The DOI matches its Crossref record; 53 of the 53 references it cites were found in a registry or an index.
PGC-1α protects skeletal muscle from atrophy by suppressing FoxO3 action and atrophy-specific gene transcription
Open accessAbstract
Maintaining muscle size and fiber composition requires contractile activity. Increased activity stimulates expression of the transcriptional coactivator PGC-1α (peroxisome proliferator-activated receptor γ coactivator 1α), which promotes fiber-type switching from glycolytic toward more oxidative fibers. In response to disuse or denervation, but also in fasting and many systemic diseases, muscles undergo marked atrophy through a common set of transcriptional changes. FoxO family transcription factors play a critical role in this loss of cell protein, and when activated, FoxO3 causes expression of the atrophy-related ubiquitin ligases atrogin-1 and MuRF-1 and profound loss of muscle mass. To understand how exercise might retard muscle atrophy, we investigated the possible interplay between PGC-1α and the FoxO family in regulation of muscle size. Rodent muscles showed a large decrease in PGC-1α mRNA during atrophy induced by denervation as well as by cancer cachexia, diabetes, and renal failure. Furthermore, in transgenic mice overexpressing PGC-1α, denervation and fasting caused a much smaller decrease in muscle fiber diameter and a smaller induction of atrogin-1 and MuRF-1 than in control mice. Increased expression of PGC-1α also increased mRNA for several genes involved in energy metabolism whose expression decreases during atrophy. Transfection of PGC-1α into adult fibers reduced the capacity of FoxO3 to cause fiber atrophy and to bind to and transcribe from the atrogin-1 promoter. Thus, the high levels of PGC-1α in dark and exercising muscles can explain their resistance to atrophy, and the rapid fall in PGC-1α during atrophy should enhance the FoxO-dependent loss of muscle mass.
Overview
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
Verification
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“PPARGC1A, the gene that encodes PGC‐1α, is most well‐known for its role in mitochondrial biogenesis but has been reported to protect muscle mass in the context of muscle atrophy triggered by aging (Yang et al., 2020), chronic heart failure, and various other muscle wasting conditions (Sandri et al., 2006).”
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 ( SOMMA ) (2024) · cites this paper as Sandri et al., 2006
Experimental — accuracy not yet measuredIn the citing paper
“PGC-1α is a transcriptional coactivator that has reduced gene expression in muscles of patients with type 2 diabetes,55 and might have a role in preventing muscle atrophy.53,56”
From Age-related and disease-related muscle loss: The effect of diabetes, obesity, and other diseases (2014) · cites this paper as [53]
In the citing paper
“Myofibre size in skeletal muscle is also reduced in people with type 2 diabetes.53”
From Age-related and disease-related muscle loss: The effect of diabetes, obesity, and other diseases (2014) · cites this paper as [53]
In the citing paper
“First, skeletal muscles are heterogeneous with respect to fiber type and metabolic properties and therefore they vary, often drastically, in their response to the same stimulus.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [2]
In the citing paper
“For instance, slow muscles, such as the soleus, are less sensitive to starvation compared to fast muscles2, while during disuse such as that induced by hind limb suspension, the soleus atrophies faster than glycolytic (fast) muscles3.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [2]
In the citing paper
“For instance, JunB, PGC1α, and PGC1β all inhibit FoxO activity in skeletal muscles2,67,68, while the glucocorticoid receptor and β−catenin synergize with FoxOs to promote muscle wasting69.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [2]
In the citing paper
“With aging, PGC-1α levels dramatically fall in the skeletal muscle [86], while the maintenance of PGC-1α expression preserves muscle mass during sarcopenia, cachexia, denervation, and fasting [85,87].”
From Role of Age-Related Mitochondrial Dysfunction in Sarcopenia (2020) · cites this paper as [85]
In the citing paper
“This phenomenon seems to be mediated by the promotion of mitochondrial turnover and quality control [85,87].”
From Role of Age-Related Mitochondrial Dysfunction in Sarcopenia (2020) · cites this paper as [85]
In the citing paper
“PGC-1α may also prevent muscle atrophy through the regulation of autophagy [85].”
From Role of Age-Related Mitochondrial Dysfunction in Sarcopenia (2020) · cites this paper as [85]
In the citing paper
“Because exercise and ApN share similar signaling pathways [75,76] and the potential of counteracting several facets of this metabolic syndrome, numerous studies attempted to establish relationships between exercise and ApN parameters.”
From Adiponectin and Its Mimics on Skeletal Muscle: Insulin Sensitizers, Fat Burners, Exercise Mimickers, Muscling Pills … or Everything Together? (2020) · cites this paper as [75]
In the citing paper
“The transcriptional activity of FoxO3 is inhibited, on one hand, by PGC-1α and on the other hand, by the insulin/IGF1 signaling pathway, which also activates protein synthesis [75].”
From Adiponectin and Its Mimics on Skeletal Muscle: Insulin Sensitizers, Fat Burners, Exercise Mimickers, Muscling Pills … or Everything Together? (2020) · cites this paper as [75]
In the citing paper
“Forkhead box O (FoxO) family TF play a critical role in protein breakdown by activating the expression of atrogenes (which include two muscle-specific ubiquitin ligases, atrogin-1 and MuRF1) responsible for profound loss of muscle mass [75].”
From Adiponectin and Its Mimics on Skeletal Muscle: Insulin Sensitizers, Fat Burners, Exercise Mimickers, Muscling Pills … or Everything Together? (2020) · cites this paper as [75]
In the citing paper
“PGC-1α reduces muscle protein degradation by the UPS via blocking nuclear factor κB (NF-κB) and FoxO3 activity (16, 124).”
From Mitochondria initiate and regulate sarcopenia (2017) · cites this paper as [124]
In the citing paper
“Thus, high-level expression of PGC-1 may actually cause accumulation of lipids and/or incomplete oxidation products, leading to reduced insulin sensitivity, as observed in PGC-1␣ transgenic mice (267-269).”
From The role of mitochondria in the pathogenesis of type 2 diabetes (2010) · cites this paper as [269]
In the citing paper
“When PGC-1␣ overexpression is restricted to skeletal muscle but overexpressed throughout development by the use of the creatine kinase gene promoter, very large increases in mitochondrial mass, OXPHOS, and fatty acid oxidation genes are observed (267-269).”
From The role of mitochondria in the pathogenesis of type 2 diabetes (2010) · cites this paper as [269]
In the citing paper
“Despite these effects, insulin sensitivity is normal in PGC-1␣ transgenic mice fed a chow diet and, surprisingly, is reduced during high-fat feeding.”
From The role of mitochondria in the pathogenesis of type 2 diabetes (2010) · cites this paper as [269]
In the citing paper
“In this model, ATP synthesis rate and exercise performance are increased, and fatty acid oxidation is also enhanced.”
From The role of mitochondria in the pathogenesis of type 2 diabetes (2010) · cites this paper as [269]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Calcium's Role in Mechanotransduction during Muscle Development
Damm, T. B., & Egli, M. (2014) · Cellular Physiology and Biochemistry · doi:10.1159/000356667 · Cited by 14,552
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
Self-citationA 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
Self-citationIdentification of ubiquitin ligases required for skeletal muscle atrophy.
Bodine, S. C., Latres, E., Baumhueter, S., Lai, V. K.-M., Nunez, L., Clarke, B. A., Poueymirou, W. T., Panaro, F. J., Na, E., Dharmarajan, K., et al. (2001) · Science · doi:10.1126/science.1065874 · Cited by 3,521
Sandri, M., Sandri, C., Gilbert, A., Skurk, C., Calabria, E., Picard, A., Walsh, K., Schiaffino, S., Lecker, S. H., & Goldberg, A. L. (2004) · Cell · doi:10.1016/s0092-8674(04)00400-3 · Cited by 3,012
Self-citationTranscriptional 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
Self-citationMetabolic 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
Self-citationStitt, T. N., Drujan, D., Clarke, B. A., Panaro, F., Timofeyva, Y., Kline, W. O., Gonzalez, M., Yancopoulos, G. D., & Glass, D. J. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00211-4 · Cited by 1,964
Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy
Gomes, M. D., Lecker, S. H., Jagoe, R. T., Navon, A., & Goldberg, A. L. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.251541198 · Cited by 1,774
Self-citationMultiple types of skeletal muscle atrophy involve a common program of changes in gene expression
Lecker, S. H., Jagoe, R. T., Gilbert, A., Gomes, M., Baracos, V., Bailey, J., Price, S. R., Mitch, W. E., & Goldberg, A. L. (2004) · The FASEB Journal · doi:10.1096/fj.03-0610com · Cited by 1,539
Self-citation
Research works printed but not linked: 7
- JM Sacheck, J-P Hyatt, A Raffaello, RT Jagoe, RR Roy, VR Edgerton, SH Lecker, AL Goldberg FASEB J, in press. (2006).
- G Tiao, M Lieberman, JE Fischer, PO Hasselgren Am J Physiol 272, R849–R856 (1997).
- VE Baracos, C DeVivo, DH Hoyle, AL Goldberg Am J Physiol 268, E996–E1006 (1995).
- 10.1172/JCI200420174 · DOI
- GJ Herbison, MM Jaweed, JF Ditunno Arch Phys Med Rehab 60, 401–404 (1979).
- IC Kettelhut, MT Pepato, RH Migliorini, R Medina, AL Goldberg Braz J Med Biol Res 27, 981–993 (1994).
- SS Wing, AL Goldberg Am J Physiol 264, E668–E676 (1993).
Cited by
Sorted by citations
Items 501–600 of 973
The Function of Metformin in Aging-Related Musculoskeletal Disorders
Song, Y., Wu, Z., & Zhao, P. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.865524 · Cited by 32
FOXO1 and GSK-3β Are Main Targets of Insulin-Mediated Myogenesis in C2C12 Muscle Cells
Litwiniuk, A., Pijet, B., Pijet-Kucicka, M., Gajewska, M., Pająk, B., & Orzechowski, A. (2016) · PLoS ONE · doi:10.1371/journal.pone.0146726 · Cited by 33
Controlled Heat Stress Promotes Myofibrillogenesis during Myogenesis
Guo, Q., Miller, D., An, H., Wang, H., Lopez, J., Lough, D., He, L., & Kumar, A. (2016) · PLoS ONE · doi:10.1371/journal.pone.0166294 · Cited by 32
Guo, Q., Luo, Q., & Song, G. (2024) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.13440 · Cited by 35
Guigni, B. A., Fix, D. K., Bivona, J. J., Palmer, B. M., Carson, J. A., & Toth, M. J. (2019) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00148.2019 · Cited by 32
Epigenetic drugs in the treatment of skeletal muscle atrophy
Guasconi, V., & Puri, P. (2008) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0b013e3282fa1810 · Cited by 32
Exercise capacity, physical activity, and morbidity
Brunjes, D. L., Kennel, P. J., & Schulze, P. C. (2017) · Heart Failure Reviews · doi:10.1007/s10741-016-9592-1 · Cited by 31
A Peculiar Formula of Essential Amino Acids Prevents Rosuvastatin Myopathy in Mice
D’Antona, G., Tedesco, L., Ruocco, C., Corsetti, G., Ragni, M., Fossati, A., Saba, E., Fenaroli, F., Montinaro, M., Carruba, M. O., et al. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6582 · Cited by 30
Muscle alterations in the development and progression of cancer-induced muscle atrophy: a review
Rosa‐Caldwell, M. E., Fix, D. K., Washington, T. A., & Greene, N. P. (2019) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00622.2019 · Cited by 30
Antioxidant Activity of Valeriana fauriei Protects against Dexamethasone‐Induced Muscle Atrophy
Kim, Y. I., Lee, H., Nirmala, F. S., Seo, H., Ha, T. Y., Jung, C. H., & Ahn, J. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/3645431 · Cited by 30
Lee, I., Hüttemann, M., Kruger, A., Bollig-Fischer, A. B., & Malek, M. H. (2015) · Frontiers in Pharmacology · doi:10.3389/fphar.2015.00043 · Cited by 29
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
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
Tyganov, S. A., Mochalova, E. P., Belova, S. P., Sharlo, K. A., Rozhkov, S. V., Vilchinskaya, N. A., Paramonova, I. I., Mirzoev, T. M., & Shenkman, B. S. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.01252 · Cited by 31
Yoo, A., Jang, Y. J., Ahn, J., Jung, C. H., Seo, H., & Ha, T. Y. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21082811 · Cited by 29
Ginseng and ginsenosides: Therapeutic potential for sarcopenia
Zha, W., Sun, Y., Gong, W., Li, L., Kim, W., & Li, H. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113876 · Cited by 31
Molecular mechanisms of post‐burn muscle wasting and the therapeutic potential of physical exercise
Dombrecht, D., Daele, U. V., Asbroeck, B. V., Schieffelers, D. R., Guns, P., Gebruers, N., Meirte, J., & van Breda, E. (2023) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.13188 · Cited by 28
Living long and ageing well: is epigenomics the missing link between nature and nurture?
The ACUME2 Project, Rea, I. M., Dellett, M., & Mills, K. (2015) · Biogerontology · doi:10.1007/s10522-015-9589-5 · Cited by 29
mTOR Signaling as a Target of Amino Acid Treatment of the Age-Related Sarcopenia
D’Antona, G., & Nisoli, E. (2010) · Interdisciplinary topics in gerontology and geriatrics · doi:10.1159/000319998 · Cited by 29
The Effects of Omega-3 Fatty Acid Supplementation on Dexamethasone-Induced Muscle Atrophy
Fappi, A., Godoy, T. S., Maximino, J. R., Rizzato, V. R., Neves, J. D. C., Chadi, G., & Zanoteli, E. (2014) · BioMed Research International · doi:10.1155/2014/961438 · Cited by 29
Progressive development of melanoma-induced cachexia differentially impacts organ systems in mice
Graça, F. A., Stephan, A., Wang, Y., Shirinifard, A., Jiao, J., Vogel, P., Labelle, M., & Demontis, F. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111934 · Cited by 27
Tack, W., Cock, A. D., Dirinck, E. L., Bastijns, S., Ariën, F., & Perkisas, S. (2023) · Diabetes Obesity and Metabolism · doi:10.1111/dom.15321 · Cited by 34
α‐Cedrene, a Newly Identified Ligand of MOR23, Increases Skeletal Muscle Mass and Strength
Tong, T., Kim, M., & Park, T. (2018) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201800173 · Cited by 28
Russo, C., Valle, M. S., Casabona, A., Spicuzza, L., Sambataro, G., & Malaguarnera, L. (2022) · Biomedicines · doi:10.3390/biomedicines10040898 · Cited by 32
High Intensity Interval Training: A Potential Method for Treating Sarcopenia
Liu, Q., Xie, W., Luo, Y., Li, Y., Huang, W., Wu, Y., & Li, Y. (2022) · Clinical Interventions in Aging · doi:10.2147/cia.s366245 · Cited by 34
Yang, X., Li, M., Ji, Y., Lin, Y., Xu, L., Gu, X., Sun, H., Wang, W., Shen, Y., Liu, H., et al. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.923190 · Cited by 28
Rinaldi, B., Donniacuo, M., Sodano, L., Gritti, G., Signoriello, S., Parretta, E., Berrino, L., Urbanek, K., Capuano, A., & Rossi, F. (2013) · PLoS ONE · doi:10.1371/journal.pone.0069954 · Cited by 28
Altering aspects of mitochondrial quality to improve musculoskeletal outcomes in disuse atrophy
Rosa‐Caldwell, M. E., Lim, S., Haynie, W. S., Jansen, L. T., Westervelt, L. C., Amos, M. G., Washington, T. A., & Greene, N. P. (2020) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00407.2020 · Cited by 29
Ruparelia, A. A., Salavaty, A., Barlow, C. K., Lu, Y., Sonntag, C., Hersey, L., Eramo, M. J., Krug, J., Reuter, H., Schittenhelm, R. B., et al. (2023) · Aging Cell · doi:10.1111/acel.13862 · Cited by 28
Forman, D. E., Daniels, K. M., Cahalin, L. P., Zavin, A., Allsup, K., Cao, P., Santhanam, M., Joseph, J., Arena, R. A., Lazzari, A. A., et al. (2014) · Journal of Cardiac Failure · doi:10.1016/j.cardfail.2014.03.007 · Cited by 27
Self-citationGraça, F. A., Gonçalves, D. A. P., Silveira, W. A., Lira, E. C., Chaves, V. E., Zanon, N. M., Garófalo, M. A. R., Kettelhut, Í. D. C., & Navegantes, L. C. C. (2013) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00267.2013 · Cited by 27
Summermatter, S., Troxler, H., Santos, G., & Handschin, C. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.04.012 · Cited by 27
Self-citationRegulation of autophagy by Forkhead box (FOX) O transcription factors
van der Vos, K. E., Gomez‐Puerto, M. C., & Coffer, P. J. (2011) · Advances in Biological Regulation · doi:10.1016/j.advenzreg.2011.10.002 · Cited by 29
The loss of muscle mass and sarcopenia: Non hormonal intervention
Sanchis‐Gomar, F., Gómez‐Cabrera, M. C., & Viña, J. (2011) · Experimental Gerontology · doi:10.1016/j.exger.2011.08.012 · Cited by 27
Gopinath, S. D. (2017) · Skeletal Muscle · doi:10.1186/s13395-017-0121-2 · Cited by 27
Potential role of omega-3 fatty acids on the myogenic program of satellite cells
Bhullar, A. S., Putman, C. T., & Mazurak, V. C. (2016) · Nutrition and Metabolic Insights · doi:10.4137/nmi.s27481 · Cited by 26
Veeranki, S., & Tyagi, S. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms16011252 · Cited by 26
Okamura, T., Hashimoto, Y., Osaka, T., Fukuda, T., Hamaguchi, M., & Fukui, M. (2019) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.18-114 · Cited by 28
Cellular mechanism of immobilization-induced muscle atrophy: A mini review
Ji, L. L., & Yeo, D. (2019) · Sports Medicine and Health Science · doi:10.1016/j.smhs.2019.08.004 · Cited by 26
Singh, A. P., Yadav, A., Phogat, J., & Dabur, R. (2021) · Current Molecular Pharmacology · doi:10.2174/1874467214666210806163851 · Cited by 26
Arribas, L., Sabaté-Llobera, A., Domingo, M. C., Taberna, M., Sospedra, M., Martin, L., González-Tampán, A. R., Pallarés, N., Mesı́a, R., & Baracos, V. E. (2022) · Clinical Nutrition · doi:10.1016/j.clnu.2022.03.016 · Cited by 26
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 28
The beneficial role of exercise in preventing doxorubicin-induced cardiotoxicity
Gaytan, S. L., Lawan, A., Chang, J., Nurunnabi, M., Bajpeyi, S., Boyle, J. B., Han, S. M., & Min, K. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1133423 · Cited by 30
PGC‐1α mediates a rapid, exercise‐induced downregulation of glycogenolysis in rat skeletal muscle
Kim, S. H., Koh, J., Higashida, K., Jung, S. R., Holloszy, J. O., & Han, D. (2014) · The Journal of Physiology · doi:10.1113/jphysiol.2014.283820 · Cited by 26
Tzika (2009) · International Journal of Molecular Medicine · doi:10.3892/ijmm_00000244 · Cited by 28
Franz, A., Queitsch, F. P., Behringer, M., Mayer, C. U., Krauspe, R., & Zilkens, C. (2017) · Medical Hypotheses · doi:10.1016/j.mehy.2017.10.029 · Cited by 29
Zak, R., Hassenstab, B., Zuehlke, L. K., Heesch, M., Shute, R. J., Laursen, T. L., Salle, D. T. L., & Slivka, D. R. (2017) · European Journal of Applied Physiology · doi:10.1007/s00421-017-3749-z · Cited by 26
Guo, J., Shang, Y., Fratiglioni, L., Johnell, K., Welmer, A., Marseglia, A., & Xu, W. (2021) · Age and Ageing · doi:10.1093/ageing/afab045 · Cited by 26
Impaired Exercise Capacity and Skeletal Muscle Function in a Mouse Model of Pulmonary Inflammation
Tang, K., Murano, G., Wagner, H., Nogueira, L., Wagner, P. D., Tang, A., Dalton, N. D., Gu, Y., Peterson, K. L., & Breen, E. C. (2013) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00607.2012 · Cited by 30
GADD45A is a mediator of mitochondrial loss, atrophy, and weakness in skeletal muscle
Marcotte, G. R., Miller, M. J., Kunz, H., Ryan, Z. C., Strub, M. D., Vanderboom, P. M., Heppelmann, C. J. H., Chau, S., Ruff, Z. D. V., Kilroe, S. P., et al. (2023) · JCI Insight · doi:10.1172/jci.insight.171772 · Cited by 26
Resistance exercise and skeletal muscle: protein synthesis, degradation, and controversies
Ji, F., Lee, H. S., & Kim, J.-H. (2025) · European Journal of Applied Physiology · doi:10.1007/s00421-025-05832-z · Cited by 26
Sato, T., Ito, Y., & Nagasawa, T. (2016) · Biogerontology · doi:10.1007/s10522-016-9663-7 · Cited by 25
Bahreinipour, M.-A., Joukar, S., Hovanloo, F., Najafipour, H., Naderi-Boldaji, V., Raji-Amirhasani, A., & Esmaeili‐Mahani, S. (2018) · Life Sciences · doi:10.1016/j.lfs.2018.03.051 · Cited by 25
Omi, N., Shiba, H., Nishimura, E., Tsukamoto, S., Maruki‐Uchida, H., Oda, M., & Morita, M. (2019) · Journal of the International Society of Sports Nutrition · doi:10.1186/s12970-019-0303-x · Cited by 25
The Novel Role of PGC1α in Bone Metabolism
Buccoliero, C., Dicarlo, M., Pignataro, P., Gaccione, F., Colucci, S. C., Colaianni, G., & Grano, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094670 · Cited by 25
Blanqué, R., Lepescheux, L., Auberval, M., Minet, D., Merciris, D., Cottereaux, C., Clément-Lacroix, P., Delerive, P., & Namour, F. (2014) · BMC Musculoskeletal Disorders · doi:10.1186/1471-2474-15-291 · Cited by 25
Chen, W., Lv, Y. T., Zhang, H. X., Ruan, D., Wang, S., & Lin, Y. C. (2013) · Poultry Science · doi:10.3382/ps.2013-03099 · Cited by 27
Khamoui, A. V., & KIM, J. S. (2011) · European Journal of Cancer Care · doi:10.1111/j.1365-2354.2011.01287.x · Cited by 24
Mônico‐Neto, M., Giampá, S. Q. D. C., Lee, K. S., de Melo, C. M., Souza, H. D. S., Dattilo, M., Minali, P. A., Prado, P. H. S., Tufik, S., de Mello, M. T., et al. (2015) · International Journal of Endocrinology · doi:10.1155/2015/908159 · Cited by 25
Molecular Basis for Statin-Induced Muscle Toxicity: Implications and Possibilities
Buettner, C., & Lecker, S. H. (2008) · Pharmacogenomics · doi:10.2217/14622416.9.8.1133 · Cited by 25
Self-citationRossetti, M. L., Steiner, J. L., & Gordon, B. S. (2018) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2018.01.017 · Cited by 24
Kang, M., Kang, M., Yoo, J., Lee, J., Lee, S., Yun, B., Song, M., Kim, J., Kim, H., Yang, J., et al. (2024) · Food & Function · doi:10.1039/d3fo05420a · Cited by 26
Bacurau, A. V. N., Cunha, T. F., de Souza, R. W. A., Voltarelli, V. A., Gabriel‐Costa, D., & Brum, P. C. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/4374671 · Cited by 27
Mitochondrial transplantation as a possible therapeutic option for sarcopenia
Türkel, İ., Özerkliğ, B., Yılmaz, M., Ülger, Ö., Kubat, G. B., & Tuncer, M. (2023) · Journal of Molecular Medicine · doi:10.1007/s00109-023-02326-3 · Cited by 25
Sun, R., Zhang, S., Lü, X. Q., Hu, W., Lou, N., Zhao, Y. Q., Zhou, J., Zhang, X., & Yang, H. (2016) · Oncology Reports · doi:10.3892/or.2016.5165 · Cited by 24
Ohira, T., Higashibata, A., Seki, M., Kurata, Y., Kimura, Y., Hirano, H., Kusakari, Y., Minamisawa, S., Kudo, T., Takahashi, S., et al. (2017) · Physiological Reports · doi:10.14814/phy2.13350 · Cited by 25
Epigenetic mechanisms in amyotrophic lateral sclerosis: A short review
Dolinar, A., Ravnik‐Glavač, M., & Glavač, D. (2018) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2018.03.005 · Cited by 25
Tong, T., Kim, M., & Park, T. (2019) · Food & Function · doi:10.1039/c8fo01992d · Cited by 23
SIRT1: An Intermediator of Key Pathways Regulating Pulmonary Diseases
Jiang, Y.-Z., Huang, X.-R., Chang, J., Zhou, Y., & Huang, X.-T. (2024) · Laboratory Investigation · doi:10.1016/j.labinv.2024.102044 · Cited by 24
Rahman, F. A., Graham, M. Q., Adam, A., Juracic, E. S., Tupling, A. R., & Quadrilatero, J. (2025) · Journal of Biomedical Science · doi:10.1186/s12929-025-01118-w · Cited by 26
Bae, J., Jo, A., Cho, S. C., Lee, Y., Kam, T., You, C.-L., Jeong, H., Kim, H., Jeong, M., Jeong, Y., et al. (2023) · Science Translational Medicine · doi:10.1126/scitranslmed.abh3489 · Cited by 23
Liu, X., Gao, H., Huang, X., Chen, Y., Feng, X., He, Y., Li, Z.-M., & Liu, P.-Q. (2015) · Translational research · doi:10.1016/j.trsl.2015.06.003 · Cited by 23
Ruven, C., Badea, S. R., Wong, W., & Wu, W. (2018) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nly009 · Cited by 23
Sun, W., Wang, X.-C., Novaković, A., Wang, J., He, G., & Yang, Q. (2018) · Vascular Pharmacology · doi:10.1016/j.vph.2018.10.009 · Cited by 23
Exercise Training for the Elderly: Inflammaging and the Central Role for HSP70
Muller, C. H. D. L., de Matos, J. R., Grigolo, G. B., Schroeder, H. T., Rodrigues-Krause, J. D. C., & Krause, M. D. S. (2019) · Journal of Science in Sport and Exercise · doi:10.1007/s42978-019-0015-6 · Cited by 25
Sun, X., Thorne, R. F., Zhang, X. D., He, M., Li, J., Feng, S., Liu, X., & Wu, M. (2020) · EMBO Reports · doi:10.15252/embr.201948796 · Cited by 22
The impact of mRNA turnover and translation on age-related muscle loss
Ma, J. F., Hall, D. T., & Gallouzi, I. (2012) · Ageing Research Reviews · doi:10.1016/j.arr.2012.05.004 · Cited by 23
Maruta, H., Abe, R., & Yamashita, H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094691 · Cited by 22
YAP/TAZ as Molecular Targets in Skeletal Muscle Atrophy and Osteoporosis
Kwon, Y. (2024) · Aging and Disease · doi:10.14336/ad.2024.0306 · Cited by 23
Charrier, D., Cerullo, G., Carpenito, R., Vindigni, V., Bassetto, F., Simoni, L., Moro, T., & Paoli, A. (2024) · Antioxidants · doi:10.3390/antiox13091027 · Cited by 23
Kamal, K. Y., & Trombetta-Lima, M. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26062802 · Cited by 25
Deval, C., Calonne, J., Coudy‐Gandilhon, C., Vazeille, E., Béchet, D., Polge, C., Taillandier, D., Attaix, D., & Combaret, L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21103691 · Cited by 22
Multimodal Approach to Malnutrition in Malnourished Maintenance Hemodialysis Patients
Cano, N., Heng, A.-É., & Pison, C. M. (2011) · Journal of Renal Nutrition · doi:10.1053/j.jrn.2010.10.016 · Cited by 22
Urocortin 3 activates AMPK and AKT pathways and enhances glucose disposal in rat skeletal muscle
Roustit, M. M., Vaughan, J. M., Jamieson, P. M., & Cleasby, M. E. (2014) · Journal of Endocrinology · doi:10.1530/joe-14-0181 · Cited by 24
Tessier, S. N., & Storey, K. B. (2016) · BioMolecular Concepts · doi:10.1515/bmc-2015-0031 · Cited by 23
Karlsson, L., Alvarado, M. N. G., Motalleb, R., Blomgren, K., Börjesson, M., & Kuhn, H. G. (2019) · Scientific Reports · doi:10.1038/s41598-019-48795-w · Cited by 24
A Jack of All Trades: Impact of Glucocorticoids on Cellular Cross-Talk in Osteoimmunology
Ahmad, M., Hachemi, Y., Paxian, K., Mengele, F., Koenen, M., & Tuckermann, J. P. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02460 · Cited by 22
Cahill, T., Cope, H., Bass, J. J., Overbey, E. G., Gilbert, R., da Silveira, W. A., Paul, A. M., Mishra, T., Herranz, R., Reinsch, S. S., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179470 · Cited by 22
Pietrangelo, T., Mancinelli, R., Toniolo, L., Montanari, G., Vecchiet, J., Fanò, G., & Fulle, S. (2009) · International Journal of Immunopathology and Pharmacology · doi:10.1177/039463200902200326 · Cited by 22
Lee, D., & Goldberg, A. L. (2011) · Circulation Research · doi:10.1161/circresaha.111.248872 · Cited by 22
Self-citationGerlinger‐Romero, F., Yonamine, C. Y., Junior, D. C. P., Esteves, J. V. D. C., & Machado, U. F. (2016) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-016-2910-z · Cited by 22
Ucci, S., Renzini, A., Russi, V., Mangialardo, C., Cammarata, I., Cavioli, G., Santaguida, M. G., Virili, C., Centanni, M., Adamo, S., et al. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20225754 · Cited by 21
Dojuksan ameliorates tubulointerstitial fibrosis through irisin-mediated muscle-kidney crosstalk
Jiang, S., Oh, D., Dorotea, D., Son, E., Kim, D.-S., & Ha, H. (2020) · Phytomedicine · doi:10.1016/j.phymed.2020.153393 · Cited by 21
Lin, R., Xu, B., Ye, Z., Gao, Y., Fang, H., Song, J., Liang, D., Liu, L., Hu, Z., Zhang, M., et al. (2023) · Journal of Orthopaedic Translation · doi:10.1016/j.jot.2023.05.002 · Cited by 21
Mechanisms and effects of metformin on skeletal muscle disorders
Shang, R., & Miao, J. (2023) · Frontiers in Neurology · doi:10.3389/fneur.2023.1275266 · Cited by 23
Petasin Activates AMP-Activated Protein Kinase and Modulates Glucose Metabolism
Adachi, Y., Kanbayashi, Y., Harata, I., Ubagai, R., Takimoto, T., Suzuki, K., Miwa, T., & Noguchi, Y. (2014) · Journal of Natural Products · doi:10.1021/np400867m · Cited by 21
Integrative Data Mining Highlights Candidate Genes for Monogenic Myopathies
Neto, O. L. A., Tassy, O., Biancalana, V., Zanoteli, E., Pourquié, O., & Laporte, J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0110888 · Cited by 21
Functional overload in ground squirrel plantaris muscle fails to induce myosin isoform shifts
Choi, H. J., Selpides, P., Nowell, M. M., & Rourke, B. C. (2009) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00236.2009 · Cited by 21
Park, W., Kim, J., Kim, H. J., Choi, J., Park, J.-W., Cho, H.-W., Kim, B.-W., Park, M. H., Shin, T.-S., Cho, S., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0091418 · Cited by 21
Wang, H., Wilson, G. J., Zhou, D., Lezmi, S., Chen, X., Layman, D. K., & Pan, Y. (2015) · British Journal Of Nutrition · doi:10.1017/s0007114515002172 · Cited by 21
Metadata
- Authors
- Sandri, M., Lin, J., Handschin, C., Yang, W., Arany, Z. P., Lecker, S. H., Goldberg, A. L., & Spiegelman, B. M.
- Affiliations
- Harvard University (US)
- Beth Israel Deaconess Medical Center (US)
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2006-10-31
- Volume
- 103
- Issue
- 44
- Pages
- 16260-16265
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC1637570
- OpenAlex
- W1977548231
- Cited by
- 974
- References
- 53
- Citations by year
- 2026: 20 · 2025: 38 · 2024: 44 · 2023: 51 · 2022: 56 · 2021: 42 · 2020: 66 · 2019: 64 · 2018: 54 · 2017: 40 · 2016: 51 · 2015: 57 · 2014: 65 · 2013: 68 · 2012: 52
- FWCI
- 13.20
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- edoc (University of Basel) (submittedVersion)
- Digital Access to Scholarship at Harvard (DASH) (Harvard University) (submittedVersion, cc-by)
- edoc (University of Basel)
- Funders
- Muscular Dystrophy Association
- Compagnia di San Paolo
- National Institutes of Health (DK6230701)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01-DK-6230701, R01DK062307, R56DK054477, P30DK040561)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- PGC-1α, skeletal muscle atrophy, FOXO3, atrogin-1, MuRF1, ubiquitin ligase, denervation, cancer cachexia, diabetes mellitus, renal failure, fasting, physical activity, muscle fiber diameter, energy metabolism, transcriptional coactivator, muscle fiber type shift
- MeSH terms
- Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha, Animals, Gene Expression Regulation, Mice, Transgenic, Muscular Atrophy, Nerve Tissue Proteins, Transcription Factors, Transcription, Genetic, Biomarkers, Trans-Activators, Muscle, Skeletal, Mice, Forkhead Transcription Factors
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