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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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Lara‐Pezzi, E., Winn, N., Paul, A. C., McCullagh, K. J. A., Slominsky, E., Santini, M. P., Mourkioti, F., Sarathchandra, P., Fukushima, S., Suzuki, K., et al. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200704179 · Cited by 69
Salanova, M., Gelfi, C., Moriggi, M., Vasso, M., Viganò, A., Minafra, L., Bonifacio, G., Schiffl, G., Gutsmann, M., Felsenberg, D., et al. (2014) · The FASEB Journal · doi:10.1096/fj.14-252825 · Cited by 68
GSK3-β promotes calpain-1–mediated desmin filament depolymerization and myofibril loss in atrophy
Aweida, D., Rudesky, I., Volodin, A., Shimko, E., & Cohen, S. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201802018 · Cited by 73
Iron Metabolism of the Skeletal Muscle and Neurodegeneration
Hałoń, M., Borkowska, A., Herman-Antosiewicz, A., & Antosiewicz, J. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00165 · Cited by 73
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Li, Z., Liu, C., Li, S., Li, T., Li, Y., Wang, N., Bao, X., Peng, X., & Liu, S. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.681267 · Cited by 73
Garibotto, G., Sofia, A., Russo, R., Paoletti, E., Bonanni, A., Parodi, E. L., Viazzi, F. C., & Verzola, D. (2015) · Kidney International · doi:10.1038/ki.2015.247 · Cited by 69
DHPR α1S subunit controls skeletal muscle mass and morphogenesis
Piétri‐Rouxel, F., Gentil, C., Vassilopoulos, S., Baas, D., Mouisel, É., Ferry, A., Vignaud, A., Hourdé, C., Marty, I., Schaeffer, L., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.366 · Cited by 68
Mitochondrial biogenesis and fragmentation as regulators of protein degradation in striated muscles
Romanello, V., & Sandri, M. (2012) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2012.08.001 · Cited by 70
Self-citationMST1, a key player, in enhancing fast skeletal muscle atrophy
Wei, B. K., Dui, W., Liu, D., Yan, X., Yuan, Z., & Ji, G. (2013) · BMC Biology · doi:10.1186/1741-7007-11-12 · Cited by 71
Expression and activity of C/EBPβ and δ are upregulated by dexamethasone in skeletal muscle
Yang, H., Mammen, J. M. V., Wei, W., Menconi, M. J., Evenson, A. R., Fareed, M. U., Petkova, V., & Hasselgren, P.-O. J. (2005) · Journal of Cellular Physiology · doi:10.1002/jcp.20278 · Cited by 70
Trobec, K. Č., von Haehling, S., Anker, S. D., & Lainščak, M. (2011) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-011-0043-5 · Cited by 69
Taetzsch, T., Tenga, M. J., & Valdez, G. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.2992-16.2016 · Cited by 69
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Stevenson, E. J., Koncarevic, A., Giresi, P. G., Jackman, R. W., & Kandarian, S. C. (2004) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01055.2004 · Cited by 71
Lambertucci, A. C., Lambertucci, R. H., Hirabara, S. M., Curi, R., Moriscot, A. S., Alba-Loureiro, T. C., Guimarães-Ferreira, L., Levada-Pires, A. C., Vasconcelos, D. A. A., Sellitti, D. F., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0050390 · Cited by 67
Catechins enhance skeletal muscle performance
Li, P., Liu, A., Xiong, W., Lin, H., Xiao, W., Huang, J., Zhang, S., & Liu, Z. (2019) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2018.1549534 · Cited by 67
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Kumagai, H., Coelho, A. R., Wan, J., Mehta, H. H., Yen, K., Huang, A., Zempo, H., Fuku, N., Maeda, S., Oliveira, P. J., et al. (2021) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00275.2020 · Cited by 68
Myostatin: Basic biology to clinical application
Esposito, P. B., Picciotto, D., Battaglia, Y., Costigliolo, F., Viazzi, F. C., & Verzola, D. (2022) · Advances in clinical chemistry · doi:10.1016/bs.acc.2021.09.006 · Cited by 72
Jones, A. J., Hwang, D., Narayanan, R., Miller, D. D., & Dalton, J. T. (2010) · Endocrinology · doi:10.1210/en.2010-0150 · Cited by 67
Calcineurin: A poorly understood regulator of muscle mass
Hudson, M. B., & Price, S. R. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.06.029 · Cited by 67
Calura, E., Cagnin, S., Raffaello, A., Laveder, P., Lanfranchi, G., & Romualdi, C. (2008) · BMC Genomics · doi:10.1186/1471-2164-9-630 · Cited by 67
The translation inhibitor pateamine A prevents cachexia-induced muscle wasting in mice
Marco, S. D., Cammas, A., Lian, X. J., Kovács, E. N., Ma, J. F., Hall, D. T., Mazrouï, R., Richardson, J., Pelletier, J., & Gallouzi, I. (2012) · Nature Communications · doi:10.1038/ncomms1899 · Cited by 66
Joassard, O. R., Amirouche, A., Gallot, Y. S., Desgeorges, M. M., Castells, J., Durieux, A., Berthon, P. M., & Freyssenet, D. G. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.07.019 · Cited by 70
Bricceno, K. V., Sampognaro, P. J., Meerbeke, J. P. V., Sumner, C. J., Fischbeck, K. H., & Burnett, B. G. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds286 · Cited by 70
Lü, T., Chai, Q., Yu, L., d’Uscio, L. V., Katušić, Z. S., He, T., & Lee, H.-C. (2012) · Diabetes · doi:10.2337/db11-1658 · Cited by 68
Constantin, D., Constantin‐Teodosiu, D., Layfield, R., Tsintzas, K., Bennett, A. J., & Greenhaff, P. L. (2007) · The Journal of Physiology · doi:10.1113/jphysiol.2007.135459 · Cited by 69
Feeding critically ill patients the right ‘whey’: thinking outside of the box. A personal view
Marik, P. E. (2015) · Annals of Intensive Care · doi:10.1186/s13613-015-0051-2 · Cited by 69
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Attaix, D., & Baracos, V. E. (2010) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0b013e328338b9a6 · Cited by 73
Skeletal muscle atrogenes: From rodent models to human pathologies
Taillandier, D., & Polge, C. (2019) · Biochimie · doi:10.1016/j.biochi.2019.07.014 · Cited by 66
Ageta, H., & Tsuchida, K. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03246-7 · Cited by 67
Shi, H., Zeng, C., Ricome, A., Hannon, K., Grant, A. L., & Gerrard, D. E. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00466.2006 · Cited by 69
Zhou, N., Lee, W. R., & Abasht, B. (2015) · BMC Genomics · doi:10.1186/s12864-015-1364-0 · Cited by 72
Muscle-specific GSK-3β ablation accelerates regeneration of disuse-atrophied skeletal muscle
Pansters, N. A. M., Schols, A. M. W. J., Verhees, K. J. P., de Theije, C. C., Snepvangers, F. J. M., KELDERS, M. C. J. M., Ubags, N. D. J., Haegens, A., & LANGEN, R. C. J. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.12.006 · Cited by 66
Qin, W., Pan, J., Wu, Y., Bauman, W. A., & Cardozo, C. P. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.11.061 · Cited by 68
MacDonald, E. M., Andrés‐Mateos, E., Mejías, R., Simmers, J. L., Mi, R., Park, J.-S., Ying, S., Höke, A., Lee, S., & Cohn, R. D. (2014) · Disease Models & Mechanisms · doi:10.1242/dmm.014126 · Cited by 67
Re Cecconi, A. D., Forti, M., Chiappa, M., Zhu, Z., Zingman, L. V., Cervo, L., Beltrame, L., Marchini, S., & Piccirillo, R. (2019) · Cancers · doi:10.3390/cancers11101541 · Cited by 66
Cai, X., Yuan, Y., Liao, Z., Xing, K., Zhu, C., Xu, Y., Yu, L., Wang, L., Wang, S., Zhu, X., et al. (2018) · The FASEB Journal · doi:10.1096/fj.201700670r · Cited by 65
Mirzoev, T. M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21217940 · Cited by 65
Chen, B., Xu, J., He, X., Xu, H., Li, G., Du, H., Nie, Q., & Zhang, X. (2015) · PLoS ONE · doi:10.1371/journal.pone.0137087 · Cited by 71
Paez, H. G., Pitzer, C. R., & Alway, S. E. (2023) · Cells · doi:10.3390/cells12020249 · Cited by 71
SMAD3 augments FoxO3-induced MuRF-1 promoter activity in a DNA-binding-dependent manner
Bollinger, L. M., Witczak, C. A., Houmard, J. A., & Brault, J. J. (2014) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00391.2013 · Cited by 67
Genetics vs. entropy: Longevity factors suppress the NF-κB-driven entropic aging process
Salminen, A., & Kaarniranta, K. (2009) · Ageing Research Reviews · doi:10.1016/j.arr.2009.11.001 · Cited by 67
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Tando, T., Hirayama, A., Furukawa, M., Sato, Y., Kobayashi, T., Funayama, A., Kanaji, A., Wu, H., Watanabe, R., Morita, M., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.680579 · Cited by 70
Protein turnover in cardiac cell growth and survival
Hedhli, N., Pelat, M., & Depre, C. (2005) · Cardiovascular Research · doi:10.1016/j.cardiores.2005.06.025 · Cited by 65
Morales, M. G., Olguín, H., Di Capua, G., Brandan, E., Simon, F., & Cabello-Verrugio, C. (2015) · Clinical Science · doi:10.1042/cs20140840 · Cited by 62
Molecular mechanisms of cancer cachexia‑induced muscle atrophy (Review)
Yang, W., Huang, J., Wu, H., Wang, Y., Du, Z., Ling, Y., Wang, W., Wu, Q., & Gao, W. (2020) · Molecular Medicine Reports · doi:10.3892/mmr.2020.11608 · Cited by 67
Chabi, B., Adhihetty, P. J., O′Leary, M. F. N., Menzies, K. J., & Hood, D. A. (2009) · Journal of Applied Physiology · doi:10.1152/japplphysiol.91451.2008 · Cited by 64
Identification of cardiac myocytes as the target of interleukin 11, a cardioprotective cytokine
Kimura, R., Maeda, M., Arita, A., Oshima, Y., Obana, M., Ito, T., Yamamoto, Y., Mohri, T., Kishimoto, T., Kawase, I., et al. (2007) · Cytokine · doi:10.1016/j.cyto.2007.05.011 · Cited by 64
Reed, S. A., Senf, S. M., Cornwell, E. W., Kandarian, S. C., & Judge, S. M. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.01.059 · Cited by 62
PKB signaling and atrogene expression in skeletal muscle of aged mice
Gaugler, M., Brown, A., Merrell, E., DiSanto‐Rose, M., Rathmacher, J. A., & Reynolds, T. (2011) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00175.2011 · Cited by 66
Keller, J., Ringseis, R., Koc, A., Lukas, I., Kluge, H., & Eder, K. (2011) · animal · doi:10.1017/s1751731111001327 · Cited by 65
Insulin-Like Growth Factor I: The Yin and Yang of Muscle Atrophy
Heszele, M. F. C., & Price, S. R. (2004) · Endocrinology · doi:10.1210/en.2004-1037 · Cited by 64
Pugh, J. K., Faulkner, S. H., Jackson, A. P., King, J. A., & Nimmo, M. A. (2015) · Physiological Reports · doi:10.14814/phy2.12364 · Cited by 63
Differences in muscle satellite cell dynamics during muscle hypertrophy and regeneration
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Cleveland, B. M., & Evenhuis, J. P. (2010) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2010.06.010 · Cited by 64
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Sheriff, S., Kadeer, N., Joshi, R., Friend, L. A., James, J. H., & Balasubramaniam, A. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2011.12.021 · Cited by 64
Pires-Oliveira, M., Maragno, A. L., Parreiras‐e‐Silva, L. T., Chiavegatti, T., Gomes, M. D., & Godinho, R. O. (2009) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00490.2009 · Cited by 63
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Jones, A., Friedrich, K., Rohm, M., Schäfer, M., Algire, C., Kulozik, P., Seibert, O., Müller‐Decker, K., Sijmonsma, T., Strzoda, D., et al. (2013) · EMBO Molecular Medicine · doi:10.1002/emmm.201201869 · Cited by 64
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Yamazaki, Y., Kamei, Y., Sugita, S., Akaike, F., Kanai, S., Miura, S., Hirata, Y., Troen, B. R., Kitamura, T., Nishino, I., et al. (2010) · Biochemical Journal · doi:10.1042/bj20091346 · Cited by 63
Toledo, M., Busquets, S., Penna, F., Zhou, X., Marmonti, E., Betancourt, A., Massa, D., López-Soriano, F. J., Han, H. Q., & Argilés, J. M. A. (2015) · International Journal of Cancer · doi:10.1002/ijc.29930 · Cited by 63
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Mayeuf-Louchart, A., Thorel, Q., Delhaye, S., Beauchamp, J., Duhem, C., Danckaert, A., Lancel, S., Pourcet, B., Woldt, E., Boulinguiez, A., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-14596-2 · Cited by 66
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Manickam, R., Oh, H. Y. P., Tan, C. K., Paramalingam, E., & Wahli, W. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082418 · Cited by 66
Rinaldi, C., Bott, L. C., Chen, K., Harmison, G. G., Katsuno, M., Sobue, G., Pennuto, M., & Fischbeck, K. H. (2012) · Molecular Medicine · doi:10.2119/molmed.2012.00271 · Cited by 63
Hypercatabolism in dialysis patients
Raj, D. S., Sun, Y., & Tzamaloukas, A. H. (2008) · Current Opinion in Nephrology & Hypertension · doi:10.1097/mnh.0b013e32830d5bfa · Cited by 66
Zanchi, N. E., Filho, M. A. D. S., Felitti, V., Nicastro, H., Lorenzeti, F. M., & Lancha, A. H. (2010) · Journal of Cellular Physiology · doi:10.1002/jcp.22141 · Cited by 62
Uchida, T., Sakashita, Y., Kitahata, K., Yamashita, Y., Tomida, C., Kimori, Y., Komatsu, A., Hirasaka, K., Ohno, A., Nakao, R., et al. (2018) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00184.2017 · Cited by 62
Cellular and molecular features of neurogenic skeletal muscle atrophy
Ehmsen, J. T., & Höke, A. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113379 · Cited by 63
Solagna, F., Tezze, C., Lindenmeyer, M. T., Lu, S. Y., Wu, G., Liu, S., Zhao, Y., Mitchell, R., Meyer, C., Omairi, S., et al. (2021) · Journal of Clinical Investigation · doi:10.1172/jci135821 · Cited by 66
Self-citationSzekeres, Z., Nagy, A., Jahner, K., & Szabados, E. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25158214 · Cited by 67
Soyiri, I., Collaborators, G. 2. D., Abbafati, C., Machado, D. B., Cislaghi, B., Salman, O. M., Karanikolos, M., McKee, M., Abbas, K. M., Brady, O. J., et al. (2020) · Repository@Hull (Worktribe) (University of Hull) · doi:10.1016/s0140-6736%2820%2930977-6 · Cited by 62
Zhang, W., Yano, N., Deng, M., Mao, Q., Shaw, S. K., & Tseng, Y. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026581 · Cited by 62
Cleveland, B. M., Weber, G. M., Blemings, K. P., & Silverstein, J. T. (2009) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00272.2009 · Cited by 63
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Nicot, A.-S., Verso, F. L., Ratti, F., Pilot‐Storck, F., Streichenberger, N., Sandri, M., Schaeffer, L., & Goillot, E. (2014) · Autophagy · doi:10.4161/auto.28479 · Cited by 61
Self-citationCOPD elicits remodeling of the diaphragm and vastus lateralis muscles in humans
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Alliouachene, S., Tuttle, R. L., Boumard, S., Lapointe, T., Bérissi, S., Germain, S., Jaubert, F., Tosh, D., Birnbaum, M. J., & Pende, M. (2008) · Journal of Clinical Investigation · doi:10.1172/jci35237 · Cited by 64
Glucocorticoids Enhance Muscle Proteolysis through a Myostatin-Dependent Pathway at the Early Stage
Wang, R., Jiao, H., Zhao, J., Wang, X., & Lin, H. (2016) · PLoS ONE · doi:10.1371/journal.pone.0156225 · Cited by 68
Volodin, A., Kosti, I., Goldberg, A. L., & Cohen, S. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1612988114 · Cited by 62
Self-citationFisher, A. G., Seaborne, R. A., Hughes, T. M., Gutteridge, A., Stewart, C., Coulson, J., Sharples, A., & Jarvis, J. (2017) · The FASEB Journal · doi:10.1096/fj.201700089rr · Cited by 54
Proteolytic Mechanisms, Not Malnutrition, Cause Loss of Muscle Mass in Kidney Failure
Mitch, W. E. (2006) · Journal of Renal Nutrition · doi:10.1053/j.jrn.2006.04.014 · Cited by 61
Isotretinoin and FoxO1: A scientific hypothesis.
Melnik, B. C. (2011) · Europe PMC (PubMed Central) · doi:10.4161/derm.3.3.15331 · Cited by 62
Liu, H.-W., Chang, Y.-C., Chan, Y.-C., Hu, S.-H., Liu, M.-Y., & Chang, S.-J. (2020) · Biogerontology · doi:10.1007/s10522-020-09867-x · Cited by 60
Ozaki, Y., Ohashi, K., Otaka, N., Kawanishi, H., Takikawa, T., Fang, L., Takahara, K., Tatsumi, M., Ishihama, S., Takefuji, M., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-40435-2 · Cited by 63
Hanson, A. M., Harrison, B. C., Young, M. H., Stodieck, L., & Ferguson, V. L. (2012) · Muscle & Nerve · doi:10.1002/mus.23753 · Cited by 65
Calpain small-1 modulates Akt/FoxO3A signaling and apoptosis through PP2A
Bertoli, C., Copetti, T., Lam, E. W. ‐., Demarchi, F., & Schneider, C. (2008) · Oncogene · doi:10.1038/onc.2008.425 · Cited by 61
Bongers, K. S., Fox, D. K., Kunkel, S. D., Stebounova, L. V., Murry, D. J., Pufall, M. A., Ebert, S. M., Dyle, M. C., Bullard, S. A., Dierdorff, J. M., et al. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00472.2014 · Cited by 64
Bonifacio, A., Mullen, P. J., Mityko, I. S., Navegantes, L. C. C., Bouitbir, J., & Krähenbühl, S. (2014) · Archives of Toxicology · doi:10.1007/s00204-014-1378-4 · Cited by 61
Insulin and amino acid availability regulate atrogin-1 in avian QT6 cells
Tesseraud, S., Métayer, S., Ezzine, S. B.-O., Crochet, S., Cailleau-Audouin, E., Derouet, M., & Seiliez, I. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.03.131 · Cited by 61
Stockley, R. A. (2009) · Current Medical Research and Opinion · doi:10.1185/03007990902868971 · Cited by 61
Pigna, E., Simonazzi, E., Sanna, K., Bernadzki, K. M., Proszynski, T., Heil, C., Palacios, D., Adamo, S., & Moresi, V. (2019) · EBioMedicine · doi:10.1016/j.ebiom.2019.01.038 · Cited by 61
Callaway, C. S., Delitto, A. E., D’Lugos, A. C., Patel, R., Nosacka, R. L., Delitto, D., Deyhle, M. R., Trevino, J. G., Judge, S. M., & Judge, A. R. (2019) · Cancers · doi:10.3390/cancers11121863 · Cited by 61
Oyabu, M., Takigawa, K., Mizutani, S., Hatazawa, Y., Fujita, M., Ohira, Y., Sugimoto, T., Suzuki, O., Tsuchiya, K., Suganami, T., et al. (2022) · The FASEB Journal · doi:10.1096/fj.202101385rr · Cited by 63
Bo, T., & Fujii, J. (2024) · Molecules · doi:10.3390/molecules30010056 · Cited by 70
Baviera, A. M., Zanon, N. M., Navegantes, L. C. C., & Kettelhut, Í. D. C. (2009) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2009.09.028 · Cited by 60
Molecular mechanism underlying muscle mass retention in hibernating bats: Role of periodic arousal
Lee, K., So, H., Gwag, T., Ju, H., Lee, J.-W., Yamashita, M., & Choi, I. (2009) · Journal of Cellular Physiology · doi:10.1002/jcp.21952 · Cited by 60
Moresi, V., Garcia-Alvarez, G., Pristerà, A., Rizzuto, E., Albertini, M. C., Rocchi, M., Marazzi, G., Sassoon, D., Adamo, S., & Coletti, D. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005570 · Cited by 60
Sirtuin inhibition protects from the polyalanine muscular dystrophy protein PABPN1
Catoire, H., Pasco, M. Y., Abu‐Baker, A., Holbert, S., Tourette, C., Brais, B., Rouleau, G. A., Parker, J. A., & Néri, C. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn109 · Cited by 65
Oyabu, J., Yamaguchi, O., Hikoso, S., Takeda, T., Oka, T., Murakawa, T., Yasui, H., Ueda, H., Nakayama, H., Taneike, M., et al. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.10.135 · Cited by 60
Gene expression and muscle fiber function in a porcine ICU model
Banduseela, V. C., Ochala, J., Chen, Y., Göransson, H., Norman, H. S., Radell, P. J., Eriksson, L. I., Hoffman, E. P., & Larsson, L. (2009) · Physiological Genomics · doi:10.1152/physiolgenomics.00026.2009 · Cited by 62
Wu, C., Cornwell, E. W., Jackman, R. W., & Kandarian, S. C. (2014) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00361.2013 · Cited by 65
Skeletal muscle atrophy: disease-induced mechanisms may mask disuse atrophy
Malavaki, C. J., Sakkas, G. K., Mitrou, G. I., Kalyva, A., Stefanidis, I., Myburgh, K. H., & Karatzaferi, C. (2015) · Journal of Muscle Research and Cell Motility · doi:10.1007/s10974-015-9439-8 · Cited by 65
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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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.
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