Mitochondrial fusion is frequent in skeletal muscle and supports excitation–contraction coupling
Open accessAbstract
Genetic targeting experiments indicate a fundamental role for mitochondrial fusion proteins in mammalian physiology. However, owing to the multiple functions of fusion proteins, their related phenotypes are not necessarily caused by altered mitochondrial fusion. Perhaps the biggest mystery is presented by skeletal muscle, where mostly globular-shaped mitochondria are densely packed into the narrow intermyofilamental space, limiting the interorganellar interactions. We show here that mitochondria form local networks and regularly undergo fusion events to share matrix content in skeletal muscle fibers. However, fusion events are less frequent and more stable in the fibers than in nondifferentiated myoblasts. Complementation among muscle mitochondria was suppressed by both in vivo genetic perturbations and chronic alcohol consumption that cause myopathy. An Mfn1-dependent pathway is revealed whereby fusion inhibition weakens the metabolic reserve of mitochondria to cause dysregulation of calcium oscillations during prolonged stimulation. Thus, fusion dynamically connects skeletal muscle mitochondria and its prolonged loss jeopardizes bioenergetics and excitation–contraction coupling, providing a potential pathomechanism contributing to myopathies.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
Mitochondrial fusion enables redistribution of energy in the form of mitochondrial potential, metabolites, proteins, and mtDNA, improving calcium handling and ATP synthesis.
“This process enables the redistribution of energy in the form of mitochondrial potential, metabolites, proteins, and mtDNA, improving calcium handling, and ATP synthesis [24, 54–57].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [54]
Mitochondrial fusion in skeletal muscle is necessary to adapt to the cell's specific functional needs and support skeletal muscle myofiber contractile function.
“mitochondrial fusion in skeletal muscle is necessary to adapt to the cell's specific functional needs and support skeletal muscle myofibers contractile function [54].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [54]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
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
Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., & Chan, D. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211046 · Cited by 2,601 · see citing works
Mitofusin 2 tethers endoplasmic reticulum to mitochondria
de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442 · 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 1× · see citing works
“Several studies have established mitochondrial fusion in yeast and eukaryotic cell lines (Hoppins and Nunnari, 2009; Chen and Chan, 2010; Westermann, 2010); however, mitochondrial fusion dynamics studies in terminally differentiated primary cells are still a work in progress.”
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
Disruption of Fusion Results in Mitochondrial Heterogeneity and Dysfunction
Chen, H., Chomyn, A., & Chan, D. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503062200 · Cited by 1,376 · cited 3× · see citing works
“Notably, the MEFs were also appealing because their mitochondrial fusion activity seems to be primarily on Mfn1 (Chen et al., 2005) like we found it in SM.”
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
Lemasters, J. J. (2005) · Rejuvenation Research · doi:10.1089/rej.2005.8.3 · Cited by 1,342 · 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
Organelle isolation: functional mitochondria from mouse liver, muscle and cultured filroblasts
Frezza, C., Cipolat, S., & Scorrano, L. (2007) · Nature Protocols · doi:10.1038/nprot.2006.478 · Cited by 1,188 · see citing works
Dephosphorylation by calcineurin regulates translocation of Drp1 to mitochondria
Cereghetti, G. M., Stangherlin, A., de Brito, O. M., Chang, C. R., Blackstone, C., Bernardi, P., & Scorrano, L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808249105 · Cited by 1,129 · see citing works
Decoding of cytosolic calcium oscillations in the mitochondria
Hajnóczky, G., Gaspers, L. D., Seitz, M. B., & Thomas, A. P. (1995) · Cell · doi:10.1016/0092-8674(95)90430-1 · Cited by 1,110 · see citing works
Self-citationRegulation of mitochondrial ATP synthesis by calcium: Evidence for a long-term metabolic priming
Jouaville, L. S., Pinton, P., Bastianutto, C., Rutter, G. A., & Rizzuto, R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.24.13807 · Cited by 814 · see citing works
Akerboom, J., Calderón, N. C., Tian, L., Wabnig, S., Prigge, M., Tolö, J., Gordus, A. G., Orger, M. B., Severi, K. E., Macklin, J. J., et al. (2013) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2013.00002 · Cited by 710 · see citing works
Quality control of mitochondria: protection against neurodegeneration and ageing
Tatsuta, T., & Langer, T. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601972 · Cited by 519 · see citing works
Mitochondrial Fusion is Essential for Organelle Function and Cardiac Homeostasis
Chen, Y., Liu, Y., & Dorn, G. W. (2011) · Circulation Research · doi:10.1161/circresaha.111.258723 · Cited by 506 · see citing works
Szabadkai, G., Simoni, A. M., Chami, M., Wieckowski, M. R., Youle, R. J., & Rizzuto, R. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.09.026 · Cited by 468 · see citing works
Multi-system neurological disease is common in patients with OPA1 mutations
Yu‐Wai‐Man, P., Griffiths, P. G., Gorman, G. S., Lourenço, C. M., Wright, A. F., Auer‐Grumbach, M., Toscano, A., Musumeci, O., Valentino, M. L., Caporali, L., et al. (2010) · Brain · doi:10.1093/brain/awq007 · Cited by 446 · see citing works
Self-citationMitofusin-1 protein is a generally expressed mediator of mitochondrial fusion in mammalian cells
Santel, A., Frank, S., Gaume, B. R., Herrler, M., Youle, R. J., & Fuller, M. T. (2003) · Journal of Cell Science · doi:10.1242/jcs.00479 · Cited by 445 · see citing works
Karbowski, M., Arnoult, D., Chen, H., Chan, D. C., Smith, C. L., & Youle, R. J. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200309082 · Cited by 433 · see citing works
Synchronization of calcium waves by mitochondrial substrates in Xenopus laevis oocytes
Jouaville, L. S., Ichas, F., Holmuhamedov, E., Camacho, P., & Lechleiter, J. D. (1995) · Nature · doi:10.1038/377438a0 · Cited by 427 · see citing works
Ono, T., Isobe, K., Nakada, K., & Hayashi, J.-I. (2001) · Nature Genetics · doi:10.1038/90116 · Cited by 420 · see citing works
Cellular mechanisms of fatigue in skeletal muscle
Westerblad, H., Lee, J. A., Lännergren, J., & Allen, D. G. (1991) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1991.261.2.c195 · Cited by 410 · see citing works
Integrating cytosolic calcium signals into mitochondrial metabolic responses
Gaspers, L. D., Burnett, P., Rutter, G. A., Denton, R. M., Rizzuto, R., & Thomas, A. P. (1998) · The EMBO Journal · doi:10.1093/emboj/17.17.4987 · Cited by 370 · see citing works
Papanicolaou, K. N., Khairallah, R. J., Ngoh, G. A., Chikando, A. C., Luptak, I., O’Shea, K. M., Riley, D. D., Lugus, J. J., Colucci, W. S., Lederer, W. J., et al. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.00911-10 · Cited by 358 · see citing works
Chen, Y., Csordás, G., Jowdy, C. C., Schneider, T. G., Csordás, N., Wang, W., Liu, Y., Kohlhaas, M., Meiser, M., Bergem, S., et al. (2012) · Circulation Research · doi:10.1161/circresaha.112.266585 · Cited by 348 · see citing works
Mitochondrial ‘kiss‐and‐run’: interplay between mitochondrial motility and fusion–fission dynamics
Liu, X., Weaver, D., Shirihai, O. S., & Hajnóczky, G. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.255 · Cited by 344 · see citing works
Self-citationMitochondrial Ca2+ homeostasis in intact cells.
Rizzuto, R., Bastianutto, C., Brini, M., Murgia, M., & Pozzan, T. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.126.5.1183 · Cited by 322 · see citing works
Boncompagni, S., Rossi, A. E., Micaroni, M., Beznoussenko, G. V., Polishchuk, R., Dirksen, R. T., & Protasi, F. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-07-0783 · Cited by 285 · see citing works
Amchenkova, A. A., Bakeeva, L. E., Chentsov, Y. S., Skulachev, V. P., & Zorov, D. B. (1988) · The Journal of cell biology · doi:10.1083/jcb.107.2.481 · Cited by 284 · see citing works
Picard, M. A., White, K., & Turnbull, D. M. (2012) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01096.2012 · Cited by 260 · see citing works
Regulating mitochondrial outer membrane proteins by ubiquitination and proteasomal degradation
Karbowski, M., & Youle, R. J. (2011) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2011.05.007 · Cited by 256 · see citing works
Rapid Diffusion of Green Fluorescent Protein in the Mitochondrial Matrix
Partikian, A., Ölveczky, B. P., Swaminathan, R., Li, Y., & Verkman, A. S. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.140.4.821 · Cited by 228 · see citing works
Physiological functions of mitochondrial fusion
Chen, H., & Chan, D. C. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05615.x · Cited by 221 · see citing works
MFN2 mutations cause severe phenotypes in most patients with CMT2A
Feely, S. M. E., Laurá, M., Siskind, C. E., Sottile, S. L., Davis, M. B., Gibbons, V. S., Reilly, M. M., & Shy, M. E. (2011) · Neurology · doi:10.1212/wnl.0b013e31821a441e · Cited by 217 · see citing works
Eisner, V., Csordás, G., & Hajnóczky, G. (2013) · Journal of Cell Science · doi:10.1242/jcs.093609 · Cited by 215 · see citing works
Self-citationCa2+ Homeostasis during Mitochondrial Fragmentation and Perinuclear Clustering Induced by hFis1
Frieden, M., James, D. I., Castelbou, C., Danckaert, A., Martinou, J., & Demaurex, N. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312366200 · Cited by 203 · see citing works
Ethanol Produces Muscle Damage in Human Volunteers
Song, S. K., & Rubin, E. (1972) · Science · doi:10.1126/science.175.4019.327 · Cited by 198 · see citing works
Mitochondrial regular arrangement in muscle cells: a “crystal-like” pattern
Vendelin, M., Béraud, N., Guerrero, K., Andrienko, T., Kuznetsov, A. V., Olivares, J., Kay, L., & Saks, V. A. (2005) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00281.2004 · Cited by 193 · see citing works
In vivo monitoring of Ca2 + uptake into mitochondria of mouse skeletal muscle during contraction
Rudolf, R., Mongillo, M., Magalhães, P. J., & Pozzan, T. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200403102 · Cited by 193 · see citing works
Kissing and nanotunneling mediate intermitochondrial communication in the heart
Huang, X., Sun, L., Ji, S., Zhao, T. S., Zhang, W., Xu, J., Zhang, J., Wang, Y., Wang, X., Franzini‐Armstrong, C., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1300741110 · Cited by 164 · see citing works
Effects of OPA1 mutations on mitochondrial morphology and apoptosis: Relevance to ADOA pathogenesis
Olichon, A., Landes, T., Pelloquin, L., Emorine, L. J., Mils, V., Guichet, A., Delettre, C., Hamel, C., Amati‐Bonneau, P., Bonneau, D., et al. (2006) · Journal of Cellular Physiology · doi:10.1002/jcp.20950 · Cited by 163 · see citing works
Self-citationCa 2+ marks: Miniature calcium signals in single mitochondria driven by ryanodine receptors
Pacher, P., Thomas, A. P., & Hajnóczky, G. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.032423699 · Cited by 152 · see citing works
Self-citationZhou, J., Yi, J., Fu, R., Liu, E., Siddique, T., Rı́os, E., & Deng, H. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.041319 · Cited by 147 · see citing works
Hom, J., Gewandter, J. S., Michael, L., Sheu, S., & Yoon, Y. (2007) · Journal of Cellular Physiology · doi:10.1002/jcp.21051 · Cited by 142 · see citing works
The molecular mechanism of mitochondrial fusion
Hoppins, S. C., & Nunnari, J. M. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.07.005 · Cited by 141 · see citing works
The molecular mechanism and cellular functions of mitochondrial division
Lackner, L. L., & Nunnari, J. M. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.11.011 · Cited by 133 · see citing works
Subcellular analysis of Ca2+ homeostasis in primary cultures of skeletal muscle myotubes.
Brini, M., Giorgi, F. D., Murgia, M., Marsault, R., Massimino, M. L., Cantini, M., Rizzuto, R., & Pozzan, T. (1997) · Molecular Biology of the Cell · doi:10.1091/mbc.8.1.129 · Cited by 118 · see citing works
Palma, C. D., Falcone, S., Pisoni, S., Cipolat, S., Panzeri, C., Pambianco, S., Pisconti, A., Allevi, R., Bassi, M. T., Cossu, G., et al. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2010.48 · Cited by 117 · see citing works
Loss of OPA1 disturbs cellular calcium homeostasis and sensitizes for excitotoxicity
Kushnareva, Y. E., Gerencser, A. A., Bossy, B., Ju, W.-K., White, A. D., Waggoner, J., Ellisman, M. H., Perkins, G. A., & Bossy‐Wetzel, E. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.128 · Cited by 115 · see citing works
Transfer and Tunneling of Ca2+ from Sarcoplasmic Reticulum to Mitochondria in Skeletal Muscle
Shkryl, V. M., & Shirokova, N. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505024200 · Cited by 102 · see citing works
DNA Transfection of Mammalian Skeletal Muscles using In Vivo Electroporation
DiFranco, M., Quiñonez, M., Capote, J. C., & Vergara, J. L. (2009) · Journal of Visualized Experiments · doi:10.3791/1520 · Cited by 101 · see citing works
Pouvreau, S. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013035 · Cited by 100 · see citing works
Mitochondrial superoxide flashes: metabolic biomarkers of skeletal muscle activity and disease
Wei, L., Salahura, G., Boncompagni, S., Kasischke, K. A., Protasi, F., Sheu, S., & Dirksen, R. T. (2011) · The FASEB Journal · doi:10.1096/fj.11-187252 · Cited by 95 · see citing works
Bhat, M. B., Zhao, J., Zang, W., Balke, C. W., Takeshima, H., Wier, W. G., & Ma, J. (1997) · The Journal of General Physiology · doi:10.1085/jgp.110.6.749 · Cited by 91 · see citing works
Non-Invasive In Vivo Imaging of Calcium Signaling in Mice
Rogers, K. L., Picaud, S., Roncali, E., Boisgard, R., Colasante, C., Stinnakre, J., Tavitian, B., & Brûlet, P. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000974 · Cited by 88 · see citing works
Twig, G., Liu, X., Liesa, M., Wikström, J. D., Molina, A. J. A., Las, G., Yaniv, G., Hajnóczky, G., & Shirihai, O. S. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00427.2009 · Cited by 88 · see citing works
Self-citationMitochondrial morphology and dynamics in hepatocytes from normal and ethanol-fed rats
Das, S., Hajnóczky, N., Antony, A. N., Csordás, G., Gaspers, L. D., Clemens, D. L., Hoek, J. B., & Hajnóczky, G. (2012) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-012-1100-4 · Cited by 73 · see citing works
Self-citationCasas, M., Figueroa, R., Jorquera, G., Escobar, M., Molgó, J., & Jaimovich, E. (2010) · The Journal of General Physiology · doi:10.1085/jgp.200910397 · Cited by 65 · see citing works
The Effect of OPA1 on Mitochondrial Ca2+ Signaling
Fülöp, L., Szanda, G., Enyedi, B., Várnai, P., & Spät, A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025199 · Cited by 60 · see citing works
Mitchell, T., Chacko, B., Ballinger, S. W., Bailey, S. M., Zhang, J., & Darley-Usmar, V. (2013) · Biochemical Society Transactions · doi:10.1042/bst20120231 · Cited by 57 · see citing works
Rossi, A. E., Boncompagni, S., Wei, L., Protasi, F., & Dirksen, R. T. (2011) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00194.2011 · Cited by 56 · see citing works
Natural History of Alcoholic Myopathy: A 5‐Year Study
Estruch, R., Sacanella, E., Fernandez‐Solà, J., Nicolás, J. M., Rubin, E., & Urbano-Márquez, A. (1998) · Alcoholism Clinical and Experimental Research · doi:10.1111/j.1530-0277.1998.tb05911.x · Cited by 54 · see citing works
Lodi, R., Tonon, C., Valentino, M. L., Manners, D. N., Testa, C. M., Malucelli, E., Morgia, C. L., Barboni, P., Carbonelli, M., Schimpf, S., et al. (2010) · Archives of Neurology · doi:10.1001/archneurol.2010.228 · Cited by 44 · see citing works
Ethanol Acutely Decreases Calcium Transients in Cultured Human Myotubes
Nicolás, J. M., Antúnez, E., Thomas, A. P., Fernández‐Solà, J., Tobías, E., Estruch, R., & Urbano-Márquez, A. (1998) · Alcoholism Clinical and Experimental Research · doi:10.1111/j.1530-0277.1998.tb03705.x · Cited by 42 · see citing works
Low-dose ethanol consumption allows strength recovery in chronic alcoholic myopathy
Fernández-Solá, J. (2000) · QJM · doi:10.1093/qjmed/93.1.35 · Cited by 42 · see citing works
Mitochondria and Peripheral Neuropathies
Vital, A., & Vital, C. (2012) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3182764d47 · Cited by 38 · see citing works
Switch from ER-mitochondrial to SR-mitochondrial calcium coupling during muscle differentiation
Yi, M., Weaver, D., Eisner, V., Várnai, P., Hunyady, L., Ma, J., Csordás, G., & Hajnóczky, G. (2012) · Cell Calcium · doi:10.1016/j.ceca.2012.05.012 · Cited by 35 · see citing works
Self-citationEisner, V., Parra, V., Lavandero, S., Hidalgo, C., & Jaimovich, E. (2010) · Cell Calcium · doi:10.1016/j.ceca.2010.11.001 · Cited by 31 · see citing works
Self-citationFranzini‐Armstrong, C., & Boncompagni, S. (2011) · BioMed Research International · doi:10.1155/2011/830573 · Cited by 28 · see citing works
Effect of mitochondria poisoning by FCCP on Ca2+ signaling in mouse skeletal muscle fibers
Caputo, C. A., & Bolaños, P. (2007) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-007-0317-0 · Cited by 28 · see citing works
Altered myoplasmic Ca2+ handling in rat fast-twitch skeletal muscle fibres during disuse atrophy
Weiss, N., Andrianjafiniony, T., Dupré-Aucouturier, S., Pouvreau, S., Dominique Desplanches, C., & Jacquemond, V. (2009) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-009-0764-x · Cited by 25 · see citing works
Ogata (1997) · doi:10.1002/(sici)1097-0185(199706)248:2
Flagged first, then by citations
1 of the 74 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Metabolic regulation of mitochondrial dynamics
Mishra, P., & Chan, D. C. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201511036 · Cited by 1,096 · see citing works
Rambold, A. S., Cohen, S., & Lippincott-Schwartz, J. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.01.029 · Cited by 1,038 · see citing works
Mitochondrial signal transduction
Picard, M. A., & Shirihai, O. S. (2022) · Cell Metabolism · doi:10.1016/j.cmet.2022.10.008 · Cited by 666 · see citing works
Mitochondrial dynamics in adaptive and maladaptive cellular stress responses
Eisner, V., Picard, M., & Hajnóczky, G. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0133-0 · Cited by 622 · see citing works
Self-citationMitochondrial reticulum for cellular energy distribution in muscle
Glancy, B., Hartnell, L. M., Malide, D., Yu, Z.-X., Combs, C. A., Connelly, P. S., Subramaniam, S., & Balaban, R. S. (2015) · Nature · doi:10.1038/nature14614 · Cited by 450 · see citing works
Mitochondrial quality control and muscle mass maintenance.
Romanello, V., & Sandri, M. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2015.00422 · Cited by 434 · see citing works
Mishra, P., Varuzhanyan, G., Pham, A. H., & Chan, D. C. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.09.027 · Cited by 290 · see citing works
The Functional Impact of Mitochondrial Structure Across Subcellular Scales
Glancy, B. C., Kim, Y., Katti, P., & Willingham, T. B. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.541040 · Cited by 259 · see citing works
Molecular mechanisms for mitochondrial adaptation to exercise training in skeletal muscle
Drake, J. C., Wilson, R. J., & Yan, Z. (2016) · The FASEB Journal · doi:10.1096/fj.15-276337 · Cited by 263 · see citing works
Calcium Transport and Signaling in Mitochondria
Bravo, R., Parra, V., López‐Crisosto, C., Díaz, P., Quest, A. F. G., & Lavandero, S. (2017) · Comprehensive physiology · doi:10.1002/cphy.c160013 · Cited by 249 · see citing works
The Spectrum of Mitochondrial Ultrastructural Defects in Mitochondrial Myopathy
Vincent, A. E., Ng, Y. S., White, K., Davey, T., Mannella, C. A., Falkous, G., Feeney, C. L., Schaefer, A. M., McFarland, R., Gorman, G. S., et al. (2016) · Scientific Reports · doi:10.1038/srep30610 · Cited by 234 · see citing works
Mitochondrial lactate metabolism: history and implications for exercise and disease
Glancy, B. C., Kane, D. A., Kavazis, A. N., Goodwin, M. L., Willis, W. T., & Gladden, L. B. (2020) · The Journal of Physiology · doi:10.1113/jp278930 · Cited by 203 · see citing works
Romanello, V., & Sandri, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03662-0 · Cited by 197 · see citing works
Quantitative 3D Mapping of the Human Skeletal Muscle Mitochondrial Network
Vincent, A. E., White, K., Davey, T., Philips, J., Ogden, R. T., Lawless, C., Warren, C., Hall, M. G., Ng, Y. S., Falkous, G., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.01.010 · Cited by 195 · see citing works
Mitochondrial function in development and disease
Rossmann, M. P., Dubois, S. M., Agarwal, S., & Zon, L. I. (2021) · Disease Models & Mechanisms · doi:10.1242/dmm.048912 · Cited by 191 · see citing works
Mitochondrial Dynamics in Basal and Stressful Conditions
Zemirli, N., Morel, É., & Molino, D. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020564 · Cited by 186 · see citing works
Trumpff, C., Michelson, J., Lagranha, C. J., Taleon, V., Karan, K. R., Sturm, G., Lindqvist, D., Fernström, J., Moser, D., Kaufman, B. A., et al. (2021) · Mitochondrion · doi:10.1016/j.mito.2021.04.002 · Cited by 181 · see citing works
The rise and rise of mitochondrial DNA mutations
Lawless, C., Greaves, L. C., Reeve, A. K., Turnbull, D. M., & Vincent, A. E. (2020) · Open Biology · doi:10.1098/rsob.200061 · Cited by 174 · see citing works
Power Grid Protection of the Muscle Mitochondrial Reticulum
Glancy, B., Hartnell, L. M., Combs, C. A., Femnou, A., Sun, J., Murphy, E., Subramaniam, S., & Balaban, R. S. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.03.063 · Cited by 172 · see citing works
Eisner, V., Cupo, R. R., Gao, E., Csordás, G., Slovinsky, W. S., Paillard, M., Cheng, L., Ibetti, J., Chen, S. R. W., Chuprun, J. K., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1617288114 · Cited by 161 · see citing works
Self-citationChronology of mitochondrial and cellular events during skeletal muscle ischemia-reperfusion
Paradis, S., Charles, A., Meyer, A., Lejay, A., Scholey, J. W., Chakfé, N., Zoll, J., & Gény, B. (2016) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00356.2015 · Cited by 145 · see citing works
Muscle-specific Drp1 overexpression impairs skeletal muscle growth via translational attenuation
Touvier, T., De Palma, C., Rigamonti, E., Scagliola, A., Incerti, E., Mazelin, L., Thomas, J.-L., D'Antonio, M., Politi, L., Schaeffer, L., et al. (2015) · Cell Death & Disease · doi:10.1038/cddis.2014.595 · Cited by 140 · see citing works
Mitochondrial Involvement in Cisplatin Resistance
Cocetta, V., Ragazzi, E., & Montopoli, M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20143384 · Cited by 140 · see citing works
Dysregulation of skeletal muscle protein metabolism by alcohol.
Steiner, J., & Lang, C. H. (2015) · American Journal of Physiology. Endocrinology and Metabolism · doi:10.1152/ajpendo.00006.2015 · Cited by 124 · see citing works
Vincent, A. E., Turnbull, D. M., Eisner, V., Hajnóczky, G., & Picard, M. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.08.009 · Cited by 135 · see citing works
Self-citationROS Control Mitochondrial Motility through p38 and the Motor Adaptor Miro/Trak
Debattisti, V., Gerencser, A. A., Saotome, M., Das, S., & Hajnóczky, G. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.10.060 · Cited by 132 · see citing works
Self-citationThe roles of mitochondria in global and local intracellular calcium signalling
Cartes-Saavedra, B., Ghosh, A., & Hajnóczky, G. (2025) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00820-1 · Cited by 126 · see citing works
Self-citationAdaniya, S. M., O‐Uchi, J., Cypress, M. W., Kusakari, Y., & Jhun, B. S. (2019) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00523.2018 · Cited by 115 · see citing works
Muscle function decline and mitochondria changes in middle age precede sarcopenia in mice
del Campo, A., Contreras‐Hernandez, I., Castro‐Sepúlveda, M., Campos, C. A., Figueroa, R., Tevy, M. F., Eisner, V., Casas, M., & Jaimovich, E. (2018) · Aging · doi:10.18632/aging.101358 · Cited by 110 · see citing works
Self-citationQin, J., Guo, Y., Xue, B., Shi, P., Yang, C., Su, Q. P., Hao, H., Zhao, S., Wu, C., Yu, L., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-18202-4 · Cited by 110 · see citing works
Pokharel, M. D., Flores, A. G., Marciano, D. P., Franco, M. C., Fineman, J. R., Aggarwal, S., Wang, T., & Black, S. M. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103049 · Cited by 113 · see citing works
Autophagy, Innate Immunity and Tissue Repair in Acute Kidney Injury
Duann, P., Lianos, E. A., Ma, J., & Lin, P. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17050662 · Cited by 108 · see citing works
Selective removal of deletion-bearing mitochondrial DNA in heteroplasmic Drosophila
Kandul, N. P., Zhang, T., Hay, B. A., & Guo, M. (2016) · Nature Communications · doi:10.1038/ncomms13100 · Cited by 103 · see citing works
Alcohol Misuse and Kidney Injury: Epidemiological Evidence and Potential Mechanisms
Varga, Z. V. (2017) · Alcohol research · doi:10.35946/arcr.v38.2.10 · Cited by 102 · see citing works
Alcoholic Myopathy: Pathophysiologic Mechanisms and Clinical Implications
Simon, L. (2017) · Alcohol research · doi:10.35946/arcr.v38.2.05 · Cited by 102 · see citing works
The Interplay between Mitochondrial Morphology and Myomitokines in Aging Sarcopenia
Romanello, V. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms22010091 · Cited by 101 · see citing works
Debattisti, V., Horn, A. J., Singh, R. P., Seifert, E. L., Hogarth, M. W., Mázala, D. A. G., Huang, K. T., Horváth, R., Jaiswal, J. K., & Hajnóczky, G. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.09.063 · Cited by 100 · see citing works
Self-citationLei, Y., Gan, M., Qiu, Y., Chen, Q., Wang, X., Liao, T., Zhao, M., Chen, L., Zhang, S., Zhao, Y., et al. (2024) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-024-00572-y · Cited by 102 · see citing works
Lipid droplet dynamics in skeletal muscle
Bosma, M. (2016) · Experimental Cell Research · doi:10.1016/j.yexcr.2015.10.023 · Cited by 91 · see citing works
Review of RyR1 pathway and associated pathomechanisms
Witherspoon, J. W., & Meilleur, K. G. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0392-6 · Cited by 86 · see citing works
Mechanical ventilation triggers abnormal mitochondrial dynamics and morphology in the diaphragm
Picard, M. A., Azuelos, I., Jung, B., Giordano, C., Matecki, S., Hussain, S. N. A., White, K., Li, T., Liang, F., Benedetti, A., et al. (2015) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00873.2014 · Cited by 84 · see citing works
Gonçalves, I. O., Passos, E., Diogo, C. V., Rocha‐Rodrigues, S., Alves, E. S., Oliveira, P. J., Ascensão, A. A. M. R., & Magalhães, J. (2015) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/apnm-2015-0470 · Cited by 84 · see citing works
Weil, R., Laplantine, E., Curic, S., & Génin, P. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01243 · Cited by 80 · see citing works
Energy metabolism design of the striated muscle cell
Glancy, B. C., & Balaban, R. S. (2021) · Physiological Reviews · doi:10.1152/physrev.00040.2020 · Cited by 83 · see citing works
Lavorato, M., Iyer, V. R., Dewight, W., Cupo, R. R., Debattisti, V., Gomez, L., de la Fuente, S., Zhao, Y.-T., Valdivia, H. H., Hajnóczky, G., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1617788113 · Cited by 81 · see citing works
Self-citationRahman, F. A., & Quadrilatero, J. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03807-9 · Cited by 76 · see citing works
Subcellular Specialization of Mitochondrial Form and Function in Skeletal Muscle Cells
Willingham, T. B., Ajayi, P. T., & Glancy, B. C. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.757305 · Cited by 72 · see citing works
Palma, C. D., Morisi, F., Pambianco, S., Assi, E., Touvier, T., Russo, S., Perrotta, C., Romanello, V., Carnio, S., Cappello, V., et al. (2014) · Skeletal Muscle · doi:10.1186/s13395-014-0022-6 · Cited by 72 · see citing works
Role of mitochondria in renal ischemia-reperfusion injury
Huang, R., Zhang, C., Xiang, Z., Lin, T., Ling, J., & Hu, H. (2024) · The FEBS Journal · doi:10.1111/febs.17130 · Cited by 72 · see citing works
A novel mechanism causing imbalance of mitochondrial fusion and fission in human myopathies
Bartsakoulia, M., Pyle, A., Troncoso-Chandía, D., Vial-Brizzi, J., Paz-Fiblas, M. V., Duff, J., Griffin, H., Boczonadi, V., Lochmüller, H., Kleinle, S., et al. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy033 · Cited by 68 · see citing works
Self-citationMitochondrial health, the epigenome and healthspan
Aon, M. A., Cortassa, S., Juhaszova, M., & Sollott, S. J. (2016) · Clinical Science · doi:10.1042/cs20160002 · Cited by 66 · see citing works
Recessive mutations in MSTO1 cause mitochondrial dynamics impairment, leading to myopathy and ataxia
Nasca, A., Scotton, C., Zaharieva, I. T., Neri, M., Selvatici, R., Magnússon, Ó. Þ., Gál, A., Weaver, D., Rossi, R., Armaroli, A., et al. (2017) · Human Mutation · doi:10.1002/humu.23262 · Cited by 64 · see citing works
Self-citationMSTO1 is a cytoplasmic pro‐mitochondrial fusion protein
Gál, A., Balicza, P., Weaver, D., Naghdi, S., Joseph, S. K., Várnai, P., Gyuris, T., Horváth, A., Nagy, L., Seifert, E. L., et al. (2017) · EMBO Molecular Medicine · doi:10.15252/emmm.201607058 · Cited by 65 · see citing works
Self-citationAgeing of skeletal muscle extracellular matrix and mitochondria: finding a potential link
Cai, L., Shi, L., Peng, Z., Sun, Y., & Chen, J. (2023) · Annals of Medicine · doi:10.1080/07853890.2023.2240707 · Cited by 60 · see citing works
The Role of Mitochondrial Dynamic Dysfunction in Age-Associated Type 2 Diabetes
Vezza, T., Díaz-Pozo, P., Canet, F., de Marañón, A. M., Abad-Jiménez, Z., García-Gargallo, C., Roldan, I., Solá, E., Bañuls, C., López‐Domènech, S., et al. (2022) · The World Journal of Men s Health · doi:10.5534/wjmh.210146 · Cited by 58 · see citing works
Calcium Transport and Signaling in Mitochondria
Bravo, R., Parra, V., López‐Crisosto, C., Díaz, P., Quest, A. F. G., & Lavandero, S. (2017) · Comprehensive physiology · doi:10.1002/j.2040-4603.2017.tb00748.x · Cited by 56 · see citing works
Therapeutic applications of mitochondrial transplantation
Ülger, Ö., & Kubat, G. B. (2022) · Biochimie · doi:10.1016/j.biochi.2022.01.002 · Cited by 56 · see citing works
The emerging role of skeletal muscle mitochondrial dynamics in exercise and ageing
Casuso, R. A., & Huertas, J. R. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101025 · Cited by 54 · see citing works
Siggins, R. W., McTernan, P. M., Simon, L., Souza‐Smith, F. M., & Molina, P. E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24108650 · Cited by 50 · see citing works
Sotomayor-Flores, C., Rivera-Mejías, P., Vásquez-Trincado, C., López‐Crisosto, C., Morales, P. E., Pennanen, C., Polakovičová, I., Aliaga-Tobar, V., Garcı́a, L., Roa, J. C., et al. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-0522-3 · Cited by 48 · see citing works
Molecular and biochemical regulation of skeletal muscle metabolism
Zumbaugh, M. D., Johnson, S., Shi, T. H., & Gerrard, D. E. (2022) · Journal of Animal Science · doi:10.1093/jas/skac035 · Cited by 53 · see citing works
Implications of mitochondrial fusion and fission in skeletal muscle mass and health
Romanello, V., & Sandri, M. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.02.011 · Cited by 44 · see citing works
Kitaoka, Y., Nakazato, K., & Ogasawara, R. (2016) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00465.2016 · Cited by 43 · see citing works
Simmen, T., & Tagaya, M. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-4567-7_1 · Cited by 43 · see citing works
Leermakers, P. A., Remels, A. H. V., Zonneveld, M. I., Rouschop, K. M. A., Schols, A. M. W. J., & Gosker, H. R. (2020) · The FASEB Journal · doi:10.1096/fj.201901815r · Cited by 43 · see citing works
Mitochondrial Function and Reactive Oxygen/Nitrogen Species in Skeletal Muscle
Chen, M., Li, Y., Deng, S., Zhao, Y., Lian, Z., & Yu, K. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.826981 · Cited by 42 · see citing works
Cellular Bioenergetics: Experimental Evidence for Alcohol-induced Adaptations
Simon, L., & Molina, P. E. (2022) · Function · doi:10.1093/function/zqac039 · Cited by 42 · see citing works
Karam, C. N., Yi, J., Xiao, Y., Dhakal, K. R., Zhang, L., Li, X., Manno, C. D., Xu, J., Li, K., Cheng, H., et al. (2017) · Skeletal Muscle · doi:10.1186/s13395-017-0123-0 · Cited by 42 · see citing works
Adrenergic Regulation of Drp1-Driven Mitochondrial Fission in Cardiac Physio-Pathology
Jhun, B. S., O‐Uchi, J., Adaniya, S. M., Cypress, M. W., & Yoon, Y. (2018) · Antioxidants · doi:10.3390/antiox7120195 · Cited by 41 · see citing works
The enigma of an interconnected mitochondrial reticulum: new insights into mitochondrial fusion
Mattie, S., Krols, M., & McBride, H. M. (2019) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2019.05.004 · Cited by 40 · see citing works
Overweight in the Elderly Induces a Switch in Energy Metabolism that Undermines Muscle Integrity
Potes, Y., Pérez-Martínez, Z., Bermejo-Millo, J. C., Rubio‐González, A., Fernández, M. F., Bermúdez, M., Arche-Coto, J. M., Solano, J. J., Boga, J. A., Oliván, M., et al. (2018) · Aging and Disease · doi:10.14336/ad.2018.0430 · Cited by 39 · see citing works
OPA1 Modulates Mitochondrial Ca2+ Uptake Through ER-Mitochondria Coupling
Cartes-Saavedra, B., Macuada, J., Lagos, D., Arancibia, D., Andrés, M. E., Yu‐Wai‐Man, P., Hajnóczky, G., & Eisner, V. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.774108 · Cited by 40 · see citing works
Self-citationKlawitter, F., Ehler, J., Bajorat, R., & Patejdl, R. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24065516 · Cited by 40 · see citing works
Rodríguez, L. R., Lapeña-Luzón, T., Benetó, N., Beltran-Beltran, V., Pallardó, F. V., González‐Cabo, P., & Navarro, J. A. (2022) · Antioxidants · doi:10.3390/antiox11010165 · Cited by 39 · see citing works
Alcohol and Skeletal Muscle in Health and Disease
Simon, L. (2023) · Alcohol research · doi:10.35946/arcr.v43.1.04 · Cited by 38 · see citing works
Human muscular mitochondrial fusion in athletes during exercise
Huertas, J. R., Ruiz‐Ojeda, F. J., Plaza‐Díaz, J., Nordsborg, N. B., Martín‐Albo, J., Rueda‐Robles, A., & Casuso, R. A. (2019) · The FASEB Journal · doi:10.1096/fj.201900365rr · Cited by 36 · see citing works
Simson, P., Jepihhina, N., Laasmaa, M., Peterson, P., Birkedal, R., & Vendelin, M. (2016) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2016.04.012 · Cited by 35 · see citing works
OPA1 disease-causing mutants have domain-specific effects on mitochondrial ultrastructure and fusion
Cartes-Saavedra, B., Lagos, D., Macuada, J., Arancibia, D., Burté, F., Sjöberg-Herrera, M. K., Andrés, M. E., Horváth, R., Yu‐Wai‐Man, P., Hajnóczky, G., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2207471120 · Cited by 36 · see citing works
Self-citationEshima, H. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.758316 · Cited by 32 · see citing works
Espinosa, A., Casas, M., & Jaimovich, E. (2023) · Antioxidants · doi:10.3390/antiox12081624 · Cited by 31 · see citing works
Skeletal muscle excitation-metabolism coupling
Díaz‐Vegas, A., Eisner, V., & Jaimovich, E. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.01.037 · Cited by 31 · see citing works
Self-citationOh, K. H., Sheoran, S., Richmond, J. E., & Kim, H. (2020) · The FASEB Journal · doi:10.1096/fj.201903166r · Cited by 31 · see citing works
Voltarelli, V. A., Coronado, M. J., Fernandes, L. G., Campos, J. C., Jannig, P. R., Ferreira, J. C. B., Fajardo, G., Brum, P. C., & Bernstein, D. (2021) · Cells · doi:10.3390/cells10010146 · Cited by 31 · see citing works
Sarcopenia and perioperative management of elderly surgical patients
Shi, Y., Zhou, L., Yan, E., Ling, Y., Yang, C., & Liu, C. (2021) · Frontiers in Bioscience-Landmark · doi:10.52586/4995 · Cited by 32 · see citing works
Mitochondrial-derived vesicles in skeletal muscle remodeling and adaptation
Picca, A., Guerra, F., Calvani, R., Romanò, R., Coelho‐Júnior, H. J., Bucci, C., Leeuwenburgh, C., & Marzetti, E. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.03.023 · Cited by 28 · see citing works
Monsalves‐Álvarez, M., Morales, P. E., Castro‐Sepúlveda, M., Sepúlveda, C., Rodriguez, J. M., Chiong, M., Eisner, V., Lavandero, S., & Troncoso, R. (2020) · Nutrients · doi:10.3390/nu12071930 · Cited by 27 · see citing works
Self-citationEthanol-Impaired Myogenic Differentiation is Associated with Decreased Myoblast Glycolytic Function
Levitt, D., Chalapati, N., Prendergast, M. J., Simon, L., & Molina, P. (2020) · Alcoholism: Clinical and Experimental Research · doi:10.1111/acer.14453 · Cited by 18 · see citing works
Alleyne, J., & Dopico, A. M. (2021) · Advances in Drug and Alcohol Research · doi:10.3389/adar.2021.10011 · Cited by 27 · see citing works
Perspectives on mitochondrial dysfunction in the regeneration of aging skeletal muscle
Wang, K., Gan, M., Lei, Y., Liao, T., Li, J., Niu, L., Zhao, Y., Chen, L., Wang, Y., Zhu, L., et al. (2025) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-025-00771-1 · Cited by 33 · see citing works
High-Fat Diet Augments the Effect of Alcohol on Skeletal Muscle Mitochondrial Dysfunction in Mice
Ismaeel, A., Laudato, J. A., Fletcher, E., Papoutsi, E., Tice, A. L., Hwa, L. S., Miserlis, D., Jamurtas, A. Z., Steiner, J. L., & Koutakis, P. (2022) · Nutrients · doi:10.3390/nu14051016 · Cited by 26 · see citing works
Photochemical Targeting of Mitochondria to Overcome Chemoresistance in Ovarian Cancer †
Rickard, B. P., Overchuk, M., Obaid, G., Ruhi, M. K., Demirci, U., Fenton, S. E., Santos, J. H., Kessel, D. H., & Rizvi, I. (2022) · Photochemistry and Photobiology · doi:10.1111/php.13723 · Cited by 26 · see citing works
Alghamdi, A. (2024) · Saudi Pharmaceutical Journal · doi:10.1016/j.jsps.2024.102012 · Cited by 25 · see citing works
Parry, H. A., Willingham, T. B., Giordano, K. A., Kim, Y., Qazi, S., Knutson, J. R., Combs, C. A., & Glancy, B. C. (2024) · The Journal of Physiology · doi:10.1113/jp286246 · Cited by 25 · see citing works
Emerging role of mitophagy in myoblast differentiation and skeletal muscle remodeling
Rahman, F. A., & Quadrilatero, J. (2021) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2021.11.026 · Cited by 25 · see citing works
Li, J., Kanasaki, M., Xu, L., Kitada, M., Nagao, K., Adachi, Y., Jinzu, H., Noguchi, Y., Kohno, M., Kanasaki, K., et al. (2018) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2018.03.013 · Cited by 24 · see citing works
Shaping the multi-scale architecture of mitochondria.
Jayashankar, V., Mueller, I., & Rafelski, S. M. (2016) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2016.02.006 · Cited by 21 · see citing works
Natural and Induced Mitochondrial Phosphate Carrier Loss
Seifert, E. L., Gál, A., Acoba, M. G., Li, Q., Anderson‐Pullinger, L., Golenár, T., Moffat, C., Sondheimer, N., Claypool, S. M., & Hajnóczky, G. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.744714 · Cited by 23 · see citing works
Self-citationNaghdi, S., Slovinsky, W. S., Madesh, M., Rubin, E., & Hajnóczky, G. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-1070-3 · Cited by 23 · see citing works
Self-citationAnalysis of mitochondrial structure and function in the Drosophila larval musculature
Wang, Z.-H., Clark, C. P., & Geisbrecht, E. R. (2015) · Mitochondrion · doi:10.1016/j.mito.2015.11.005 · Cited by 23 · see citing works
Effects of alcohol on skeletal muscle contractile performance in male and female mice
Laudato, J. A., Tice, A. L., Call, J. A., Gordon, B. S., & Steiner, J. L. (2021) · PLoS ONE · doi:10.1371/journal.pone.0255946 · Cited by 22 · see citing works
- Authors
- Eisner, V., Lenaers, G., & Hajnóczky, G.
- Affiliations
- Thomas Jefferson University (US)
- Inserm (FR)
- Corresponding author
- Hajnóczky, György
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2014-04-21
- Volume
- 205
- Issue
- 2
- Pages
- 179-195
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC4003250
- OpenAlex
- W2007546912
- Cited by
- 177
- References
- 74
- Citations by year
- 2026: 4 · 2025: 15 · 2024: 16 · 2023: 11 · 2022: 20 · 2021: 21 · 2020: 19 · 2019: 10 · 2018: 12 · 2017: 17 · 2016: 16 · 2015: 14 · 2014: 2
- FWCI
- 6.70
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- Duchenne Parent Project
- National Institutes of Health
- Hospital Universiti Sains Malaysia
- National Institute on Alcohol Abuse and Alcoholism (R01AA017773, U01AA021122, AA017773, RC2AA019416)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK051526)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- mitochondrial fusion, skeletal muscle, excitation-contraction coupling, Mfn1, mitochondrial network, myoblasts, chronic alcohol consumption, myopathy, calcium oscillations
- MeSH terms
- Animals, Cell Line, Female, Humans, Male, Membrane Proteins, Mitochondria, Muscle, Muscle Contraction, Muscle, Skeletal, Calcium Signaling, GTP Phosphohydrolases, Mitochondrial Proteins, Mitochondrial Membrane Transport Proteins, Mice, Rats, Mitochondrial Dynamics
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