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Denervation-induced skeletal muscle atrophy is associated with increased mitochondrial ROS production
Abstract
Reactive oxygen species (ROS), especially mitochondrial ROS, are postulated to play a significant role in muscle atrophy. We report a dramatic increase in mitochondrial ROS generation in three conditions associated with muscle atrophy: in aging, in mice lacking CuZn-SOD (Sod1(-/-)), and in the neurodegenerative disease, amyotrophic lateral sclerosis (ALS). ROS generation in muscle mitochondria is nearly threefold higher in 28- to 32-mo-old than in 10-mo-old mice and is associated with a 30% loss in gastrocnemius mass. In Sod1(-/-) mice, muscle mitochondrial ROS production is increased >100% in 20-mo compared with 5-mo-old mice along with a >50% loss in muscle mass. ALS G93A mutant mice show a 75% loss of muscle mass during disease progression and up to 12-fold higher muscle mitochondrial ROS generation. In a second ALS mutant model, H46RH48Q mice, ROS production is approximately fourfold higher than in control mice and is associated with a less dramatic loss (30%) in muscle mass. Thus ROS production is strongly correlated with the extent of muscle atrophy in these models. Because each of the models of muscle atrophy studied are associated to some degree with a loss of innervation, we were interested in determining whether denervation plays a role in ROS generation in muscle mitochondria isolated from hindlimb muscle following surgical sciatic nerve transection. Seven days post-denervation, muscle mitochondrial ROS production increased nearly 30-fold. We conclude that enhanced generation of mitochondrial ROS may be a common factor in the mechanism underlying denervation-induced atrophy.
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“Enhanced generation of mitochondrial ROS may be a common factor in the mechanism underlying denervation-induced atrophy [15].”
From Nutraceuticals in the Prevention and Treatment of the Muscle Atrophy (2021) · cites this paper as [15]
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Cites
Motor Neuron Degeneration in Mice that Express a Human Cu,Zn Superoxide Dismutase Mutation
Gurney, M. E., Pu, H., Chiu, A. Y., Dal Canto, M. C., Polchow, C. Y., Alexander, D. D., Caliendo, J., Hentati, A., Kwon, Y. W., Deng, H.-X., et al. (1994) · Science · doi:10.1126/science.8209258 · Cited by 4,143
Reactivity of HO2/O− 2 radicals in aqueous solution
Bielski, B. H. J., Cabelli, D. E., Arudi, R. L., & Ross, A. B. (1985) · Journal of Physical and Chemical Reference Data · doi:10.1063/1.555739 · Cited by 2,169
The Respiratory Chain and Oxidative Phosphorylation
Chance, B., & Williams, G. R. (1956) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470122624.ch2 · Cited by 2,084
[7] Mitochondrial respiratory control and the polarographic measurement of ADP : O ratios
Estabrook, R. W. (1967) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(67)10010-4 · Cited by 1,781
Production of Reactive Oxygen Species by Mitochondria
Chen, Q., Vazquez, E. J., Moghaddas, S., Hoppel, C. L., & Lesnefsky, E. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304854200 · Cited by 1,616
Zhou, M., Diwu, Z. J., Panchuk-Voloshina, N., & Haugland, R. P. (1997) · Analytical Biochemistry · doi:10.1006/abio.1997.2391 · Cited by 1,400
Amyotrophic lateral sclerosis is a distal axonopathy: evidence in mice and man
Fischer, L. R., Culver, D. G., Tennant, P., Davis, A. A., Wang, M.-S., Castellano-Sanchez, A. A., Khan, J., Polak, M. A., & Glass, J. D. (2004) · Experimental Neurology · doi:10.1016/j.expneurol.2003.10.004 · Cited by 1,383
IKKβ/NF-κB Activation Causes Severe Muscle Wasting in Mice
Cai, D., Frantz, J. D., Tawa, N. E., Melendez, P. A., Oh, B.-C., Lidov, H. G. W., Hasselgren, P.-O., Frontera, W. R., Lee, J., Glass, D. J., et al. (2004) · Cell · doi:10.1016/j.cell.2004.09.027 · Cited by 1,367
Partial Resolution of the Enzymes Catalyzing Oxidative Phosphorylation
Kagawa, Y., & Racker, E. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61930-1 · Cited by 1,361
Mitochondrial metabolism of reactive oxygen species
Andreyev, A. Y., Kushnareva, Y. E., & Starkov, A. A. (2005) · Biochemistry (Moscow) · doi:10.1007/s10541-005-0102-7 · Cited by 1,336
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Cleasby, M. E., Jamieson, P. M., & Atherton, P. J. (2016) · Journal of Endocrinology · doi:10.1530/joe-15-0533 · Cited by 596
Szeto, H. H. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12461 · Cited by 561
Innervation and neuromuscular control in ageing skeletal muscle
Hepple, R. T., & Rice, C. L. (2015) · The Journal of Physiology · doi:10.1113/jp270561 · Cited by 417
Lovelace, M. D., Varney, B., Sundaram, G., Lennon, M. J., Lim, C. K., Jacobs, K., Guillemin, G. J., & Brew, B. J. (2017) · Neuropharmacology · doi:10.1016/j.neuropharm.2016.03.024 · Cited by 393
The Neuromuscular Junction: Aging at the Crossroad between Nerves and Muscle
González‐Freire, M., de Cabo, R., Studenski, S. A., & Ferrucci, L. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00208 · Cited by 386
Mitochondrial dysfunction: roles in skeletal muscle atrophy
Chen, X., Ji, Y., Liu, R., Zhu, X., Wang, K., Yang, X., Liu, B., Gao, Z., Huang, Y. H., Shen, Y., et al. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04369-z · Cited by 362
Clinical perspective on oxidative stress in sporadic amyotrophic lateral sclerosis
D’Amico, E., Factor-Litvak, P. R., Santella, R. M., & Mitsumoto, H. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.06.029 · Cited by 328
Wong, M., & Martin, L. J. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq106 · Cited by 318
Clinical Spectrum of Amyotrophic Lateral Sclerosis (ALS)Preprint
Grad, L. I., Rouleau, G. A., Ravits, J., & Cashman, N. R. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024117 · Cited by 344
Barja, G. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.5148 · Cited by 290
Jang, Y. C., Lustgarten, M. S., Liu, Y., Müller, F. L., Bhattacharya, A., Liang, H., Salmon, A. B., Brooks, S. V., Larkin, L. M., Hayworth, C. R., et al. (2009) · The FASEB Journal · doi:10.1096/fj.09-146308 · Cited by 290
Mitochondrial signaling contributes to disuse muscle atrophy
Powers, S. K., Wiggs, M. P., Duarte, J. A., Zergeroğlu, A. M., & Demirel, H. A. (2012) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00609.2011 · Cited by 251
Picard, M., Ritchie, D., Wright, K. J., Romestaing, C., Thomas, M. M., Rowan, S. L., Taivassalo, T., & Hepple, R. T. (2010) · Aging Cell · doi:10.1111/j.1474-9726.2010.00628.x · Cited by 238
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Powers, S. K., Smuder, A. J., & Judge, A. R. (2012) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0b013e328352b4c2 · Cited by 234
Hyatt, H. W., Deminice, R., Yoshihara, T., & Powers, S. K. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.11.005 · Cited by 226
Kavazis, A. N., Talbert, E. E., Smuder, A. J., Hudson, M. B., Nelson, W. B., & Powers, S. K. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.01.002 · Cited by 213
Abadi, A., Glover, E. I., Isfort, R. J., Raha, S., Safdar, A., Yasuda, N., Kaczor, J. J., Melov, S., Hubbard, A., Qu, X., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006518 · Cited by 189
VanderVeen, B. N., Fix, D. K., & Carson, J. A. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/3292087 · Cited by 188
Buffenstein, R., Edrey, Y. H., Yang, T., & Mele, J. (2008) · AGE · doi:10.1007/s11357-008-9058-z · Cited by 185
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Sanz, A., & Stefanatos, R. K. A. (2008) · Current Aging Science · doi:10.2174/1874609810801010010 · Cited by 177
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Bouvière, J., Fortunato, R. S., Dupuy, C., Werneck‐de‐Castro, J. P., de Carvalho, D. P., & Louzada, R. A. N. (2021) · Antioxidants · doi:10.3390/antiox10040537 · Cited by 184
Arouche-Delaperche, L., Allenbach, Y., Amelin, D., Preuße, C., Mouly, V., Mauhin, W., Dzangué-Tchoupou, G., Drouot, L., Boyer, O., Stenzel, W., et al. (2017) · Annals of Neurology · doi:10.1002/ana.24902 · Cited by 182
Ravits, J., Appel, S. H., Baloh, R. H., Barohn, R. J., Brooks, B. R., Elman, L. B., Floeter, M. K., Henderson, C. E., Lomen, C. E., Macklis, J. D., et al. (2013) · Amyotrophic Lateral Sclerosis and Frontotemporal Degeneration · doi:10.3109/21678421.2013.778548 · Cited by 179
Unravelling the mechanisms regulating muscle mitochondrial biogenesis
Hood, D. A., Tryon, L. D., Carter, H. N., Kim, Y., & Chen, C. C. W. (2016) · Biochemical Journal · doi:10.1042/bcj20160009 · Cited by 159
Mitochondria as a Target for Mitigating Sarcopenia
Coen, P. M., Musci, R. V., Hinkley, J. M., & Miller, B. F. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2018.01883 · Cited by 163
Mitochondrial Involvement and Impact in Aging Skeletal Muscle
Hepple, R. T. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00211 · Cited by 161
Mitochondria initiate and regulate sarcopenia
Alway, S. E., Mohamed, J. S., & Myers, M. J. (2017) · Exercise and Sport Sciences Reviews · doi:10.1249/jes.0000000000000101 · Cited by 153
“Thus, we would expect that altered neuronal signaling is due at least in part to high ROS production and mitochondrial dysfunction in the muscle cells, and conversely, that neural dysfunction will be communicated to muscle cells (57,100).”
BackgroundAngiotensin II, Oxidative Stress and Skeletal Muscle Wasting
Sukhanov, S., Yoshida, T., Tabony, A. M., Higashi, Y., Galvez, S., Delafontaine, P., & Semprun‐Prieto, L. (2011) · The American Journal of the Medical Sciences · doi:10.1097/maj.0b013e318222e620 · Cited by 158
Muller, F. L., Liu, Y., Abdul-Ghani, M. A., Lustgarten, M. S., Bhattacharya, A., Jang, Y. C., & Van Remmen, H. (2008) · Biochemical Journal · doi:10.1042/bj20071162 · Cited by 150
Self-citationPicard, M. A., Ritchie, D., Thomas, M. M., Wright, K. J., & Hepple, R. T. (2011) · Aging Cell · doi:10.1111/j.1474-9726.2011.00745.x · Cited by 154
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Chen, L., Na, R., Gu, M., Salmon, A. B., Liu, Y., Liang, H., Qi, W., Remmen, H. V., Richardson, A. G., & Ran, Q. (2008) · Aging Cell · doi:10.1111/j.1474-9726.2008.00432.x · Cited by 146
Yoshida, T., Tabony, A. M., Galvez, S., Mitch, W. E., Higashi, Y., Sukhanov, S., & Delafontaine, P. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.05.035 · Cited by 144
Hyatt, H. W., & Powers, S. K. (2021) · Antioxidants · doi:10.3390/antiox10040588 · Cited by 134
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Verma, S., Khurana, S., Vats, A., Sahu, B., Ganguly, N. K., Chakraborti, P., Gourie-Devi, M., & Taneja, V. (2022) · Molecular Neurobiology · doi:10.1007/s12035-021-02658-6 · Cited by 127
Fischer, L. R., Igoudjil, A., Magrané, J., Li, Y., Hansen, J. M., Manfredi, G., & Glass, J. D. (2010) · Brain · doi:10.1093/brain/awq314 · Cited by 117
Ayyadevara, S., Bharill, P., Dandapat, A., Hu, C., Khaidakov, M., Mitra, S., Reis, R. J. S., & Mehta, J. L. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4151 · Cited by 116
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Yoshida, T., & Delafontaine, P. (2015) · The American Journal of the Medical Sciences · doi:10.1097/maj.0000000000000511 · Cited by 117
Damiano, S., Muscariello, E., Rosa, G. L., Maro, M. D., Mondola, P., & Santillo, M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20153815 · Cited by 116
Jackson, J. R., Ryan, M. J., Hao, Y., & Alway, S. E. (2010) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00489.2010 · Cited by 105
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Spendiff, S., Vuda, M., Gouspillou, G., Aare, S., Pérez, A., Morais, J. A., Jagoe, R. T., Filion, M., Glicksman, R., Kapchinsky, S., et al. (2016) · The Journal of Physiology · doi:10.1113/jp272487 · Cited by 101
Fischer, L. R., Li, Y., Asress, S. A., Jones, D. P., & Glass, J. D. (2011) · Experimental Neurology · doi:10.1016/j.expneurol.2011.09.020 · Cited by 98
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 100
Shen, Y., Zhang, Q., Huang, Z., Zhu, J., Qiu, J., Ma, W., Yang, X., Ding, F., & Sun, H. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00988 · Cited by 95
Qaisar, R., Bhaskaran, S., Premkumar, P., Ranjit, R., Natarajan, K. S., Ahn, B., Riddle, K., Claflin, D. R., Richardson, A., Brooks, S. V., et al. (2018) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12339 · Cited by 95
Self-citationNrf2 deficiency exacerbates age-related contractile dysfunction and loss of skeletal muscle mass
Ahn, B., Pharaoh, G. A., Premkumar, P., Huseman, K., Ranjit, R., Kinter, M. T., Szweda, L. I., Kiss, T., Fülöp, G. Á., Tarantini, S., et al. (2018) · Redox Biology · doi:10.1016/j.redox.2018.04.004 · Cited by 94
Bhatnagar, S., Panguluri, S. K., Gupta, S. K., Dahiya, S., Lundy, R. F., & Kumar, A. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013262 · Cited by 94
Lustgarten, M. S., Jang, Y. C., Liu, Y., Qi, W., Qin, Y., Dahia, P. L. M., Shi, Y., Bhattacharya, A., Müller, F. L., Shimizu, T., et al. (2011) · Aging Cell · doi:10.1111/j.1474-9726.2011.00695.x · Cited by 96
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Qaisar, R., Bhaskaran, S., Ranjit, R., Sataranatarajan, K., Premkumar, P., Huseman, K., & Remmen, H. V. (2018) · Redox Biology · doi:10.1016/j.redox.2018.09.018 · Cited by 92
Oxidative stress as a therapeutic target during muscle wasting: considering the complex interactions
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Sakellariou, G. K., Davis, C. S., Shi, Y., Ivannikov, M. V., Zhang, Y., Vasilaki, A., Macleod, G. T., Richardson, A. G., Remmen, H. V., Jackson, M. J., et al. (2013) · The FASEB Journal · doi:10.1096/fj.13-240390 · Cited by 90
Bhattacharya, A., Müller, F. L., Liu, Y., Sabia, M., Liang, H., Song, W. J., Jang, Y. C., Ran, Q., & Remmen, H. V. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806311200 · Cited by 90
Age-related changes in skeletal muscle mitochondria: the role of exercise
Seo, D. Y., Lee, S. R., Kim, N., Ko, K. S., Rhee, B. D., & Han, J. (2016) · Integrative Medicine Research · doi:10.1016/j.imr.2016.07.003 · Cited by 89
Mitochondrial Dysfunction in Skeletal Muscle Pathologies
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Liang, Y., Xie, S., He, Y., Xu, M., Qiao, X., Zhu, Y. H., & Wu, W. (2022) · Disease Markers · doi:10.1155/2022/9484217 · Cited by 92
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Dynamic changes in the skeletal muscle proteome during denervation-induced atrophy
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Increased serum ferritin levels in amyotrophic lateral sclerosis (ALS) patients
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Tamura, Y., Kitaoka, Y., Matsunaga, Y., Hoshino, D., & Hatta, H. (2015) · The Journal of Physiology · doi:10.1113/jp270093 · Cited by 83
Accelerated sarcopenia in Cu/Zn superoxide dismutase knockout mice
Deepa, S. S., Van Remmen, H., Brooks, S. V., Faulkner, J. A., Larkin, L., McArdle, A., Jackson, M. J., Vasilaki, A., & Richardson, A. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.06.032 · Cited by 78
Thomas, D. T., DelCimmuto, N. R., Flack, K. D., Stec, D. E., & Hinds, T. D. (2022) · Antioxidants · doi:10.3390/antiox11020179 · Cited by 79
Jackson, M. J. (2016) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2016.05.002 · Cited by 83
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Shukla, S. K., Markov, S. D., Attri, K. S., Vernucci, E., King, R. J., Dasgupta, A., Grandgenett, P. M., Hollingsworth, M. A., Singh, P. K., Yu, F., et al. (2020) · Cancer Letters · doi:10.1016/j.canlet.2020.04.017 · Cited by 81
Tang, H., Lee, M. C., Budak, M. T., Pietras, N., Hittinger, S. A., Vu, M. D., Khuong, A., Hoang, C. D., Hussain, S. N. A., Levine, S., et al. (2011) · The FASEB Journal · doi:10.1096/fj.11-183798 · Cited by 78
Mukai, R., Matsui, N., Fujikura, Y., Matsumoto, N., Hou, D., Kanzaki, N., Shibata, H., Horikawa, M., Iwasa, K., Hirasaka, K., et al. (2016) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2016.02.001 · Cited by 76
Palomero, J., Vasilaki, A., Pye, D., McArdle, A., & Jackson, M. J. (2013) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00530.2012 · Cited by 71
Pierce, A. P., Mirzaei, H., Müller, F. L., de Waal, E., Taylor, A. B., Leonard, S., Remmen, H. V., Regnier, F. E., Richardson, A., & Chaudhuri, A. R. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.07.088 · Cited by 72
Madungwe, N. B., Zilberstein, N., Feng, Y., & Bopassa, J. C. (2016) · PubMed Central · Cited by 71
Ahn, B., Ranjit, R., Premkumar, P., Pharaoh, G. A., Piekarz, K. M., Matsuzaki, S., Claflin, D. R., Riddle, K., Judge, J., Bhaskaran, S., et al. (2019) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12375 · Cited by 70
Michelucci, A., Chen, L., Protasi, F., & Dirksen, R. T. (2021) · Metabolites · doi:10.3390/metabo11070424 · Cited by 75
Nutritional and metabolic support in patients with amyotrophic lateral sclerosis
Muscaritoli, M., Kushta, I., Molfino, A., Inghilleri, M., Sabatelli, M., & Fanelli, F. R. (2012) · Nutrition · doi:10.1016/j.nut.2012.01.011 · Cited by 70
Sidlauskaite, E., Gibson, J. W., Megson, I. L., Whitfield, P. D., Tovmasyan, A. G., Batinic̈‐Haberle, I., Murphy, M. P., Moult, P. R., & Cobley, J. N. (2018) · Redox Biology · doi:10.1016/j.redox.2018.03.012 · Cited by 68
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Agostini, D., Gervasi, M., Ferrini, F., Bartolacci, A., Stranieri, A., Piccoli, G., Barbieri, E., Sestili, P., Patti, A., Stocchi, V., et al. (2023) · Nutrients · doi:10.3390/nu15081802 · Cited by 81
Uchida, T., Sakashita, Y., Kitahata, K., Yamashita, Y., Tomida, C., Kimori, Y., Komatsu, A., Hirasaka, K., Ohno, A., Nakao, R., et al. (2018) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00184.2017 · Cited by 62
Watanabe, K., Shibuya, S., Ozawa, Y., Nojiri, H., Izuo, N., Yokote, K., & Shimizu, T. (2014) · BioMed Research International · doi:10.1155/2014/140165 · Cited by 63
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Zhou, J., Li, A., Li, X., & Yi, J. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.01.024 · Cited by 59
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Bhaskaran, S., Pollock, N., Macpherson, P. C. D., Ahn, B., Piekarz, K. M., Staunton, C. A., Brown, J. L., Qaisar, R., Vasilaki, A., Richardson, A. G., et al. (2020) · Aging Cell · doi:10.1111/acel.13225 · Cited by 61
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Xu, H., Brown, J. L., Bhaskaran, S., & Van Remmen, H. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.11.046 · Cited by 61
Mitochondrial health and muscle plasticity after spinal cord injury
Gorgey, A. S., Witt, O., O’Brien, L. C., Cardozo, C. P., Chen, Q., Lesnefsky, E. J., & Graham, Z. (2018) · European Journal of Applied Physiology · doi:10.1007/s00421-018-4039-0 · Cited by 64
Redox Characterization of Functioning Skeletal Muscle
Zuo, L., & Pannell, B. K. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00338 · Cited by 60
Vasilaki, A., van der Meulen, J. H., Larkin, L. M., Harrison, D. C., Pearson, T., Remmen, H. V., Richardson, A., Brooks, S. V., Jackson, M. J., & McArdle, A. (2010) · Aging Cell · doi:10.1111/j.1474-9726.2010.00635.x · Cited by 60
Halter, B., de Aguilar, J. G., René, F., Petri, S., Fricker, B., Echaniz‐Laguna, A., Dupuis, L., Larmet, Y., & Loeffler, J. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.01.014 · Cited by 61
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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
Czyżowska, A., Brown, J. L., Xu, H., Sataranatarajan, K., Kinter, M. T., Tyrrell, V. J., O’Donnell, V. B., & Remmen, H. V. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102761 · Cited by 58
Qaisar, R., Pharaoh, G. A., Bhaskaran, S., Xu, H., Ranjit, R., Bian, J., Ahn, B., Georgescu, C., Wren, J. D., & Remmen, H. V. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms22010037 · Cited by 57
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Benedusi, V., Martorana, F., Brambilla, L., Maggi, A. C., & Rossi, D. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.366419 · Cited by 58
Rahman, A., Rao, M. S. R., & Khan, K. M. (2018) · Journal of Neuroinflammation · doi:10.1186/s12974-018-1306-2 · Cited by 59
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Sánchez-Castellano, C., Martín‐Aragón, S., Bermejo‐Bescós, P., Vaquero-Pinto, N., Miret-Corchado, C., de Miguel, A. M., & Cruz-Jentoft, A. J. (2020) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12508 · Cited by 58
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Jin, K., Imada, T., Hisamura, R., Ito, M., Toriumi, H., Tanaka, K. F., Nakamura, S., & Tsubota, K. (2020) · American Journal Of Pathology · doi:10.1016/j.ajpath.2020.01.007 · Cited by 59
Squecco, R., Carraro, U., Kern, H., Pond, A. L., Adami, N., Biral, D., Vindigni, V., Boncompagni, S., Pietrangelo, T., Bosco, G., et al. (2009) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181c18416 · Cited by 55
SOD1 nanozyme with reduced toxicity and MPS accumulation
Jiang, Y., Arounleut, P., Rheiner, S., Bae, Y., Kabanov, A. V., Milligan, C., & Manickam, D. S. (2016) · Journal of Controlled Release · doi:10.1016/j.jconrel.2016.02.038 · Cited by 55
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Lawler, J. M., Rodriguez, D., & Hord, J. M. (2016) · The Journal of Physiology · doi:10.1113/jp270656 · Cited by 53
Britto, F. A., Cortade, F., Belloum, Y., Blaquière, M., Gallot, Y. S., Docquier, A., Pagano, A. F., Jublanc, É., Bendridi, N., Koechlin‐Ramonatxo, C., et al. (2018) · BMC Biology · doi:10.1186/s12915-018-0525-4 · Cited by 68
Ko, I. K., Lee, B., Lee, S. J., Andersson, K., Atala, A., & Yoo, J. J. (2013) · Biomaterials · doi:10.1016/j.biomaterials.2013.01.029 · Cited by 53
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Hamilton, R. T. (2012) · Journal of Clinical & Experimental Pathology · doi:10.4172/2161-0681.s4-005 · Cited by 53
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Metadata
- Authors
- Muller, F. L., Song, W., Jang, Y. C., Liu, Y., Sabia, M., Richardson, A., & Van Remmen, H.
- Affiliations
- Seoul National University (KR)
- The University of Texas at San Antonio Health Science Center (US)
- Venue
- American Journal of Physiology-Regulatory, Integrative and Comparative Physiology
- Publisher
- American Physiological Society
- Published
- 2007-09
- Volume
- 293
- Issue
- 3
- Pages
- R1159-R1168
- ISSN
- 0363-6119 (ISSN-L)
- 1522-1490
- OpenAlex
- W2137182040
- Cited by
- 355
- References
- 88
- Citations by year
- 2026: 11 · 2025: 14 · 2024: 16 · 2023: 14 · 2022: 35 · 2021: 23 · 2020: 29 · 2019: 23 · 2018: 25 · 2017: 19 · 2016: 26 · 2015: 18 · 2014: 13 · 2013: 20 · 2012: 16
- FWCI
- 5.03
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- American Journal of Physiology-Regulatory, Integrative and Comparative Physiology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (5T3 AG 021890 02, P01 AG-20591, P01AG020591, T32AG021890)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
- Keywords
- skeletal muscle atrophy, denervation, mitochondrial reactive oxygen species, oxidative stress, sciatic nerve transection, aging, amyotrophic lateral sclerosis, muscle mass loss, hindlimb muscles
- MeSH terms
- Superoxide Dismutase-1, Amyotrophic Lateral Sclerosis, Animals, Female, Mice, Inbred C57BL, Mitochondria, Muscle, Muscle Denervation, Muscular Atrophy, Organ Size, Oxygen Consumption, Sciatic Nerve, Superoxide Dismutase, Reactive Oxygen Species, Mice, Knockout, Oxidative Stress, Muscle, Skeletal, Mice
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