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 801–900 of 973
Suh, J., Eom, J., Baik, J., Shim, W., Tischfield, M. A., Woo, H. A., & Lee, Y. (2025) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.70098 · Cited by 3
Role of mitochondrial dysfunction in muscle wasting in cancer cachexia: a narrative review
Su, X., Wang, S., Qu, Y., Wang, Y., Tian, Z., Chao, X., Li, Z., & Ma, D. (2026) · Journal of Translational Medicine · doi:10.1186/s12967-026-07906-8 · Cited by 7
Schmid, S., Kupr, B., Pérez‐Schindler, J., Mansingh, S., Beer, M., Mittal, N., Ehrenfeuchter, N., & Handschin, C. (2022) · Molecular Metabolism · doi:10.1016/j.molmet.2022.101643 · Cited by 3
Self-citationApocynin Mitigates Diabetic Muscle Atrophy by Lowering Muscle Triglycerides and Oxidative Stress
Sánchez‐Duarte, S., Sánchez‐Duarte, E., Sánchez‐Briones, L. A., Meléndez‐Herrera, E., Herrera‐Vargas, M. A., Márquez‐Gamiño, S., Vera‐Delgado, K. S., & Montoya-Pérez, R. D. C. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26125636 · Cited by 4
Kim, A., Tran, M. N., Lee, A. Y., Yeo, H., Baek, S., Kim, N. S., Cha, S., & Park, S. (2025) · Antioxidants · doi:10.3390/antiox14070795 · Cited by 3
Scheffler, T. L., & Gerrard, D. E. (2016) · Journal of Animal Science · doi:10.2527/jas.2015-0055 · Cited by 3
The Role and Regulation of PGC-1α and PGC-1β in Skeletal Muscle Adaptation
Lamon, S., & Russell, A. P. (2017) · Springer eBooks · doi:10.1007/978-981-10-3292-9_8 · Cited by 3
Regular exercise attenuates alcoholic myopathy in zebrafish by modulating mitochondrial homeostasis
Wen, W., Guo, C., Chen, Z., Yang, D. K., Zhu, D., Jing, Q., Zheng, L., Sun, C., & Tang, C. (2023) · PLoS ONE · doi:10.1371/journal.pone.0294700 · Cited by 3
Lee, Y.-J., Jang, Y.-N., Han, Y.-M., Kim, H., Seo, H. S., Kim, H. J., Jung, T. W., Jeong, J. H., El‐Aty, A. M. A., & Jung, K. O. (2024) · Journal of Medicinal Food · doi:10.1089/jmf.2024.k.0027 · Cited by 3
Coelho‐Júnior, H. J., Marzetti, E., Sexton, C. L., Wu, K., Mankowski, R. T., Anton, S. D., Leeuwenburgh, C., & Picca, A. (2024) · The journal of nutrition health & aging · doi:10.1016/j.jnha.2024.100408 · Cited by 4
Wang, C.-L., Kung, H., Wu, C., & Huang, C. (2018) · Food & Function · doi:10.1039/c8fo01777h · Cited by 3
Laha, A., Singh, M., George, A. K., Homme, R. P., & Tyagi, S. C. (2019) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/cjpp-2019-0227 · Cited by 3
Effects of Moderate Exercise Training on Cancer-Induced Muscle Wasting
Figueira, A. C., Pereira, A., Leitão, L., Ferreira, R. M., Oliveira, P. A., & Duarte, J. A. (2023) · Healthcare · doi:10.3390/healthcare11192652 · Cited by 3
Anabolic and Catabolic Signaling Pathways that Regulate Skeletal Muscle Mass
McCarthy, J. J. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-396454-0.00024-2 · Cited by 3
New Strategies to Fight against Sarcopenia at Old Age
Meynial‐Denis, D., Guérin, O., Schneider, S. M., Volkert, D., & Sieber, C. C. (2012) · Journal of Aging Research · doi:10.1155/2012/676042 · Cited by 5
PGC-1α régule la jonction neuromusculaire et améliore la dystrophie musculaire de Duchenne
Arnold, A. (2007) · médecine/sciences · doi:10.1051/medsci/200723111034 · Cited by 3
Gordon, B. S., Rossetti, M. L., & Casero, R. A. (2020) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/apnm-2020-0404 · Cited by 3
Vitamin D supplementation modulates autophagy in the pristane-induced lupus model
dos Santos, M., Silva, J. M. D. S., Bartikoski, B. J., Freitas, E. C., Busatto, A., Santo, R. C. D. E., Monticielo, O. A., & Xavier, R. M. (2022) · Revista Brasileira de Reumatologia · doi:10.1186/s42358-022-00261-4 · Cited by 3
Reduction of circulating sphingosine‐1‐phosphate worsens mdx soleus muscle dystrophic phenotype
Germinario, E., Bondı̀, M., Blaauw, B., Betto, R., & Danieli‐Betto, D. (2020) · Experimental Physiology · doi:10.1113/ep088603 · Cited by 3
Davies, K. E., & Khurana, T. S. (2007) · Nature Medicine · doi:10.1038/nm0507-538 · Cited by 3
Yeo, D. (2025) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-88361-3_8 · Cited by 4
Fan, K., Li, X., & Wang, Z. (2025) · The FASEB Journal · doi:10.1096/fj.202501901r · Cited by 2
C9ORF72 Is Pivotal to Maintain a Proper Protein Homeostasis in Mouse Skeletal Muscle
Sironi, F. M., Parlanti, P., Margotta, C., Cassarà, J., Bonetto, V., Bendotti, C., Tortarolo, M., & Cappello, V. (2025) · Cells · doi:10.3390/cells14221765 · Cited by 2
Pollak, N., Janáček, J., Saudek, F., Cvetko, E., Radochová, B., Alibegović, A., Ugwoke, C. K., Basello, D. A., Šink, Ž., Pušnik, L., et al. (2026) · Histochemistry and Cell Biology · doi:10.1007/s00418-026-02477-7 · Cited by 2
Évaluation de la composition corporelle en réanimation : avantages et limites
Thibault, R., & Pichard, C. (2011) · Réanimation · doi:10.1007/s13546-011-0288-1 · Cited by 2
Bamba, J., Parenté, A., Duprat, N., Forestier, L., & Blanquet, V. (2018) · Gene Reports · doi:10.1016/j.genrep.2018.10.012 · Cited by 2
Qin, H., Rui, J., & Lao, J. (2023) · Muscle & Nerve · doi:10.1002/mus.27972 · Cited by 2
Molecular changes in skeletal muscle in chronic kidney disease: A systematic review
Wong, L., Kenny, R., Howard, J., & McMahon, L. P. (2023) · JCSM Rapid Communications · doi:10.1002/rco2.82 · Cited by 2
Doxorubicin-dependent skeletal muscle atrophy: exercise and mitochondrial dysfunction
Kubat, G. B., & Tuncer, M. (2024) · Turkish Journal of Sports Medicine · doi:10.47447/tjsm.0799 · Cited by 2
Nishida, R., Fukui, T., Niikura, T., Kumabe, Y., Yoshikawa, R., Takase, K., Yamamoto, Y., Kuroda, R., & Oe, K. (2024) · Bone · doi:10.1016/j.bone.2024.117262 · Cited by 3
Paul, S., Donath, L., Hoppstädter, J., & Hecksteden, A. (2024) · European Journal of Applied Physiology · doi:10.1007/s00421-024-05644-7 · Cited by 2
Tunçyürekli, M., Tülüce, Y., & Lermioǧlu, F. (2024) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-024-03663-x · Cited by 2
Metabolic dysregulation contributes to the development of dysferlinopathy
Furrer, R., Dilbaz, S., Steurer, S. A., Santos, G., Karrer‐Cardel, B., Ritz, D., Sinnreich, M., & Handschin, C. (2025) · Life Science Alliance · doi:10.26508/lsa.202402991 · Cited by 2
Self-citationKo, H., Le, T. T., Nguyen, N. B., Kang, S. W., Hyun, K., Yang, N., Jung, S. H., & Kim, M. (2025) · Phytotherapy Research · doi:10.1002/ptr.8478 · Cited by 2
Mitochondrial quality control in exercise-mitigated muscular atrophy
Fan, J., Wen, X., Duan, X., Zhu, X., Bai, J., & Zhang, T. (2025) · Mitochondrion · doi:10.1016/j.mito.2025.102074 · Cited by 2
Age-Related Changes in the Molecular Regulation of Skeletal Muscle Mass
Russell, A. P., & Léger, B. (2010) · Springer eBooks · doi:10.1007/978-90-481-9713-2_10 · Cited by 2
Nerve Root Reimplantation in Brachial Plexus Injuries
Vanaclocha, V., Sáiz‐Sapena, N., Ortiz-Criado, J. M., & Vanaclocha, L. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.82431 · Cited by 2
Diagnosis of Osteosarcopenia – Biochemistry and Pathology
Obermayer-Pietsch, B. M., & Herrmann, M. (2019) · Springer eBooks · doi:10.1007/978-3-030-25890-0_13 · Cited by 2
Novel Intriguing Strategies Attenuating to Sarcopenia
Sakuma, K., & Yamaguchi, A. (2016) · Apple Academic Press eBooks · doi:10.1201/b19985-13 · Cited by 2
Myosin: Cellular Molecular Motor
Jena, B. P. (2020) · Springer eBooks · doi:10.1007/978-3-030-44496-9_7 · Cited by 2
Signaling Pathways That Promote Muscle Catabolism in Cachexia
Gilda, J. E., & Cohen, S. (2022) · Springer eBooks · doi:10.1007/978-3-031-09518-4_5 · Cited by 2
Genes in Skeletal Muscle Remodeling and Impact of Feeding
Chen, Y.-W., Barberio, M. D., & Hubal, M. J. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802167-5.00023-2 · Cited by 1
Kubat, G. B., Türkel, İ., & Akat, F. (2025) · Turkish Journal of Sports Medicine · doi:10.47447/tjsm.0872 · Cited by 1
Redox signalling and microRNA feedback in exercise-mediated skeletal muscle remodelling
Qin, X., Goljanek‐Whysall, K., & McDonagh, B. (2025) · Advances in Redox Research · doi:10.1016/j.arres.2025.100133 · Cited by 1
Ding, K., Jiang, W., Yao, H., & Gao, Y. (2025) · Scandinavian Journal of Rheumatology · doi:10.1080/03009742.2025.2549613 · Cited by 1
Leptin’s potential mechanisms in ICU-acquired weakness
Li, M., Yang, L., Li, T., Miao, Y., Yang, J., Chen, S., Ma, X., & Xie, P. (2025) · Lipids in Health and Disease · doi:10.1186/s12944-025-02748-7 · Cited by 1
Vieira, P. D. C., Epifânio, C., Horita, S. I. M., Rodrigues, K. L., Pereira, E. N. G. D. S., Daliry, A., de Castro, L. L., da Rosa, B. G., Kahn, S., Cascabulho, C. M., et al. (2026) · Communications Biology · doi:10.1038/s42003-026-09810-9 · Cited by 1
RAGE Re‐Expressed at Myofibre Level Drives Muscle Wasting in Cancer Conditions
Chiappalupi, S., Gentili, G., Salvadori, L., Paiella, M., Manfredi, M., Borrini, V. F., Mangar, K., Schmidt, A. M., Muscaritoli, M., Riuzzi, F., et al. (2026) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.70302 · Cited by 1
Brain senescence drives sarcopenia-like transcriptomic remodeling in skeletal muscle
Ekambaram, S., Patai, R., Gulej, R., Kiss, T., Chandragiri, S. S., Nagy, D., Kordestan, K. V., Lakat, T., Tarantini, S., Mukli, P., et al. (2026) · GeroScience · doi:10.1007/s11357-026-02205-y · Cited by 1
Gao, X., Feng, X., Feng, G., Zhong, J., Liu, Y., Pan, S., Wang, Z., Miao, S., Lu, R., (630771), K. S., et al. (2026) · Phytomedicine · doi:10.1016/j.phymed.2026.158409 · Cited by 1
Rééducation motrice dans le cadre d’un séjour en réanimation
Норренберг, М., & Vincent, J. (2011) · Réanimation · doi:10.1007/s13546-011-0320-5 · Cited by 2
Activité physique, nutrition, et insuffisance cardiaque chronique
Thibault, R., Meyer, P., & Cano, N. (2014) · Nutrition Clinique et Métabolisme · doi:10.1016/j.nupar.2014.10.005 · Cited by 1
Molecular Determinants of Skeletal Muscle Hypertrophy in Animals
Yamaguchi, K. S. A. (2012) · Journal of Sports Medicine & Doping Studies · doi:10.4172/2161-0673.s1-002 · Cited by 1
Exercise dependent skeletal muscle plasticity and signaling in cancer cachexia
Khamoui, A. V. (2014) · Cited by 1
Jongen, A. C. H. M., van Woerden, V., van Vugt, J. L. A., de Hoogt, P. A., de Wijkerslooth, E. M. L., Tegels, J. J. W., Bouvy, N. D., & Stoot, J. H. M. B. (2016) · InTech eBooks · doi:10.5772/64775 · Cited by 2
Linking mitochondrial dysfunction to sarcopenia
Alway, S. E. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822146-4.00004-1 · Cited by 1
Mitochondrial biogenesis for the treatment of spinal cord injury
Simmons, E. C., Scholpa, N. E., Crossman, J. D., & Schnellmann, R. G. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-822498-4.00028-2 · Cited by 1
Ji, M., Cho, C., & Lee, S. (2022) · Exercise Science · doi:10.15857/ksep.2022.00318 · Cited by 1
Qi, Z., Wang, S., Xuan, A., Gu, X., Deng, J., Huang, C., Zhang, L., & Yin, X. (2022) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2022.10.005 · Cited by 1
Ryoke, K., Ishizuka, K., Yasui, Y., Kondo, K., Suzuki‐Kemuriyama, N., Maekawa, T., & Miyajima, K. (2024) · Fundamental Toxicological Sciences · doi:10.2131/fts.11.159 · Cited by 1
Pierre-Jerome, C. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-13328-2.00008-8 · Cited by 1
Takemura, A., Egawa, T., Takagi, R., Iyama, R., Haiyu, Z., Suzuki, S., Fujino, R., Fukunaga, T., Hayashi, T., & Fujita, S. (2025) · Physiological Reports · doi:10.14814/phy2.70350 · Cited by 1
Chen, Y., Liu, Z., Chen, L., Yang, D., Xiao, M., Li, Z., & Xie, Z. (2025) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2025.5569 · Cited by 1
Duan, Y., Sun, L., Liu, J., Fu, W., Wang, S., Ni, Y., & Zhao, R. (2018) · Animal Production Science · doi:10.1071/an16401 · Cited by 1
Kvedaras, M., Minderis, P., & Ratkevičius, A. (2020) · Baltic Journal of Sport and Health Sciences · doi:10.33607/bjshs.v1i116.900 · Cited by 1
Low-Dose Metformin as a Monotherapy Does Not Reduce Non-Small-Cell Lung Cancer Tumor Burden in Mice
Stott, N. L., Dréau, D., Marriott, I., Bennett, J. M., Turner, M. J., Arthur, S. T., & Marino, J. S. (2021) · Biomedicines · doi:10.3390/biomedicines9111685 · Cited by 1
Miedany, Y. M. E. (2022) · Springer eBooks · doi:10.1007/978-3-030-87950-1_3 · Cited by 1
Therapy-Induced Toxicities Associated with the Onset of Cachexia
Huot, J. R., Pin, F., & Bonetto, A. (2022) · Springer eBooks · doi:10.1007/978-3-031-09518-4_8 · Cited by 1
Aging of the Human Neuromuscular System: Pathological Aspects
Engel, W. K., & Askanas, V. (2011) · Wiley eBooks · doi:10.1002/9781444398311.ch1 · Cited by 1
Aljawadi, A. (2013) · ThinkTech (Texas Tech University) · Cited by 1
PGC-1a in muscle links metabolism to inflammation
Handschin, C. (2009) · edoc (University of Basel) · doi:10.5451/unibas-ep33741 · Cited by 1
Self-citationA novel and complex mechanism regulating PGC ‐1α4 expression
Gordon, B. S. (2016) · Acta Physiologica · doi:10.1111/apha.12846 · Cited by 1
Curtis, K. (2016) · Spiral (Imperial College London) · doi:10.25560/44728 · Cited by 1
The Role of Mitochondria in Age‐Related Sarcopenia
Ferrucci, L., Zampino, M., Coen, P. M., & Goodpaster, B. H. (2021) · Wiley eBooks · doi:10.1002/9781119597896.ch3 · Cited by 2
Kubo, A., Hitachi, K., Shirakawa, R., & Ogura, T. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.09.552644 · Cited by 2
CHARACTERIZING THE ACUTE MITOCHONDRIAL RESPONSE TO RESISTANCE EXERCISE IN AGING
Ogborn, D. I. (2013) · MacSphere (McMaster University) · doi:10.71548/15322 · Cited by 1
Chelh, I., Meunier, B., Picard, B. B., Hocquette, J.-F. J.-F., & Cassar‐Malek, I. (2008) · HAL · Cited by 1
Mechanisms of hypertrophy after 12 weeks of aerobic training in elderly women
Konopka, A. R. (2009) · Cardinal Scholar (Ball State University)
Loss of Mitochondria during Skeletal Muscle Atrophy
Lokireddy, S. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-405528-5.00016-x
Gene x lifestyle interactions in type 2 diabetes mellitus and related traits
Brito, E. C. (2010) · DiVA at Umeå University (Umeå University)
Combinatorial Gene Therapy Strategies for Treating Muscular Dystrophies
Winbanks, C. E., & Gregorevic, P. (2009) · Springer eBooks · doi:10.1007/978-1-4419-1207-7_8
DiMauro, S., Schon, E. A., & Hirano, M. (2011) · doi:10.1002/9781444398311.ch4
Yang, L. (2009) · Infoscience (Ecole Polytechnique Fédérale de Lausanne) · doi:10.5075/epfl-thesis-4413
Marmolino, D., & Pandolfo, M. (2011) · Dépôt institutionnel de l'Université libre de Bruxelles (Université Libre de Bruxelles)
Mangum, J. E. (2013) · Scholar Commons (University of South Carolina)
Molecular mechanisms of statin-induced myotoxicity
Mullen, P. (2011) · edoc (University of Basel) · doi:10.5451/unibas-005591169
function in a mouse model of pulmonary inflammation Impaired exercise capacity and skeletal muscle
Tang, A., Dalton, N. D., Gu, Y., Peterson, K. L., Tang, E., Murano, G., Nogueira, L., Zuo, L., Hallman, A. H., Roberts, W. J., et al. (2015)
Permanent LMN denervated human muscle: management and monitoring of h-bFES
Kern, H., Carraro, U., & Wien, W. (2010)
cytokine signaling in determining muscle mass Protein kinase B/Akt: a nexus of growth factor and
Frost, R. A., Lang, C. H., Zanon, N. M., Antonieta, M., Garofalo, R. S., Kettelhut, Í. D. C., Graça, A. T., Gonçalves, D. A. P., Silveira, W. A., Lira, E. C., et al. (2015)
Hollinger, K. (2014) · Iowa State University Digital Repository (Iowa State University) · doi:10.31274/etd-180810-3711
Mrad, R. L. (2016) · uO Research (University of Ottawa) · doi:10.20381/ruor-5228
Tryon, L. D., Vainshtein, A., Memme, J. M., Crilly, M. J., & Hood, D. A. (2016) · Integrative Medicine Research · doi:10.1016/j.imr.2014.08.006
and is directly regulated by Hsp70 FOXO signaling is required for disuse muscle atrophy
Senf, S. M., DODD, S. L., Judge, A. R., Reich, K. A., Chen, Y., Thompson, P. D., Hoffman, E. P., Argadine, H. M., Mantilla, C. B., Zhan, W., et al. (2011)
Is metabolic flexibility determined by early life nutrition
Norman, A. M. (2013) · ResearchSpace (University of Auckland)
Davis, P. R. (2015) · The Scholarship East Carolina University's Institutional Repository (East Carolina University)
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