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Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy.
Open accessAbstract
Skeletal muscle atrophy is a debilitating response to fasting, disuse, cancer, and other systemic diseases. In atrophying muscles, the ubiquitin ligase, atrogin-1 (MAFbx), is dramatically induced, and this response is necessary for rapid atrophy. Here, we show that in cultured myotubes undergoing atrophy, the activity of the PI3K/AKT pathway decreases, leading to activation of Foxo transcription factors and atrogin-1 induction. IGF-1 treatment or AKT overexpression inhibits Foxo and atrogin-1 expression. Moreover, constitutively active Foxo3 acts on the atrogin-1 promoter to cause atrogin-1 transcription and dramatic atrophy of myotubes and muscle fibers. When Foxo activation is blocked by a dominant-negative construct in myotubes or by RNAi in mouse muscles in vivo, atrogin-1 induction during starvation and atrophy of myotubes induced by glucocorticoids are prevented. Thus, forkhead factor(s) play a critical role in the development of muscle atrophy, and inhibition of Foxo factors is an attractive approach to combat muscle wasting.
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“Two muscle-specific E3 ubiquitin ligases, muscle RING finger 1 (MuRF1, also known as TRIM63) and muscle atrophy F-Box (MAFbx, also known as atrogin-1 or FBXO32), are thought to be key regulators of proteasomal proteolysis in skeletal muscle, especially under atrophy-inducing conditions (Cai et al., 2004; Sandri et al., 2004; Stitt et al., 2004).”
From Proteasome dysfunction induces muscle growth defects and protein aggregation (2014) · cites this paper as Sandri et al., 2004
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Two muscle-specific E3 ubiquitin ligases, MuRF1 and Atrogin1, are thought to be key regulators of proteasomal proteolysis in skeletal muscle, especially under atrophy-inducing conditions (Cai et al., 2004; Sandri et al., 2004).”
From Inducible Rpt3, a Proteasome Component, Knockout in Adult Skeletal Muscle Results in Muscle Atrophy (2020) · cites this paper as Sandri et al., 2004
Experimental — accuracy not yet measuredIn the citing paper
“Atrogin-1 plays a key role in muscle atrophy as muscle specific ubiquitin ligase.”
From GLP-1RA Liraglutide and Semaglutide Improves Obesity-Induced Muscle Atrophy via SIRT1 Pathway (2023) · cites this paper as [48]
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“FoxO family of transcription factors (FoxO1, FoxO3, and FoxO4) are critical mediators of the catabolic response during atrophy [9, 15, 16].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [9]
In the citing paper
“The IGF1–AKT-–mTOR axis increases protein synthesis by stimulating the translational machinery and simultaneously blocks FoxOs transcription factors and protein degradation [9].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [9]
In the citing paper
“Alterations in mPTP function are undoubtedly contributing to the aging-related loss of muscle mass and function, since mPTP opening can trigger several atrophy-regulating pathways.”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [17]
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Cites
Akt Promotes Cell Survival by Phosphorylating and Inhibiting a Forkhead Transcription Factor
Brunet, A., Bonni, A., Zigmond, M. J., Lin, M. Z., Juo, P., Hu, L. S., Anderson, M. J., Arden, K. C., Blenis, J., & Greenberg, M. E. (1999) · Cell · doi:10.1016/s0092-8674(00)80595-4 · Cited by 5,594
A System for Stable Expression of Short Interfering RNAs in Mammalian Cells
Brummelkamp, T. R., Bernards, R., & Agami, R. (2002) · Science · doi:10.1126/science.1068999 · Cited by 4,295
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
Bodine, S. C., Stitt, T. N., Gonzalez, M., Kline, W. O., Stover, G. L., Bauerlein, R., Zlotchenko, E., Scrimgeour, A., Lawrence, J. C., Glass, D. J., et al. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-1014 · Cited by 2,752
Stitt, 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-citationRommel, C., Bodine, S. C., Clarke, B. A., Rossman, R., Nunez, L., Stitt, T. N., Yancopoulos, G. D., & Glass, D. J. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-1009 · Cited by 1,583
Multiple 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-citationRubinson, D. A., Dillon, C. P., Kwiatkowski, A. V., Sievers, C., Yang, L., Kopinja, J. E., Rooney, D. L., Zhang, M., Ihrig, M. M., McManus, M. T., et al. (2003) · Nature Genetics · doi:10.1038/ng1117 · Cited by 1,499
Insulin-regulated hepatic gluconeogenesis through FOXO1–PGC-1α interaction
Puigserver, P., Rhee, J., Donovan, J., Walkey, C. J., Yoon, J. C., Oriente, F., Kitamura, Y., Altomonte, J., Dong, H., Accili, D., et al. (2003) · Nature · doi:10.1038/nature01667 · Cited by 1,487
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Link, W., & Fernández-Marcos, P. J. (2017) · International Journal of Cancer · doi:10.1002/ijc.30840 · Cited by 118
Mechanical ventilation induces alterations of the ubiquitin-proteasome pathway in the diaphragm
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Role of glucocorticoids in the molecular regulation of muscle wasting
Menconi, M. J., Fareed, M. U., O’Neal, P., Poylin, V. Y., Wei, W., & Hasselgren, P. (2007) · Critical Care Medicine · doi:10.1097/01.ccm.0000279194.11328.77 · Cited by 118
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Constantin‐Teodosiu, D., & Constantin, D. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111587 · Cited by 134
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Puppa, M., White, J. P., Velázquez, K. T., Baltgalvis, K. A., Sato, S., Baynes, J., & Carson, J. A. (2011) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-011-0047-1 · Cited by 120
Duscha, B. D., Schulze, P. C., Robbins, J. L., & Forman, D. E. (2007) · Heart Failure Reviews · doi:10.1007/s10741-007-9056-8 · Cited by 114
Resistance exercise, muscle loading/unloading and the control of muscle mass
Baar, K., Nader, G. A., & Bodine, S. C. (2006) · Essays in Biochemistry · doi:10.1042/bse0420061 · Cited by 116
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Bertaggia, E., Coletto, L., & Sandri, M. (2012) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00142.2011 · Cited by 114
Self-citationCellular and molecular mechanisms of sarcopenia: The S100B perspective
Riuzzi, F., Sorci, G., Arcuri, C., Giambanco, I., Bellezza, I., Minelli, A., & Donato, R. (2018) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12363 · Cited by 114
“They are activated in multiple models of muscle atrophy and are both suf fi cient and required for muscle atrophy 38 ( Figure 2).”
Peng, S., Zhao, S., Yan, F., Cheng, J., Huang, L., Chen, H., Liu, Q., Ji, X., & Yuan, Z. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.2444-14.2015 · Cited by 115
Protein imbalance in the development of skeletal muscle wasting in tumour‐bearing mice
Brown, J. L., Lee, D. E., Rosa‐Caldwell, M. E., Brown, L. A., Perry, R. A., Haynie, W. S., Huseman, K., Sataranatarajan, K., Remmen, H. V., Washington, T. A., et al. (2018) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12354 · Cited by 117
Muscle-to-tumor crosstalk: The effect of exercise-induced myokine on cancer progression
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Cao, D. J., Jiang, N., Blagg, A. G., Johnstone, J. L., Gondalia, R., Oh, M., Luo, X., Yang, K., Shelton, J. M., Rothermel, B. A., et al. (2013) · Journal of the American Heart Association · doi:10.1161/jaha.113.000016 · Cited by 113
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Teleman, A. A., Chen, Y., & Cohen, S. M. (2005) · Developmental Cell · doi:10.1016/j.devcel.2005.07.004 · Cited by 116
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Kitamura, T., & Kitamura, Y. (2007) · Endocrine Journal · doi:10.1507/endocrj.kr-109 · Cited by 112
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Moylan, J. S., Smith, J. D., Chambers, M. A., McLoughlin, T. J., & Reid, M. B. (2008) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00041.2008 · Cited by 117
Herningtyas, E. H., Okimura, Y., Handayaningsih, A. E., Yamamoto, D., Maki, T., Iida, K., Takahashi, Y., Kaji, H., & Chihara, K. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.06.004 · Cited by 114
Judge, S. M., Wu, C.-L., Beharry, A. W., Roberts, B. M., Ferreira, L. F., Kandarian, S. C., & Judge, A. R. (2014) · BMC Cancer · doi:10.1186/1471-2407-14-997 · Cited by 111
Autophagy Exacerbates Muscle Wasting in Cancer Cachexia and Impairs Mitochondrial Function
Penna, F., Ballarò, R., Martínez-Cristóbal, P., Sala, D., Sebastián, D., Busquets, S., Muscaritoli, M., Argilés, J. M. A., Costelli, P., & Antonio Zorzano, A. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.05.032 · Cited by 113
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Papanicolaou, K. N., Izumiya, Y., & Walsh, K. X. (2008) · Circulation Research · doi:10.1161/circresaha.107.164186 · Cited by 111
Self-citationMolecular Mechanisms of Muscle Plasticity with Exercise
Hoppeler, H. H., Baum, O., Lurman, G. J., & Mueller, M. (2011) · Comprehensive physiology · doi:10.1002/cphy.c100042 · Cited by 131
Guo, A., Li, K., Tian, H., Fan, Z., Chen, Q., Yang, Y., Yu, J., Wu, Y., & Xiao, Q. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16448 · Cited by 118
Role for IκBα, but not c-Rel, in skeletal muscle atrophy
Judge, A. R., Koncarevic, A., Hunter, R. B., Liou, H., Jackman, R. W., & Kandarian, S. C. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00293.2006 · Cited by 111
Judge, S. M. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00330 · Cited by 116
Monsalve, M., & Olmos, Y. (2011) · Current Drug Targets · doi:10.2174/138945011796150307 · Cited by 113
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Rüegg, M. A., & Glass, D. J. (2011) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010510-100537 · Cited by 114
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Magomedova, L., & Cummins, C. L. (2015) · Handbook of experimental pharmacology · doi:10.1007/164_2015_1 · Cited by 116
Razeghi, P., Baskin, K. K., Sharma, S., Young, M. E., Stepkowski, S. M., Essop, M. F., & Taegtmeyer, H. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.01.163 · Cited by 111
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Saini, A., Faulkner, S., Al-Shanti, N., & Stewart, C. (2009) · Ageing Research Reviews · doi:10.1016/j.arr.2009.02.001 · Cited by 109
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Sugita, H., Kaneki, M., Sugita, M., Yasukawa, T., Yasuhara, S., & Martyn, J. A. J. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00321.2004 · Cited by 110
Kamolrat, T., & Gray, S. R. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.02.041 · Cited by 108
Koutakis, P., Weiss, D. J., Miserlis, D., Shostrom, V., Papoutsi, E., Ha, D. M., Carpenter, L. A., McComb, R. D., Casale, G. P., & Pipinos, I. I. (2014) · Redox Biology · doi:10.1016/j.redox.2014.07.002 · Cited by 108
Csibi, A., Leibovitch, M.-P., Cornille, K., Tintignac, L. A. J., & Leibovitch, S. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807641200 · Cited by 126
Judge, S. M., Sandesara, P. B., Reed, S. A., & Judge, A. R. (2011) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00255.2010 · Cited by 114
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Klein, G. L. (2015) · Osteoporosis and Sarcopenia · doi:10.1016/j.afos.2015.07.008 · Cited by 108
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Qu, Q., Chen, Y., Wang, Y., Long, S., Wang, W., Yang, H.-Y., Li, M., Tian, X., Wei, X., Liu, Y., et al. (2024) · Nature · doi:10.1038/s41586-024-08329-5 · Cited by 123
Derbré, F., Ferrando, B., Gómez‐Cabrera, M. C., Sanchis‐Gomar, F., Martinez-Bello, V. E., González, G. O., Díaz, A., Gratas‐Delamarche, A., Cerda, M., & Viña, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046668 · Cited by 108
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Troncoso, R., Paredes, F., Parra, V., Gatica, D., Vásquez-Trincado, C., Quiroga, C., Bravo, R., López‐Crisosto, C., Rodriguez, A. E., Oyarzún, A. P., et al. (2014) · Cell Cycle · doi:10.4161/cc.29272 · Cited by 113
Kavazis, A. N., Smuder, A. J., & Powers, S. K. (2014) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00210.2014 · Cited by 114
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Kim, H., Han, L., Iyer, S. V., de Cabo, R., Zhao, H., O’Brien, C. A., Manolagas, S. C., & Almeida, M. (2015) · Molecular Endocrinology · doi:10.1210/me.2015-1133 · Cited by 111
The role of autophagy in the pathogenesis of glycogen storage disease type II (GSDII)
Nascimbeni, A. C., Fanin, M., Masiero, E., Angelini, C. I., & Sandri, M. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.52 · Cited by 106
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Ohno, Y., Oyama, A., Kaneko, H., Egawa, T., YOKOYAMA, S., Sugiura, T., Ohira, Y., Yoshioka, T., & Goto, K. (2018) · Acta Physiologica · doi:10.1111/apha.13042 · Cited by 109
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Hitachi, K., & Tsuchida, K. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2013.00408 · Cited by 106
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Kloet, D. E. A., & Burgering, B. M. T. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.04.003 · Cited by 106
Muscle atrophy in experimental cancer cachexia: Is the IGF‐1 signaling pathway involved?
Penna, F., Bonetto, A., Muscaritoli, M., Costamagna, D., Minero, V. G., Bonelli, G., Fanelli, F. R., Baccino, F. M., & Costelli, P. (2009) · International Journal of Cancer · doi:10.1002/ijc.25146 · Cited by 109
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Southgate, R. J., Neill, B., Prelovsek, O., El‐Osta, A., Kamei, Y., Miura, S., Ezaki, O., McLoughlin, T. J., Zhang, W., Unterman, T. G., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702039200 · Cited by 112
Retractedde Souza, R. W. A., Piedade, W. P., Soares, L. C., Castro, P. A. T. D. S., Aguiar, A. F., Vechetti, I. J., de Campos, D. H. S., Fernandes, A. A. H., Okoshi, K., Carvalho, R. F., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0110020 · Cited by 104
Wang, C., Shen, J., Ying, J., Xiao, D., & O’Keefe, R. J. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2017056117 · Cited by 104
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Díaz, M. B., Rohm, M., & Herzig, S. (2024) · Nature Metabolism · doi:10.1038/s42255-024-01167-9 · Cited by 113
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Macpherson, P. C. D., Wang, X., & Goldman, D. J. (2011) · Journal of Cellular Biochemistry · doi:10.1002/jcb.23136 · Cited by 107
Fang, C. X., Dong, F., Thomas, D. P., Ma, H., He, L., & Ren, J. T. (2008) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00319.2008 · Cited by 108
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Self-citationYamada, 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
Pin, F., Barreto, R., Kitase, Y., Mitra, S., Erne, C. E., Novinger, L. J., Zimmers, T. A., Couch, M. E., Bonewald, L. F., & Bonetto, A. (2018) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12311 · Cited by 100
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Khan, M. M., Strack, S., Wild, F., Hanashima, A., Gasch, A., Brohm, K., Reischl, M., Carnio, S., Labeit, D., Sandri, M., et al. (2013) · Autophagy · doi:10.4161/auto.26841 · Cited by 106
Self-citationZhou, Q., Du, J., Hu, Z., Walsh, K. X., & Wang, X. H. (2007) · Endocrinology · doi:10.1210/en.2007-0183 · Cited by 105
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Braun, T. P., Grossberg, A. J., Krasnow, S. M., Levasseur, P. R., Szumowski, M., Zhu, X., Maxson, J. E., Knoll, J. G., Barnes, A. P., & Marks, D. L. (2013) · The FASEB Journal · doi:10.1096/fj.13-230375 · Cited by 107
Clavel, S., Siffroi‐Fernandez, S., Coldefy, A.-S., Boulukos, K. E., Pisani, D. F., & Dérijard, B. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00666-09 · Cited by 104
Nakashima, K., Ishida, A., Yamazaki, M., & Abé, H. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.08.138 · Cited by 102
Cleveland, B. M., & Weber, G. M. (2009) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00516.2009 · Cited by 105
Haddad, F., Adams, G., Bodell, P. W., & Baldwin, K. M. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01203.2005 · Cited by 109
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Hudson, M. B., Rahnert, J. A., Zheng, B., Woodworth‐Hobbs, M. E., Franch, H. A., & Price, S. R. (2014) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00395.2013 · Cited by 101
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Jin, B., & Li, Y. (2006) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21060 · Cited by 103
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Powell, S. R., Herrmann, J., Lerman, A., Patterson, C., & Wang, X. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-397863-9.00009-2 · Cited by 103
Mieulet, V., Roceri, M., Espeillac, C., Sotiropoulos, A., Ohanna, M., Oorschot, V., Klumperman, J., Sandri, M., & Pende, M. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00499.2006 · Cited by 99
Self-citationAging- and obesity-related peri-muscular adipose tissue accelerates muscle atrophy
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Constantin, D., McCullough, J., Mahajan, R. P., & Greenhaff, P. L. (2011) · The Journal of Physiology · doi:10.1113/jphysiol.2011.206193 · Cited by 105
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Gammeren, D. V., Damrauer, J. S., Jackman, R. W., & Kandarian, S. C. (2008) · The FASEB Journal · doi:10.1096/fj.08-114249 · Cited by 102
Transcriptomic profile of leg muscle during early growth in chicken
Xue, Q., Zhang, G., Li, T., Ling, J., Zhang, X., & Wang, J. (2017) · PLoS ONE · doi:10.1371/journal.pone.0173824 · Cited by 101
Rapid muscle atrophy response to unloading: pretranslational processes involving MHC and actin
Giger, J. M., Bodell, P. W., Zeng, M., Baldwin, K. M., & Haddad, F. (2009) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00344.2009 · Cited by 105
FoxO, Autophagy, and Cardiac Remodeling
Ferdous, A., Battiprolu, P. K., Ni, Y. G., Rothermel, B. A., & Hill, J. A. (2010) · Journal of Cardiovascular Translational Research · doi:10.1007/s12265-010-9200-z · Cited by 100
Foxo3a induces motoneuron death through the Fas pathway in cooperation with JNK
Barthélémy, C., Henderson, C. E., & Pettmann, B. (2004) · BMC Neuroscience · doi:10.1186/1471-2202-5-48 · Cited by 100
Su, J., Ekman, C., Oskolkov, N., Lahti, L., Ström, K., Brāzma, A., Groop, L., Rung, J., & Hansson, O. (2015) · Skeletal Muscle · doi:10.1186/s13395-015-0059-1 · Cited by 100
Kang, S., Lee, H., Kim, M. K., Lee, E., Sohn, U. D., & Kim, I. (2017) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00389.2016 · Cited by 100
Mediators and Patterns of Muscle Loss in Chronic Systemic Inflammation
Pérez-Baos, S., Prieto‐Potín, I., Roman‐Blas, J. A., Sánchez‐Pernaute, O., Largo, R., & Herrero‐Beaumont, G. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00409 · Cited by 101
Reactive Oxygen Species as a Link between Antioxidant Pathways and Autophagy
Li, D., Ding, Z., Du, K., Ye, X., & Cheng, S. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/5583215 · Cited by 107
Lei, Y., Gan, M., Qiu, Y., Chen, Q., Wang, X., Liao, T., Zhao, M., Chen, L., Zhang, S., Zhao, Y., et al. (2024) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-024-00572-y · Cited by 111
Atrogin-1 ubiquitin ligase is upregulated by doxorubicin via p38-MAP kinase in cardiac myocytes
Yamamoto, Y., Hoshino, Y., Ito, T., Nariai, T., Mohri, T., Obana, M., Hayata, N., Uozumi, Y., Maeda, M., Fujio, Y., et al. (2008) · Cardiovascular Research · doi:10.1093/cvr/cvn076 · Cited by 99
Sishi, B., & Engelbrecht, A. (2011) · Cytokine · doi:10.1016/j.cyto.2011.01.009 · Cited by 101
Glycine administration attenuates skeletal muscle wasting in a mouse model of cancer cachexia
Ham, D. J., Murphy, K. T., Chee, A., Lynch, G. S., & Koopman, R. (2013) · Clinical Nutrition · doi:10.1016/j.clnu.2013.06.013 · Cited by 99
Chopard, A., Hillock, S., & Jasmin, B. J. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00864.x · Cited by 106
Pino, E., Amamoto, R., Zheng, L., Cacquevel, M., Sarria, J. ‐. F., Knott, G. W., & Schneider, B. L. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt530 · Cited by 105
Mitogen-activated protein kinase signaling is necessary for the maintenance of skeletal muscle mass
Shi, H., Scheffler, J. M., Zeng, C., Pleitner, J. M., Hannon, K., Grant, A. L., & Gerrard, D. E. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00475.2008 · Cited by 102
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Song, Y., Song, J. L., Delafontaine, P., & Godard, M. P. (2013) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2013.03.004 · Cited by 102
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Sakai, H., Sagara, A., Arakawa, K., Sugiyama, R., Hirosaki, A., Takase, K., Jo, A., Sato, K., Chiba, Y., Yamazaki, M., et al. (2014) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2014.05.001 · Cited by 103
Tong, J. F., Yan, X., Zhu, M. J., & Du, . (2009) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22272 · Cited by 100
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Jang, W., Puchkov, D., Samsó, P., Liang, Y., Nadler-Holly, M., Sigrist, S. J., Kintscher, U., Liu, F., Mamchaoui, K., Mouly, V., et al. (2022) · Science · doi:10.1126/science.abq5209 · Cited by 94
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Morris, B. J. (2005) · Journal of Hypertension · doi:10.1097/01.hjh.0000173509.45363.dd · Cited by 98
Pietrangelo, T., Puglielli, C., Mancinelli, R., Beccafico, S., Fanò, G., & Fulle, S. (2009) · Experimental Gerontology · doi:10.1016/j.exger.2009.05.002 · Cited by 101
Lützner, N., Kalbacher, H., Krones, A., & Rösl, F. (2012) · PLoS ONE · doi:10.1371/journal.pone.0042166 · Cited by 101
Xie, P., Guo, S., Fan, Y., Zhang, H., Gu, D., & Li, H. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m806487200 · Cited by 99
Metadata
- Authors
- Sandri, M., Sandri, C., Gilbert, A., Skurk, C., Calabria, E., Picard, A., Walsh, K., Schiaffino, S., Lecker, S. H., & Goldberg, A. L.
- Affiliations
- Harvard University (US)
- Veneto Institute of Molecular Medicine (IT)
- Beth Israel Deaconess Medical Center (US)
- Boston University (US)
- Corresponding author
- Lecker, Stewart H
- Goldberg, Alfred L
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2004-04
- Volume
- 117
- Issue
- 3
- Pages
- 399-412
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC3619734
- OpenAlex
- W2033797333
- Cited by
- 3,012
- References
- 41
- Citations by year
- 2026: 129 · 2025: 122 · 2024: 121 · 2023: 118 · 2022: 141 · 2021: 153 · 2020: 165 · 2019: 159 · 2018: 151 · 2017: 117 · 2016: 134 · 2015: 171 · 2014: 176 · 2013: 177 · 2012: 150
- FWCI
- 33.75
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Padua Research Archive (University of Padova) (submittedVersion)
- Funders
- National Space Biomedical Research Institute
- European Commission (QLRT-2000-00530)
- National Institutes of Health (DK02707, DK62307)
- Ministero dell’Istruzione, dell’Università e della Ricerca
- Agenzia Spaziale Italiana
- Muscular Dystrophy Association
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › FOXO transcription factor regulation
- Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
- Keywords
- FOXO transcription factors, atrogin-1, skeletal muscle atrophy, ubiquitin ligase, PI3K/Akt signaling, insulin-like growth factor I, FOXO3, forkhead transcription factor, starvation, glucocorticoids, myotubes, muscle atrophy, transcriptional regulation
- MeSH terms
- Adenoviridae, Animals, Cells, Cultured, Cloning, Molecular, Fasting, Gene Expression Regulation, Genetic Vectors, Glucocorticoids, Insulin-Like Growth Factor I, Ligases, Models, Biological, Muscle Proteins, Muscular Atrophy, Promoter Regions, Genetic, Proto-Oncogene Proteins, Transcription Factors, Signal Transduction, Protein Serine-Threonine Kinases, Muscle, Skeletal, Phosphatidylinositol 3-Kinases, Muscle Cells, RNA Interference, Ubiquitin-Protein Ligases, SKP Cullin F-Box Protein Ligases, Proto-Oncogene Proteins c-akt, Mice
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