The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
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.
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
“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]
In the citing paper
“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]
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
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
Cited by
Sorted by citations
Items 601–700 of 1,032
Understanding of sarcopenia: from definition to therapeutic strategies
Kim, J. W., Kim, R., Choi, H., Lee, S., & Bae, G. (2021) · Archives of Pharmacal Research · doi:10.1007/s12272-021-01349-z · Cited by 103
Autophagy and Protein Turnover Signaling in Slow-Twitch Muscle during Exercise
PAGANO, A. F., PY, G., BERNARDI, H., CANDAU, R. B., & SANCHEZ, A. M. J. (2014) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0000000000000237 · Cited by 96
p62/SQSTM1 but not LC3 is accumulated in sarcopenic muscle of mice
Sakuma, K., Kinoshita, M., Ito, Y., Aizawa, M., Aoi, W., & Yamaguchi, A. (2015) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12045 · Cited by 99
Skeletal muscle mitochondrial uncoupling in a murine cancer cachexia model
Tzika, A. A., de Oliveira, C. C. F., Shestov, A. A., Constantinou, C., Psychogios, N., Righi, V., Mintzopoulos, D., Busquets, S., López-Soriano, F. J., Milot, S. M., et al. (2013) · International Journal of Oncology · doi:10.3892/ijo.2013.1998 · Cited by 96
Recent advances in understanding the role of FOXO3
Stefanetti, R. J., Voisin, S. A. C., Russell, A. P., & Lamon, S. (2018) · F1000Research · doi:10.12688/f1000research.15258.1 · Cited by 95
Physiological myocardial hypertrophy: how and why?
Catalucci, D. (2007) · Frontiers in bioscience · doi:10.2741/2681 · Cited by 94
Fasting Energy Homeostasis in Mice with Adipose Deficiency of Desnutrin/Adipose Triglyceride Lipase
Wu, J. W., Wang, S. P., Casavant, S., Moreau, A., Yang, G. S., & Mitchell, G. A. (2012) · Endocrinology · doi:10.1210/en.2011-1518 · Cited by 98
FOXO3‐mTOR metabolic cooperation in the regulation of erythroid cell maturation and homeostasis
Zhang, X., Campreciós, G., Rimmelé, P., Liang, R. H.-S., Yalcin, S., Mungamuri, S. K., Barminko, J., d’Escamard, V., Baron, M. H., Brugnara, C., et al. (2014) · American Journal of Hematology · doi:10.1002/ajh.23786 · Cited by 100
Mechanical Properties of Respiratory Muscles
Sieck, G. C., Ferreira, L. F., Reid, M. B., & Mantilla, C. B. (2013) · Comprehensive physiology · doi:10.1002/cphy.c130003 · Cited by 111
Androgen-mediated regulation of skeletal muscle protein balance
Rossetti, M. L., Steiner, J. L., & Gordon, B. S. (2017) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2017.02.031 · Cited by 95
Myostatin is a novel tumoral factor that induces cancer cachexia
Lokireddy, S., Wijesoma, I. W., Bonala, S., Wei, M., Sze, S. K., McFarlane, C., Kambadur, R., & Sharma, M. (2012) · Biochemical Journal · doi:10.1042/bj20112024 · Cited by 96
RetractedMueller, T. C., Bachmann, J., Prokopchuk, O., Friess, H., & Martignoni, M. E. (2016) · BMC Cancer · doi:10.1186/s12885-016-2121-8 · Cited by 95
Lipina, C., Kendall, H., McPherron, A. C., Taylor, P. M., & Hundal, H. S. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.04.039 · Cited by 98
The Hippo signal transduction network in skeletal and cardiac muscle
Wackerhage, H., Del Re, D. P., Judson, R. N., Sudol, M., & Sadoshima, J. (2014) · Science Signaling · doi:10.1126/scisignal.2005096 · Cited by 92
Regulation of AMPK by the Ubiquitin Proteasome System
Zungu, M., Schisler, J. C., Essop, M. F., McCudden, C. R., Patterson, C., & Willis, M. S. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2010.11.030 · Cited by 96
Depuydt, G., Xie, F., Petyuk, V., Shanmugam, N., Smolders, A., Dhondt, I., Brewer, H. M., Camp, D., Smith, R. D., & Braeckman, B. P. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.027383 · Cited by 92
Tseng, Y., Kulp, S. K., Lai, I., Hsu, E., He, W., Frankhouser, D. E., Yan, P. S., Mo, X. M., Bloomston, M., Lesinski, G. B., et al. (2015) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djv274 · Cited by 94
Hasselgren, P.-O. J., Alamdari, N., Aversa, Z., GONNELLA, P. A., Smith, I. J., & Tizio, S. (2010) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0b013e32833a5107 · Cited by 94
Hariharan, N., Ikeda, Y., Hong, C., Alcendor, R. R., Usui, S., Gao, S., Maejima, Y., & Sadoshima, J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0051632 · Cited by 93
Impact of glucocorticoid on neurogenesis
Numakawa, T., Odaka, H., & Adachi, N. (2017) · Neural Regeneration Research · doi:10.4103/1673-5374.211174 · Cited by 93
de Sire, R., Rizzatti, G., Ingravalle, F., Pizzoferrato, M., Petito, V., Lopetuso, L. R., Graziani, C., Alessandro de, S. I. R. E., Mentella, M. C., Mele, M. C., et al. (2018) · Minerva Gastroenterologica e Dietologica · doi:10.23736/s1121-421x.18.02511-4 · Cited by 93
Braun, T. P., Szumowski, M., Levasseur, P. R., Grossberg, A. J., Zhu, X., Agarwal, A., & Marks, D. L. (2014) · PLoS ONE · doi:10.1371/journal.pone.0106489 · Cited by 95
The AKT/mTOR signaling pathway plays a key role in statin-induced myotoxicity
Bonifacio, A., Sanvee, G. M., Bouitbir, J., & Krähenbühl, S. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.04.010 · Cited by 93
FOXO1: A Potential Target for Human Diseases
Lu, H., & Huang, H. (2011) · Current Drug Targets · doi:10.2174/138945011796150280 · Cited by 94
Muscle Wasting Diseases: Novel Targets and Treatments
Furrer, R., & Handschin, C. (2018) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010818-021041 · Cited by 94
Wang, D., Yang, Y., Huang, R.-H., Zhang, Z.-H., & Lin, X. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/684965 · Cited by 96
Molecular signaling pathways regulating muscle proteolysis during atrophy
Franch, H. A., & Price, S. R. (2005) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/01.mco.0000165005.01331.45 · Cited by 94
Murine models of atrophy, cachexia, and sarcopenia in skeletal muscle
Romanick, M. A., Thompson, L. V., & Brown‐Borg, H. M. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.03.011 · Cited by 104
The p97/VCP ATPase is critical in muscle atrophy and the accelerated degradation of muscle proteins
Piccirillo, R., & Goldberg, A. L. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.178 · Cited by 85
Self-citationBaehr, L. M., Tunzi, M. A., & Bodine, S. C. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00069 · Cited by 94
Neuromuscular Junction as an Entity of Nerve-Muscle Communication
Lepore, E., Casola, I., Dobrowolny, G., & Musarò, A. (2019) · Cells · doi:10.3390/cells8080906 · Cited by 98
Marceca, G. P., Londhe, P., & Calore, F. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.00298 · Cited by 92
Macroautophagy and aging: The impact of cellular recycling on health and longevity
Nieto-Torres, J. L., & Hansen, M. (2021) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2021.101020 · Cited by 93
Mitochondrial Dysfunction as an Underlying Cause of Skeletal Muscle Disorders
Chen, T., Koh, K.-Y., Lin, K. M.-C., & Chou, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232112926 · Cited by 95
Dieli-Conwright, C. M., Spektor, T. M., Rice, J. C., Sattler, F. R., & Schroeder, E. T. (2009) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00590.2009 · Cited by 93
Seiliez, I., Panserat, S., Cassy, S., Fricot, A., Vachot, C., Kaushik, S., & Tesseraud, S. (2008) · Journal of Nutrition · doi:10.1093/jn/138.3.487 · Cited by 93
Dulac, M., Leduc‐Gaudet, J., Reynaud, O., Ayoub, M., Guérin, A., Finkelchtein, M., Hussain, S. N., & Gouspillou, G. (2020) · The Journal of Physiology · doi:10.1113/jp279802 · Cited by 90
Absence of caspase-3 protects against denervation-induced skeletal muscle atrophy
Plant, P. J., Bain, J. R., Correa, J., Woo, M., & Batt, J. A. E. (2009) · Journal of Applied Physiology · doi:10.1152/japplphysiol.90932.2008 · Cited by 96
Smith, I. J., Alamdari, N., O’Neal, P., GONNELLA, P. A., Aversa, Z., & Hasselgren, P.-O. (2010) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2010.01.006 · Cited by 88
Geng, T., Li, P., Yin, X., & Yan, Z. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2011.01.005 · Cited by 90
Proteolysis in illness-associated skeletal muscle atrophy: from pathways to networks
Wing, S. S., Lecker, S. H., & Jagoe, R. T. (2011) · Critical Reviews in Clinical Laboratory Sciences · doi:10.3109/10408363.2011.586171 · Cited by 93
Self-citationMoberg, M., Apró, W., & Blomstrand, E. (2011) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00353.2011 · Cited by 93
Poor maternal nutrition inhibits muscle development in ovine offspring
Reed, S. A., Raja, J., Hoffman, M. L., Zinn, S. A., & Govoni, K. E. (2014) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/2049-1891-5-43 · Cited by 99
FoxO1 induces apoptosis in skeletal myotubes in a DNA-binding-dependent manner
McLoughlin, T. J., Smith, S. M., DeLong, A. D., Wang, H., Unterman, T. G., & Esser, K. A. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00502.2008 · Cited by 93
Huang, T., Zheng, D., Houmard, J. A., Brault, J. J., Hickner, R. C., & Cortright, R. N. (2017) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00331.2016 · Cited by 92
Mitochondrial dynamics in cancer-induced cachexia
van der Ende, M., Grefte, S., Plas, R., Meijerink, J., Witkamp, R. F., Keijer, J., & van Norren, K. (2018) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2018.07.008 · Cited by 87
Inoue, A., Cheng, X. W., Huang, Z., Hu, L., Kikuchi, R., Jiang, H., Piao, L., Sasaki, T., Itakura, K., Wu, H., et al. (2017) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12166 · Cited by 89
Wang, X. H., Zhang, L., Mitch, W. E., LeDoux, J. M., Hu, J., & Du, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.041707 · Cited by 89
NF-κB Activation Is Required for the Transition of Pulmonary Inflammation to Muscle Atrophy
LANGEN, R. C. J., Haegens, A., Vernooy, J. H. J., Wouters, E. F. �., de Winther, M. P. J., Carlsen, H., Steele, C. H., Shoelson, S. E., & Schols, A. M. W. J. (2012) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2011-0119oc · Cited by 91
Álvarez-García, Ó., Matsuzaki, T., Olmer, M., Miyata, K., Mokuda, S., Sakai, D., Masuda, K., Asahara, H., & Lotz, M. (2018) · Aging Cell · doi:10.1111/acel.12800 · Cited by 89
Xia, P., Chen, J., Liu, Y., Fletcher, M., Jensen, B. C., & Cheng, Z. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.011571 · Cited by 89
Argilés, J. M. A. (2010) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2010.557 · Cited by 92
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
Self-citationGonçalves, D. A. P., Silveira, W. A., Lira, E. C., Graça, F. A., Paula-Gomes, S., Zanon, N. M., Kettelhut, Í. D. C., & Navegantes, L. C. C. (2011) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00188.2011 · Cited by 92
Role of IGF-I and the TNFα/NF-κB pathway in the induction of muscle atrogenes by acute inflammation
Schakman, O., Dehoux, M., Bouchuari, S., Delaere, S., Lause, P., Decroly, N., Shoelson, S. E., & Thissen, J. P. (2012) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00060.2012 · Cited by 89
TACE release of TNF-α mediates mechanotransduction-induced activation of p38 MAPK and myogenesis
Zhan, M., Jin, B., Chen, S., Reecy, J. M., & Li, Y.-P. (2007) · Journal of Cell Science · doi:10.1242/jcs.03372 · Cited by 90
FBXO32 Targets c-Myc for Proteasomal Degradation and Inhibits c-Myc Activity
Mei, Z., Zhang, D., Hu, B., Wang, J., Shen, X., & Xiao, W. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.645978 · Cited by 88
Zampieri, S., Mammucari, C., Romanello, V., Barberi, L., Pietrangelo, L., Fusella, A., Mosole, S., Gherardi, G., Höfer, C., Löfler, S., et al. (2016) · Physiological Reports · doi:10.14814/phy2.13005 · Cited by 92
Self-citationThe Role of IGF-1 Signaling in Skeletal Muscle Atrophy
Timmer, L. T., Hoogaars, W. M. H., & Jaspers, R. T. (2018) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-1435-3_6 · Cited by 90
The effect of vitamin D on sarcopenia depends on the level of physical activity in older adults
Yang, A., Lv, Q., Chen, F., Wang, Y., Liu, Y., Shi, W., Liu, Y., & Wang, D. (2020) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12545 · Cited by 93
Regulation of the mTOR signaling network in hibernating thirteen-lined ground squirrels
Wu, C., & Storey, K. B. (2012) · Journal of Experimental Biology · doi:10.1242/jeb.066225 · Cited by 91
Akasaki, Y., Ouchi, N., Izumiya, Y., Bernardo, B. L., LeBrasseur, N. K., & Walsh, K. X. (2013) · Aging Cell · doi:10.1111/acel.12153 · Cited by 93
Self-citationFiber Type-Specific Nitric Oxide Protects Oxidative Myofibers against Cachectic Stimuli
Yu, Z., Li, P., Zhang, M., Hannink, M., Stamler, J. S., & Yan, Z. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002086 · Cited by 91
Molecular and neuroendocrine mechanisms of cancer cachexia
Mendes, M. C. S., Pimentel, G. D., Costa, F. O., & Carvalheira, J. B. C. (2015) · Journal of Endocrinology · doi:10.1530/joe-15-0170 · Cited by 89
AMPK inhibits myoblast differentiation through a PGC-1α-dependent mechanism
Williamson, D. L., Butler, D. C., & Alway, S. E. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.91007.2008 · Cited by 91
Tearin' Up My Heart: Proteolysis in the Cardiac Sarcomere
Portbury, A. L., Willis, M. S., & Patterson, C. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.r110.170571 · Cited by 88
Muscle unloading: A comparison between spaceflight and ground‐based models
Qaisar, R., Karim, A., & Elmoselhi, A. B. (2019) · Acta Physiologica · doi:10.1111/apha.13431 · Cited by 89
TRIM72 negatively regulates myogenesis via targeting insulin receptor substrate-1
Lee, C. S., Yi, J.-S., Jung, S.-Y., Kim, B., Lee, N.-R., Choo, H.-J., Jang, S.-Y., Han, J., Chi, S.-G., Park, M., et al. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2010.1 · Cited by 88
Autophagy in Skeletal Muscle Homeostasis and in Muscular Dystrophies
Grumati, P., & Bonaldo, P. (2012) · Cells · doi:10.3390/cells1030325 · Cited by 96
Zhao, W., Pan, J., Zhao, Z., Wu, Y., Bauman, W. A., & Cardozo, C. P. (2008) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2008.03.024 · Cited by 89
Glycogen synthase kinase-3β is required for the induction of skeletal muscle atrophy
Verhees, K. J. P., Schols, A. M. W. J., KELDERS, M. C. J. M., den Kamp, C. M. O., van der Velden, J. L. J., & LANGEN, R. C. J. (2011) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00520.2010 · Cited by 90
Fyfe, J. J., Bishop, D. J., Zacharewicz, E., Russell, A. P., & Stepto, N. K. (2016) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00479.2015 · Cited by 87
Chronic kidney disease induces autophagy leading to dysfunction of mitochondria in skeletal muscle
Su, Z., Klein, J. D., Du, J., Franch, H. A., Zhang, L., Hassounah, F., Hudson, M. B., & Wang, X. H. (2017) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00600.2016 · Cited by 85
Mitochondrial dysregulation and muscle disuse atrophy
Ji, L. L., & Yeo, D. (2019) · F1000Research · doi:10.12688/f1000research.19139.1 · Cited by 88
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 86
Self-citationHsp27 inhibits IKKβ‐induced NF‐κΕ activity and skeletal muscle atrophy
DODD, S. L., Hain, B. A., Judge, S. M., & Judge, A. R. (2009) · The FASEB Journal · doi:10.1096/fj.08-124602 · Cited by 87
Maki, T., Yamamoto, D., Nakanishi, S., Iida, K., Iguchi, G., Takahashi, Y., Kaji, H., Chihara, K., & Okimura, Y. (2012) · Nutrition Research · doi:10.1016/j.nutres.2012.07.005 · Cited by 85
Glucocorticoid-induced apoptosis and cellular mechanisms of myopathy
Dirks‐Naylor, A. J., & Griffiths, C. L. (2009) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2009.05.014 · Cited by 90
Ketone Bodies Attenuate Wasting in Models of Atrophy
Koutnik, A., Poff, A., Ward, N. P., Deblasi, J., Soliven, M. A., Romero, M., Roberson, P. A., Fox, C. D., Roberts, M., & D'Agostino, D. (2020) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12554 · Cited by 64
Hirner, S., Krohne, C., Schuster, A., Hoffmann, S., Witt, S. H., Erber, R., Sticht, C., Gasch, A., Labeit, S., & Labeit, D. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.03.049 · Cited by 89
Bosurgi, L., Manfredi, A. A., & Rovere, P. Q. (2011) · Frontiers in Immunology · doi:10.3389/fimmu.2011.00062 · Cited by 87
Energy sensing and regulation of gene expression in skeletal muscle
Freyssenet, D. G. (2006) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01126.2005 · Cited by 88
Novel aspects on the regulation of muscle wasting in sepsis
Hasselgren, P.-O., Menconi, M. J., Fareed, M. U., Yang, H., Wei, W., & Evenson, A. R. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.01.017 · Cited by 85
Blaauw, B., Mammucari, C., Toniolo, L., Agatea, L., Abraham, R., Sandri, M., Reggiani, C., & Schiaffino, S. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn264 · Cited by 84
Self-citationSIRT1–NOX4 signaling axis regulates cancer cachexia
Dasgupta, A., Shukla, S. K., Vernucci, E., King, R. J., Abrego, J., Mulder, S. E., Mullen, N. J., Graves, G., Buettner, K. B., Thakur, R. K., et al. (2020) · The Journal of Experimental Medicine · doi:10.1084/jem.20190745 · Cited by 87
Deletion of skeletal muscle Akt1/2 causes osteosarcopenia and reduces lifespan in mice
Sasako, T., Umehara, T., Soeda, K., Kaneko, K., Suzuki, M., Kobayashi, N., Okazaki, Y., Tamura‐Nakano, M., Chiba, T., Accili, D., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-33008-2 · Cited by 88
Signalling and the control of skeletal muscle size
Otto, A., & Patel, K. (2010) · Experimental Cell Research · doi:10.1016/j.yexcr.2010.04.009 · Cited by 84
Yang, H., Zhao, R., Yang, H.-Y., & Lee, M. (2005) · Oncogene · doi:10.1038/sj.onc.1208352 · Cited by 84
Evaluation of Akt/mTOR activity in muscle atrophy after rotator cuff tears in a rat model
Liu, X., Joshi, S. K., Samagh, S. P., Dang, Y., Laron, D., Lovett, D. H., Bodine, S. C., Kim, H. T., & Feeley, B. T. (2012) · Journal of Orthopaedic Research® · doi:10.1002/jor.22096 · Cited by 83
The Molecular Mechanisms of Calpains Action on Skeletal Muscle Atrophy
HUANG, J., & Zhu, X. (2016) · Physiological Research · doi:10.33549/physiolres.933087 · Cited by 88
Cisternas, F., Morales, M. G., Meneses, C., Simon, F., Brandan, E., Abrigo, J., Vazquez, Y., & Cabello-Verrugio, C. (2015) · Clinical Science · doi:10.1042/cs20140215 · Cited by 83
Prevention of Disuse Muscle Atrophy by Dietary Ingestion of 8-Prenylnaringenin in Denervated Mice
Mukai, R., Horikawa, H., Fujikura, Y., Kawamura, T., Nemoto, H., Nikawa, T., & Terao, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0045048 · Cited by 83
Nutritional status in chronic obstructive pulmonary disease: Role of hypoxia
Raguso, C. A., & Luthy, C. (2010) · Nutrition · doi:10.1016/j.nut.2010.07.009 · Cited by 85
Mechanisms and Clinical Applications of Glucocorticoid Steroids in Muscular Dystrophy
Quattrocelli, M., Zelikovich, A. S., Salamone, I. M., Fischer, J. A., & McNally, E. M. (2020) · Journal of Neuromuscular Diseases · doi:10.3233/jnd-200556 · Cited by 82
Huang, M., Yan, Y., Deng, Z., Zhou, L., She, M., Yang, Y., Zhang, M., & Wang, D. (2023) · Phytomedicine · doi:10.1016/j.phymed.2023.154766 · Cited by 83
Insulin and aging – a disappointing relationship
Kolb, H., Kempf, K., & Martin, S. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1261298 · Cited by 92
Palstra, A. P., Rovira, M., Rizo‐Roca, D., Torrella, J. R., Spaink, H. P., & Planas, J. V. (2014) · BMC Genomics · doi:10.1186/1471-2164-15-1136 · Cited by 88
Seiliez, I., Gutiérrez, J., Salmerón, C., Cassy, S., Chauvin, C., Dias, K., Kaushik, S., Tesseraud, S., & Panserat, S. (2010) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2010.06.011 · Cited by 89
Zhang, H., Sun, L., Liang, J., Yu, W., Zhang, Y., Wang, Y., Chen, Y., Li, R., Sun, X., & Shang, Y. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601306 · Cited by 81
Activin A induces skeletal muscle catabolism via p38β mitogen‐activated protein kinase
Ding, H. J., Zhang, G., Sin, K. W. T., Liu, Z., Lin, R., Li, M., & Li, Y. (2016) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12145 · Cited by 86
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
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