Long-Term PGC1β Overexpression Leads to Apoptosis, Autophagy and Muscle Wasting
Open accessAbstract
Skeletal muscle wasting is prevalent in many chronic diseases, necessitating inquiries into molecular regulation of muscle mass. Nuclear receptor co-activator peroxisome proliferator-activated receptor co-activator 1 alpha (PGC1α) and its splice variant PGC1α4 increase skeletal muscle mass. However, the effect of the other PGC1 sub-type, PGC1β, on muscle size is unclear. In transgenic mice selectively over-expressing PGC1β in the skeletal muscle, we have found that PGC1β progressively decreases skeletal muscle mass predominantly associated with loss of type 2b fast-twitch myofibers. Paradoxically, PGC1β represses the ubiquitin-proteolysis degradation pathway genes resulting in ubiquitinated protein accumulation in muscle. However, PGC1β overexpression triggers up-regulation of apoptosis and autophagy genes, resulting in robust activation of these cell degenerative processes, and a concomitant increase in muscle protein oxidation. Concurrently, PGC1β up-regulates apoptosis and/or autophagy transcriptional factors such as E2f1, Atf3, Stat1, and Stat3, which may be facilitating myopathy. Therefore, PGC1β activation negatively affects muscle mass over time, particularly fast-twitch muscles, which should be taken into consideration along with its known aerobic effects in the skeletal muscle.
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?
PGC1-β overexpression was responsible for muscular atrophy due to enhanced apoptosis and autophagy in a transgenic mouse model.
“PGC1-β overexpression was responsible for muscular atrophy due to an enhanced apoptosis and autophagy in a transgenic mouse model [91].”
From Main Pathogenic Mechanisms and Recent Advances in COPD Peripheral Skeletal Muscle Wasting (2023) · cites this paper as [91]
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
RetractedApoptosis: A Review of Programmed Cell Death
Elmore, S. (2007) · Toxicologic Pathology · doi:10.1080/01926230701320337 · Cited by 13,853 · see citing works
Mootha, 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
Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).
Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, M. J., Abeliovich, H., Acevedo Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., et al. (2016) · Autophagy · doi:10.1080/15548627.2015.1100356 · Cited by 5,894 · see citing works
Regulation mechanisms and signaling pathways of autophagy
He, C., & Klionsky, D. J. (2009) · Annual Review of Genetics · doi:10.1146/annurev-genet-102808-114910 · Cited by 3,609 · see citing works
Identification 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 · 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
FoxO3 Controls Autophagy in Skeletal Muscle In Vivo
Mammucari, C., Milan, G., Romanello, V., Masiero, E., Rudolf, R., Del Piccolo, P., Burden, S. J., Di Lisi, R., Sandri, C., Zhao, J., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.001 · Cited by 1,953 · see citing works
Zhao, J., Brault, J. J., Schild, A., Cao, P., Sandri, M., Schiaffino, S., Lecker, S. H., & Goldberg, A. L. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.004 · Cited by 1,489 · see citing works
Autophagy maintains stemness by preventing senescence
García-Prat, L., Martínez-Vicente, M., Perdiguero, E., Ortet, L., Rodríguez-Ubreva, J., Rebollo, E., Ruiz-Bonilla, V., Gutarra, S., Ballestar, E., Serrano, A. L., et al. (2016) · Nature · doi:10.1038/nature16187 · Cited by 1,355 · see citing works
Cellular and molecular mechanisms of muscle atrophy
Bonaldo, P., & Sandri, M. (2013) · Disease Models & Mechanisms · doi:10.1242/dmm.010389 · Cited by 1,284 · see citing works
Mitochondrial Oxidative Stress: Implications for Cell Death
Orrenius, S., Gogvadze, V. G., & Zhivotovsky, B. (2006) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.47.120505.105122 · Cited by 1,266 · see citing works
Exercise-induced BCL2-regulated autophagy is required for muscle glucose homeostasis
He, C., Bassik, M. C., Moresi, V., Sun, K., Wei, Y., Zou, Z., An, Z., Loh, J., Fisher, J., Sun, Q., et al. (2012) · Nature · doi:10.1038/nature10758 · Cited by 1,136 · see citing works
Muscle wasting in disease: molecular mechanisms and promising therapies
Cohen, S., Nathan, J. A., & Goldberg, A. L. (2015) · Nature Reviews Drug Discovery · doi:10.1038/nrd4467 · Cited by 1,089 · see citing works
HIF-independent regulation of VEGF and angiogenesis by the transcriptional coactivator PGC-1α
Arany, Z., Foo, S.-Y., Ma, Y., Ruas, J. L., Bommi-Reddy, A., Girnun, G., Cooper, M., Laznik, D., Chinsomboon, J., Rangwala, S. M., et al. (2008) · Nature · doi:10.1038/nature06613 · Cited by 1,054 · 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
Nucleolar Arf sequesters Mdm2 and activates p53
Weber, J. D., Taylor, L. J., Roussel, M. F., Sherr, C. J., & Bar-Sagi, D. (1999) · Nature Cell Biology · doi:10.1038/8991 · Cited by 940 · see citing works
The machinery of programmed cell death
Zimmermann, K. C., Bonzon, C., & Green, D. R. (2001) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(01)00159-0 · Cited by 829 · see citing works
Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models
Schiaffino, S., & Mammucari, C. (2011) · Skeletal Muscle · doi:10.1186/2044-5040-1-4 · Cited by 816 · see citing works
A Complex with Chromatin Modifiers That Occupies E2F- and Myc-Responsive Genes in G 0 Cells
Ogawa, H., Ishiguro, K., Gaubatz, S., Livingston, D. M., & Nakatani, Y. (2002) · Science · doi:10.1126/science.1069861 · Cited by 769 · see citing works
A PGC-1α isoform induced by resistance training regulates skeletal muscle hypertrophy
Ruas, J. L., White, J. P., Rao, R. R., Kleiner, S., Brannan, K. T., Harrison, B. C., Greene, N. P., Wu, J., Estall, J. L., Irving, B. A., et al. (2012) · Cell · doi:10.1016/j.cell.2012.10.050 · Cited by 677 · see citing works
GENECODIS: a web-based tool for finding significant concurrent annotations in gene lists
Carmona‐Sáez, P., Chagoyen, M., Tirado, F., Carazo, J. M., & Pascual-Montano, A. (2007) · Genome biology · doi:10.1186/gb-2007-8-1-r3 · Cited by 591 · see citing works
Bonetto, A., Aydogdu, T., Jin, X., Zhang, Z., Zhan, R., Puzis, L., Koniaris, L. G., & Zimmers, T. A. (2012) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00039.2012 · Cited by 463 · see citing works
Russell, A. P., Feilchenfeldt, J. W., Schreiber, S., Praz, M., Crettenand, A., Gobelet, C., Meier, C. A., Bell, D., Kralli, A., Giacobino, J., et al. (2003) · Diabetes · doi:10.2337/diabetes.52.12.2874 · Cited by 451 · see citing works
Mitochondrial function and apoptotic susceptibility in aging skeletal muscle
Chabi, B., Ljubicic, V., Menzies, K. J., Huang, J. H., Saleem, A., & Hood, D. A. (2008) · Aging Cell · doi:10.1111/j.1474-9726.2007.00347.x · Cited by 437 · see citing works
Lira, V. A., Okutsu, M., Zhang, M., Greene, N. P., Laker, R. C., Breen, D. S., Hoehn, K. L., & Yan, Z. (2013) · The FASEB Journal · doi:10.1096/fj.13-228486 · Cited by 432 · see citing works
Autophagy Impairment in Muscle Induces Neuromuscular Junction Degeneration and Precocious Aging
Carnio, S., LoVerso, F., Baraibar, M. A., Longa, E., Khan, M. M., Maffei, M., Reischl, M., Canepari, M., Loefler, S., Kern, H., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.07.061 · Cited by 423 · see citing works
Molecular and cellular mechanisms of skeletal muscle atrophy: an update
Fanzani, A., Conraads, V. M., Penna, F., & Martinet, W. (2012) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-012-0074-6 · Cited by 372 · see citing works
Arany, Z., Lebrasseur, N., Morris, C., Smith, E., Yang, W., Ma, Y., Chin, S., & Spiegelman, B. M. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2006.12.003 · Cited by 370 · 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
Skeletal Muscle Apoptosis and Weight Loss in Chronic Obstructive Pulmonary Disease
Agustí, A. G. N., Sauleda, J., Miralles, C., Gomez, C., Togores, B., Sala, E., Batle, S., & Busquets, X. (2002) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.2108013 · Cited by 343 · see citing works
Fas Ligand-independent, FADD-mediated Activation of the Fas Death Pathway by Anticancer Drugs
Micheau, O., Solary, É., Hammann, A., & Dimanche‐Boitrel, M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.12.7987 · Cited by 320 · see citing works
Role of PGC-1α during acute exercise-induced autophagy and mitophagy in skeletal muscle
Vainshtein, A., Tryon, L. D., Pauly, M., & Hood, D. A. (2015) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00380.2014 · Cited by 273 · see citing works
E2F1 regulates autophagy and the transcription of autophagy genes
Polager, S., Ofir, M., & Ginsberg, D. (2008) · Oncogene · doi:10.1038/onc.2008.117 · Cited by 260 · see citing works
Doyle, A., Zhang, G., Fattah, E. A. A., Eissa, N. T., & Li, Y. (2011) · The FASEB Journal · doi:10.1096/fj.10-164152 · Cited by 256 · see citing works
Silva, K. A. S., Dong, J., Dong, Y., Dong, Y., Schor, N., Tweardy, D. J., Zhang, L., & Mitch, W. E. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.641514 · Cited by 229 · see citing works
Cannavino, J., Brocca, L., Sandri, M., Bottinelli, R., & Pellegrino, M. A. (2014) · The Journal of Physiology · doi:10.1113/jphysiol.2014.275545 · Cited by 220 · see citing works
Brault, J. J., Jespersen, J. G., & Goldberg, A. L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.113092 · Cited by 217 · see citing works
Activating transcription factor 3, a stress sensor, activates p53 by blocking its ubiquitination
Yan, C., Lü, D., Hai, T., & Boyd, D. D. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600712 · Cited by 214 · see citing works
Nakanishi, K., SUDO, T., & Morishima, N. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200412024 · Cited by 210 · see citing works
Excessive fatty acid oxidation induces muscle atrophy in cancer cachexia
Fukawa, T., Chua, B. Y.-J., Min‐Wen, J. C., Jun‐Hao, E. T., Huang, D. Y., Qian, C.-N., Ong, P., Li, Z., Chen, S., Mak, S. Y., et al. (2016) · Nature Medicine · doi:10.1038/nm.4093 · Cited by 206 · see citing works
Pal, R., Palmieri, M., Loehr, J. A., Li, S., Abo‐Zahrah, R., Monroe, T. O., Thakur, P. B., Sardiello, M., & Rodney, G. G. (2014) · Nature Communications · doi:10.1038/ncomms5425 · Cited by 195 · see citing works
Self-citationGinsberg, D. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03270-2 · Cited by 186 · see citing works
Autophagy is induced in the skeletal muscle of cachectic cancer patients
Aversa, Z., Pin, F., Lucia, S., Penna, F., Verzaro, R., Fazi, M., Colasante, G., Tirone, A., Fanelli, F. R., Ramaccini, C., et al. (2016) · Scientific Reports · doi:10.1038/srep30340 · Cited by 158 · see citing works
JunB transcription factor maintains skeletal muscle mass and promotes hypertrophy
Raffaello, A., Milan, G., Masiero, E., Carnio, S., Lee, D., Lanfranchi, G., Goldberg, A. L., & Sandri, M. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201001136 · Cited by 156 · see citing works
Mitochondrial DNA damage triggers mitochondrial-superoxide generation and apoptosis
Ricci, C., Pastukh, V. M., Leonard, J. N., Turrens, J. F., Wilson, G. L., Schaffer, D., & Schaffer, S. W. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00362.2007 · Cited by 142 · see citing works
Sáinz, N., Rodríguez, A., Catalán, V., Becerril, S., Ramírez, B., Gómez-Ambrosi, J., & Frühbeck, G. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006808 · Cited by 135 · see citing works
Depletion of membrane cholesterol causes ligand-independent activation of Fas and apoptosis
Gniadecki, R. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.05.145 · Cited by 132 · see citing works
Carmignac, V., Svensson, M., Körner, Z., Elowsson, L., Matsumura, C. Y., Gawlik, K. I., Allamand, V., & Durbeej, M. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr427 · Cited by 121 · see citing works
Myostatin Gene Inactivation Prevents Skeletal Muscle Wasting in Cancer
Gallot, Y. S., Durieux, A., Castells, J., Desgeorges, M. M., Vernus, B., Plantureux, L., Rémond, D., Jahnke, V. E., Lefai, É., Dardevet, D. P., et al. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-0057 · Cited by 117 · see citing works
Zhao, J. C., Li, X., Guo, M., Yu, J., & Yan, C. (2016) · BMC Genomics · doi:10.1186/s12864-016-2664-8 · Cited by 111 · 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
Cheema, N., Herbst, A., McKenzie, D., & Aiken, J. M. (2015) · Aging Cell · doi:10.1111/acel.12399 · Cited by 107 · see citing works
Yamada, E., Bastie, C. C., Koga, H., Wang, Y., Cuervo, A. M., & Pessin, J. E. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.03.014 · Cited by 103 · see citing works
O′Leary, M. F. N., Vainshtein, A., Carter, H. N., Zhang, Y., & Hood, D. A. (2012) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00451.2011 · Cited by 98 · see citing works
Normal myogenesis and increased apoptosis in myotonic dystrophy type-1 muscle cells
Loro, E., Rinaldi, F., Malena, A., Masiero, E., Novelli, G., Angelini, C. I., Romeo, V., Sandri, M. F., Botta, A., & Vergani, L. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2010.33 · Cited by 89 · see citing works
Young, C., Sinadinos, A., Lefebvre, A., Chan, P., Arkle, S., Vaudry, D., & Górecki, D. C. (2015) · Autophagy · doi:10.4161/15548627.2014.994402 · Cited by 84 · see citing works
Autophagy-regulating TP53INP2 mediates muscle wasting and is repressed in diabetes
Sala, D., Ivanova, S., Plana, N., Ribas, V., Durán, J., Bach, D., Türkseven, S., Laville, M., Vidal, H., Karczewska‐Kupczewska, M., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci72327 · Cited by 83 · see citing works
Pgc-1α overexpression Via local transfection attenuates mitophagy pathway in muscle disuse atrophy
Kang, C., & Ji, L. L. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.12.032 · Cited by 83 · see citing works
The E2F family and the role of E2F1 in apoptosis
Wu, Z., Zheng, S., & Yu, Q. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.06.004 · Cited by 81 · see citing works
Inflammatory Cells and Apoptosis in Respiratory and Limb Muscles of Patients with COPD
Barreiro, E., Ferrer, D., Sanchez, F., Minguella, J., Marin-Corral, J., Martinez-Llorens, J., Lloreta, J., & Gea, J. (2011) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01017.2010 · Cited by 79 · see citing works
Bargiela, A., Cerro-Herreros, E., Fernández‐Costa, J. M., Vilchez, J. J., Llamusí, B., & Artero, R. D. (2015) · Disease Models & Mechanisms · doi:10.1242/dmm.018127 · Cited by 77 · see citing works
Ramamoorthy, T. G., LAVERNY, G., Schlagowski, A.-I., Zoll, J., Messaddeq, N., Bornert, J., Panza, S., Ferry, A., Gény, B., & METZGER, D. (2015) · Nature Communications · doi:10.1038/ncomms10210 · Cited by 76 · see citing works
Impaired autophagy contributes to muscle atrophy in glycogen storage disease type II patients
Nascimbeni, A. C., Fanin, M., Masiero, E., Angelini, C. I., & Sandri, M. (2012) · Autophagy · doi:10.4161/auto.21691 · Cited by 68 · see citing works
Regulatory circuitry of TWEAK‐Fn14 system and PGC‐1α in skeletal muscle atrophy program
Hindi, S. M., Mishra, V. K., Bhatnagar, S., Tajrishi, M. M., Ogura, Y., Yan, Z., Burkly, L. C., Zheng, T. S., & Kumar, A. (2013) · The FASEB Journal · doi:10.1096/fj.13-242123 · Cited by 68 · see citing works
Reactive Oxygen Species Regulate Autophagy through Redox-Sensitive Proteases
Liu, Z., & Lenardo, M. J. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.03.016 · Cited by 64 · see citing works
Argilés, J. M. A., López-Soriano, F. J., & Busquets, S. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.02.001 · Cited by 57 · see citing works
Revascularization of Ischemic Skeletal Muscle by Estrogen-Related Receptor-γ
Matsakas, A., Yadav, V., Lorca, S., Evans, R. M., & Narkar, V. A. (2012) · Circulation Research · doi:10.1161/circresaha.112.266478 · Cited by 57 · see citing works
Self-citationPGC-1αpromotes exercise-induced autophagy in mouse skeletal muscle
Halling, J. F., Ringholm, S., Nielsen, M. M., Overby, P., & Pilegaard, H. (2016) · Physiological Reports · doi:10.14814/phy2.12698 · Cited by 49 · see citing works
Cea, L. A., Puebla, C., Cisterna, B. A., Escamilla, R., Vargas, A. A., Frank, M., Martínez‐Montero, P., Prior, C., Molano, J., Esteban‐Rodríguez, I., et al. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2132-2 · Cited by 41 · see citing works
Menconi, M. J., Arany, Z. P., Alamdari, N., Aversa, Z., GONNELLA, P. A., O’Neal, P., Smith, I. J., Tizio, S., & Hasselgren, P.-O. J. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00596.2009 · Cited by 35 · see citing works
AMP-activated kinase α2 deficiency protects mice from denervation-induced skeletal muscle atrophy
Guo, Y., Meng, J., Tang, Y., Wang, T., Wei, B. K., Feng, R. M., Gong, B., Wang, H., Ji, G., & Lu, Z. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.04.015 · Cited by 31 · see citing works
Dysregulation of nuclear receptor COUP-TFII impairs skeletal muscle development
Lee, H.-J., Kao, C., Lin, S., Xu, M., Xie, X., Tsai, S. Y., & Tsai, M. (2017) · Scientific Reports · doi:10.1038/s41598-017-03475-5 · Cited by 31 · see citing works
Wang, Q., Shu, C., Su, J., & Li, X. (2015) · PubMed Central · Cited by 30 · see citing works
COUP-TFII regulates satellite cell function and muscular dystrophy
Xie, X., Tsai, S. Y., & Tsai, M. (2016) · Journal of Clinical Investigation · doi:10.1172/jci87414 · Cited by 29 · see citing works
Badin, P.-M., Vila, I. K., Sopariwala, D. H., Yadav, V., Lorca, S., Louche, K., Kim, E. R., Tong, Q., Song, M. S., Moro, C., et al. (2016) · Scientific Reports · doi:10.1038/srep26442 · Cited by 21 · see citing works
Self-citationYamauchi, J., Kumar, A., Duarte, L., Mehuron, T., & Girgenrath, M. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt280 · Cited by 20 · see citing works
Park, S. Y., Lee, J. H., Kim, H. Y., Yoon, K. H., Park, S. K., & Chang, M. S. (2014) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2014.1675 · Cited by 15 · see citing works
PGC1β Activates an Antiangiogenic Program to Repress Neoangiogenesis in Muscle Ischemia
Yadav, V., Matsakas, A., Lorca, S., & Narkar, V. A. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.06.040 · Cited by 15 · see citing works
Self-citation(2012) · Circulation Research · doi:10.1161/res.0b013e31827806cf · Cited by 3 · see citing works
Flagged first, then by citations
1 of the 82 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
microRNA-378 promotes autophagy and inhibits apoptosis in skeletal muscle
Li, Y., Jiang, J., Liu, W., Wang, H., Zhao, L., Liu, S., Li, P., Zhang, S., Sun, C., Wu, Y., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1803377115 · Cited by 134 · see citing works
Main Pathogenic Mechanisms and Recent Advances in COPD Peripheral Skeletal Muscle Wasting
Henrot, P., Dupin, I., Schilfarth, P., Esteves, P., Blervaque, L., Zysman, M., Gouzi, F., Hayot, M., Pomiès, P., & Berger, P. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076454 · Cited by 85 · see citing works
Quorum sensing molecules as a novel microbial factor impacting muscle cells
Spiegeleer, A. D., Elewaut, D. S., Noortgate, N. J. V. D., Janssens, Y., Debunne, N., Langenhove, S. V., Govindarajan, S., Spiegeleer, B. M. J. D., & Wynendaele, E. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2019.165646 · Cited by 49 · see citing works
Goropashnaya, A. V., Barnes, B. M., & Fedorov, V. B. (2020) · Scientific Reports · doi:10.1038/s41598-020-66030-9 · Cited by 40 · see citing works
Lin, J., Liu, Y., Ma, J., Mo, Y., Chen, C., Chen, L., Li, Q., Yang, Z., Zheng, D.-H., Ling, L., et al. (2020) · Therapeutic Advances in Musculoskeletal Disease · doi:10.1177/1759720x20946220 · Cited by 28 · see citing works
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 · see citing works
Galasso, C., Nuzzo, G., Brunet, C., Ianora, A., Sardo, A., Fontana, A., & Sansone, C. (2018) · Marine Drugs · doi:10.3390/md16120502 · Cited by 28 · see citing works
Queiroz, A. L., Lessard, S. J., Ouchida, A. T., Araújo, H. N., Gonçalves, D. A. P., Guimarães, D. S. P. S. F., Teodoro, B. G., So, K., Espreáfico, E. M., Hirshman, M. F., et al. (2021) · Molecular Metabolism · doi:10.1016/j.molmet.2021.101226 · Cited by 25 · see citing works
PGC-1β maintains mitochondrial metabolism and restrains inflammatory gene expression
Guak, H., Sheldon, R. D., Beddows, I., Ark, A. V., Weiland, M. J., Shen, H., Jones, R. G., St‐Pierre, J., Ma, E. H., & Krawczyk, C. M. (2022) · Scientific Reports · doi:10.1038/s41598-022-20215-6 · Cited by 17 · see citing works
The Role of the MYL4 Gene in Porcine Muscle Development and Its Molecular Regulatory Mechanisms
Ye, Y., Wu, G., Wang, H., Duan, M., Shang, P., & Chamba, Y. (2024) · Animals · doi:10.3390/ani14091370 · Cited by 8 · see citing works
NEDD4 enhances bone‑tendon healing in rotator cuff tears by reducing fatty infiltration
Li, J., Peng, Y., Zhen, D., Guo, C., & Peng, W. (2024) · Molecular Medicine Reports · doi:10.3892/mmr.2024.13420 · Cited by 4 · see citing works
Senescence dynamics define therapeutic windows for Duchenne muscular dystrophy in DBA/2-mdx mice
Calls, A., Tàrrega, A. B., Cisneros, A., Rommelfanger, M., Campanario, S., Grima-Terrén, M., Ramírez‐Pardo, I., Moiseeva, V., Lukesova, V., Andrés, E., et al. (2026) · Skeletal Muscle · doi:10.1186/s13395-026-00426-5 · Cited by 1 · see citing works
WITHDRAWN: This article has been withdrawn
Spiegeleer, A. D., Elewaut, D. S., Noortgate, N. J. V. D., Janssens, Y., Debunne, N., Langenhove, S. V., Govindarajan, S., Spiegeleer, B. M. J. D., & Wynendaele, E. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2019.165585
RetractedMolecular mechanism of sarcopenia
井上愛子, 憲武, 成., 大貴, 五., & 葛谷, 雅. (2018) · Nippon Ronen Igakkai Zasshi Japanese Journal of Geriatrics · doi:10.3143/geriatrics.55.13
- Authors
- Sopariwala, D. H., Yadav, V., Badin, P.-M., Likhite, N., Sheth, M., Lorca, S., Vila, I. K., Kim, E. R., Tong, Q., Song, M. S., Rodney, G. G., & Narkar, V. A.
- Affiliations
- Rice University (US)
- The University of Texas MD Anderson Cancer Center (US)
- Baylor College of Medicine (US)
- The University of Texas Health Science Center at Houston (US)
- Corresponding author
- Narkar, Vihang A.
- ORCID
- Venue
- Scientific Reports
- Published
- 2017-08-31
- Volume
- 7
- Issue
- 1
- Pages
- 10237-10237
- ISSN
- 2045-2322 (ISSN-L)
- PMC
- PMC5578977
- OpenAlex
- W2745470229
- Cited by
- 14
- References
- 82
- Citations by year
- 2026: 1 · 2024: 2 · 2023: 1 · 2022: 2 · 2021: 1 · 2020: 2 · 2019: 2 · 2018: 3
- FWCI
- 0.78
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Scientific Reports (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Funders
- Welch Foundation (L-AU0002)
- University of Texas Health Science Center at Houston
- National Heart, Lung, and Blood Institute (R01HL129191)
- 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 › Metabolism, Diabetes, and Cancer
- Keywords
- PGC-1β, skeletal muscle atrophy, muscle atrophy, apoptosis, autophagy, ubiquitin-proteasome degradation, protein oxidation, E2F1, ATF3, STAT1, STAT3, transgenic mice, muscle mass regulation, myopathy
- MeSH terms
- Animals, Autophagy, Mice, Transgenic, Muscular Atrophy, Nuclear Proteins, Organ Size, Transcription Factors, Apoptosis, Oxidative Stress, Muscle, Skeletal, Mice, Ubiquitination, Proteolysis
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
