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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]
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]
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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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Items 201–300 of 1,032
Disruption of either the Nfkb1 or the Bcl3 gene inhibits skeletal muscle atrophy
Hunter, R. B., & Kandarian, S. C. (2004) · Journal of Clinical Investigation · doi:10.1172/jci21696 · Cited by 256
Aging Hallmarks: The Benefits of Physical Exercise
Rebelo-Marques, A., De Sousa Lages, A., Andrade, R., Ribeiro, C. F., Mota-Pinto, A., Carrilho, F., & Espregueira-Mendes, J. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00258 · Cited by 246
Costa, A., Toschi, A., Murfuni, I., Pelosi, L., Sica, G., Adamo, S., & Scicchitano, B. M. (2014) · BioMed Research International · doi:10.1155/2014/235426 · Cited by 248
Li, H., Willis, M. S., Lockyer, P. P., Miller, N., McDonough, H., Glass, D. J., & Patterson, C. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31757 · Cited by 254
Kidney cachexia or protein‐energy wasting in chronic kidney disease: facts and numbers
Koppe, L., Fouque, D. P., & Kalantar‐Zadeh, K. (2019) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12421 · Cited by 254
Blaauw, B., Canato, M., Agatea, L., Toniolo, L., Mammucari, C., Masiero, E., Abraham, R., Sandri, M., Schiaffino, S., & Reggiani, C. (2009) · The FASEB Journal · doi:10.1096/fj.09-131870 · Cited by 244
Self-citationThe Extending Network of FOXO Transcriptional Target Genes
van der Vos, K. E., & Coffer, P. J. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3419 · Cited by 249
TNF‐related weak inducer of apoptosis (TWEAK) is a potent skeletal muscle‐wasting cytokine
Dogra, C., Changoua, H., Wedhas, N., Qin, X., Wergedal, J. E., & Kumar, A. (2007) · The FASEB Journal · doi:10.1096/fj.06-7537com · Cited by 248
Skeletal Muscle Wasting and Renewal: A Pivotal Role of Myokine IL-6
Belizário, J. E., Fontes-Oliveira, C. C., Borges, J. P., Kashiabara, J. A., & Vannier, E. (2016) · SpringerPlus · doi:10.1186/s40064-016-2197-2 · Cited by 244
Muscle Atrophy and Hypertrophy Signaling in Patients with Chronic Obstructive Pulmonary Disease
Doucet, M., Russell, A. P., Léger, B., Debigaré, R., Joanisse, D. R., Caron, M.-A., LeBlanc, P., & Maltais, F. (2007) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200605-704oc · Cited by 243
Pathophysiology of muscle dysfunction in COPD
Gea, J., Agustí, A. G. N., & Roca, J. (2013) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00981.2012 · Cited by 250
Stress-induced Skeletal Muscle Gadd45a Expression Reprograms Myonuclei and Causes Muscle Atrophy
Ebert, S. M., Dyle, M. C., Kunkel, S. D., Bullard, S. A., Bongers, K. S., Fox, D. K., Dierdorff, J. M., Foster, E. D., & Adams, C. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.374777 · Cited by 221
The role of FOXO in the regulation of metabolism
Gross, D. N., Wan, M., & Birnbaum, M. J. (2009) · Current Diabetes Reports · doi:10.1007/s11892-009-0034-5 · Cited by 244
IL-6 and Serum Amyloid A Synergy Mediates Angiotensin II–Induced Muscle Wasting
Zhang, L., Du, J., Hu, Z., Han, G., Delafontaine, P., García, G., & Mitch, W. E. (2009) · Journal of the American Society of Nephrology · doi:10.1681/asn.2008060628 · Cited by 246
Metabolic functions of glucocorticoid receptor in skeletal muscle
Kuo, T., Harris, C. A., & Wang, J.-C. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2013.03.003 · Cited by 254
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Backer, J. (2016) · Biochemical Journal · doi:10.1042/bcj20160170 · Cited by 247
FoxO1, the transcriptional chief of staff of energy metabolism
Kousteni, S. (2011) · Bone · doi:10.1016/j.bone.2011.06.034 · Cited by 248
Bailey, J. L., Zheng, B., Hu, Z., Price, S. R., & Mitch, W. E. (2006) · Journal of the American Society of Nephrology · doi:10.1681/asn.2004100842 · Cited by 238
Mechanisms of skeletal muscle aging: insights from Drosophila and mammalian models
Demontis, F., Piccirillo, R., Goldberg, A. L., & Perrimon, N. (2013) · Disease Models & Mechanisms · doi:10.1242/dmm.012559 · Cited by 238
Self-citationPerry, B. D., Caldow, M. K., Brennan‐Speranza, T. C., Sbaraglia, M., Jerums, G., GARNHAM, A. P., Wong, C. Y., Levinger, P., Haq, M. A. U., Hare, D. L., et al. (2016) · PubMed · Cited by 239
Insulin resistance: a contributing factor to age-related muscle mass loss?
Guillet, C., & Boirie, Y. (2005) · Diabetes & Metabolism · doi:10.1016/s1262-3636(05)73648-x · Cited by 245
Muscle sparing in muscle RING finger 1 null mice: response to synthetic glucocorticoids
Baehr, L. M., Furlow, J. D., & Bodine, S. C. (2011) · The Journal of Physiology · doi:10.1113/jphysiol.2011.212845 · Cited by 234
SRT 2104 extends survival of male mice on a standard diet and preserves bone and muscle mass
Mercken, E. M., Mitchell, S. J., Martín‐Montalvo, A., Minor, R. K., Almeida, M., Gomes, A. P., Scheibye‐Knudsen, M., Palacios, H. H., Licata, J. J., Zhang, Y., et al. (2014) · Aging Cell · doi:10.1111/acel.12220 · Cited by 238
Inhibition of prostaglandin-degrading enzyme 15-PGDH rejuvenates aged muscle mass and strength
Palla, A. R., Ravichandran, M., Wang, Y. X., Alexandrova, L., Yang, A. V., Kraft, P., Holbrook, C. A., Schürch, C. M., Ho, A. T. V., & Blau, H. M. (2021) · Science · doi:10.1126/science.abc8059 · Cited by 232
Diaphragm Muscle Fiber Weakness and Ubiquitin–Proteasome Activation in Critically Ill Patients
Hooijman, P. E., Beishuizen, A., Witt, C. C., de Waard, M. C., Girbes, A. R. J., de Man, A., Niessen, H. W. M., Manders, E., van Hees, H. W. H., van den Brom, C. E., et al. (2015) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201412-2214oc · Cited by 234
Varma, V., Yao-Borengasser, A., Rasouli, N., Nolen, G. T., Phanavanh, B., Starks, T., Gurley, C., Simpson, P., McGehee, R. E., Kern, P. A., et al. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90885.2008 · Cited by 229
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
Lysosome: regulator of lipid degradation pathways
Settembre, C., & Ballabio, A. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.06.006 · Cited by 231
Altun, M., Besche, H. C., Overkleeft, H. S., Piccirillo, R., Edelmann, M. J., Kessler, B. M., Goldberg, A. L., & Ulfhake, B. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.129718 · Cited by 226
Self-citationThe bone morphogenetic protein axis is a positive regulator of skeletal muscle mass
Winbanks, C. E., Chen, J. L., Qian, H., Liu, Y., Bernardo, B. C., Beyer, C., Watt, K. I., Thomson, R. E., Connor, T., Turner, B. J., et al. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201211134 · Cited by 225
Sex-Related Differences in Gene Expression in Human Skeletal Muscle
Welle, S., Tawil, R., & Thornton, C. A. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001385 · Cited by 224
“In its active non-phosphorylated state, this transcription factor stimulates expression of the ubiquitin ligase atrogin-1 (also known as MAFbx or F-box protein 32) [47].”
STAT3 in the systemic inflammation of cancer cachexia
Zimmers, T. A., Fishel, M. L., & Bonetto, A. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.02.009 · Cited by 231
Moussa, M., Lajeunesse, D., Hilal, G., Atat, O. E., Haykal, G., Serhal, R., Chalhoub, A., Khalil, C., & Alaaeddine, N. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.02.012 · Cited by 227
Skeletal muscle dysfunction in patients with chronic obstructive pulmonary disease
Hussain, S., Cheol, K., & Mofarrahi, M. (2008) · International Journal of Chronic Obstructive Pulmonary Disease · doi:10.2147/copd.s4480 · Cited by 224
Reed, S. A., Sandesara, P. B., Judge, S. M., & Judge, A. R. (2011) · The FASEB Journal · doi:10.1096/fj.11-189977 · Cited by 231
FoxO Transcription Factors Support Oxidative Stress Resistance in Human Chondrocytes
Akasaki, Y., Álvarez-García, Ó., Saito, M., Caramés, B., Iwamoto, Y., & Lotz, M. (2014) · Arthritis & Rheumatology · doi:10.1002/art.38868 · Cited by 228
FOXO transcription factors as mediators of stress adaptation
Colman, M. J. R., Dansen, T. B., & Burgering, B. M. T. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00649-0 · Cited by 228
Role of Oxidative Stress as Key Regulator of Muscle Wasting during Cachexia
Ábrigo, J., Elorza, Á. A., Riedel, C. A., Vilos, C., Simón, F., Cabrera, D., Estrada, L. D., & Cabello‐Verrugio, C. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/2063179 · Cited by 225
Hyatt, H. W., Deminice, R., Yoshihara, T., & Powers, S. K. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.11.005 · Cited by 226
Clavel, S., Coldefy, A.-S., Kurkdjian, E., Salles, J., Margaritis, I., & Dérijard, B. (2006) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2006.07.005 · Cited by 233
Role of IGF-I in skeletal muscle mass maintenance
Clemmons, D. R. (2009) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2009.04.002 · Cited by 225
Brault, J. J., Jespersen, J. G., & Goldberg, A. L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.113092 · Cited by 217
Self-citationXu, J., Li, R., Workeneh, B., Dong, Y., Wang, X., & Hu, Z. (2012) · Kidney International · doi:10.1038/ki.2012.84 · Cited by 218
Bouzakri, K., Zachrisson, A., Al‐Khalili, L., Zhang, B. B., Koistinen, H. A., Krook, A., & Zierath, J. R. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.04.008 · Cited by 222
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Vainshtein, A., & Sandri, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21134759 · Cited by 222
Self-citationPalazzolo, I., Stack, C. M., Kong, L., Musarò, A., Adachi, H., Katsuno, M., Sobue, G., Taylor, J. P., Sumner, C. J., Fischbeck, K. H., et al. (2009) · Neuron · doi:10.1016/j.neuron.2009.07.019 · Cited by 217
Braun, T. P., Zhu, X., Szumowski, M., Scott, G. D., Grossberg, A. J., Levasseur, P. R., Graham, K., Khan, S., Damaraju, S., Colmers, W. F., et al. (2011) · Journal of Experimental Medicine · doi:10.1084/jem.20111020 · Cited by 213
Lee, D., & Goldberg, A. L. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.489716 · Cited by 211
Self-citationOxidative stress and ageing: is ageing a cysteine deficiency syndrome?
Dröge, W. (2005) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2005.1770 · Cited by 213
Cohen, S., Zhai, B., Gygi, S. P., & Goldberg, A. L. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201110067 · Cited by 205
Self-citationNovel concepts of acute lung injury and alveolar-capillary barrier dysfunction
Herold, S., Gabrielli, N. M., & Vadász, I. (2013) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00232.2013 · Cited by 210
Intracellular cAMP Sensor EPAC: Physiology, Pathophysiology, and Therapeutics Development
Robichaux, W. G., & Cheng, X. (2018) · Physiological Reviews · doi:10.1152/physrev.00025.2017 · Cited by 222
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van der Vos, K. E., & Coffer, P. J. (2008) · Oncogene · doi:10.1038/onc.2008.22 · Cited by 212
Bohnert, K. R., McMillan, J. D., & Kumar, A. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.25852 · Cited by 223
Hu, Z., Wang, H., Lee, I. H., Du, J., & Mitch, W. E. (2009) · Journal of Clinical Investigation · doi:10.1172/jci38770 · Cited by 205
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Morissette, M. R., Cook, S. A., Buranasombati, C., Rosenberg, M. A., & Rosenzweig, A. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00043.2009 · Cited by 231
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Zhang, P., Chen, X., & Fan, M. (2007) · Medical Hypotheses · doi:10.1016/j.mehy.2006.11.043 · Cited by 209
Gielen, S., Sandri, M., Kozarez, I., Kratzsch, J., Teupser, D., Thiery, J., Erbs, S., Mangner, N., Lenk, K., Hambrecht, R., et al. (2012) · Circulation · doi:10.1161/circulationaha.111.047381 · Cited by 204
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Lagirand-Cantaloube, J., Cornille, K., Csibi, A., Batonnet‐Pichon, S., Leibovitch, M.-P., & Leibovitch, S. A. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004973 · Cited by 218
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Chen, J., Splenser, A. E., Guillory, B., Luo, J., Mendiratta, M., Belinova, B., Halder, T., Zhang, G., Li, Y., & Garcia, J. M. (2015) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12023 · Cited by 201
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Fu, W., Ma, Q., Chen, L., Li, P., Zhang, M., Ramamoorthy, S., Nawaz, Z., Shimojima, T., Wang, H., Yang, Y., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m901758200 · Cited by 209
Sharples, A. P., Hughes, D. C., Deane, C. S., Saini, A. S., Selman, C., & Stewart, C. E. (2015) · Aging Cell · doi:10.1111/acel.12342 · Cited by 204
Mangine, G. T., Hoffman, J. R., Gonzalez, A. M., Townsend, J. R., Wells, A. J., Jajtner, A. R., Beyer, K. S., Boone, C. H., Miramonti, A. A., Wang, R., et al. (2015) · Physiological Reports · doi:10.14814/phy2.12472 · Cited by 204
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Frost, R. A., & Lang, C. H. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00089.2007 · Cited by 200
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Edstrom, E., Altun, M., Hagglund, M., & Ulfhake, B. (2006) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/61.7.663 · Cited by 196
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Romanello, V., & Sandri, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03662-0 · Cited by 197
Self-citationFOXO signaling is required for disuse muscle atrophy and is directly regulated by Hsp70
Judge, S. M., DODD, S. L., & Judge, A. R. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00315.2009 · Cited by 202
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Cheng, Z., & White, M. F. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3370 · Cited by 198
Serra, C., Palacios, D., Mozzetta, C., Forcales, S. V., Morantte, I. G., Ripani, M., Jones, D. R., Du, K., Jhala, U. S., Simone, C., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.08.021 · Cited by 196
Brooks, N. E., & Myburgh, K. H. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00099 · Cited by 206
Rudrappa, S. S., Wilkinson, D. J., Greenhaff, P. L., Smith, K., IDRIS, I. R., & Atherton, P. J. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2016.00361 · Cited by 206
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Schefold, J. C., Wollersheim, T., Grunow, J. J., Luedi, M. M., Z'Graggen, W. J., & Weber‐Carstens, S. (2020) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12620 · Cited by 193
Judson, R. N., Tremblay, A. M., Knopp, P., White, R. B., Urcia, R., De Bari, C., Zammit, P. S., Camargo, F. D., & Wackerhage, H. (2012) · Journal of Cell Science · doi:10.1242/jcs.109546 · Cited by 190
Demontis, F., & Perrimon, N. (2009) · Development · doi:10.1242/dev.027466 · Cited by 191
Abadi, A., Glover, E. I., Isfort, R. J., Raha, S., Safdar, A., Yasuda, N., Kaczor, J. J., Melov, S., Hubbard, A., Qu, X., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006518 · Cited by 189
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Porporato, P. E., Filigheddu, N., Reano, S., Ferrara, M., Angelino, E., Gnocchi, V. F., Prodam, F., Ronchi, G., Fagoonee, S., Fornaro, M., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci39920 · Cited by 194
Nakao, R., Hirasaka, K., Goto, J., Ishidoh, K., Yamada, C., Ohno, A., Okumura, Y., Nonaka, I., Yasutomo, K., Baldwin, K. M., et al. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01347-08 · Cited by 194
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Suzuki, N., Motohashi, N., Uezumi, A., Fukada, S., Yoshimura, T., Itoyama, Y., Aoki, M., Miyagoe‐Suzuki, Y., & Takeda, S. (2007) · Journal of Clinical Investigation · doi:10.1172/jci30654 · Cited by 189
Mendias, C. L., Gumucio, J. P., Davis, M. E., Bromley, C. W., Davis, C. S., & Brooks, S. V. (2011) · Muscle & Nerve · doi:10.1002/mus.22232 · Cited by 192
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Crossland, H., Constantin‐Teodosiu, D., Gardiner, S. M., Constantin, D., & Greenhaff, P. L. (2008) · The Journal of Physiology · doi:10.1113/jphysiol.2008.160150 · Cited by 184
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Aguilar, V. M., Alliouachene, S., Sotiropoulos, A., Sobering, A. K., Athéa, Y., Djouadi, F., Miraux, S., Thiaudière, E., Foretz, M., Viollet, B., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.05.006 · Cited by 189
Self-citation
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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