see citing works
Leick, L., Wojtaszewski, J. F. P., Johansen, S. T., Kiilerich, K., Comes, G., Hellsten, Y., Hidalgo, J., & Pilegaard, H. (2007) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00666.2007 · Cited by 236 · see citing works
Kavazis, A. N., Talbert, E. E., Smuder, A. J., Hudson, M. B., Nelson, W. B., & Powers, S. K. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.01.002 · Cited by 205 · see citing works
Kang, C., OʼMoore, K. M., Dickman, J. R., & Ji, L. L. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.08.007 · Cited by 204 · see citing works
Self-citationSelsby, J. T., Morine, K., Pendrak, K., Barton, E. R., & Sweeney, H. L. (2012) · PLoS ONE · doi:10.1371/journal.pone.0030063 · Cited by 196 · see citing works
Álvarez-Guardia, D., Palomer, X., Coll, T., Davidson, M. M., Chan, T. O., Feldman, A. M., Laguna, J. C., & Vázquez‐Carrera, M. (2010) · Cardiovascular Research · doi:10.1093/cvr/cvq080 · Cited by 187 · see citing works
Leick, L., Lyngby, S. S., Wojtaszewski, J. F. P., & Pilegaard, H. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.01.011 · Cited by 116 · see citing works
Vercauteren, K., Pasko, R. A., Gleyzer, N., Marino, V. M., & Scarpulla, R. C. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00585-06 · Cited by 109 · see citing works
Miura, S., Tomitsuka, E., Kamei, Y., Yamazaki, T., Kai, Y., Tamura, M., Kita, K., Nishino, I., & Ezaki, O. (2006) · The American Journal of Pathology · doi:10.2353/ajpath.2006.060034 · Cited by 107 · see citing works
Frailty in the elderly: the physical dimension.
Abate, M., Iorio, A. D., Renzo, D. D., Paganelli, R., Saggini, R., & Abate, G. (2007) · PubMed · Cited by 103 · see citing works
Mitochondrial damage and intralysosomal degradation in cellular aging
Terman, A., Gustafsson, B., & Brunk, U. T. (2006) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2006.08.006 · Cited by 103 · see citing works
Plasticity of skeletal muscle mitochondria: structure and function.
Hoppeler, H. H., & Flück, M. (2003) · PubMed · doi:10.1249/01.mss.0000043292.99104.12 · Cited by 92 · see citing works
PGC-1α and Myokines in the Aging Muscle – A Mini-Review
Arnold, A.-S., Egger, A., & Handschin, C. (2011) · Gerontology · doi:10.1159/000281883 · Cited by 65 · see citing works
Jänkälä, H., Harjola, V., Petersen, N. E., & Härkönen, M. (1997) · Journal of Applied Physiology · doi:10.1152/jappl.1997.82.3.977 · Cited by 57 · see citing works
Handschin, C. (2010) · Journal of Receptors and Signal Transduction · doi:10.3109/10799891003641074 · Cited by 56 · see citing works
PGC-1&#945; and Exercise: Important Partners in Combating Insulin Resistance
Russell, A. (2005) · Current Diabetes Reviews · doi:10.2174/1573399054022811 · Cited by 48 · see citing works
Handschin, C. (2009) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/j.1440-1681.2009.05275.x · Cited by 38 · see citing works
PGC-1α: a master gene that is hard to master
Lindholm, D., Eriksson, O., Mäkelä, J., Belluardo, N., & Korhonen, L. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1043-0 · Cited by 31 · see citing works
Kang, C., Chung, E., Diffee, G. M., & Ji, L. L. (2009) · Medicine & Science in Sports & Exercise · doi:10.1249/01.mss.0000353449.06824.c0 · Cited by 4 · see citing works
Self-citation
Flagged first, then by citations
Research works printed but not linked: 2
- [14]Wu Z Puigserver P Andersson U Mechanisms controlling mitochondrial biogenesis and respiration through the thermogeniccoactivator PGC-1 Cell 1999 98 115 124 10412986
- [15]Lin J Wu H Tarr PT Transcriptional co-activator PGC-1α drives the formation of slow-twitch muscle fibres Nature 2002 418 797 801 12181572
Cited by
Sorted by citations
Role of ROS and RNS Sources in Physiological and Pathological Conditions
Meo, S. D., Reed, T. T., Venditti, P., & Víctor, V. M. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/1245049 · Cited by 1,638 · see citing works
Mitochondrial Dysfunction and Oxidative Stress in Alzheimer’s Disease
Misrani, A., Tabassum, S., & Yang, L. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.617588 · Cited by 654 · see citing works
PGC-1 α , Inflammation, and Oxidative Stress: An Integrative View in Metabolism
Rius‐Pérez, S., Torres-Cuevas, I., Millán, I., Ortega, Á., & Pérez, S. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/1452696 · Cited by 648 · see citing works
PGC-1α Is a Master Regulator of Mitochondrial Lifecycle and ROS Stress Response
Abu Shelbayeh, O., Arroum, T., Morris, S., & Busch, K. B. (2023) · Antioxidants · doi:10.3390/antiox12051075 · Cited by 552 · see citing works
Mechanisms for fiber-type specificity of skeletal muscle atrophy
Wang, Y., & Pessin, J. E. (2013) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0b013e328360272d · Cited by 415 · see citing works
Mitochondrial dysfunction in metabolic syndrome
Prasun, P. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.165838 · Cited by 375 · see citing works
Mitochondrial dysfunction in aging
Guo, Y., Guan, T., Shafiq, K., Yu, Q., Jiao, X., Na, D., Li, M., Zhang, G., & Kong, J. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101955 · Cited by 350 · see citing works
Wang, Y., Zhao, X., Lotz, M., Terkeltaub, R. A., & Liu‐Bryan, R. (2015) · Arthritis & Rheumatology · doi:10.1002/art.39182 · Cited by 303 · see citing works
Butyrate enhances mitochondrial function during oxidative stress in cell lines from boys with autism
Rose, S., Bennuri, S. C., Davis, J. E., Wynne, R., Slattery, J. C., Tippett, M., Delhey, L., Melnyk, S., Kahler, S. G., MacFabe, D. F., et al. (2018) · Translational Psychiatry · doi:10.1038/s41398-017-0089-z · Cited by 226 · see citing works
Kotiadis, V. N., Duchen, M. R., & Osellame, L. D. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.10.041 · Cited by 212 · see citing works
Therapies for mitochondrial diseases and current clinical trials
El‐Hattab, A. W., Zarante, A. M., Almannai, M., & Scaglia, F. (2017) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2017.09.009 · Cited by 188 · see citing works
Oxidative stress and mitochondrial dysfunction in early-onset and late-onset preeclampsia
Marı́n, R., Chiarello, D. I., Abad, C., Rojas, D., Toledo, F., & Sobrevía, L. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.165961 · Cited by 190 · see citing works
The Role of Reactive Oxygen Species in the Life Cycle of the Mitochondrion
Venditti, P., & Meo, S. D. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21062173 · Cited by 170 · see citing works
Mediators of Physical Activity Protection against ROS-Linked Skeletal Muscle Damage
Meo, S. D., Napolitano, G., & Venditti, P. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20123024 · Cited by 146 · see citing works
Liu, D., Cai, Z., Yang, Y.-T., Lu, W.-H., Pan, L.-Y., Xiao, W.-F., & Li, Y. (2021) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2021.10.009 · Cited by 137 · see citing works
The AMPK-PPARGC1A pathway is required for antimicrobial host defense through activation of autophagy
Yang, C.-S., Kim, J.-J., Lee, H.-M., Jin, H. S., Lee, S.-H., Park, J.-H., Kim, S. J., Kim, J.-M., Han, Y.-M., Lee, M.-S., et al. (2014) · Autophagy · doi:10.4161/auto.28072 · Cited by 131 · see citing works
Mitochondrial Dysfunction in Lung Pathogenesis
Piantadosi, C. A., & Suliman, H. B. (2016) · Annual Review of Physiology · doi:10.1146/annurev-physiol-022516-034322 · Cited by 122 · see citing works
Xu, M., Chen, X., Chen, D., Yu, B., & Huang, Z. (2016) · Oncotarget · doi:10.18632/oncotarget.12891 · Cited by 119 · see citing works
Zhao, X., Petursson, F., Viollet, B., Lotz, M., Terkeltaub, R. A., & Liu‐Bryan, R. (2014) · Arthritis & Rheumatology · doi:10.1002/art.38791 · Cited by 114 · see citing works
Inflammation and intracellular metabolism: new targets in OA
Liu‐Bryan, R. (2015) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2014.12.016 · Cited by 113 · see citing works
Guo, A., Li, K., Tian, H., Fan, Z., Chen, Q., Yang, Y., Yu, J., Wu, Y., & Xiao, Q. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16448 · Cited by 112 · see citing works
Melatonin prevents mitochondrial dysfunction and insulin resistance in rat skeletal muscle
Teodoro, B. G., Baraldi, F. G., Sampaio, I. H., Bomfim, L. H. M., Queiroz, A. L., Passos, M. A., Carneiro, E. M., Alberici, L. C., Gomis, R., Amaral, F. G., et al. (2014) · Journal of Pineal Research · doi:10.1111/jpi.12157 · Cited by 106 · see citing works
Multiple roles of short-chain fatty acids in Alzheimer disease
Chen, H., Meng, L., & Shen, L. (2021) · Nutrition · doi:10.1016/j.nut.2021.111499 · Cited by 107 · see citing works
Natural products, PGC-1 , and Duchenne muscular dystrophy
Süntar, I. P., Sureda, A., Belwal, T., Sanches-Silva, A. T., Vacca, R. A., Tewari, D., Sobarzo‐Sánchez, E., Nabavi, S. F., Shirooie, S., Dehpour, A. R., et al. (2020) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2020.01.001 · Cited by 103 · see citing works
Nierenberg, A. A., Ghaznavi, S., Mathias, I. S., Ellard, K. K., JANOS, J. A., & Sylvia, L. G. (2018) · Biological Psychiatry · doi:10.1016/j.biopsych.2017.12.014 · Cited by 95 · see citing works
El‐Hattab, A. W., & Scaglia, F. (2016) · Cell Calcium · doi:10.1016/j.ceca.2016.03.003 · Cited by 98 · see citing works
Whitaker, R. M., Wills, L. P., Stallons, L. J., & Schnellmann, R. G. (2013) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.113.208017 · Cited by 92 · see citing works
Sciorati, C., Clementi, E., Manfredi, A. A., & Rovere, P. Q. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1857-7 · Cited by 92 · see citing works
The protective effects of Resveratrol against radiation-induced intestinal injury
Zhang, H., Yan, H., Zhou, X., Wang, H., Yang, Y., Zhang, J., & Wang, H. (2017) · BMC Complementary and Alternative Medicine · doi:10.1186/s12906-017-1915-9 · Cited by 91 · see citing works
Mitochondria: Potential Targets for Osteoarthritis
Mao, X.-J., Fu, P., Wang, L.-L., & Xiang, C. (2020) · Frontiers in Medicine · doi:10.3389/fmed.2020.581402 · Cited by 89 · see citing works
Schlernitzauer, A., Oiry, C., Hamad, R., Galas, S., Cortade, F., Chabi, B., Casas, F., Pessemesse, L., Fouret, G., Feillet‐Coudray, C., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0078788 · Cited by 86 · see citing works
Sujkowski, A. L., Bazzell, B. G., Carpenter, K., Arking, R., & Wessells, R. J. (2015) · Aging · doi:10.18632/aging.100789 · Cited by 84 · see citing works
Aguirre-Rueda, D., Guerra‐Ojeda, S., Aldasoro, M., Iradi, A., Obrador, E., Ortega, Á., Mauricio, M. D., Vila, J. M., & Vallés, S. L. (2014) · International Journal of Medical Sciences · doi:10.7150/ijms.10035 · Cited by 84 · see citing works
Remels, A. H. V., Gosker, H. R., Verhees, K. J. P., Langen, R. C. J., & Schols, A. M. W. J. (2015) · Endocrinology · doi:10.1210/en.2014-1591 · Cited by 82 · see citing works
Dikalov, S., & Dikalova, A. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7632 · Cited by 79 · see citing works
Yap, J. L. Y., Tai, Y. K., Fröhlich, J., Fong, C. H. H., Yin, J. N., Foo, Z. L., Ramanan, S., Beyer, C., Toh, S. J., Casarosa, M., et al. (2019) · The FASEB Journal · doi:10.1096/fj.201900057r · Cited by 74 · see citing works
The Role of Myocardial Mitochondrial Quality Control in Heart Failure
Qiu, Z., Yi, W., Song, Q., Du, B., Wang, H., Chu, Y., & Hu, Y. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01404 · Cited by 74 · see citing works
Clinical trials in mitochondrial disorders, an update
Almannai, M., El‐Hattab, A. W., Ali, M. N., Soler‐Alfonso, C., & Scaglia, F. (2020) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2020.10.002 · Cited by 73 · see citing works
Abou-Samra, M., Selvais, C. M., Dubuisson, N., & Brichard, S. M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21072620 · Cited by 72 · see citing works
Nitric oxide regulation of cellular metabolism: Adaptive tuning of cellular energy
Pappas, G., Wilkinson, M. L., & Gow, A. J. (2022) · Nitric Oxide · doi:10.1016/j.niox.2022.11.006 · Cited by 71 · see citing works
Kayhan, M., Vouillamoz, J., Rodríguez, D. G., Bugarski, M., Mitamura, Y., Gschwend, J., Schneider, C., Hall, A. M., Legouis, D., Akdiş, C. A., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-39050-y · Cited by 69 · see citing works
Khalil, M., Shanmugam, H., Abdallah, H., JohnBritto, J. S., Galerati, I., Gómez‐Ambrosi, J., Frühbeck, G., & Portincasa, P. (2022) · Nutrients · doi:10.3390/nu14153112 · Cited by 66 · see citing works
Mechanism of skeletal muscle atrophy after spinal cord injury: A narrative review
Xu, X. P., Talifu, Z., Zhang, C.-J., Gao, F., Ke, H., Pan, Y., Gong, H., Du, H., Yu, Y. H., Jing, Y.-L., et al. (2023) · Frontiers in Nutrition · doi:10.3389/fnut.2023.1099143 · Cited by 65 · see citing works
Valine improves mitochondrial function and protects against oxidative stress
Sharma, S., Zhang, X., Azhar, G., Patyal, P., Verma, A., Grishma, K. C., & Wei, J. Y. (2023) · Bioscience Biotechnology and Biochemistry · doi:10.1093/bbb/zbad169 · Cited by 64 · see citing works
Improvement of obesity-linked skeletal muscle insulin resistance by strength and endurance training
Meo, S. D., Iossa, S., & Venditti, P. (2017) · Journal of Endocrinology · doi:10.1530/joe-17-0186 · Cited by 62 · see citing works
Buso, A., Comelli, M., Picco, R., Isola, M., Magnesa, B., Pišot, R., Rittweger, J., Salvadego, D., Šimunič, B., Grassi, B., et al. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00474 · Cited by 63 · see citing works
Inactivation of glycogen synthase kinase-3β (GSK-3β) enhances skeletal muscle oxidative metabolism
Theeuwes, W. F., Gosker, H. R., LANGEN, R. C. J., Verhees, K. J. P., Pansters, N., Schols, A. M. W. J., & Remels, A. H. V. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.09.018 · Cited by 62 · see citing works
Nutrition, Bioenergetics, and Metabolic Syndrome
García‐García, F. J., Monistrol-Mula, A., Cardellach, F., & Garrabou, G. (2020) · Nutrients · doi:10.3390/nu12092785 · Cited by 66 · see citing works
Muscle–brain crosstalk mediated by exercise-induced myokines - insights from experimental studies
Kostka, M., Morys, J., Małecki, A., & Nowacka-Chmielewska, M. M. (2024) · Frontiers in Physiology · doi:10.3389/fphys.2024.1488375 · Cited by 68 · see citing works
GPER mediates the effects of 17β-estradiol in cardiac mitochondrial biogenesis and function
Sbert-Roig, M., Bauzá-Thorbrügge, M., Galmés-Pascual, B. M., Capllonch-Amer, G., García-Palmer, F., Lladó, I., Proenza, A. M., & Gianotti, M. (2015) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2015.11.027 · Cited by 58 · see citing works
Wen, X., Wu, J., Chang, J. S., Zhang, P., Wang, J., Zhang, Y., Gettys, T. W., & Zhang, Y. (2014) · BioMed Research International · doi:10.1155/2014/402175 · Cited by 55 · see citing works
Ábrigo, J., Olguín, H. C., Tacchi, F., Orozco-Aguilar, J., Valero‐Breton, M., Soto, J. A., Castro‐Sepúlveda, M., Elorza, Á. A., Simón, F., & Cabello‐Verrugio, C. (2023) · Biological Research · doi:10.1186/s40659-023-00436-3 · Cited by 54 · see citing works
Mitochondria in the middle: exercise preconditioning protection of striated muscle
Lawler, J. M., Rodriguez, D., & Hord, J. M. (2016) · The Journal of Physiology · doi:10.1113/jp270656 · Cited by 53 · see citing works
Chung, N., Park, J., & Lim, K. (2017) · Physical Activity and Nutrition · doi:10.20463/jenb.2017.0020 · Cited by 54 · see citing works
Osório Alves, J., Matta Pereira, L., Cabral Coutinho do Rêgo Monteiro, I., Pontes dos Santos, L. H., Soares Marreiros Ferraz, A., Carneiro Loureiro, A. C., Calado Lima, C., Leal-Cardoso, J. H., Pires Carvalho, D., Soares Fortunato, R., et al. (2020) · Antioxidants · doi:10.3390/antiox9010057 · Cited by 53 · see citing works
van den Hoek, A. M., de Jong, J. C. B. C., Worms, N., van Nieuwkoop, A., Voskuilen, M., Menke, A. L., Lek, S., Caspers, M. P. M., Verschuren, L., & Kleemann, R. (2021) · Metabolism · doi:10.1016/j.metabol.2021.154873 · Cited by 53 · see citing works
Dam, A. D., Mitchell, A. S., & Quadrilatero, J. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.04.014 · Cited by 51 · see citing works
Current Evidence of the Role of the Myokine Irisin in Cancer
Tsiani, E., Tsakiridis, N., Kouvelioti, R., Jaglanian, A., & Klentrou, P. (2021) · Cancers · doi:10.3390/cancers13112628 · Cited by 51 · see citing works
Golko-Perez, S., Amit, T., Bar‐Am, O., Youdim, M. B. H., & Weinreb, O. (2016) · Neurotoxicity Research · doi:10.1007/s12640-016-9677-6 · Cited by 47 · see citing works
Permpoon, U., Moon, J., Kim, C. Y., & Nam, T. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26157616 · Cited by 52 · see citing works
Exercise preconditioning diminishes skeletal muscle atrophy after hindlimb suspension in mice
Theilen, N. T., Jeremic, N. S., Weber, G. J., & Tyagi, S. C. (2018) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00137.2018 · Cited by 46 · see citing works
Stocks, B., Ashcroft, S. P., Joanisse, S., Dansereau, L. C., Koay, Y. C., Elhassan, Y., Lavery, G. G., Quek, L., O’Sullivan, J., Philp, A. M., et al. (2021) · The Journal of Physiology · doi:10.1113/jp280825 · Cited by 44 · see citing works
Beyond antioxidants: Selenium and skeletal muscle mitochondria
Wesolowski, L. T., Semanchik, P. L., & White-Springer, S. H. (2022) · Frontiers in Veterinary Science · doi:10.3389/fvets.2022.1011159 · Cited by 43 · see citing works
The cyclic metabolic switching theory of intermittent fasting
Mattson, M. P. (2025) · Nature Metabolism · doi:10.1038/s42255-025-01254-5 · Cited by 45 · see citing works
Polydatin Alleviates Small Intestine Injury during Hemorrhagic Shock as a SIRT1 Activator
Zeng, Z., Chen, Z., Xu, S., Song, R., Yang, H. S., & Zhao, K. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/965961 · Cited by 42 · see citing works
Tero-Vescan, A., Degens, H., Matsakas, A., Ștefănescu, R., Ősz, B. E., & Slevin, M. (2025) · Pharmaceuticals · doi:10.3390/ph18081222 · Cited by 44 · see citing works
Ou, H., Chou, W., Chu, P., Hsieh, P., Hung, C., & Tsai, K. (2019) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201801353 · Cited by 41 · see citing works
Cheung, C., Tu, S., Feng, Y., Wan, C., Ai, H., & Chen, Z. (2024) · Archives of Gerontology and Geriatrics · doi:10.1016/j.archger.2024.105522 · Cited by 43 · see citing works
Brady, P., DeKoninck, P. L. J., Fryns, J. P., Devriendt, K., Deprest, J. A., & Vermeesch, J. R. (2013) · Prenatal Diagnosis · doi:10.1002/pd.4244 · Cited by 41 · see citing works
Alvehus, M., Boman, N., Söderlund, K., Svensson, M., & Burén, J. (2014) · European Journal of Applied Physiology · doi:10.1007/s00421-014-2879-9 · Cited by 39 · see citing works
Physical exercise: An inducer of positive oxidative stress in skeletal muscle aging
Thirupathi, A., Pinho, R. A., & Chang, Y. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.117630 · Cited by 39 · see citing works
Mohammadinejad, F., Mohammadabadi, M., Roudbari, Z., & Sadkowski, T. (2022) · Animals · doi:10.3390/ani12243471 · Cited by 38 · see citing works
The BACE1 product sAPPβ induces ER stress and inflammation and impairs insulin signaling
Botteri, G., Salvadó, L., Gumà, A., Hamilton, D. L., Meakin, P. J., Montagut, G., Ashford, M. L. J., Ceperuelo‐Mallafré, V., Fernández‐Veledo, S., Vendrell, J. J., et al. (2018) · Metabolism · doi:10.1016/j.metabol.2018.03.005 · Cited by 38 · see citing works
Otzel, D. M., Lee, J., Ye, F., Borst, S. E., & Yarrow, J. F. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19061701 · Cited by 39 · see citing works
Lee, S.-J., Bae, J. H., Lee, H., Lee, H., Park, J., Kang, J.-S., & Bae, G.-U. (2019) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2019.112054 · Cited by 38 · see citing works
Takanche, J. S., Lee, Y., Kim, J. ‐., Kim, J. ‐., Han, S., Lee, S. ‐., & Yi, H. (2017) · International Endodontic Journal · doi:10.1111/iej.12861 · Cited by 37 · see citing works
Liu, X., Du, Y., Trakooljul, N., Brand, B., Muráni, E., Krischek, C., Wicke, M., Schwerin, M., Wimmers, K., & Ponsuksili, S. (2015) · International Journal of Biological Sciences · doi:10.7150/ijbs.13132 · Cited by 37 · see citing works
Skeletal muscle redox signaling in rheumatoid arthritis
Steinz, M. M., Alves, E. S., & Lanner, J. T. (2020) · Clinical Science · doi:10.1042/cs20190728 · Cited by 37 · see citing works
Song, M. S., Lim, S.-K., Wang, J., & Kim, H. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19010278 · Cited by 37 · see citing works
Role of PGC-1α in muscle function and aging
Kang, C., & Ji, L. L. (2013) · Journal of sport and health science/Journal of Sport and Health Science · doi:10.1016/j.jshs.2013.03.005 · Cited by 37 · see citing works
Self-citationTai, Y. K., Ng, C., Purnamawati, K., Yap, J. L. Y., Yin, J. N., Wong, C. J. K., Patel, B. K., Soong, P. L., Pelczar, P., Fröhlich, J., et al. (2020) · The FASEB Journal · doi:10.1096/fj.201903005rr · Cited by 36 · see citing works
Mitochondrial Quality Control: the Role in Cardiac Injury
Sygitowicz, G., & Sitkiewicz, D. (2022) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2703096 · Cited by 34 · see citing works
Role of Adipokines in Sarcopenia
Lu, W., Feng, W., Lai, J., Yuan, D., Xiao, W., & Li, Y. (2023) · Chinese Medical Journal · doi:10.1097/cm9.0000000000002255 · Cited by 34 · see citing works
Low-frequency stimulation regulates metabolic gene expression in paralyzed muscle
Petrie, M. A., Suneja, M., & Shields, R. K. (2015) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00628.2014 · Cited by 33 · see citing works
Lee, K., Jin, H., Chei, S., Oh, H., Lee, J., & Lee, B.-Y. (2020) · Cells · doi:10.3390/cells9020377 · Cited by 33 · see citing works
Mitochondrial-induced Epigenetic Modifications: From Biology to Clinical Translation
Sharma, J., Kumari, R., Bhargava, A., Tiwari, R. R., & Mishra, P. K. (2020) · Current Pharmaceutical Design · doi:10.2174/1381612826666200826165735 · Cited by 32 · see citing works
IL-6 can singlehandedly drive many features of frailty in mice
Jergović, M., Thompson, H. L., Bradshaw, C. M., Sonar, S. A., Ashgar, A., Mohty, N. M., Joseph, B. A., Fain, M. J., Cleveland, K. H., Schnellman, R. G., et al. (2021) · GeroScience · doi:10.1007/s11357-021-00343-z · Cited by 32 · see citing works
Dzięgielewska-Gęsiak, S. (2021) · Clinical Interventions in Aging · doi:10.2147/cia.s306982 · Cited by 32 · see citing works
RNA Deregulation in Amyotrophic Lateral Sclerosis: The Noncoding Perspective
Laneve, P., Tollis, P., & Caffarelli, E. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910285 · Cited by 32 · see citing works
Assessed and Emerging Biomarkers in Stroke and Training-Mediated Stroke Recovery: State of the Art
Gandolfi, M., Smania, N., Vella, A., Picelli, A., & Chirumbolo, S. (2017) · Neural Plasticity · doi:10.1155/2017/1389475 · Cited by 31 · see citing works
Recent advances in mitochondrial diseases: From molecular insights to therapeutic perspectives
Aldossary, A. M., Tawfik, E. A., Alomary, M. N., Alsudir, S. A., Alfahad, A. J., Alshehri, A. A., Almughem, F. A., Mohammed, R. Y., & Alzaydi, M. M. (2022) · Saudi Pharmaceutical Journal · doi:10.1016/j.jsps.2022.05.011 · Cited by 31 · see citing works
Essential role of the PGC‐1α/PPARβ axis in Ucp3 gene induction
de Lima, T. I., Guimarães, D. S. P. S. F., Sponton, C. H., Bajgelman, M. C., Palameta, S., Toscaro, J. M., Reis, O., & Silveira, L. R. (2019) · The Journal of Physiology · doi:10.1113/jp278006 · Cited by 30 · see citing works
Laurindo, L. F., Rodrigues, V. D., Laurindo, L. F., Cherain, L. M. A., de Lima, E. P., Boaro, B. L., Oliveira, J. D. S. C., Chagas, E. F. B., Catharin, V. C. S., Haber, J. F. D. S., et al. (2024) · Life Sciences · doi:10.1016/j.lfs.2024.123230 · Cited by 31 · see citing works
Regulation of mitochondrial quality following repeated bouts of hindlimb unloading
Rosa‐Caldwell, M. E., Brown, J. L., Perry, R. A., Shimkus, K. L., Shirazi‐Fard, Y., Brown, L. A., Hogan, H. A., Fluckey, J. D., Washington, T. A., Wiggs, M. P., et al. (2019) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/apnm-2019-0218 · Cited by 30 · see citing works
Petrie, M. A., Sharma, A., Taylor, E. B., Suneja, M., & Shields, R. K. (2019) · Physiological Genomics · doi:10.1152/physiolgenomics.00064.2019 · Cited by 28 · see citing works
The role of mitochondrial dynamics in the pathophysiology of endometriosis
Kobayashi, H., Matsubara, S., Yoshimoto, C., Shigetomi, H., & Imanaka, S. (2023) · Journal of obstetrics and gynaecology research · doi:10.1111/jog.15791 · Cited by 29 · see citing works
Shin, E. J., Jo, S., Choi, S., Cho, C., Lim, W., Hong, H., Lim, T., Jang, Y. J., Jang, M., Byun, S., et al. (2020) · Molecules · doi:10.3390/molecules25040865 · Cited by 28 · see citing works
Advances in drug therapy for mitochondrial diseases
Zhang, L., Zhang, Z., Khan, A., Zheng, H., Yuan, C., & Jiang, H. (2020) · Annals of Translational Medicine · doi:10.21037/atm.2019.10.113 · Cited by 27 · see citing works
RetractedStremming, J., Chang, E. I., Knaub, L. A., Armstrong, M., Baker, P. R., Wesolowski, S. R., Reisdorph, N. A., Reusch, J. E. B., & Brown, L. D. (2021) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00222.2021 · Cited by 29 · see citing works
Byeon, H. R., Jang, S.-Y., Lee, Y., Kim, D., Hong, M.-G., Lee, D., Shin, J., & Seo, J. (2022) · Journal of Medicinal Food · doi:10.1089/jmf.2021.k.0148 · Cited by 26 · see citing works
- Authors
- Kang, C., & Li Ji, L.
- Affiliations
- University of Minnesota (US)
- ORCID
- Kang, Chounghun
- Venue
- Annals of the New York Academy of Sciences
- Publisher
- Wiley
- Published
- 2012-10
- Volume
- 1271
- Issue
- 1
- Pages
- 110-117
- ISSN
- 0077-8923 (ISSN-L)
- 1749-6632
- PMC
- PMC3499658
- OpenAlex
- W1524273338
- Cited by
- 291
- References
- 60
- Citations by year
- 2026: 24 · 2025: 32 · 2024: 35 · 2023: 31 · 2022: 20 · 2021: 30 · 2020: 30 · 2019: 17 · 2018: 18 · 2017: 12 · 2016: 9 · 2015: 15 · 2014: 11 · 2013: 7
- FWCI
- 0.96
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Annals of the New York Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- PGC-1α, skeletal muscle atrophy, immobilization, mitochondrial biogenesis, nuclear respiratory factors, TFAM, oxidative stress, antioxidant enzymes, manganese superoxide dismutase, uncoupling proteins, muscle health
- MeSH terms
- Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha, Aging, Animals, Heat-Shock Proteins, Humans, Muscular Atrophy, Musculoskeletal Diseases, Oxidoreductases, Transcription Factors, Signal Transduction, Exercise, Gene Expression Regulation, Enzymologic, Muscle, Skeletal, Mitochondrial Turnover
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review