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Ryanodine Receptor Oxidation Causes Intracellular Calcium Leak and Muscle Weakness in Aging
Open accessAbstract
Age-related loss of muscle mass and force (sarcopenia) contributes to disability and increased mortality. Ryanodine receptor 1 (RyR1) is the skeletal muscle sarcoplasmic reticulum calcium release channel required for muscle contraction. RyR1 from aged (24 months) rodents was oxidized, cysteine-nitrosylated, and depleted of the channel-stabilizing subunit calstabin1, compared to RyR1 from younger (3-6 months) adults. This RyR1 channel complex remodeling resulted in "leaky" channels with increased open probability, leading to intracellular calcium leak in skeletal muscle. Similarly, 6-month-old mice harboring leaky RyR1-S2844D mutant channels exhibited skeletal muscle defects comparable to 24-month-old wild-type mice. Treating aged mice with S107 stabilized binding of calstabin1 to RyR1, reduced intracellular calcium leak, decreased reactive oxygen species (ROS), and enhanced tetanic Ca(2+) release, muscle-specific force, and exercise capacity. Taken together, these data indicate that leaky RyR1 contributes to age-related loss of muscle function.
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“An increase in Ca2+ concentration induces mPTP opening, which further exacerbates the imbalance of intracellular Ca2+ homeostasis, possibly caused by leaky ryanodine receptors in aged skeletal muscle (49).”
From From mitochondria to sarcopenia: role of 17β-estradiol and testosterone (2023) · cites this paper as [49]
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Cites
Mitochondria, Oxidants, and Aging
Balaban, R. S., Nemoto, S., & Finkel, T. (2005) · Cell · doi:10.1016/j.cell.2005.02.001 · Cited by 4,388
Kenyon, C. J. (2010) · Nature · doi:10.1038/nature08980 · Cited by 2,739
Calcium, ATP, and ROS: a mitochondrial love-hate triangle
Brookes, P. S., Yoon, Y., Robotham, J. L., Anders, M. W., & Sheu, S.-S. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00139.2004 · Cited by 2,575
Skeletal muscle fatigue: cellular mechanisms
Allen, D. G., Lamb, G. D., & Westerblad, H. (2008) · Physiological Reviews · doi:10.1152/physrev.00015.2007 · Cited by 2,495
Protein S-nitrosylation: Purview and parameters
Hess, D. T., Matsumoto, A., Kim, S.-O., Marshall, H. E., & Stamler, J. S. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1569 · Cited by 2,153
Peroxynitrite: biochemistry, pathophysiology and development of therapeutics
Szabó, C., Ischiropoulos, H., & Radi, R. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2222 · Cited by 2,134
Extension of murine life span by overexpression of catalase targeted to mitochondria
Schriner, S. E., Linford, N. J., Martin, G. M., Treuting, P., Ogburn, C. E., Emond, M., Coskun, P. E., Ladiges, W., Wolf, N., Van Remmen, H., et al. (2005) · Science · doi:10.1126/science.1106653 · Cited by 1,724
Midlife Hand Grip Strength as a Predictor of Old Age Disability
Rantanen, T. (1999) · JAMA · doi:10.1001/jama.281.6.558 · Cited by 1,505
Stochastic and genetic factors influence tissue-specific decline in ageing C. elegans
Herndon, L. A., Schmeissner, P. J., Dudaronek, J. M., Brown, P. A., Listner, K. M., Sakano, Y., Paupard, M. C., Hall, D. H., & Driscoll, M. (2002) · Nature · doi:10.1038/nature01135 · Cited by 1,214
Sarcopenia: its assessment, etiology, pathogenesis, consequences and future perspectives
Rolland, Y., Czerwinski, S., van Kan, G. A., Morley, J. E., Cesari, M., Onder, G., Woo, J., Baumgartner, R., Pillard, F., Boirie, Y., et al. (2008) · The Journal of nutrition, health and aging · doi:10.1007/bf02982704 · Cited by 1,071
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Ivarsson, N., & Westerblad, H. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1004908 · Cited by 5
Cheng, A. J., Ström, J., Hwee, D. T., Malik, F. I., & Westerblad, H. (2020) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12624 · Cited by 5
Antioxidants and Polyphenols Mediate Mitochondrial Mediated Muscle Death Signaling in Sarcopenia
Alway, S. E. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-810422-4.00026-9 · Cited by 6
Braun, J. L., & Fajardo, V. A. (2024) · npj Microgravity · doi:10.1038/s41526-024-00419-y · Cited by 4
Delfinis, L. J., Khajehzadehshoushtar, S., Flewwelling, L. D., Andrews, N. J., Garibotti, M. C., Gandhi, S., Brahmbhatt, A. N., Morris, B. A., Garlisi, B., Lauks, S., et al. (2025) · Molecular Metabolism · doi:10.1016/j.molmet.2025.102211 · Cited by 5
Waheed, W., Allison, J. B., DeWitt, J. C., Hallman, S., & Tandan, R. (2020) · Practical Neurology · doi:10.1136/practneurol-2020-002736 · Cited by 4
Motor Unit Fatigability following Chronic Carnosine Supplementation in Aged Rats
Łochyński, D., Pawlak, M., Everaert, I., Podgórski, T., Gartych, M., Borucka, A.-M., Celichowski, J., Derave, W., & Kaczmarek, D. (2022) · Nutrients · doi:10.3390/nu14030514 · Cited by 4
Engel, M. A., Wörmann, Y. R., Kaestner, H., & Schüler, C. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.691829 · Cited by 4
Role of Ca2+ signaling in skeletal muscle hypertrophy and atrophy
Ito, N., & Takeda, S. (2015) · The Journal of Physical Fitness and Sports Medicine · doi:10.7600/jpfsm.4.171 · Cited by 4
Alomar, F. A., Tian, C., Dash, P. K., McMillan, J., Gendelman, H. E., Gorantla, S., & Bidasee, K. R. (2021) · Antiviral Research · doi:10.1016/j.antiviral.2020.104975 · Cited by 4
Zhang, J., Singh, D. P., Ko, C. Y., Nikolaienko, R. M., Yuen, S. M. W. K., Schwarz, J. A., Treinen, L. M., Tung, C., Rožman, K., Svensson, B., et al. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101412 · Cited by 4
Regenerative Rehabilitation in Sarcopenia, Dynapenia, and Frailty
Baumann, C. W., Clark, B. C., Phillips, B. E., Szewczyk, N. J., & Consitt, L. A. (2022) · Physiology in health and disease · doi:10.1007/978-3-030-95884-8_5 · Cited by 4
Graham, B., Shaw, M., & Hope, I. A. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2020.00037 · Cited by 4
Chivet, M., Marchioretti, C., Pirazzini, M., Piol, D., Scaramuzzino, C., Polanco, J., Nath, S., Zuccaro, E., Nogara, L., Canato, M., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/618405 · Cited by 3
Acheson, J., Joanisse, S., Sale, C., & Hodson, N. W. (2024) · Bioscience Reports · doi:10.1042/bsr20240137 · Cited by 4
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Southern, W. M., Johnson, E. E., Fasbender, E. K., Fallon, K. S., Cavazos, C. L., Lowe, D. A., Rodney, G. G., & Ervasti, J. M. (2025) · Journal of Clinical Investigation · doi:10.1172/jci176942 · Cited by 3
Samanta, K., Ahel, I., & Kar, P. (2025) · Advances in Redox Research · doi:10.1016/j.arres.2025.100124 · Cited by 3
Ryanodane diterpenes: occurrence, structural diversity, bioactivities, and synthesis
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Mitochondrial calcium regulation during and following contractions in skeletal muscle
Eshima, H., Poole, D. C., & Kano, Y. (2018) · The Journal of Physical Fitness and Sports Medicine · doi:10.7600/jpfsm.7.205 · Cited by 3
Influence of obesity on skeletal muscle contractile dysfunction in aging
Eshima, H. (2020) · The Journal of Physical Fitness and Sports Medicine · doi:10.7600/jpfsm.9.199 · Cited by 3
Sharlo, K. A., Lvova, I. D., Tyganov, S. A., Sidorenko, D. A., & Shenkman, E. A. (2023) · Journal of Evolutionary Biochemistry and Physiology · doi:10.1134/s0022093023020278 · Cited by 3
The Complex Relation between Muscle Mass and Muscle Strength
Manini, T. M., Russ, D. W., & Clark, B. C. (2012) · Wiley eBooks · doi:10.1002/9781118338032.ch6 · Cited by 3
Valdés, Á. O., Barrios, G., Ponce, N., Dulce, R. A., & González, D. R. (2018) · Preprints.org · doi:10.20944/preprints201804.0190.v1 · Cited by 3
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Michalik, M., Lorenc, T., Muras, M., Marcinkowski, K., Mikszta, N., Mikszta, J., & Marcinkowska, J. (2025) · Quality in Sport · doi:10.12775/qs.2025.42.61192 · Cited by 3
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Lawal, T. A., Riekhof, W., Groom, L. A., Varma, P., Chrismer, I. C., Kokkinis, A. D., Grunseich, C., Witherspoon, J. W., Razaqyar, M. S., Sinaii, N., et al. (2025) · Skeletal Muscle · doi:10.1186/s13395-025-00390-6 · Cited by 3
From aging to space: A comparative biology of skeletal muscle degeneration
Qaisar, R. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2025.168058 · Cited by 3
Mukhtar, S., Kataria, S., Cimaglia, G., & Beccano-Kelly, D. A. (2025) · Current Research in Physiology · doi:10.1016/j.crphys.2025.100166 · Cited by 2
Gunasekaran, S. K., Khan, M. A., Mirza, M. A., Bhupathi, S. S., & Azeeze, M. S. T. A. (2026) · Muscles · doi:10.3390/muscles5010013 · Cited by 2
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Bahgat, N. M., Abdel-Salam, M., Latif, M. A., & Abdel‐Hady, E. A. (2022) · Experimental Gerontology · doi:10.1016/j.exger.2022.111711 · Cited by 2
Richardson, S. J., Thekkedam, C. G., Casarotto, M. G., Beard, N. A., & Dulhunty, A. F. (2025) · Cells · doi:10.3390/cells14030157 · Cited by 2
Zhu, F., Liu, H., Cao, Y., Dai, B., Wu, H., Zhu, Y.-T., & Li, W. (2025) · Mediators of Inflammation · doi:10.1155/mi/3096848 · Cited by 2
Breckner, A., Ganz, M., Marcellin, D., Richter, J., Gerwin, N., & Rausch, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0081277 · Cited by 2
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Fauré, J., Lunardi, J., Monnier, N., & Marty, I. (2013) · Springer eBooks · doi:10.1007/978-3-642-40282-1_9 · Cited by 2
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Asada, Y., & Imai, T. (2020) · Physical Therapy Research · doi:10.1298/ptr.e10053 · Cited by 2
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Lin, G., Shi, W., Zhang, N., Lee, Y., Wang, Y., & Ji, J. (2022) · Biochemical Journal · doi:10.1042/bcj20220382 · Cited by 2
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Cefis, M., Marcangeli, V., Hammad, R., Granet, J., Leduc‐Gaudet, J., Gaudreau, P., Trumpff, C., Huang, H., Picard, M. A., Aubertin‐Leheudre, M., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.09.602758 · Cited by 2
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Kim, K., Fazzone, B. J., Cort, T. A., Kunz, E. M., Alvarez, S., Moerschel, J., Palzkill, V. R., Dong, G., Anderson, E. M., O’Malley, K. A., et al. (2024) · Scientific Reports · doi:10.1038/s41598-024-58805-1 · Cited by 1
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Huang, Y., Chen, L., Tang, L., Wu, Y., Wu, W., Zhong, Y., Luo, Y., & Wang, M. (2023) · Neurophysiology · doi:10.1007/s11062-025-09962-0 · Cited by 1
Deng, W., Li, C., & Zhao, X. (2025) · Experimental Gerontology · doi:10.1016/j.exger.2025.112972 · Cited by 1
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Wang, L., Hua, X., Ma, X., Wang, J., Xiao, L., Wang, S., Liu, H., Zhao, Y., Valdivia, H. H., Xiao, L., et al. (2025) · Toxicon · doi:10.1016/j.toxicon.2025.108967 · Cited by 1
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Inoguchi, Y., Inoguchi, Y., Yasukawa, K., Fukuhara, S., Etoh, T., Masakado, M., Yamato, M., Umeda, F., Yatomi, Y., Yamauchi, T., et al. (2026) · Journal of Diabetes Investigation · doi:10.1111/jdi.70311 · Cited by 1
Yehya, M., Dridi, H., Estève, E., Moreau, J., Reiken, S. R., Marks, A. R., Lacampagne, A., & Matecki, S. (2026) · Muscle & Nerve · doi:10.1002/mus.70253 · Cited by 1
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Duvshani, A. (2014) · doi:10.7916/d8vd6wm1 · Cited by 1
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Manzano, M., Mohammad, K. S., Guise, T. A., & Vallet‐Regí, M. (2017) · International Journal of Cancer and Oncology · doi:10.15436/2377-0902.17.1188 · Cited by 1
Zullo, A., Frisso, G., & Carsana, A. (2020) · Gazzetta Medica Italiana Archivio per le Scienze Mediche · doi:10.23736/s0393-3660.19.04238-4 · Cited by 1
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Alway, S. E. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822146-4.00004-1 · Cited by 1
Trinh, M. D., Fišerová, I., Vacek, L., Heide, M., Pala, J., Toušek, P., & Polak, J. (2022) · The Anatolian Journal of Cardiology · doi:10.5152/anatoljcardiol.2022.1223 · Cited by 1
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Zhao, Z. (2024) · Highlights in Science Engineering and Technology · doi:10.54097/df3jp957 · Cited by 1
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Dupont, C., Deardorff, A. S., Nawaz, M., Voss, A. A., & Rich, M. M. (2025) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.70134 · Cited by 2
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Buonocore, D., Rucci, S., Negro, M., & Marzatico, F. (2014) · Springer eBooks · doi:10.1007/978-3-642-30018-9_127 · Cited by 1
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Radak, Z. O., & Koltai, E. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-814593-7.00014-1 · Cited by 1
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Waning, D. L. (2022) · Springer eBooks · doi:10.1007/978-3-031-09518-4_9 · Cited by 1
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Suresh, S., & Guise, T. A. (2022) · Springer eBooks · doi:10.1007/978-3-031-09518-4_3 · Cited by 1
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Owen, L. (2000) · doi:10.15760/etd.2070 · Cited by 1
Pagnotti, G. M., Trivedi, T., Wright, L. E., John, S. K., Murthy, S., Pattyn, R. R., Willis, M. S., She, Y., Suresh, S., Thompson, W. R., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.03.12.531571 · Cited by 1
Delfinis, L. J., Khajehzadehshoushtar, S., Flewwelling, L. D., Andrews, N. J., Garibotti, M. C., Gandhi, S., Brahmbhatt, A. N., Morris, B. A., Garlisi, B., Lauks, S., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.22.619751 · Cited by 1
Cheng, A. J., Chaillou, T., Gineste, C., & Schlittler, M. (2015) · The Journal of Physiology · doi:10.1113/jp270960
The role of sarcoplasmic calcium in skeletal muscle training adaptation
Ivarsson, N. (2015) · Figshare
Vigna, C. (2015) · UWSpace (University of Waterloo)
García, R. C., Margarita, A., & Uribazo, L. (2016)
Skeletal Muscle Metabolic Dysfunction in Patients with Malignant Hyperthermia
Thompson, S. J. (2016) · TSpace (University of Toronto)
Physical Performance and Antioxidants
Aoi, W., & Naito, Y. (2019) · CRC Press eBooks · doi:10.1201/9781315108025-11
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Delrio-Lorenzo, A. (2020) · UVaDOC UVaDOC University of Valladolid Documentary Repository (University of Valladolid) · doi:10.35376/10324/43643
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Zhang, J., Yuen, S. M. W. K., Schwarz, J. A., Treinen, L. M., Tung, C., Rebbeck, R. T., Berg, K. G., Svensson, B., Aldrich, C. C., Thomas, D. D., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.02.07.430153
Atrophie, croissance et fonction musculaire : l'impact des leucocytes et de la triade RANK/RANKL/OPG
Dumont, N. A. (2013) · Corpus Université Laval (Université Laval)
(2012) · Current Opinion in Rheumatology · doi:10.1097/bor.0b013e328359ee5b
Faculty Opinions recommendation of Ryanodine receptor structure and function in health and disease.
Dulhunty, A. F. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.732754805.793552458
Sharlo, K. A., Lvova, I. D., & Shenkman, E. A. (2022) · Journal of Evolutionary Biochemistry and Physiology · doi:10.1134/s0022093022030012
Ali, A. E., Mohamed, S. A. H., Ali, S. A., & Elmahdi, S. A. (2022) · International Journal of Biological and Pharmaceutical Sciences Archive · doi:10.53771/ijbpsa.2022.4.2.0081
RyR1 protein content is reduced in inflammatory and mitochondrial myopathies and induces ER stressPreprint
Vidal, J., Fernandez, E., Wohlwend, M., Laurila, P., Mejia, A. L., Ochala, J., López‐Mejía, I. C., Lobrinus, J. A., Kayser, B., Place, N., et al. (2023) · medRxiv · doi:10.1101/2023.02.01.23285343
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Lal, N. N., Cornwall, J., & Sheard, P. W. (2023) · Biogerontology · doi:10.1007/s10522-023-10021-6
Toro, C. A., Gasperi, R. D., Aslan, A., Johnson, N. P., Siddiq, M. M., Chow, C., Zhao, W., Harlow, L., Graham, Z., Liu, X., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.04.551985
Sharlo, K. A., Lvova, I. D., Tyganov, S. A., Зарипова, К. А., Belova, S. P., & Nemirovskaya, T. L. (2023) · Journal of Evolutionary Biochemistry and Physiology · doi:10.1134/s0022093023040178
Toro, C. A., Gasperi, R. D., Aslan, A., Johnson, N. P., Siddiq, M. M., Chow, C., Zhao, W., Harlow, L., Graham, Z., Liu, X., et al. (2024) · Neurotrauma Reports · doi:10.1089/neur.2023.0089
Sharlo, K. A., Lvova, I. D., Tyganov, S. A., Sidorenko, D. A., & Shenkman, B. S. (2023) · Российский физиологический журнал им И М Сеченова · doi:10.31857/s086981392304009x
Influence of the SERCA Activity on Rat’s Soleus Contractile Properties during Functional Unloading
Sharlo, K. A., Lvova, I. D., Tyganov, S. A., Зарипова, К. А., Belova, S. P., & Nemirovskaya, T. L. (2023) · Российский физиологический журнал им И М Сеченова · doi:10.31857/s0869813923070117
García-Puga, M., Gereñu, G., Bargiela, A., Espinosa-Espinosa, J., Mosqueira‐Martín, L., Sagartzazu‐Aizpurua, M., Aizpurua, J. M., Vallejo‐Illarramendi, A., Artero, R. D., de Munaín, A. L., et al. (2024) · Cells · doi:10.3390/cells13231939
Eshima, H., Ishihara, T., Tabuchi, A., Kano, Y., Kurokawa, K., & Shchepinov, M. S. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.12.17.627433
Peng, Y., Zhang, L., Chen, S., Tian, Y., Qin, X., & Yin, P. (2025) · Journal of the American Medical Directors Association · doi:10.1016/j.jamda.2025.105823
Yee, R. S. Z., Lee, C. S., Chang, T., Jung, S. Y., Yousif, O., Cavazos, C. L., Colyer, J., Petegem, F. V., Rodney, G. G., & Hamilton, S. L. (2025) · Science Signaling · doi:10.1126/scisignal.adx3087
Ruiz, A., Benucci, S., Meier, H., Schulz, G. V., Buczak, K., Handschin, C., Pena, R. C. G., Treves, S., & Zorzato, F. (2025) · The Journal of Physiology · doi:10.1113/jp287832 · Cited by 1
Deardorff, A. S., Burford, M. J., & Rich, M. M. (2025) · Case Reports in Neurological Medicine · doi:10.1155/crnm/6647563
Alcohol and musculoskeletal physiology
Rodríguez‐Graciani, K. M., & Simon, L. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-34258-5.00009-8
Lawal, T. A., Wires, E. S., Terry, N. L., Dowling, J. J., & Todd, J. J. (2020) · Figshare · doi:10.6084/m9.figshare.12270545
Fidelis, M., Wojcieszek, M., Gondek, K., Gacka, D., Zalewska, A., Mączyńska, A., Al-karawi, N. A., Kędziorek, P., & Tanç, Z. (2026) · International Journal of Innovative Technologies in Social Science · doi:10.31435/ijitss.1(49).2026.4959
Metadata
- Authors
- Andersson, D. C., Betzenhauser, M. J., Reiken, S., Meli, A. C., Umanskaya, A., Xie, W., Shiomi, T., Zalk, R., Lacampagne, A., & Marks, A. R.
- Affiliations
- Columbia University Irving Medical Center (US)
- Inserm (FR)
- Corresponding author
- Marks, Andrew R.
- ORCID
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2011-08
- Volume
- 14
- Issue
- 2
- Pages
- 196-207
- ISSN
- 1550-4131 (ISSN-L)
- PMC
- PMC3690519
- OpenAlex
- W2078833625
- Cited by
- 424
- References
- 73
- Citations by year
- 2026: 24 · 2025: 31 · 2024: 28 · 2023: 33 · 2022: 36 · 2021: 29 · 2020: 36 · 2019: 22 · 2018: 26 · 2017: 25 · 2016: 33 · 2015: 24 · 2014: 25 · 2013: 34 · 2012: 16
- FWCI
- 9.86
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Vetenskapsrådet
- National Heart, Lung, and Blood Institute (R01HL056180, R01HL061503)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01AR060037)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- RyR1, sarcopenia, aging, skeletal muscle, reactive oxygen species, muscle weakness, calcium release channel, exercise capacity, muscle force
- MeSH terms
- Aging, Animals, Calcium, Mice, Inbred C57BL, Mice, Transgenic, Mitochondria, Motor Activity, Muscle Contraction, Oxidation-Reduction, Thiazepines, Reactive Oxygen Species, Oxidative Stress, Muscle, Skeletal, Muscle Weakness, Ryanodine Receptor Calcium Release Channel, Tacrolimus Binding Proteins, Mice, Sarcopenia
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