Autophagy as a Potential Target for Sarcopenia: AUTOPHAGY REGULATION IN SARCOPENIA
Abstract
Sarcopenia is an aging-related disease with a significant reduction in mass and strength of skeletal muscle due to the imbalance between protein synthesis and protein degradation. The loss of skeletal muscle is an inevitable event during aging process, which can result in the significant impact on the quality of life, and also can increase the risk for other aging-associated diseases in the elderly. However, the underlying molecular mechanism of aging-related skeletal muscle loss is still poorly understood. Autophagy is a degradation pathway for the clearance of dysfunctional organelles and damaged macromolecules during aging process. Appropriate induction or accurate regulation of autophagic process and improved quality control of mitochondria through autophagy or other strategies are required for the maintenance of skeletal muscle mass. In this article, we have summarized the current understanding of autophagic pathways in sarcopenia, and discussed the functional status of autophagy and autophagy-associated quality control of mitochondria in the pathogenesis of sarcopenia. Moreover, this article will provide some theoretical references for the exploration of scientific and optimal intervention strategies such as exercise and caloric restriction for the prevention and treatment of sarcopenia through the regulation of autophagic pathways.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
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?
Aging is associated with a decline in muscle mass (sarcopenia) and mitochondrial function, both of which are associated with dysregulated autophagy.
“Aging is associated with a decline in muscle mass (termed sarcopenia) and mitochondrial function, both of which are associated with dysregulated autophagy [489].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [489]
Cites
1 retracted
Wenz, T., Rossi, S. G., Rotundo, R. L., Spiegelman, B. M., & Moraes, C. T. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911570106 · Cited by 600 · see citing works
RetractedAMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
Kim, J., Kundu, M., Viollet, B., & Guan, K.-L. (2011) · Nature Cell Biology · doi:10.1038/ncb2152 · Cited by 7,227 · see citing works
Autophagy fights disease through cellular self-digestion
Mizushima, N., Levine, B., Cuervo, A. M., & Klionsky, D. J. (2008) · Nature · doi:10.1038/nature06639 · Cited by 6,452 · see citing works
Pankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J.-A., Outzen, H., Øvervatn, A., Bjørkøy, G., & Johansen, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702824200 · Cited by 4,578 · see citing works
Regulation of skeletal muscle mass in mice by a new TGF-p superfamily member
McPherron, A. C., Lawler, A. M., & Lee, S.-J. (1997) · Nature · doi:10.1038/387083a0 · Cited by 4,013 · see citing works
TSC2 Mediates Cellular Energy Response to Control Cell Growth and Survival
Inoki, K., Zhu, T., & Guan, K.-L. (2003) · Cell · doi:10.1016/s0092-8674(03)00929-2 · Cited by 3,914 · see citing works
AMPK Phosphorylation of Raptor Mediates a Metabolic Checkpoint
Gwinn, D. M., Shackelford, D. B., Egan, D. F., Mihaylova, M. M., Mery, A., Vasquez, D. S., Turk, B. E., & Shaw, R. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.03.003 · Cited by 3,849 · see citing works
Mitochondrial Fission, Fusion, and Stress
Youle, R. J., & van der Bliek, A. M. (2012) · Science · doi:10.1126/science.1219855 · Cited by 3,674 · see citing works
Autophagy and the Integrated Stress Response
Kroemer, G., Mariño, G., & Levine, B. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.023 · Cited by 3,506 · see citing works
Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
Twig, G., Elorza, A., Molina, A. J. A., Mohamed, H., Wikstrom, J. D., Walzer, G., Stiles, L., Haigh, S. E., Katz, S., Las, G., et al. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601963 · Cited by 3,082 · see citing works
Phosphorylation of ULK1 (hATG1) by AMP-Activated Protein Kinase Connects Energy Sensing to Mitophagy
Egan, D. F., Shackelford, D. B., Mihaylova, M. M., Gelino, S., Kohnz, R. A., Mair, W., Vasquez, D. S., Joshi, A., Gwinn, D. M., Taylor, R., et al. (2011) · Science · doi:10.1126/science.1196371 · Cited by 2,600 · see citing works
Impairment of starvation-induced and constitutive autophagy in <i>Atg7</i> -deficient mice
Komatsu, M., Waguri, S., Ueno, T., Iwata, J., Murata, S., Tanida, I., Ezaki, J., Mizushima, N., Ohsumi, Y., Uchiyama, Y., et al. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200412022 · Cited by 2,331 · see citing works
Mitochondrial fusion and fission in cell life and death
Westermann, B. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3013 · Cited by 2,002 · cited 4× · see citing works
“In other studies, the decrease in Akt/mTOR signaling also exhibits the increased protein degradation (Wohlgemuth et al., 2010).”
BackgroundInfluentialFoxO3 Controls Autophagy in Skeletal Muscle In Vivo
Mammucari, C., Milan, G., Romanello, V., Masiero, E., Rudolf, R., Del Piccolo, P., Burden, S. J., Di Lisi, R., Sandri, C., Zhao, J., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.001 · Cited by 1,953 · see citing works
A lysosome‐to‐nucleus signalling mechanism senses and regulates the lysosome via mTOR and TFEB
Settembre, C., Zoncu, R., Medina, D. L., Vetrini, F., Erdin, S., Erdin, S. U., Huynh, T., Ferron, M., Karsenty, G., Vellard, M. C., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.32 · Cited by 1,932 · see citing works
Selective autophagy mediated by autophagic adapter proteins
Johansen, T., & Lamark, T. (2011) · Autophagy · doi:10.4161/auto.7.3.14487 · Cited by 1,730 · see citing works
OPA1 Controls Apoptotic Cristae Remodeling Independently from Mitochondrial Fusion
Frezza, C., Cipolat, S., Martins de Brito, O., Micaroni, M., Beznoussenko, G. V., Rudka, T., Bartoli, D., Polishuck, R. S., Danial, N. N., De Strooper, B., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.025 · Cited by 1,673 · see citing works
Rommel, 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 · see citing works
Autophagy in mammalian development and differentiation
Mizushima, N., & Levine, B. (2010) · Nature Cell Biology · doi:10.1038/ncb0910-823 · Cited by 1,555 · see citing works
Autophagic cell death: the story of a misnomer
Kroemer, G., & Levine, B. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2529 · Cited by 1,453 · see citing works
Autophagy, mitochondria and oxidative stress: cross-talk and redox signalling.
Lee, J., Giordano, S., & Zhang, J. (2012) · Biochemical Journal · doi:10.1042/bj20111451 · Cited by 1,438 · see citing works
Reactive Oxygen Species (Ros-Induced) Ros Release
Zorov, D. B., Filburn, C. R., Klotz, L.-O., Zweier, J. L., & Sollott, S. J. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.192.7.1001 · Cited by 1,412 · see citing works
Functions and dysfunctions of mitochondrial dynamics
Detmer, S. A., & Chan, D. C. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2275 · Cited by 1,369 · see citing works
JNK1-Mediated Phosphorylation of Bcl-2 Regulates Starvation-Induced Autophagy
Wei, Y., Pattingre, S., Sinha, S., Bassik, M., & Levine, B. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.06.001 · Cited by 1,329 · see citing works
Cellular and molecular mechanisms of muscle atrophy
Bonaldo, P., & Sandri, M. (2013) · Disease Models & Mechanisms · doi:10.1242/dmm.010389 · Cited by 1,284 · see citing works
Autophagy is required to maintain muscle mass.
Masiero, E., Agatea, L., Mammucari, C., Blaauw, B., Loro, E., Komatsu, M., Metzger, D., Reggiani, C., Schiaffino, S., & Sandri, M. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.10.008 · Cited by 1,282 · see citing works
Chen, H., Vermulst, M., Wang, Y. E., Chomyn, A., Prolla, T. A., McCaffery, J. M., & Chan, D. C. (2010) · Cell · doi:10.1016/j.cell.2010.02.026 · Cited by 1,211 · see citing works
Exercise-induced BCL2-regulated autophagy is required for muscle glucose homeostasis
He, C., Bassik, M. C., Moresi, V., Sun, K., Wei, Y., Zou, Z., An, Z., Loh, J., Fisher, J., Sun, Q., et al. (2012) · Nature · doi:10.1038/nature10758 · Cited by 1,136 · see citing works
Mitophagy: mechanisms, pathophysiological roles, and analysis
Ding, W.-X., & Yin, X.-M. (2012) · bchm · doi:10.1515/hsz-2012-0119 · Cited by 1,032 · see citing works
An overview of sarcopenia: facts and numbers on prevalence and clinical impact
von Haehling, S., Morley, J. E., & Anker, S. D. (2010) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1007/s13539-010-0014-2 · Cited by 888 · see citing works
Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models
Schiaffino, S., & Mammucari, C. (2011) · Skeletal Muscle · doi:10.1186/2044-5040-1-4 · Cited by 816 · cited 2× · see citing works
“For instance, the activation of Akt signaling by insulin or IGF-1 inactivates FoxO-dependent transcription (Schiaffino and Mammucari, 2011), and mice with the musclespecific loss of IGF-1 receptor have reduced mass and fiber number of skeletal muscle (Mavalli et al., 2010), suggesting that…”
BackgroundUbiquitination and selective autophagy
Shaid, S., Brandts, C. H., Serve, H., & Dikic, I. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2012.72 · Cited by 800 · see citing works
Autophagy and aging: The importance of maintaining "clean" cells
Cuervo, A. M., Bergamini, E., Brunk, U. T., Dröge, W., Ffrench, M., & Terman, A. (2005) · Autophagy · doi:10.4161/auto.1.3.2017 · Cited by 792 · see citing works
Calorie Restriction Increases Muscle Mitochondrial Biogenesis in Healthy Humans
Civitarese, A. E., Carling, S., Heilbronn, L. K., Hulver, M. H., Ukropcova, B., Deutsch, W. A., Smith, S. R., & Ravussin, E. (2007) · PLoS Medicine · doi:10.1371/journal.pmed.0040076 · Cited by 790 · see citing works
Sarcopenia: origins and clinical relevance
Rosenberg, I. H. (2011) · Clinics in Geriatric Medicine · doi:10.1016/j.cger.2011.03.003 · Cited by 786 · see citing works
The mitochondrial‐lysosomal axis theory of aging
Brunk, U. T., & Terman, A. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.02869.x · Cited by 729 · see citing works
The E3 Ligase MuRF1 Degrades Myosin Heavy Chain Protein in Dexamethasone-Treated Skeletal Muscle
Clarke, B. A., Drujan, D., Willis, M. S., Murphy, L. O., Corpina, R. A., Burova, E., Rakhilin, S. V., Stitt, T. N., Patterson, C., Latres, E., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.09.009 · Cited by 683 · see citing works
Oxidative Stress, Molecular Inflammation and Sarcopenia
Meng, S.-J., & Yu, L.-J. (2010) · International Journal of Molecular Sciences · doi:10.3390/ijms11041509 · Cited by 637 · see citing works
Mitochondrial dysfunction and sarcopenia of aging: from signaling pathways to clinical trials
Marzetti, E., Calvani, R., Cesari, M., Buford, T. W., Lorenzi, M., Behnke, B. J., & Leeuwenburgh, C. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.06.024 · Cited by 627 · see citing works
Morley, J. E., Anker, S. D., & von Haehling, S. (2014) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-014-0161-y · Cited by 611 · see citing works
Redox regulation of mitochondrial function
Handy, D. E., & Loscalzo, J. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4123 · Cited by 588 · see citing works
Aging-associated reductions in AMP-activated protein kinase activity and mitochondrial biogenesis
Reznick, R. M., Zong, H., Li, J., Morino, K., Moore, I. K., Yu, H. J., Liu, Z.-X., Dong, J., Mustard, K. J., Hawley, S. A., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.01.008 · Cited by 555 · see citing works
Grumati, P., Coletto, L., Sabatelli, P., Cescon, M., Angelin, A., Bertaggia, E., Blaauw, B., Urciuolo, A., Tiepolo, T., Merlini, L., et al. (2010) · Nature Medicine · doi:10.1038/nm.2247 · Cited by 540 · see citing works
The Molecular Mechanism of Autophagy
Wang, C.-W., & Klionsky, D. J. (2003) · Molecular Medicine · doi:10.1007/bf03402040 · Cited by 530 · see citing works
New insights into the role of mitochondria in aging: mitochondrial dynamics and more
Seo, A. Y., Joseph, A.-M., Dutta, D., Hwang, J. C. Y., Aris, J. P., & Leeuwenburgh, C. (2010) · Journal of Cell Science · doi:10.1242/jcs.070490 · Cited by 522 · cited 1× · see citing works
“…of PGC-1a can improve oxidative capacity and suppress mitochondrial degradation, suggesting that mitochondrial dynamics plays an important role in regulating the balance betweenmitochondrial biogenesis and mitochondrial degradation through autophagy during aging process (Seo et al., 2010).”
BackgroundMitochondria—A Nexus for Aging, Calorie Restriction, and Sirtuins?
Guarente, L. (2008) · Cell · doi:10.1016/j.cell.2008.01.007 · Cited by 513 · see citing works
Terman, A., Kurz, T., Navratil, M., Arriaga, E. A., & Brunk, U. T. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2598 · Cited by 490 · see citing works
The Association of AMPK with ULK1 Regulates Autophagy
Lee, J. W., Park, S., Takahashi, Y., & Wang, H.-G. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015394 · Cited by 482 · see citing works
Leenders, M., Verdijk, L. B., van der Hoeven, L., Adam, J. J., van Kranenburg, J. M. X., Nilwik, R., & van Loon, L. J. C. (2013) · Journal of the American Medical Directors Association · doi:10.1016/j.jamda.2013.02.006 · Cited by 481 · see citing works
SirT1 Regulates Energy Metabolism and Response to Caloric Restriction in Mice
Boily, G., Seifert, E. L., Bevilacqua, L., He, X. H., Sabourin, G., Estey, C., Moffat, C., Crawford, S., Saliba, S., Jardine, K., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001759 · Cited by 444 · see citing works
Bua, E., Johnson, J., Herbst, A., Delong, B., McKenzie, D., Salamat, S., & Aiken, J. M. (2006) · The American Journal of Human Genetics · doi:10.1086/507132 · Cited by 442 · see citing works
Conditional Activation of Akt in Adult Skeletal Muscle Induces Rapid Hypertrophy
Lai, K.-M. V., Gonzalez, M., Poueymirou, W. T., Kline, W. O., Na, E., Zlotchenko, E., Stitt, T. N., Economides, A. N., Yancopoulos, G. D., & Glass, D. J. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.21.9295-9304.2004 · Cited by 442 · see citing works
The contribution of reactive oxygen species to sarcopenia and muscle ageing
Fulle, S., Protasi, F., Tano, G. D., Pietrangelo, T., Beltramin, A., Boncompagni, S., Vecchiet, L., & Fanò, G. (2003) · Experimental Gerontology · doi:10.1016/j.exger.2003.09.012 · Cited by 439 · see citing works
Lira, V. A., Okutsu, M., Zhang, M., Greene, N. P., Laker, R. C., Breen, D. S., Hoehn, K. L., & Yan, Z. (2013) · The FASEB Journal · doi:10.1096/fj.13-228486 · Cited by 432 · see citing works
Guo, Y.-F., Xiao, P., Lei, S., Deng, F., Xiao, G. G., Liu, Y., Chen, X., Li, L., Wu, S., Chen, Y., et al. (2008) · Acta Biochimica et Biophysica Sinica · doi:10.1111/j.1745-7270.2008.00418.x · Cited by 424 · see citing works
Autophagy Impairment in Muscle Induces Neuromuscular Junction Degeneration and Precocious Aging
Carnio, S., LoVerso, F., Baraibar, M. A., Longa, E., Khan, M. M., Maffei, M., Reischl, M., Canepari, M., Loefler, S., Kern, H., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.07.061 · Cited by 423 · see citing works
Lipofuscin: Formation, Distribution, and Metabolic Consequences
JUNG, T., BADER, N., & GRUNE, T. (2007) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1404.008 · Cited by 415 · see citing works
Mitofusins 1/2 and ERRα expression are increased in human skeletal muscle after physical exercise
Cartoni, R., Léger, B., Hock, M. B., Praz, M., Crettenand, A., Pich, S., Ziltener, J., Luthi, F., Dériaz, O., Zorzano, A., et al. (2005) · The Journal of Physiology · doi:10.1113/jphysiol.2005.092031 · Cited by 406 · see citing works
Wohlgemuth, S. E., Seo, A. Y., Marzetti, E., Lees, H. A., & Leeuwenburgh, C. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2009.11.002 · Cited by 397 · see citing works
Scarpulla, R. C. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1427.006 · Cited by 389 · see citing works
Editorial (Thematic Issue: Mitochondrial Biogenesis: Pharmacological Approaches)
Valero, T. (2014) · Current Pharmaceutical Design · doi:10.2174/138161282035140911142118 · Cited by 369 · see citing works
He, C., Zhu, H., Li, H., Zou, M., & Xie, Z. (2012) · Diabetes · doi:10.2337/db12-0533 · Cited by 366 · see citing works
Oxidative Stress, Accumulation of Biological 'Garbage', and Aging
Terman, A., & Brunk, U. T. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.197 · Cited by 363 · see citing works
Role and regulation of autophagy in cancer
Chen, N., & Karantza‐Wadsworth, V. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.12.013 · Cited by 355 · see citing works
Self-citationThe role of myostatin in muscle wasting: an overview
Elkina, Y., von Haehling, S., Anker, S. D., & Springer, J. (2011) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-011-0035-5 · Cited by 349 · see citing works
Resistance Exercise Reverses Aging in Human Skeletal Muscle
Melov, S., Tarnopolsky, M. A., Beckman, K. B., Felkey, K., & Hubbard, A. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000465 · Cited by 344 · see citing works
Sandri, M., Barberi, L., Bijlsma, A. Y., Blaauw, B., Dyar, K. A., Milan, G., Mammucari, C., Meskers, C. G. M., Pallafacchina, G., Paoli, A., et al. (2013) · Biogerontology · doi:10.1007/s10522-013-9432-9 · Cited by 340 · see citing works
Sanchez, A. M. J., Csibi, A., Raibon, A., Cornille, K., Gay, S., Bernardi, H., & Candau, R. B. (2011) · Journal of Cellular Biochemistry · doi:10.1002/jcb.23399 · Cited by 329 · see citing works
Mitochondrial pathways in sarcopenia of aging and disuse muscle atrophy
Calvani, R., Joseph, A.-M., Adhihetty, P. J., Miccheli, A., Bossola, M., Leeuwenburgh, C., Bernabei, R., & Marzetti, E. (2013) · bchm · doi:10.1515/hsz-2012-0247 · Cited by 328 · see citing works
Lee, H.-Y., Choi, C. S., Birkenfeld, A. L., Alves, T. C., Jornayvaz, F. R., Jurczak, M. J., Zhang, D., Woo, D. K., Shadel, G. S., Ladiges, W., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.11.004 · Cited by 319 · see citing works
Autophagy as a therapeutic target in cancer
Chen, N., & Karantza, V. (2011) · Cancer Biology & Therapy · doi:10.4161/cbt.11.2.14622 · Cited by 303 · see citing works
Self-citationCastets, P., Lin, S., Rion, N., Di Fulvio, S., Romanino, K., Guridi, M., Frank, S., Tintignac, L. A., Sinnreich, M., & Rüegg, M. A. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.03.015 · Cited by 302 · see citing works
Yarasheski, K. E., Bhasin, S., Sinha‐Hikim, I., Pak-Loduca, J., & González-Cadavid, N. F. (2002) · PubMed · Cited by 293 · see citing works
Stroke induced Sarcopenia: muscle wasting and disability after stroke.
Scherbakov, N., von Haehling, S., Anker, S., Dirnagl, U., & Doehner, W. (2013) · International Journal of Cardiology · doi:10.1016/j.ijcard.2013.10.031 · Cited by 291 · see citing works
Organization of the Pre-autophagosomal Structure Responsible for Autophagosome Formation
Kawamata, T., Kamada, Y., Kabeya, Y., Sekito, T., & Ohsumi, Y. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-10-1048 · Cited by 287 · see citing works
Yoon, Y., Yoon, D., Lim, I. K., Yoon, S., Chung, H., Rojo, M., Malka, F., Jou, M., Martinou, J., & Yoon, G. (2006) · Journal of Cellular Physiology · doi:10.1002/jcp.20753 · Cited by 275 · see citing works
Grumati, P., Coletto, L., Schiavinato, A., Castagnaro, S., Bertaggia, E., Sandri, M., & Bonaldo, P. (2011) · Autophagy · doi:10.4161/auto.7.12.17877 · Cited by 267 · see citing works
Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory feedback loop
Löffler, A. S., Alers, S., Dieterle, A. M., Keppeler, H., Franz-Wachtel, M., Kundu, M., Campbell, D. G., Wesselborg, S., Alessi, D. R., & Stork, B. (2011) · Autophagy · doi:10.4161/auto.7.7.15451 · Cited by 258 · see citing works
Aging: Central role for autophagy and the lysosomal degradative system
Rajawat, Y. S., Hilioti, Z., & Bossis, I. (2009) · Ageing Research Reviews · doi:10.1016/j.arr.2009.05.001 · Cited by 247 · see citing works
Lysosomal proteolysis in skeletal muscle
Béchet, D., Tassa, A., Taillandier, D., Combaret, L., & Attaix, D. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.02.029 · Cited by 241 · see citing works
Exercise Training-Induced Regulation of Mitochondrial Quality
Yan, Z., Lira, V. A., & Greene, N. P. (2012) · Exercise and Sport Sciences Reviews · doi:10.1097/jes.0b013e3182575599 · Cited by 233 · see citing works
Mild mitochondrial uncoupling impacts cellular aging in human muscles in vivo
Amara, C. E., Shankland, E. G., Jubrias, S. A., Marcinek, D. J., Kushmerick, M. J., & Conley, K. E. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0610131104 · Cited by 223 · see citing works
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 218 · see citing works
Yang, W., Zhang, Y., Li, Y., Wu, Z., & Zhu, D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m610185200 · Cited by 218 · see citing works
Mavalli, M. D., DiGirolamo, D. J., Fan, Y., Riddle, R. C., Campbell, K. S., van Groen, T., Frank, S. J., Sperling, M. A., Esser, K. A., Bamman, M. M., et al. (2010) · Journal of Clinical Investigation · doi:10.1172/jci42447 · Cited by 213 · see citing works
Autophagy is required for extension of yeast chronological life span by rapamycin
Alvers, A. L., Wood, M. S., Hu, D., Kaywell, A. C., Dunn, W. A., & Aris, J. P. (2009) · Autophagy · doi:10.4161/auto.8824 · Cited by 212 · see citing works
Sidis, Y., Mukherjee, A., Keutmann, H., Delbaere, A., Sadatsuki, M., & Schneyer, A. (2006) · Endocrinology · doi:10.1210/en.2006-0089 · Cited by 211 · see citing works
Atrogin-1/MAFbx and MuRF1 are downregulated in aging-related loss of skeletal muscle
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 · see citing works
Mechanisms of mitochondria and autophagy crosstalk
Rambold, A. S., & Lippincott‐Schwartz, J. (2011) · Cell Cycle · doi:10.4161/cc.10.23.18384 · Cited by 191 · see citing works
The Epidemiology of Sarcopenia
Janssen, I. (2011) · Clinics in Geriatric Medicine · doi:10.1016/j.cger.2011.03.004 · Cited by 191 · see citing works
Sarcopenia of aging: Underlying cellular mechanisms and protection by calorie restriction
Marzetti, E., Lees, H. A., Wohlgemuth, S. E., & Leeuwenburgh, C. (2009) · BioFactors · doi:10.1002/biof.5 · Cited by 182 · see citing works
LeBrasseur, N. K., Schelhorn, T. M., Bernardo, B. L., Cosgrove, P. G., Loria, P. M., & Brown, T. A. (2009) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/glp068 · Cited by 180 · see citing works
Type 2 diabetes is associated with low muscle mass in older adults
Kim, K., Park, K., Kim, M., Kim, S., Cho, Y., & Park, S. W. (2014) · Geriatrics and gerontology international/Geriatrics & gerontology international · doi:10.1111/ggi.12189 · Cited by 179 · see citing works
Terada, S., & Tabata, I. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00051.2003 · Cited by 169 · see citing works
Derave, W., Ai, H., Ihlemann, J., Witters, L. A., Kristiansen, S., Richter, E. A., & Ploug, T. (2000) · Diabetes · doi:10.2337/diabetes.49.8.1281 · Cited by 168 · see citing works
GSK-3α is a central regulator of age-related pathologies in mice
Zhou, J., Freeman, T. A., Ahmad, F., Shang, X., Mangano, E. N., Gao, E., Farber, J. L., Wang, Y., Ma, X.-L., Woodgett, J. R., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci64398 · Cited by 167 · see citing works
Fry, C. S., Drummond, M. J., Glynn, E. L., Dickinson, J. M., Gundermann, D. M., Timmerman, K. L., Walker, D. K., Volpi, E., & Rasmussen, B. B. (2013) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/gls209 · Cited by 165 · see citing works
Adaptive plasticity of autophagic proteins to denervation in aging skeletal muscle
O'Leary, M. F., Vainshtein, A., Iqbal, S., Ostojic, O., & Hood, D. A. (2013) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00240.2012 · Cited by 165 · see citing works
The myostatin gene: physiology and pharmacological relevance
Joulia-Ekaza, D., & Cabello, G. (2007) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2006.11.011 · Cited by 160 · see citing works
Aging-sensitive cellular and molecular mechanisms associated with skeletal muscle hypertrophy
Haddad, F., & Adams, G. R. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01227.2005 · Cited by 158 · see citing works
Zhang, C., McFarlane, C., Lokireddy, S., Bonala, S., Ge, X., Masuda, S., Gluckman, P. D., Sharma, M., & Kambadur, R. (2011) · Diabetologia · doi:10.1007/s00125-011-2079-7 · Cited by 158 · see citing works
Modulation of autophagy and ubiquitin-proteasome pathways during ultra-endurance running
Jamart, C., Francaux, M., Millet, G. Y., Deldicque, L., Frère, D., & Féasson, L. (2012) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00952.2011 · Cited by 157 · see citing works
Autophagy in health and disease. 3. Involvement of autophagy in muscle atrophy
Sandri, M. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00531.2009 · Cited by 152 · see citing works
Autophagy is essential to support skeletal muscle plasticity in response to endurance exercise
Sanchez, A. M. J., Bernardi, H., Py, G., & Candau, R. B. (2014) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00187.2014 · Cited by 143 · see citing works
Attenuation of sarcopenia by dietary restriction in rhesus monkeys
Colman, R. J., Beasley, T. M., Allison, D. B., & Weindruch, R. (2008) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/63.6.556 · Cited by 141 · see citing works
Sarcopenia and cachexia: the adaptations of negative regulators of skeletal muscle mass
Sakuma, K., & Yamaguchi, A. (2012) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-011-0052-4 · Cited by 137 · see citing works
Ghosh, S., Lertwattanarak, R., Lefort, N., Molina-Carrion, M., Joya-Galeana, J., Bowen, B. P., Garduno-Garcia, J. D. J., Abdul-Ghani, M., Richardson, A., DeFronzo, R. A., et al. (2011) · Diabetes · doi:10.2337/db11-0121 · Cited by 128 · see citing works
Caloric restriction and genomic stability
Heydari, A. R., Unnikrishnan, A., Ventrella-Lucente, L. F., & Richardson, A. G. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm860 · Cited by 127 · see citing works
Murphy, K. T., Koopman, R., Naim, T., Léger, B., Trieu, J., Ibebunjo, C., & Lynch, G. S. (2010) · The FASEB Journal · doi:10.1096/fj.10-159608 · Cited by 124 · see citing works
Jamart, C., Benoit, N., Raymackers, J.-M., Kim, H. J., Kim, C. K., & Francaux, M. (2012) · European Journal of Applied Physiology · doi:10.1007/s00421-011-2287-3 · Cited by 121 · see citing works
Hwee, D. T., Baehr, L. M., Philp, A., Baar, K., & Bodine, S. C. (2014) · Aging Cell · doi:10.1111/acel.12150 · Cited by 121 · see citing works
Kwak, K. S., Zhou, X., Solomon, V., Baracos, V. E., Davis, J. G., Bannon, A. W., Boyle, W. J., Lacey, D. L., & Han, H. Q. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-2102 · Cited by 111 · see citing works
Autophagic response to exercise training in skeletal muscle with age
Kim, Y. A., Kim, Y. S., Oh, S. L., Kim, H.-J., & Song, W. (2013) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-013-0246-7 · Cited by 108 · see citing works
Mitochondrial dysfunction and age
Conley, K. E., Marcinek, D. J., & Villarin, J. J. (2007) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0b013e3282f0dbfb · Cited by 106 · see citing works
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 · see citing works
Li, L., Mühlfeld, C., Niemann, B., Pan, R., Li, R., Hilfiker‐Kleiner, D., Chen, Y., & Rohrbach, S. (2011) · Basic Research in Cardiology · doi:10.1007/s00395-011-0213-9 · Cited by 95 · see citing works
Jang, Y. C., Liu, Y., Hayworth, C. R., Bhattacharya, A., Lustgarten, M. S., Müller, F. L., Chaudhuri, A. R., Qi, W., Li, Y., Huang, J., et al. (2012) · Aging Cell · doi:10.1111/j.1474-9726.2012.00843.x · Cited by 94 · see citing works
Caloric restriction delays aging-induced cellular phenotypes in rhesus monkey skeletal muscle
McKiernan, S. H., Colman, R. J., Lopez, M. E., Beasley, T. M., Aiken, J. M., Anderson, R. M., & Weindruch, R. H. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.09.011 · Cited by 94 · see citing works
Giant mitochondria do not fuse and exchange their contents with normal mitochondria
Navratil, M., Terman, A., & Arriaga, E. A. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.09.013 · Cited by 94 · see citing works
mVps34 is activated following high‐resistance contractions
MacKenzie, M. G., Hamilton, D. L., Murray, J. T., Taylor, P. M., & Baar, K. (2009) · The Journal of Physiology · doi:10.1113/jphysiol.2008.159830 · Cited by 94 · see citing works
Ning, Y., Cai, G., Zhuo, L., Gao, J., Dong, D. F., Cui, S., Feng, Z., Shi, S., Bai, X., Sun, X., et al. (2013) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2013.11.006 · Cited by 91 · see citing works
Baker, D. J., Betik, A. C., Krause, D. J., & Hepple, R. T. (2006) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/61.7.675 · Cited by 89 · see citing works
Vainshtein, A., Grumati, P., Sandri, M., & Bonaldo, P. (2014) · Journal of Molecular Medicine · doi:10.1007/s00109-013-1096-z · Cited by 88 · see citing works
A midlife crisis for the mitochondrial free radical theory of aging
Stuart, J. A., Maddalena, L. A., Merilovich, M., & Robb, E. L. (2014) · Longevity & Healthspan · doi:10.1186/2046-2395-3-4 · Cited by 84 · see citing works
Long-term caloric restriction abrogates the age-related decline in skeletal muscle aerobic function
Hepple, R. T., Baker, D. J., Kaczor, J. J., & Krause, D. J. (2005) · The FASEB Journal · doi:10.1096/fj.04-3535fje · Cited by 80 · see citing works
Effects of the activin A–myostatin–follistatin system on aging bone and muscle progenitor cells
Bowser, M., Herberg, S., Arounleut, P., Shi, X., Fulzele, S., Hill, W., Isales, C. M., & Hamrick, M. W. (2012) · Experimental Gerontology · doi:10.1016/j.exger.2012.11.004 · Cited by 75 · see citing works
Payne, A. M., Dodd, S. L., & Leeuwenburgh, C. (2003) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00758.2003 · Cited by 71 · see citing works
Saleem, A., Carter, H. N., & Hood, D. A. (2013) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00270.2013 · Cited by 71 · see citing works
Autophagic response to a single bout of moderate exercise in murine skeletal muscle
Kim, Y.-A., Kim, Y. S., & Song, W. J. (2011) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-011-0135-x · Cited by 69 · see citing works
Protein homeostasis and aging: Role of ubiquitin protein ligases
Jana, N. R. (2012) · Neurochemistry International · doi:10.1016/j.neuint.2012.02.009 · Cited by 67 · see citing works
Hindlimb skeletal muscle function in myostatin‐deficient mice
Gentry, B. A., Ferreira, J. A., Phillips, C. L., & Brown, M. (2010) · Muscle & Nerve · doi:10.1002/mus.21796 · Cited by 66 · see citing works
Resistance to body fat gain in ‘double-muscled’ mice fed a high-fat diet
Hamrick, M. W., Pennington, C., Webb, C. N., & Isales, C. M. (2006) · International Journal of Obesity · doi:10.1038/sj.ijo.0803200 · Cited by 66 · see citing works
PGC-1α and Myokines in the Aging Muscle – A Mini-Review
Arnold, A.-S., Egger, A., & Handschin, C. (2011) · Gerontology · doi:10.1159/000281883 · Cited by 65 · see citing works
Age-related changes of cell death pathways in rat extraocular muscle
McMullen, C. A., Ferry, A. L., Gamboa, J. L., Andrade, F. H., & Dupont‐Versteegden, E. E. (2009) · Experimental Gerontology · doi:10.1016/j.exger.2009.03.006 · Cited by 64 · see citing works
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 64 · see citing works
Single bout of running exercise changes LC3-II expression in rat cardiac muscle
Ogura, Y., Iemitsu, M., Naıto, H., Kakigi, R., Kakehashi, C., Maeda, S., & Akema, T. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.09.152 · Cited by 63 · see citing works
Ikeda, S., Kawamoto, H., Kasaoka, K., Hitomi, Y., Kizaki, T., Sankai, Y., Ohno, H., Haga, S., & Takemasa, T. (2006) · Acta Physiologica · doi:10.1111/j.1748-1716.2006.01623.x · Cited by 58 · see citing works
Does autophagy take a front seat in lifespan extension?
Petrovski, G., & Das, D. K. (2010) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2010.01196.x · Cited by 45 · see citing works
van Norren, K., Rusli, F., van Dijk, M., Lute, C., Nagel, J., Dijk, F. J., Dwarkasing, J. T., Boekschoten, M. V., Luiking, Y. C., Witkamp, R. F., et al. (2015) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12024 · Cited by 44 · see citing works
Regulation of Skeletal Muscle Mitochondrial Content During Aging
Lyons, C. N., Mathieu-Costello, O. A., & Moyes, C. D. (2006) · The Journals of Gerontology Series A · doi:10.1093/gerona/61.1.3 · Cited by 43 · see citing works
The fine line between lifespan extension and shortening in response to caloric restriction
Szafranski, K., & Mekhail, K. (2014) · Nucleus · doi:10.4161/nucl.27929 · Cited by 33 · see citing works
Collins‐Hooper, H., Sartori, R., Macharia, R., Visanuvimol, K., Foster, K., Matsakas, A., Flasskamp, H., Ray, S., Dash, P. R., Sandri, M., et al. (2014) · The Journals of Gerontology Series A · doi:10.1093/gerona/glt170 · Cited by 29 · see citing works
Ward, J. (2011) · Australasian Journal on Ageing · doi:10.1111/j.1741-6612.2011.00536.x · Cited by 8 · see citing works
Flagged first, then by citations
1 of the 144 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Autophagy in major human diseases
Klionsky, D. J., Petroni, G., Amaravadi, R. K., Baehrecke, E. H., Ballabio, A., Boya, P., Bravo‐San Pedro, J. M., Cadwell, K., Cecconi, F., Choi, A. M. K., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2021108863 · Cited by 1,585 · see citing works
Physical activity and exercise: Strategies to manage frailty
Angulo, J., El Assar, M., Álvarez-Bustos, A., & Rodríguez-Mañas, L. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101513 · Cited by 771 · see citing works
The Role of Inflammation in Age-Related Sarcopenia
Dalle, S., Rossmeislova, L., & Koppo, K. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.01045 · Cited by 668 · see citing works
“In general, autophagy is accepted to be a promising target to counteract sarcopenia (Fan et al., 2016).”
BackgroundInfluentialThe effect of fasting or calorie restriction on autophagy induction: A review of the literature
Bagherniya, M., Butler, A. E., Barreto, G. E., & Sahebkar, A. (2018) · Ageing Research Reviews · doi:10.1016/j.arr.2018.08.004 · Cited by 317 · see citing works
Hallmarks of Aging: An Autophagic Perspective
Barbosa, M. C., Grosso, R. A., & Fader, C. M. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00790 · Cited by 265 · see citing works
“Finally, sarcopenia is characterized by a progressive loss of muscle mass and strength thanks to an imbalance between production and degradation of proteins (79).”
BackgroundAutophagy and aging: Maintaining the proteome through exercise and caloric restriction
Escobar, K. A., Cole, N. H., Mermier, C. M., & VanDusseldorp, T. A. (2018) · Aging Cell · doi:10.1111/acel.12876 · Cited by 226 · see citing works
Autophagy and ALS: mechanistic insights and therapeutic implications
Chua, J. P., De Calbiac, H., Kabashi, E., & Barmada, S. J. (2022) · Autophagy · doi:10.1080/15548627.2021.1926656 · Cited by 189 · see citing works
“mitochondrial function, both of which are associated with dysregulated autophagy [489].”
BackgroundFan, J., Yang, X., Li, J., Shu, Z., Dai, J., Liu, X., Li, B., Jia, S., Kou, X., Yang, Y., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.15728 · Cited by 179 · see citing works
“Excessive apoptosis and deficient autophagy may cause the atrophy of skeletal muscle under pathological events or aging process, and correspondingly may promote cell death and disease progression [2].”
Self-citationNew insights into the pathogenesis and treatment of sarcopenia in chronic heart failure
Yin, J., Lü, X., Qian, Z., Xu, W., & Zhou, X. (2019) · Theranostics · doi:10.7150/thno.33000 · Cited by 155 · see citing works
“Appropriate induction or accurate regulation of autophagic process and improved quality control of mitochondria through autophagy are required to maintain skeletal muscle mass [38].”
BackgroundDuan, P., Hu, C., Quan, C., Yu, T., Zhou, W., Yuan, M., Shi, Y., & Yang, K. (2016) · Toxicology · doi:10.1016/j.tox.2016.01.004 · Cited by 138 · see citing works
Biological basis and treatment of frailty and sarcopenia
Sato, R., Vatic, M., da Fonseca, G. W. P., Anker, S. D., & von Haehling, S. (2024) · Cardiovascular Research · doi:10.1093/cvr/cvae073 · Cited by 128 · see citing works
MicroRNA-Regulated Proinflammatory Cytokines in Sarcopenia
Fan, J., Kou, X., Yang, Y., & Chen, N. (2016) · Mediators of Inflammation · doi:10.1155/2016/1438686 · Cited by 86 · see citing works
“The pathogenesis of sarcopenia is associated with many intrinsic and extrinsic factors, including proinflammatory cytokine accumulation, oxidative stress, mitochondrial dysfunction, insulin resistance, and aging-related loss of anabolic hormones andmotor neuron end plates [2].”
BackgroundSelf-citationRegulation of autophagy by mitochondrial phospholipids in health and diseases
Hsu, P., & Shi, Y. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.08.003 · Cited by 84 · see citing works
Kou, X., Li, J., Liu, X., Yang, X., Fan, J., & Chen, N. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2017.03.070 · Cited by 81 · see citing works
“The progressive mass loss of skeletal muscle can result in the impact on health, thereby leading to decreased physical activity and increased risk of falls or corresponding fractures in elderly [2].”
Self-citationLenhare, L., Crisol, B. M., Silva, V. R. R., Katashima, C. K., Cordeiro, A. V., Pereira, K. D., Luchessi, A. D., da Silva, A. S. R., Cintra, D. E., Moura, L. P., et al. (2017) · Experimental Gerontology · doi:10.1016/j.exger.2017.07.009 · Cited by 79 · see citing works
“Furthermore, autophagic response seems to be affected in the skeletal muscle during aging contributing to sarcopenia (Fan et al., 2016) and insulin resistance (Li et al.”
Li, Q.-X., Jia, S.-H., Xu, L., Li, B., & Chen, N. (2019) · Food Science & Nutrition · doi:10.1002/fsn3.1006 · Cited by 77 · see citing works
Self-citationMuscle Atrophy: Present and Future
Cao, R. Y., Li, J., Dai, Q., Li, Q. X., & Yang, J. (2018) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-1435-3_29 · Cited by 75 · see citing works
Kou, X., Li, J., Liu, X., Chang, J., Zhao, Q., Jia, S., Fan, J., & Chen, N. (2017) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00018.2017 · Cited by 72 · see citing works
“Recently, the functional status of autophagy during the aging process has attracted increasing attention, but the relationship between functional status of autophagy and aging remains unclear (12, 18).”
BackgroundSelf-citationAutophagy in the Regulation of Tissue Differentiation and Homeostasis
Perrotta, C., Cattaneo, M. G., Molteni, R., & Palma, C. D. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.602901 · Cited by 72 · see citing works
“, 2012), sarcopenia (Fan et al., 2016) and cancer cachexia (de Castro et al.”
BackgroundJiang, Q., Yan, M., Zhao, Y., Zhou, X., Yin, L. W., Feng, L., Liu, Y., Jiang, W., Wu, P., Wang, Y., et al. (2021) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-021-00572-4 · Cited by 66 · see citing works
Autophagy as a Therapeutic Target to Enhance Aged Muscle Regeneration
Lee, D. E., Bareja, A., Bartlett, D. B., & White, J. P. (2019) · Cells · doi:10.3390/cells8020183 · Cited by 64 · see citing works
“Pathophysiological conditions of muscle that implicate maladaptive autophagy including Duchenne’s muscular dystrophy [33], type II diabetes mellitus/insulin resistance [34], sarcopenia [35], cancer-induced wasting [36], and myotube regeneration [37]; however, the origin of signals inducing autophagy for each scenario…”
BackgroundSarcopenia targeting with autophagy mechanism by exercise
Park, S. S., Seo, Y., & Kwon, K. (2019) · BMB Reports · doi:10.5483/bmbrep.2019.52.1.292 · Cited by 63 · see citing works
“However, a recent investigation implicated dysregulation of autophagy as a critical inducer of sarcopenia (46).”
BackgroundAutophagy as an emerging therapy target for ovarian carcinoma
Zhan, L., Zhang, Y., Wang, W., Song, E., Fan, Y., Li, J., & Wei, B. (2016) · Oncotarget · doi:10.18632/oncotarget.13080 · Cited by 60 · see citing works
Marzetti, E., Calvani, R., Lorenzi, M., Tanganelli, F., Picca, A., Bossola, M., Menghi, A., Bernabei, R., & Landi, F. (2016) · Experimental Gerontology · doi:10.1016/j.exger.2016.04.003 · Cited by 58 · see citing works
A Novel Regulator of Type II Diabetes: MicroRNA-143
Li, B., Fan, J., & Chen, N. (2018) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2018.03.019 · Cited by 59 · see citing works
Self-citationImpacts of Green Tea on Joint and Skeletal Muscle Health: Prospects of Translational Nutrition
Luk, H., Appell, C. R., Chyu, M., Chen, C., Wang, C., Yang, R., & Shen, C. (2020) · Antioxidants · doi:10.3390/antiox9111050 · Cited by 58 · see citing works
“The activation of autophagy mediates suppression of the loss of skeletal muscle through signaling pathways, including phosphatidylinositol-3-kinase (PI3K), myostatin, and proteasome pathways [39].”
BackgroundIrisin and Autophagy: First Update
Pesce, M., Ballerini, P., Paolucci, T., Puca, I., Farzaei, M. H., & Patruno, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21207587 · Cited by 59 · see citing works
“These evidences suggest that exercise-mediated autophagy could interfere with several pathology in which autophagy dysregulation is implicated, such as T2DM [93], neurodegeneration [94], cardiomyopathy [95], and chronic inflammation [96] while sustaining muscle quality and function [97].”
BackgroundLee, J. H., Jeon, J. H., & Lee, M. J. (2020) · Nutrients · doi:10.3390/nu12092597 · Cited by 56 · see citing works
Livshits, G., & Kalinkovich, A. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101852 · Cited by 55 · see citing works
Redox Signaling and Sarcopenia: Searching for the Primary Suspect
Foreman, N. A., Hesse, A. S., & Ji, L. L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22169045 · Cited by 52 · see citing works
“With insufficient autophagy, the cell accumulates dysfunctional and malformed proteins, whereas excessive autophagy promotes muscle wasting [79].”
BackgroundMechanisms of protein balance in skeletal muscle
Anthony, T. G. (2016) · Domestic Animal Endocrinology · doi:10.1016/j.domaniend.2016.02.012 · Cited by 57 · see citing works
“Macroautophagy is regulated by nutritional state, with fasting stimulating and feeding inhibiting biomarkers of autophagosome formation [77].”
BackgroundAyyadevara, S., Balasubramaniam, M., Suri, P., Mackintosh, S. G., Tackett, A. J., Sullivan, D. H., Reis, R. J. S., & Dennis, R. A. (2016) · Aging · doi:10.18632/aging.101141 · Cited by 51 · see citing works
Ryu, J. Y., Choi, H. M., Yang, H.-I., & Kim, K. S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186887 · Cited by 51 · see citing works
“Thus, AMPK controls both protein synthesis and protein degradation through an autophagic process [10].”
BackgroundChang, Y., Chen, Y.-T., Liu, H., Chan, Y., Liu, M., Hu, S., Tseng, W., Wu, H., Wang, M., & Chang, S. (2019) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201801102 · Cited by 52 · see citing works
Hosoi, T., Yakabe, M., Sasakawa, H., Sasako, T., Ueki, K., Kato, S., Tokuoka, S. M., Oda, Y., Abe, M., Matsumoto, T., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2218032120 · Cited by 47 · see citing works
Cho, J., Choi, Y., Sajgalik, P., No, M., Lee, S.-H., Kim, S., Heo, J., Cho, E., Chang, E., Kang, J., et al. (2020) · Cells · doi:10.3390/cells9102284 · Cited by 44 · see citing works
“Activation of the autophagic pathway in skeletal muscle plays a crucial role in maintaining protein homeostasis via several signaling pathways, including phosphatidylinositol-3-kinase (PI3K), myostatin, proteasome, and autophagy-lysosome pathways [44].”
BackgroundChen, Y., Ma, Y., Tang, J., Zhang, D., Zhao, Q., Liu, J., Tang, H., Zhang, J., He, G., Zhong, C., et al. (2023) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.13257 · Cited by 42 · see citing works
“moval of cellular components and leads to the atrophy of skeletal muscle.(37) In contrast, the appropriate induction of autophagy is required for the clearance of aggregated pro-”
BackgroundLivshits, G., & Kalinkovich, A. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102267 · Cited by 42 · see citing works
Pratiwi, Y. S., Lesmana, R., Goenawan, H., Sylviana, N., Setiawan, I. B., Tarawan, V. M., Lestari, K., Abdulah, R., Dwipa, L., Purba, A., et al. (2018) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2018/2810840 · Cited by 40 · see citing works
“In aging process, dysregulated autophagy is attributed to the apparent aging-related accumulation of damaged cellular components such as defective mitochondria, which results in more reactive oxygen species (ROS) [12].”
BackgroundInfluentialHuang, D., Yan, X., Fan, S.-D., Chen, X., Yan, J., Dong, Q., Chen, W., Liu, N., Chen, X., & Yu, Z. (2020) · Aging · doi:10.18632/aging.102990 · Cited by 40 · see citing works
“excessive autophagy can also be deleterious by causing cellular stress and muscle protein degradation [4].”
BackgroundPotential of Food Protein-Derived Bioactive Peptides against Sarcopenia: A Comprehensive Review
Zhu, X., Wang, J., Lu, Y., Zhao, Y., Zhang, N., Wu, W., Zhang, Y., & Fu, Y. (2023) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.2c09094 · Cited by 38 · see citing works
Zeitz, J. O., Käding, S.-C., Niewalda, I. R., Most, E., Dorigam, J. C. D. P., & Eder, K. (2019) · Poultry Science · doi:10.3382/ps/pez396 · Cited by 37 · see citing works
“, by inhibiting proteasome- and autophagy-related protein degradation (Fan et al. 2016) which are the 2 most important pathways of skeletal muscle proteolysis (Pasiakos and Carbone, 2014).”
BackgroundRegulatory role of exercise-induced autophagy for sarcopenia
Liang, J., Zeng, Z., Zhang, Y., & Chen, N. (2020) · Experimental Gerontology · doi:10.1016/j.exger.2019.110789 · Cited by 33 · see citing works
Self-citationAutophagy regulation in teleost fish: A double-edged sword
Zhou, Z., He, Y., Wang, S., Wang, Y., Shan, P., & Li, P. (2022) · Aquaculture · doi:10.1016/j.aquaculture.2022.738369 · Cited by 34 · see citing works
Exercise-driven cellular autophagy: A bridge to systematic wellness
Zhou, X.-H., Luo, Y., & Yao, X. (2025) · Journal of Advanced Research · doi:10.1016/j.jare.2024.12.036 · Cited by 33 · see citing works
“Exercise-induced autophagy reduces the accumulation of dysfunctional mitochondria, facilitates the removal of damaged proteins and metabolic waste, and promotes mitochondrial biogenesis [63,169].”
Ni, Y., Wu, T., Yang, L., Xu, Y., Ota, T., & Fu, Z. (2018) · Endocrine Journal · doi:10.1507/endocrj.ej17-0500 · Cited by 32 · see citing works
Wu, H., Xie, Y., Xu, Y., Hu, Z., Wan, X., Huang, H.-C., & Huang, D. (2018) · Natural Product Research · doi:10.1080/14786419.2018.1503261 · Cited by 31 · see citing works
“In the strategy to many diseases, how to maintain the cellular hemostasis is a serious problem, and it is also important for both apoptosis and autophagy (Fan et al. 2016).”
BackgroundNutrition and microRNAs: Novel Insights to Fight Sarcopenia
Barbiera, A., Pelosi, L., Sica, G., & Scicchitano, B. M. (2020) · Antioxidants · doi:10.3390/antiox9100951 · Cited by 32 · see citing works
“Indeed, the deficiency of basal autophagy can result in the abnormal aggregation of misfolded proteins, while excessive autophagy can also cause cellular stress and induce the loss of skeletal muscle mass due to increased protein degradation [95].”
BackgroundGinseng and ginsenosides: Therapeutic potential for sarcopenia
Zha, W., Sun, Y., Gong, W., Li, L., Kim, W., & Li, H. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113876 · Cited by 29 · see citing works
Wu, H., Qiu, Y. L., Shu, Z., Zhang, X., Li, R., Liu, S., Chen, L., Liu, H. S., & Chen, N. (2016) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/cjpp-2016-0228 · Cited by 26 · see citing works
Self-citationTherapeutic considerations of sarcopenia in heart failure patients
Saitoh, M., Ebner, N., von Haehling, S., Anker, S. D., & Springer, J. (2018) · Expert Review of Cardiovascular Therapy · doi:10.1080/14779072.2018.1424542 · Cited by 26 · see citing works
Sato, T., Ito, Y., & Nagasawa, T. (2016) · Biogerontology · doi:10.1007/s10522-016-9663-7 · Cited by 25 · see citing works
Autophagy-associated signal pathways of functional foods for chronic diseases
Xie, J., Liang, J., & Chen, N. (2019) · Food Science and Human Wellness · doi:10.1016/j.fshw.2019.03.002 · Cited by 25 · see citing works
Self-citationSarcopenia in cirrhosis: From pathophysiology to interventional therapy
Chen, H., Yang, C., Yan, S., Liu, X., Zhou, L., & Yuan, X. (2024) · Experimental Gerontology · doi:10.1016/j.exger.2024.112571 · Cited by 23 · see citing works
“Research on sarcopenia and autophagy has also suggested that auto-phagy also cause wasting of muscle (Fan et al., 2016).”
BackgroundPolyamines and Physical Activity in Musculoskeletal Diseases: A Potential Therapeutic Challenge
Galasso, L., Cappella, A., Mulè, A., Castelli, L., Ciorciari, A. M., Stacchiotti, A., & Montaruli, A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24129798 · Cited by 23 · see citing works
“Dysregulated autophagy is attributed to the apparent age-related accumulation of damaged cellular components, such as defective mitochondria [69].”
BackgroundInfluentialAutophagy Is a Promoter for Aerobic Exercise Performance during High Altitude Training
Zhang, Y., & Chen, N. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/3617508 · Cited by 20 · see citing works
Self-citationSkeletal Muscle Aging Atrophy: Assessment and Exercise-Based Treatment
Marzuca-Nassr, G. N., SanMartín-Calísto, Y., Guerra-Vega, P., Artigas-Arias, M., Alegría, A., & Curi, R. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-42667-5_6 · Cited by 19 · see citing works
Thermosensitive Hydrogel Harboring CD146/IGF-1 Nanoparticles for Skeletal-Muscle Regeneration
Lee, W., Lee, J., Lee, H. S., Yoo, Y., Shin, H., Kim, H., Min, D. S., Bae, J., & Seo, Y. (2021) · ACS Applied Bio Materials · doi:10.1021/acsabm.1c00688 · Cited by 18 · see citing works
Liu, M., Yue, Z., Zhang, B., Li, F., Liu, L., & Liu, L. (2022) · Metabolites · doi:10.3390/metabo12090788 · Cited by 18 · see citing works
“Autophagy is a degradation pathway of macromolecules and organelles during aging and muscle loss, and maintenance of skeletal muscle mass requires proper induction or accurate regulation of the autophagic process [44].”
BackgroundOpazo, R., Bárbara Angel, B., Márquez, C., Lera, L., dos Santos, G. R. C., Monnerat, G., & Cecilia Albala, B. (2021) · Metabolomics · doi:10.1007/s11306-021-01832-0 · Cited by 18 · see citing works
Regular football training down-regulates miR-1303 muscle expression in veterans
Mancini, A., Vitucci, D., Orlandella, F. M., Terracciano, A., Mariniello, R. M., Imperlini, E., Grazioli, E., Orrù, S., Krustrup, P., Salvatore, G., et al. (2021) · European Journal of Applied Physiology · doi:10.1007/s00421-021-04733-1 · Cited by 14 · see citing works
Chen, M., Li, S., Hao, M.-L., Chen, J., Zhao, Z., Hong, S., Min, J., Tang, J., Hu, M., & Li, H. (2020) · FEBS Open Bio · doi:10.1002/2211-5463.12965 · Cited by 13 · see citing works
Barbalho, S. M., Tofano, R. J., Chagas, E. F. B., Detregiachi, C. R. P., Goulart, R. D. Á., & Flato, U. A. P. (2021) · Experimental Gerontology · doi:10.1016/j.exger.2021.111302 · Cited by 12 · see citing works
Wang, M., Wu, X., Jiao, Y., Yin, W., & Zhang, L. (2024) · Aging and Disease · doi:10.14336/ad.2024.0318 · Cited by 11 · see citing works
“…(mTOR) stimulates the ubiquitin ligase muscle atrophy F-box protein (atrogin-1) and muscle specific ring finger protein 1 (MuRF1) in UPS and acts downstream of forkhead box protein O (FoxO) to promote enhanced apoptosis and are thought to be the primary controllers of muscle proteolysis [7].”
Ren, Y.-Y., Koch, L. G., Britton, S. L., Qi, N., Treutelaar, M. K., Burant, C., & Li, J. Z. (2016) · Physiological Genomics · doi:10.1152/physiolgenomics.00118.2015 · Cited by 11 · see citing works
Filippo, E. S. D., Bondi, D., Pietrangelo, T., Fanò, G., & Fulle, S. (2020) · Journal of Science in Sport and Exercise · doi:10.1007/s42978-020-00065-2 · Cited by 10 · see citing works
Muscle Insulin Resistance Elicits Muscle Atrophy in Obesity
Razi, O., Zamani, N., Saeidi, A., Hadjicharalambous, M., Ayed, K., Hackney, A. C., Coso, J. D., Laher, I., Muscogiuri, G., & Zouhal, H. (2025) · Current Obesity Reports · doi:10.1007/s13679-025-00672-6 · Cited by 11 · see citing works
The CB1 cannabinoid receptor regulates autophagy in the tibialis anterior skeletal muscle in mice
Sepúlveda, C., Rodríguez, J. M., Monsalves‐Álvarez, M., Donoso-Barraza, C., la Fuente, F. P.-D., Matias, I., Lesté-Lasserre, T., Zizzari, P., Morselli, E., Cota, D., et al. (2023) · Biological Research · doi:10.1186/s40659-023-00426-5 · Cited by 8 · see citing works
“Conversely, the stimulation of autophagy induces beneficial effects, such as retarding the age-dependent loss of muscle mass [11].”
BackgroundBondı̀, M., Germinario, E., Pirazzini, M., Zanetti, G., Cencetti, F., Donati, C., Gorza, L., Betto, R., Bruni, P., & Danieli‐Betto, D. (2017) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00027.2017 · Cited by 8 · see citing works
“old muscles (65), eventually worsening sarcopenia (25).”
MOLECULAR ASPECTS OF SARCOPENIA PATHOGENESIS IN CHRONOC KIDNEY DISEASE: INTEGRATED ROLE OF mTOR
Гасанов, М. З. (2018) · Nephrology (Saint-Petersburg) · doi:10.24884/1561-6274-2018-22-5-9-16 · Cited by 8 · see citing works
“Известно, что миостатин оказывает свое тормозное влияние на mTORC1 через SMAD2/3-Aktсигнальный путь, уменьшая его активность путем блокады транскрипции генов, ответственных за миогенез (миогенин, мио-D) и, тем самым, снижая синтез белка [49, 54, 55].”
BackgroundInfluentialRole of autophagy in bone and muscle biology
Valenti, M. T., Carbonare, L. D., & Mottes, M. (2016) · World Journal of Stem Cells · doi:10.4252/wjsc.v8.i12.396 · Cited by 8 · see citing works
Oh, G., Men, X., La, I.-J., Han, X., Lee, S.-J., Im, J., Fu, X., Lim, J.-S., Bae, K. S., Seong, G.-S., et al. (2024) · Food Science and Biotechnology · doi:10.1007/s10068-024-01702-0 · Cited by 7 · see citing works
“In aged skeletal muscles, diminished autophagic activity caused by impaired protein turnover leads to the accumulation of modified proteins (Fan et al., 2016).”
Akabane, T., Sagae, H., van Wijk, K., Saitoh, S., Kimura, T., Okano, S., Kodama, K., Takahashi, K., Nakajima, M., Tanaka, T., et al. (2024) · Scientific Reports · doi:10.1038/s41598-024-73049-9 · Cited by 7 · see citing works
“Several studies have suggested that age-dependent decreases in autophagy contribute to sarcopenia 16 .”
Sarcopenia: an Aging Perspective and Management Options
Teixeira, A. M., Nosrani, S. E., Parvani, M., Viola, J., & Mohammadi, S. (2025) · International Journal of Sports Medicine · doi:10.1055/a-2577-2577 · Cited by 7 · see citing works
Efficacy of Baduanjin Exercise for Sarcopenia in Older Adults: A 24‐Week Randomized Controlled Trial
Wu, K., Chen, X., Long, K., Yue, S., Li, W., Duan, X., Zhang, J., Liu, T., Chen, Y., Ye, K., et al. (2025) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.70163 · Cited by 6 · see citing works
“Current therapeutic strategies include exercise interventions, nutritional support and pharmacotherapy [6, 7].”
The impact of mechanically stimulated muscle-derived stromal cells on aged skeletal muscle
Huntsman, H. D., Rendeiro, C., Merritt, J. R., Pincu, Y., Cobert, A., Lisio, M. D., Kolyvas, E. A., Dvoretskiy, S., Dobrucki, I. T., Kemkemer, R., et al. (2017) · Experimental Gerontology · doi:10.1016/j.exger.2017.12.012 · Cited by 7 · see citing works
“The molecular basis for anabolic resistance and subsequent declines in mass and function is controversial, yet inadequate progenitor cell activation and muscle protein turnover likely contribute [Carnio et al., 2014; Conboy et al., 2003; Fan et al., 2016].”
Xue, X., Xu, J., Wang, H., Wang, K., Chen, Y., Xu, Y., Que, S., & Liu, Z. (2026) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2025.1710582 · Cited by 6 · see citing works
Sun, Y., Zheng, Q., Sun, J., Wang, L., & Li, Y. (2023) · Food Reviews International · doi:10.1080/87559129.2023.2274487 · Cited by 6 · see citing works
“[6,7] Amelioration of sarcopenia may be achievable by modulating autophagy.”
The Interactome in the Evolution From Frailty to Sarcopenic Dependence
Coto‐Montes, A. M., González‐Blanco, L., Antuña, E., Menéndez‐Valle, I., Bermejo-Millo, J. C., Caballero, B., Vega‐Naredo, I., & Potes, Y. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.792825 · Cited by 6 · see citing works
“The appropriate induction of autophagy through the regulation of AMP-activated protein kinase (AMPK), the phosphatidylinositol-3-kinase (PI3K)/Akt and the mammalian target of rapamycin (mTOR) signaling pathways seems to suppress skeletal muscle loss (Bonaldo and Sandri, 2013; Fan et al., 2016).”
BackgroundMishra, D., & Mohapatra, L. (2026) · Biochemical Pharmacology · doi:10.1016/j.bcp.2026.117813 · Cited by 5 · see citing works
Autophagy in striated muscle diseases
Bailin, P. L., Zhang, L., Zhang, L., & Han, R. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.1000067 · Cited by 5 · see citing works
Polycystin-2 Is Required for Starvation- and Rapamycin-Induced Atrophy in Myotubes
Kretschmar, C., Peña‐Oyarzún, D., Hernando, C., Hernández, N., Molina‐Berríos, A., Hernández‐Cáceres, M. P., Lavandero, S., Budini, M., Morselli, E., Parra, V., et al. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00280 · Cited by 5 · see citing works
Shi, F., & Chen, J. (2025) · Aging and Disease · doi:10.14336/ad.2025.0670 · Cited by 5 · see citing works
“Activation of multiple signaling pathways, such as the PI3K/Akt pathway, myostatin signaling, the UPS, and the autophagy-lysosomal system, can effectively enhance autophagic activity and delay skeletal muscle loss [115].”
Kamihara, T., Omura, T., & Shimizu, A. (2025) · Geriatrics and gerontology international/Geriatrics & gerontology international · doi:10.1111/ggi.70042 · Cited by 4 · see citing works
Jabeen, S., & Qazi, J. I. (2023) · Nutrition · doi:10.1016/j.nut.2023.112110 · Cited by 3 · see citing works
Protein Structure and Function in Aging and Age-Related Diseases
Mittal, A., & Rath, P. C. (2020) · Springer eBooks · doi:10.1007/978-981-32-9005-1_1 · Cited by 3 · see citing works
Sheptulina, A. F., Bryk, D. D., Мамутовна, М. Э., Yafarova, A. A., & Drapkina, O. M. (2024) · Russian Journal of Preventive Medicine · doi:10.17116/profmed202427081114 · Cited by 2 · see citing works
Polyamines and autophagy as a dynamic regulatory network in skeletal muscle regeneration and aging
Attili, L., Rossi, M. N., Santo, R. D., Duranti, G., Ceci, R., & Cervelli, M. (2026) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2026.112188 · Cited by 3 · see citing works
Oh, G., Han, X., Men, X., Im, J., Fu, X., Lim, J.-S., Lee, L., Kwon, M. H., Lee, H. S., Ra, M., et al. (2024) · Food Science and Biotechnology · doi:10.1007/s10068-024-01675-0 · Cited by 2 · see citing works
“In aged skeletal muscles, inhibited autophagic activity resulting from impaired protein turnover, leads to the accumulation of transformed proteins (Fan et al., 2016).”
The Relationship between the Mechanism of Sarcopenia and Exercise Based on Data Mining
Li, S., Cong, Z., & Li, L. (2022) · Computational and Mathematical Methods in Medicine · doi:10.1155/2022/9339905 · Cited by 2 · see citing works
RetractedRajasekaran, S., Santhaseela, A. R., Ragunathan, S., Venkataraman, S., & Jayavelu, T. (2022) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-022-01123-y · Cited by 2 · see citing works
Linking mitochondrial dysfunction to sarcopenia
Alway, S. E. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822146-4.00004-1 · Cited by 1 · see citing works
Studies on the Involvement of Amino Acids in the Mechanisms Regulating Degradation of Muscle Protein
Nagasawa, T. (2018) · Nippon Eiyo Shokuryo Gakkaishi · doi:10.4327/jsnfs.71.3 · Cited by 1 · see citing works
VanDusseldorp, T. A. (2016) · UNM’s Digital Repository (University of New Mexico)
SARCOPENIA : Immunological Perspective and Efficacy of Exercise Interventions
Mathur, D. A., & Gupta, A. S. (2018) · Zenodo (CERN European Organization for Nuclear Research) · doi:10.5281/zenodo.21567755
Research Progress of Chronic Obstructive Pulmonary Disease Associated with Sarcopenia
杜, 丽. (2023) · Advances in Clinical Medicine · doi:10.12677/acm.2023.1391979
Sepúlveda, C., Rodríguez, J. M., Monsalves-Álvarez, M., Donoso-Barraza, C., la Fuente, F. P.-D., Matias, I., Lesté-Lasserre, T., Zizzari, P., Morselli, E., Cota, D., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26577623
Jiang, Q., Yan, M., Zhao, Y., Zhou, X., Yin, L., Feng, L., Liu, Y., Jiang, W., Wu, P., Wang, Y., et al. (2021) · Figshare · doi:10.6084/m9.figshare.14446000
Leite, D. M. D. M., Melo, B. P., da Silva, M. A., Pizzol, G. G., Leocádio, P. C. L., Leite, J. I. A., & Soares, D. D. (2025) · Research Square · doi:10.21203/rs.3.rs-8369611/v1
- Authors
- Fan, J., Kou, X., Jia, S., Yang, X., Yang, Y., & Chen, N.
- Affiliations
- Wuhan Sports University (CN)
- Corresponding author
- Chen, Ning
- Venue
- Journal of Cellular Physiology
- Publisher
- Wiley
- Published
- 2015-12-10
- Volume
- 231
- Issue
- 7
- Pages
- 1450-1459
- ISSN
- 0021-9541 (ISSN-L)
- OpenAlex
- W2172616946
- Cited by
- 101
- References
- 144
- Citations by year
- 2026: 4 · 2025: 7 · 2024: 9 · 2023: 9 · 2022: 6 · 2021: 11 · 2020: 13 · 2019: 10 · 2018: 13 · 2017: 7 · 2016: 12
- FWCI
- 1.39
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Cellular Physiology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- The National Natural Science Foundation of China (31571228)
- Key Research Project From General Administration of Sport of China (2014B093)
- China Postdoctoral Science Foundation (2015M582292)
- The Planned Project From Education Department of Hubei Province (B2014107)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Physiology › Nutrition and Health in Aging
- Keywords
- sarcopenia, autophagy, skeletal muscle aging, mitochondrial quality control, protein degradation, protein synthesis, autophagy pathway, physical activity, caloric restriction, autophagy regulation
- MeSH terms
- Aged, Aging, Autophagy, Humans, Mitochondria, Muscle, Skeletal, Sarcopenia
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