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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]
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“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 901–1,000 of 1,032
Dzik, K. P., Skrobot, W. R., Kaczor, K. B., Flis, D. J., Karnia, M. J., Libionka, W., Antosiewicz, J., Kloc, W., & Kaczor, J. J. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/6835341 · Cited by 63
Fyfe, J. J., Broatch, J. R., Trewin, A. J., Hanson, E. D., Argus, C. K., GARNHAM, A. P., Halson, S. L., Polman, R. C. J., Bishop, D. J., & Petersen, A. C. (2019) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00127.2019 · Cited by 72
Fraysse, B., Desaphy, J., Rolland, J., Pierno, S., Liantonio, A., Giannuzzi, V., Camerino, C., Didonna, M. P., Cocchi, D., Luca, A. D., et al. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.07.012 · Cited by 60
Anversa, P. (2005) · Circulation Research · doi:10.1161/01.res.0000182212.09147.56 · Cited by 59
Mitochondrial Quality Control in Sarcopenia: Updated Overview of Mechanisms and Interventions
Liu, D., Fan, Y., Tao, X., Pan, W., Wu, Y., Wang, X., He, Y., Xiao, W., & Li, Y. (2021) · Aging and Disease · doi:10.14336/ad.2021.0427 · Cited by 62
Identification of possible genetic polymorphisms involved in cancer cachexia: a systematic review
Tan, B. H. L., Ross, J. A., Kaasa, S., Skorpen, F., & Fearon, K. C. H. (2011) · Journal of Genetics · doi:10.1007/s12041-011-0027-4 · Cited by 57
Hirasaka, K., Maeda, T., Ikeda, C., HARUNA, M., Kohno, S., Abe, T., Ochi, A., Mukai, R., Oarada, M., Kondo, S., et al. (2013) · Journal of Nutritional Science and Vitaminology · doi:10.3177/jnsv.59.317 · Cited by 59
Medeiros, C. D., Frederico, M. J. S., da Luz, G., Pauli, J. R., da Silva, A. S. R., Pinho, R. A., Velloso, L. A., Ropelle, E. R., & de Souza, C. T. (2010) · Journal of Cellular Physiology · doi:10.1002/jcp.22387 · Cited by 59
Akt/protein kinase B in skeletal muscle physiology and pathology
Wu, M., Falasca, M., & Blough, E. R. (2010) · Journal of Cellular Physiology · doi:10.1002/jcp.22353 · Cited by 60
Allen, D. L., Cleary, A. S., Lindsay, S. F., Loh, A. S., & Reed, J. M. (2010) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00504.2010 · Cited by 61
Siddiqui, R. A., Hassan, S., Harvey, K. A., Rasool, T., Das, T., Mukerji, P., & DeMichele, S. J. (2009) · British Journal Of Nutrition · doi:10.1017/s0007114509345250 · Cited by 61
Shavlakadze, T., Anwari, T., Soffe, Z., Cozens, G. S., Mark, P. J., Gondro, C., & Grounds, M. D. (2013) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00027.2013 · Cited by 61
TAK1 regulates skeletal muscle mass and mitochondrial function
Hindi, S. M., Sato, S., Xiong, G., Bohnert, K. R., Gibb, A., Gallot, Y. S., McMillan, J. D., Hill, B. G., Uchida, S., & Kumar, A. (2018) · JCI Insight · doi:10.1172/jci.insight.98441 · Cited by 61
Du, J., Hu, Z., & Mitch, W. E. (2005) · European Journal of Clinical Investigation · doi:10.1111/j.1365-2362.2005.01473.x · Cited by 59
Weber, M. D., Kinscherf, R., Krakowski‐Roosen, H., Aulmann, M., Renk, H., Künkele, A., Edler, L., Kauczor, H., & Hildebrandt, W. (2007) · Journal of Molecular Medicine · doi:10.1007/s00109-007-0220-3 · Cited by 59
Evenson, A. R., Fareed, M. U., Menconi, M. J., Mitchell, J. C., & Hasselgren, P.-O. J. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.06.002 · Cited by 62
Proteasome inhibition improves the muscle of laminin α2 chain-deficient mice.
Carmignac, V., Quéré, R., & Durbeej, M. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddq499 · Cited by 58
Chang, Y.-C., Liu, H.-W., Chan, Y.-C., Hu, S.-H., Liu, M.-Y., & Chang, S.-J. (2020) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2020.108511 · Cited by 57
The Preventive Effect of β-Carotene on Denervation-Induced Soleus Muscle Atrophy in Mice
Ogawa, M., Kariya, Y., Kitakaze, T., Yamaji, R., Harada, N., Sakamoto, T., Hosotani, K., Nakano, Y., & Inui, H. (2013) · British Journal Of Nutrition · doi:10.1017/s0007114512003297 · Cited by 58
IGF-1 treatment reduces weight loss and improves outcome in a rat model of cancer cachexia
Schmidt, K., von Haehling, S., Doehner, W., Palus, S., Anker, S. D., & Springer, J. (2011) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-011-0029-3 · Cited by 60
Brocca, L., Longa, E., Cannavino, J., Seynnes, O., VITO, G. D., McPhee, J. S., Narici, M. V., Pellegrino, M. A., & Bottinelli, R. (2015) · The Journal of Physiology · doi:10.1113/jp271188 · Cited by 60
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van den Berg, M. C. W., & Burgering, B. M. T. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3415 · Cited by 58
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Gardner, S., Anguiano, M., & Rotwein, P. S. (2012) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00259.2012 · Cited by 58
Yuan, Y., Shi, X., Liu, Y., & Yang, G.-S. (2010) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-010-0640-1 · Cited by 59
Paula-Gomes, S., Gonçalves, D. A. P., Baviera, A. M., Zanon, N., Navegantes, L. C. C., & Kettelhut, Í. D. C. (2013) · Hormone and Metabolic Research · doi:10.1055/s-0033-1347209 · Cited by 58
Autophagic Cellular Responses to Physical Exercise in Skeletal Muscle
Tam, B. T., & Siu, P. M. (2014) · Sports Medicine · doi:10.1007/s40279-013-0140-z · Cited by 60
Hanatani, S., Izumiya, Y., Araki, S., Rokutanda, T., Kimura, Y., Walsh, K., & Ogawa, H. (2014) · Journal of the American Society of Nephrology · doi:10.1681/asn.2013091025 · Cited by 58
Self-citationAn optogenetic system for interrogating the temporal dynamics of Akt
Katsura, Y., Kubota, H., Kunida, K., Kanno, A., Kuroda, S., & Ozawa, T. (2015) · Scientific Reports · doi:10.1038/srep14589 · Cited by 57
Gao, J., Cheng, T. S., Qin, A., Pavlos, N. J., Wang, T., Song, K., Wang, Y., Chen, L. K., Zhou, L., Jiang, Q. Y., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.9034 · Cited by 58
Redox modulation of muscle mass and function
Gómez‐Cabrera, M. C., Arc‐Chagnaud, C., Salvador‐Pascual, A., Brioche, T., Chopard, A., González, G. O., & Viña, J. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101531 · Cited by 61
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Memme, J. M., Slavin, M. B., Moradi, N., & Hood, D. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22105179 · Cited by 59
Wu, A.-L., Kim, J., Zhang, C., Unterman, T. G., & Chen, J. (2007) · Endocrinology · doi:10.1210/en.2007-1470 · Cited by 58
Warrier, M., Hinds, T. D., Ledford, K. J., Cash, H. A., Patel, P. R., Bowman, T. A., Stechschulte, L. A., Yong, W., Shou, W., Najjar, S. M., et al. (2010) · Endocrinology · doi:10.1210/en.2009-1158 · Cited by 57
Bialek, P., Morris, C., Parkington, J., St. Andre, M., Owens, J., Yaworsky, P., Seeherman, H., & Jelinsky, S. A. (2011) · Physiological Genomics · doi:10.1152/physiolgenomics.00247.2010 · Cited by 57
Osteoarthritis year in review 2018: biology
Sherwood, J. (2018) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2018.10.005 · Cited by 57
Sidorkiewicz, I., Niemira, M., Maliszewska, K., Erol, A., Bielska, A., Szalkowska, A., Adamska-Patruno, E., Szczerbiński, Ł., Górska, M., & Kretowski, A. J. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9072184 · Cited by 58
Yin, L., Chen, X., Li, N., Jia, W., Wang, N., Hou, B., Yang, H., Zhang, L., Qiang, G., Yang, X., et al. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110977 · Cited by 58
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Gallot, Y. S., & Bohnert, K. R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22052567 · Cited by 61
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Jing, Y., Zuo, Y., Yu, Y., Sun, L., Yu, Z., Ma, S., Zhao, Q., Sun, G., Hu, H., Li, J., et al. (2022) · Protein & Cell · doi:10.1093/procel/pwac061 · Cited by 59
Muscle Wasting in Cancer and Ageing: Cachexia Versus Sarcopenia
Argilés, J. M. A., Busquets, S., Orpí, M., Serpe, R., & López-Soriano, F. J. (2010) · Springer eBooks · doi:10.1007/978-90-481-9713-2_2 · Cited by 56
Forkhead box O transcription factors as possible mediators in the development of major depression
Wang, H., Quirion, R., Little, P. J., Cheng, Y., Feng, Z., Sun, H., Xu, J., & Zheng, W. (2015) · Neuropharmacology · doi:10.1016/j.neuropharm.2015.08.020 · Cited by 58
Okamoto, T., Torii, S., & Machida, S. (2011) · The Journal of Physiological Sciences · doi:10.1007/s12576-011-0175-6 · Cited by 57
Ubiquitination, phosphorylation, and acetylation—triple threat in muscle wasting
Hasselgren, P. (2007) · Journal of Cellular Physiology · doi:10.1002/jcp.21190 · Cited by 57
Furuya, N., Ikeda, S., Sato, S., Soma, S., Ezaki, J., Trejo, J. A. O., Takeda‐Ezaki, M., Fujimura, T., Arikawa‐Hirasawa, E., Tada, N., et al. (2014) · Autophagy · doi:10.4161/auto.27785 · Cited by 57
Mechanisms to explain wasting of muscle and fat in cancer cachexia
Argilés, J. M. A., López-Soriano, F. J., & Busquets, S. (2007) · Current Opinion in Supportive and Palliative Care · doi:10.1097/spc.0b013e3282f34738 · Cited by 58
Zhang, D., He, T., Katušić, Z. S., Lee, H.-C., & Lü, T. (2010) · Circulation Research · doi:10.1161/circresaha.110.228361 · Cited by 57
Nedergaard, A., Vissing, K., Overgaard, K., Kjær, M., & Schjerling, P. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01445.2006 · Cited by 57
Lee, D. H., & Goldberg, A. L. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.685164 · Cited by 59
Self-citationOmairi, S., Matsakas, A., Degens, H., Kretz, O., Hansson, K., Solbrå, A. V., Bruusgaard, J. C., Joch, B., Sartori, R., Giallourou, N., et al. (2016) · eLife · doi:10.7554/elife.16940 · Cited by 59
Self-citationRadigan, K. A., Nicholson, T. T., Welch, L. C., Chi, M., Amarelle, L., Angulo, M., Shigemura, M., Shigemura, A., Runyan, C. E., Morales‐Nebreda, L., et al. (2018) · The Journal of Immunology · doi:10.4049/jimmunol.1701433 · Cited by 57
Argilés, J. M. A., López-Soriano, F. J., & Busquets, S. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.02.001 · Cited by 57
PTEN Expression Contributes to the Regulation of Muscle Protein Degradation in Diabetes
Hu, Z., Lee, I. H., Wang, X., Sheng, H., Zhang, L., Du, J., & Mitch, W. E. (2007) · Diabetes · doi:10.2337/db06-1731 · Cited by 57
Gonçalves, D. A., Silveira, W. A., Manfredi, L. H., Graça, F. A., Armani, A., Bertaggia, E., O´Neill, B. T., Lautherbach, N., Machado, J., Nogara, L., et al. (2019) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12395 · Cited by 56
Self-citationExogenous insulin‐like growth factor 1 attenuates cisplatin‐induced muscle atrophy in mice
Sakai, H., Asami, M., Naito, H., Kitora, S., Suzuki, Y., Miyauchi, Y., Tachinooka, R., Yoshida, S., Kon, R., Ikarashi, N., et al. (2021) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12760 · Cited by 58
Hah, Y., Lee, W. K., Lee, S.-Y., Kim, E. J., Lee, J. H., Lee, S.-J., Ji, Y. H., Kim, S. G., Lee, H., Hong, S. Y., et al. (2022) · Nutrients · doi:10.3390/nu14142894 · Cited by 56
Du, H., Ma, Y., Wang, X., Zhang, Y., Zhu, L., Shi, S., Pan, S., & Liu, Z. (2023) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00218.2022 · Cited by 59
Time course of cigarette smoke-induced changes of systemic inflammation and muscle structure
Krüger, K., Dischereit, G., Seimetz, M., Wilhelm, J., Weißmann, N., & Mooren, F. C. (2015) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00074.2015 · Cited by 59
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Springer, J., Tschirner, A., Hartmann, K., Palus, S., Wirth, E. K., Busquets, S., Möller, N., von Haehling, S., Argilés, J. M. A., Köhrle, J., et al. (2012) · International Journal of Cancer · doi:10.1002/ijc.27494 · Cited by 56
van Ooijen, H., Hornsveld, M., Veen, C. D.-D., Velter, R., Dou, M., Verhaegh, W., Burgering, B. M. T., & van de Stolpe, A. (2018) · American Journal Of Pathology · doi:10.1016/j.ajpath.2018.05.020 · Cited by 55
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Schcolnik‐Cabrera, A., Chávez-Blanco, A. D., Domínguez-Gómez, G., & Dueñas‐González, A. (2017) · Europe PMC (PubMed Central) · Cited by 54
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Attaix, D., Combaret, L., Béchet, D., & Taillandier, D. (2008) · Current Opinion in Supportive and Palliative Care · doi:10.1097/spc.0b013e3283196ac2 · Cited by 56
Liu, J., Peng, Y., Feng, Z., Shi, W., Qu, L., Li, Y., Liu, J., & Long, J. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.01.003 · Cited by 55
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Mishra, S., Cosentino, C., Tamta, A. K., Khan, D., Srinivasan, S., Ravi, V., Abbotto, E., Arathi, B. P., Kumar, S. A., Jain, A., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-32905-w · Cited by 58
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Lan, X., Deng, C., Wang, Q., Zhao, L., Jiao, B., & Xiang, Y. (2024) · General and Comparative Endocrinology · doi:10.1016/j.ygcen.2024.114513 · Cited by 61
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Egawa, T., Goto, A., Ohno, Y., Yokoyama, S., Ikuta, A., Suzuki, M., Sugiura, T., Ohira, Y., Yoshioka, T., Hayashi, T., et al. (2015) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00165.2015 · Cited by 59
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Macedo, A. G., Krug, A. L. O., Herrera, N. A., Zago, A. S., Rush, J. W. E., & Amaral, S. L. (2014) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2014.05.010 · Cited by 55
Dehoux, M., Gobier, C., Lause, P., Bertrand, L., Ketelslegers, J., & Thissen, J. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00085.2006 · Cited by 57
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Doucet, M., Dube, A., Joanisse, D. R., Debigaré, R., Michaud, A., Paré, M., Vaillancourt, R., Fréchette, É., & Maltais, F. (2010) · Thorax · doi:10.1136/thx.2009.133827 · Cited by 55
Attenuation of skeletal muscle atrophy via protease inhibition
Morris, C. A., Morris, L. D., Kennedy, A. R., & Sweeney, H. L. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01419.2004 · Cited by 55
Nakao, R., Abe, T., Yamamoto, S., & Oishi, K. (2019) · Scientific Reports · doi:10.1038/s41598-019-56166-8 · Cited by 55
Lee, J. H., Jeon, J. H., & Lee, M. J. (2020) · Nutrients · doi:10.3390/nu12092597 · Cited by 62
Cai, X., Zhu, C., Xu, Y., Jing, Y., Yuan, Y., Wang, L., Wang, S., Zhu, X., Gao, P., Zhang, Y., et al. (2016) · Scientific Reports · doi:10.1038/srep26802 · Cited by 54
RetractedPöllänen, E., Ronkainen, P. H. A., Horttanainen, M., Takala, T., Puolakka, J., Suominen, H., Sipilä, S., & Kovanen, V. (2010) · Growth Hormone & IGF Research · doi:10.1016/j.ghir.2010.07.003 · Cited by 54
Glabridin Inhibits Dexamethasone-Induced Muscle Atrophy
Yoshioka, Y., Kubota, Y., Samukawa, Y., Yamashita, Y., & Ashida, H. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.02.006 · Cited by 54
Erol, A. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.11.023 · Cited by 56
Resistance Exercise, Skeletal Muscle FOXO3A, and 85-Year-Old Women
Williamson, D. L., Raue, U., Slivka, D. R., & Trappe, S. W. (2010) · The Journals of Gerontology Series A · doi:10.1093/gerona/glq005 · Cited by 53
Muscle Atrophy in Chronic Kidney Disease Results From Abnormalities in Insulin Signaling
Price, S. R., Gooch, J. L., Donaldson, S., & Roberts‐Wilson, T. K. (2010) · Journal of Renal Nutrition · doi:10.1053/j.jrn.2010.05.007 · Cited by 54
FOXO/DAF-16 Activation Slows Down Turnover of the Majority of Proteins in C. elegans
Dhondt, I., Petyuk, V., Cai, H., Vandemeulebroucke, L., Vierstraete, A. R., Smith, R. D., Depuydt, G., & Braeckman, B. P. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.07.088 · Cited by 55
Thakur, S. S., Swiderski, K., Ryall, J. G., & Lynch, G. S. (2017) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2016.0528 · Cited by 53
P38β MAPK Upregulates Atrogin1/MAFbx by Specific Phosphorylation of C/EBPβ
Zhang, G., & Li, Y.-P. (2012) · Skeletal Muscle · doi:10.1186/2044-5040-2-20 · Cited by 53
Dunford, E. C., & Riddell, M. C. (2016) · Metabolites · doi:10.3390/metabo6040044 · Cited by 55
Postprandial Regulation of Growth- and Metabolism-Related Factors in Zebrafish
Seiliez, I., Médale, F., Aguirre, P., Larquier, M., Lanneretonne, L., Alami-Durante, H., Panserat, S., & Cassy, S. (2013) · Zebrafish · doi:10.1089/zeb.2012.0835 · Cited by 53
Evidence for a role of immunoproteasomes in regulating cardiac muscle mass in diabetic mice
Zu, L., Bedja, D., Fox-Talbot, K., Gabrielson, K. L., Kaer, L. V., Becker, L. C., & Cai, Z. P. (2010) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2010.02.007 · Cited by 53
eIF3f: A central regulator of the antagonism atrophy/hypertrophy in skeletal muscle
Sanchez, A. M. J., Csibi, A., Raibon, A., Docquier, A., Lagirand-Cantaloube, J., Leibovitch, M.-P., Leibovitch, S. A., & Bernardi, H. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.06.001 · Cited by 53
Thomas, S. S., & Mitch, W. E. (2013) · Clinical and Experimental Nephrology · doi:10.1007/s10157-012-0729-9 · Cited by 54
A multifactorial anti-cachectic approach for cancer cachexia in a rat model undergoing chemotherapy
Toledo, M., Penna, F., Oliva, F., Luque, M., Betancourt, A., Marmonti, E., López-Soriano, F. J., Argilés, J. M. A., & Busquets, S. (2015) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12035 · Cited by 53
Araki, S., Izumiya, Y., Hanatani, S., Rokutanda, T., Usuku, H., Akasaki, Y., Takeo, T., Nakagata, N., Walsh, K. X., & Ogawa, H. (2011) · Circulation Heart Failure · doi:10.1161/circheartfailure.111.964783 · Cited by 53
Self-citationJudge, S. M., Deyhle, M. R., Neyroud, D., Nosacka, R. L., D’Lugos, A. C., Cameron, M. E., Vohra, R., Smuder, A. J., Roberts, B. M., Callaway, C. S., et al. (2020) · Cancer Research · doi:10.1158/0008-5472.can-19-1558 · Cited by 52
Inflamma-miR-21 Negatively Regulates Myogenesis during Ageing
Borja-Gonzalez, M., Casas-Martinez, J. C., McDonagh, B., & Goljanek‐Whysall, K. (2020) · Antioxidants · doi:10.3390/antiox9040345 · Cited by 56
Carvalho, R. F., Castan, E. P., Coelho, C. A. O., Pacagnelli, F. L., de Almeida, F. L. A., Michelin, A. C., de Souza, R. W. A., Araújo, J. P., Cicogna, A. C., & Dal‐Pai‐Silva, M. (2010) · Journal of Molecular Histology · doi:10.1007/s10735-010-9262-x · Cited by 53
Schiekofer, S., Shiojima, I., Sato, K., Galasso, G., Oshima, Y., & Walsh, K. X. (2006) · Physiological Genomics · doi:10.1152/physiolgenomics.00234.2005 · Cited by 53
Self-citationEmerging role and function of Hippo-YAP/TAZ signaling pathway in musculoskeletal disorders
Han, J., Zhang, J., Zhang, X., Luo, W., Liu, L., Zhu, Y., Liu, Q., & Zhang, X. (2024) · Stem Cell Research & Therapy · doi:10.1186/s13287-024-04011-9 · Cited by 59
Are antioxidants useful for treating skeletal muscle atrophy?
Bonetto, A., Penna, F., Muscaritoli, M., Minero, V. G., Fanelli, F. R., Baccino, F. M., & Costelli, P. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.07.002 · Cited by 53
Wen, C., Jiang, X., Ding, L., Wang, T., & Zhou, Y. (2017) · Scientific Reports · doi:10.1038/s41598-017-02142-z · Cited by 50
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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