Muscle-specific Drp1 overexpression impairs skeletal muscle growth via translational attenuation
Open accessAbstract
Mitochondrial fission and fusion are essential processes in the maintenance of the skeletal muscle function. The contribution of these processes to muscle development has not been properly investigated in vivo because of the early lethality of the models generated so far. To define the role of mitochondrial fission in muscle development and repair, we have generated a transgenic mouse line that overexpresses the fission-inducing protein Drp1 specifically in skeletal muscle. These mice displayed a drastic impairment in postnatal muscle growth, with reorganisation of the mitochondrial network and reduction of mtDNA quantity, without the deficiency of mitochondrial bioenergetics. Importantly we found that Drp1 overexpression activates the stress-induced PKR/eIF2 α /Fgf21 pathway thus leading to an attenuated protein synthesis and downregulation of the growth hormone pathway. These results reveal for the first time how mitochondrial network dynamics influence muscle growth and shed light on aspects of muscle physiology relevant in human muscle pathologies.
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Overexpression of fission proteins or certain metabolic conditions inducing mitochondrial fission adversely impacts skeletal muscle development and repair.
“For instance, overexpression of the fission proteins, or certain metabolic conditions inducing mitochondrial fission, adversely impacts skeletal muscle development and repair [49], leading to muscle atrophy [50].”
From Mitochondrial Adaptation in Skeletal Muscle: Impact of Obesity, Caloric Restriction, and Dietary Compounds (2024) · cites this paper as [49]
Even a mild imbalance between fusion and fission impairs skeletal muscle mass.
“Of particular importance, even a mild imbalance between fusion and fission has been demonstrated to impair skeletal muscle mass [49].”
From Mitochondrial Adaptation in Skeletal Muscle: Impact of Obesity, Caloric Restriction, and Dietary Compounds (2024) · cites this paper as [49]
Constitutive overexpression of DRP1 in skeletal muscle causes muscle loss and decreased exercise performance.
“Accordingly, the constitutive overexpression of DRP1 in skeletal muscle caused muscle loss and decreased exercise performance.”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [210]
There is strong evidence in skeletal muscle supporting a causal link between dysregulation of mitochondrial fission and alterations in muscle maintenance.
“There is strong evidence in skeletal muscle that supports a causal link between the dysregulation of mitochondrial fission and alterations in muscle maintenance [152, 196, 197, 210, 211].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [210]
In a DRP1 overexpression mouse model, stress-induced mitochondria-dependent signals activate both the UPRmt and the eIF2α-ATF4-FGF21 axis, causing a reduction in protein synthesis and a blockade of growth hormone actions that prevent muscle growth.
“In this mouse model, stress-induced mitochondria-dependent signals activate both the UPRmt and the eIF2α–ATF4– FGF21 axis, causing a reduction in protein synthesis and a blockade of growth hormones actions that prevent muscle growth [210].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [210]
Overexpression of the fission proteins Drp1 and Fis1 in muscles causes muscle atrophy.
“On the other hand, the overexpression of the fission proteins Drp1 and Fis1 in muscles causes muscle atrophy [5,7].”
From Inhibition of the Fission Machinery Mitigates OPA1 Impairment in Adult Skeletal Muscles (2019) · cites this paper as [7]
Failure in mitochondrial-shaping processes has detrimental consequences for the maintenance of muscle mass and function.
“Accordingly, the failure in mitochondrial-shaping processes has detrimental consequences for the maintenance of muscle mass and function [4,5,6,7,8,13,29].”
From Inhibition of the Fission Machinery Mitigates OPA1 Impairment in Adult Skeletal Muscles (2019) · cites this paper as [7]
Overexpression of DRP1 is sufficient to activate an atrophy program via the AMPK-FoxO3 axis.
“we and others have shown that overexpression of DRP1 is sufficient to activate an atrophy program via the AMPK-FoxO3 axis10,11.”
From DRP1-mediated mitochondrial shape controls calcium homeostasis and muscle mass (2019) · cites this paper as [11]
Loss-of-function approach shows decrease of mitofusin2 and downregulation of calnexin and upregulation of Bip/Grp78.
“Another peculiarity of the loss-of-function approach is the decrease of the ER-mitochondria tethering protein mitofusin2 and the down- and upregulation of the ER chaperones calnexin and Bip/Grp78, respectively11.”
From DRP1-mediated mitochondrial shape controls calcium homeostasis and muscle mass (2019) · cites this paper as [11]
Drp1 is a key player in regulating skeletal muscle development and maintenance.
“indicating that Drp1 is a key player in regulating skeletal muscle development and maintenance.”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [39]
Mitochondrial fission is essential for skeletal muscle health.
“Taken altogether, the findings discussed above clearly indicate that mitochondrial fission is essential for skeletal muscle health.”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [39]
Muscle-specific Drp1 overexpression impairs skeletal muscle growth in mice.
“Muscle-specific Drp1 overexpression was shown to impair skeletal muscle growth in mice [39,40].”
From Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging (2021) · cites this paper as [39]
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Cites
2 retracted
Myostatin is a novel tumoral factor that induces cancer cachexia
Lokireddy, S., Wijesoma, I. W., Bonala, S., Wei, M., Sze, S. K., McFarlane, C., Kambadur, R., & Sharma, M. (2012) · Biochemical Journal · doi:10.1042/bj20112024 · Cited by 96 · see citing works
RetractedWu, S., Grunwald, T., Kharitonenkov, A., Dam, J., Jockers, R., & Luca, F. D. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.462218 · Cited by 44 · see citing works
RetractedMutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A
Züchner, S., Mersiyanova, I. V., Muglia, M., Bissar-Tadmouri, N., Rochelle, J., Dadali, E. L., Zappia, M., Nelis, E., Patitucci, A., Senderek, J., et al. (2004) · Nature Genetics · doi:10.1038/ng1341 · Cited by 1,572 · see citing works
Delettre, C., Lenaers, G., Griffoin, J.-M., Gigarel, N., Lorenzo, C., Belenguer, P., Pelloquin, L., Grosgeorge, J., Turc-Carel, C., Perret, E., et al. (2000) · Nature Genetics · doi:10.1038/79936 · Cited by 1,446 · see citing works
Coping with stress: eIF2 kinases and translational control
Wek, R. C., Jiang, H.-Y., & Anthony, T. G. (2006) · Biochemical Society Transactions · doi:10.1042/bst0340007 · Cited by 1,290 · 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
Fusion and fission: interlinked processes critical for mitochondrial health
Chan, D. C. (2012) · Annual Review of Genetics · doi:10.1146/annurev-genet-110410-132529 · Cited by 1,196 · 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
Mitofusin-2 Determines Mitochondrial Network Architecture and Mitochondrial Metabolism
Bach, D., Pich, S., Soriano, F. X., Vega, N., Baumgartner, B., Oriola, J., Daugaard, J. R., Lloberas, J., Camps, M., Zierath, J. R., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212754200 · Cited by 832 · cited 1× · see citing works
“This kind of rearrangement has been observed in cellular models defective in fission or fusion proteins expression.(5,34,35) Little, however, is known on the”
BackgroundA Lethal Defect of Mitochondrial and Peroxisomal Fission
Waterham, H. R., Koster, J., van Roermund, C. W. T., Mooyer, P. A. W., Wanders, R. J. A., & Leonard, J. V. (2007) · New England Journal of Medicine · doi:10.1056/nejmoa064436 · Cited by 749 · see citing works
Jheng, H.-F., Tsai, P.-J., Guo, S.-M., Kuo, L.-H., Chang, C.-S., Su, I.-J., Chang, C.-R., & Tsai, Y.-S. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.05603-11 · Cited by 650 · see citing works
Mitochondrial fission and remodelling contributes to muscle atrophy
Romanello, V., Guadagnin, E., Gomes, L., Roder, I., Sandri, C., Petersen, Y., Milan, G., Masiero, E., Del Piccolo, P., Foretz, M., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.60 · Cited by 596 · see citing works
Coping with stress: eIF2 kinases and translational control
Jiang, H.-Y., Wek, R. C., & Anthony, T. G. (2005) · Biochemical Society Transactions · doi:10.1042/bst20060007 · Cited by 522 · see citing works
Mitochondrial dysfunction and apoptosis in myopathic mice with collagen VI deficiency
Irwin, W., Bergamin, N., Sabatelli, P., Reggiani, C., Megighian, A., Merlini, L., Braghetta, P., Columbaro, M., Volpin, D., Bressan, G. M., et al. (2003) · Nature Genetics · doi:10.1038/ng1270 · Cited by 509 · see citing works
New insights into the function and regulation of mitochondrial fission
Otera, H., Ishihara, N., & Mihara, K. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.02.002 · Cited by 476 · see citing works
Palam, L. R., Baird, T. D., & Wek, R. C. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.216093 · Cited by 441 · see citing works
Suomalainen, A., Elo, J. M., Pietiläinen, K. H., Hakonen, A. H., Sevastianova, K., Korpela, M., Isohanni, P., Marjavaara, S. K., Tyni, T., Kiuru-Enari, S., et al. (2011) · The Lancet Neurology · doi:10.1016/s1474-4422(11)70155-7 · Cited by 427 · see citing works
Inhibition of Growth Hormone Signaling by the Fasting-Induced Hormone FGF21
Inagaki, T., Lin, V. Y., Goetz, R., Mohammadi, M., Mangelsdorf, D. J., & Kliewer, S. A. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.05.006 · Cited by 409 · see citing works
Al‐Mehdi, A., Pastukh, V. M., Swiger, B. M., Reed, D., Patel, M., Bardwell, G. C., Pastukh, V. V., ALEXEYEV, M. F., & Gillespie, M. N. (2012) · Science Signaling · doi:10.1126/scisignal.2002712 · Cited by 386 · see citing works
Mitochondrial Fusion Directs Cardiomyocyte Differentiation via Calcineurin and Notch Signaling
Kasahara, A., Cipolat, S., Chen, Y., Dorn, G. W., & Scorrano, L. (2013) · Science · doi:10.1126/science.1241359 · Cited by 354 · see citing works
Selective induction of mitochondrial chaperones in response to loss of the mitochondrial genome.
Martinus, R., Garth, G. P., Webster, T., Cartwright, P., Naylor, D. J., Høj, P., & Hoogenraad, N. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0098h.x · Cited by 340 · see citing works
Natural Products: Bioactivity, Biochemistry, and Biological Effects in Cancer and Disease Therapy
Chang, H.-W., Chuang, L., Guleria, S., & Yasmin, S. (2013) · The Scientific World JOURNAL · doi:10.1155/2013/713480 · Cited by 313 · see citing works
Mitochondrial myopathy induces a starvation-like response
Tyynismaa, H., Carroll, C. J., Raimundo, N., Ahola-Erkkilä, S., Wenz, T., Ruhanen, H., Guse, K., Hemminki, A., Peltola-Mjøsund, K. E., Tulkki, V., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq310 · Cited by 300 · see citing works
OPA1 links human mitochondrial genome maintenance to mtDNA replication and distributionPreprint
Elachouri, G., Vidoni, S., Zanna, C., Pattyn, A., Boukhaddaoui, H., Gaget, K., Yu‐Wai‐Man, P., Gasparre, G., Sarzi, E., Delettre, C., et al. (2010) · Genome Research · doi:10.1101/gr.108696.110 · Cited by 238 · see citing works
Mouse lines with photo‐activatable mitochondria to study mitochondrial dynamics
Pham, A. H., McCaffery, J. M., & Chan, D. C. (2012) · genesis · doi:10.1002/dvg.22050 · Cited by 229 · see citing works
Stress-induced Skeletal Muscle Gadd45a Expression Reprograms Myonuclei and Causes Muscle Atrophy
Ebert, S. M., Dyle, M. C., Kunkel, S. D., Bullard, S. A., Bongers, K. S., Fox, D. K., Dierdorff, J. M., Foster, E. D., & Adams, C. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.374777 · Cited by 221 · see citing works
Horibe, T., & Hoogenraad, N. J. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000835 · Cited by 208 · see citing works
Ca2+ 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
Progenitors of skeletal muscle satellite cells express the muscle determination gene, MyoD
Kanisicak, O., Mendez, J. J., Yamamoto, S., Yamamoto, M., & Goldhamer, D. J. (2009) · Developmental Biology · doi:10.1016/j.ydbio.2009.05.554 · Cited by 192 · see citing works
Loss of Mitofusin 2 Promotes Endoplasmic Reticulum Stress
Ngoh, G. A., Papanicolaou, K. N., & Walsh, K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.359174 · Cited by 183 · see citing works
Mitochondrial fusion is frequent in skeletal muscle and supports excitation–contraction coupling
Eisner, V., Lenaers, G., & Hajnóczky, G. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201312066 · Cited by 177 · see citing works
Rath, E., Berger, E., Messlik, A., Nunes, T., Liu, B., Kim, S. C., Hoogenraad, N. J., Sans, M., Sartor, R. B., & Haller, D. (2011) · Gut · doi:10.1136/gutjnl-2011-300767 · Cited by 154 · see citing works
Skeletal Muscle Atrophy, a Link between Depression of Protein Synthesis and Increase in Degradation
Eley, H. L., & Tisdale, M. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610378200 · Cited by 151 · see citing works
Impaired Mitochondrial Dynamics and Bioenergetics in Diabetic Skeletal Muscle
Liu, R., Jin, P., LiqunYu, Wang, Y., Han, L., Shi, T., & Li, X. (2014) · PLoS ONE · doi:10.1371/journal.pone.0092810 · Cited by 146 · see citing works
Resetting translational homeostasis restores myelination in Charcot-Marie-Tooth disease type 1B mice
D’Antonio, M., Musner, N., Scapin, C., Ungaro, D., Carro, U. D., Ron, D., Feltri, M. L., & Wrabetz, L. G. (2013) · The Journal of Experimental Medicine · doi:10.1084/jem.20122005 · Cited by 136 · see citing works
Self-citationMitochondria as a Potential Regulator of Myogenesis
Wagatsuma, A., & Sakuma, K. (2013) · The Scientific World JOURNAL · doi:10.1155/2013/593267 · Cited by 134 · see citing works
The Transcription Factor ATF4 Promotes Skeletal Myofiber Atrophy during Fasting
Ebert, S. M., Monteys, A. M., Fox, D. K., Bongers, K. S., Shields, B. E., Malmberg, S. E., Davidson, B. L., Suneja, M., & Adams, C. M. (2010) · Molecular Endocrinology · doi:10.1210/me.2009-0345 · Cited by 130 · see citing works
Requirement of Inducible Nitric Oxide Synthase for Skeletal Muscle Regeneration after Acute Damage
Rigamonti, E., Touvier, T., Clementi, E., Manfredi, A. A., Brunelli, S., & Rovere, P. Q. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1202903 · Cited by 129 · see citing works
Self-citationPalma, 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
Self-citationInhibition of Drp1-dependent mitochondrial division impairs myogenic differentiation
Kim, B., Kim, J.-S., Yoon, Y., Santiago, M. C., Brown, M. D., & Park, J. (2013) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00502.2012 · Cited by 103 · see citing works
Mechanism of induction of muscle protein loss by hyperglycaemia
Russell, S. T., Rajani, S., Dhadda, R. S., & Tisdale, M. J. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.10.002 · Cited by 80 · see citing works
Muscle regeneration occurs to coincide with mitochondrial biogenesis
Wagatsuma, A., Kotake, N., & Yamada, S. (2010) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-010-0668-2 · Cited by 79 · see citing works
Chen, W. W., Birsoy, K., Mihaylova, M. M., Snitkin, H., Stasinski, I., Yücel, B., Bayraktar, E. C., Carette, J. E., Clish, C. B., Brummelkamp, T. R., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.02.046 · Cited by 79 · see citing works
Regulation of proteolysis during reloading of the unweighted soleus muscle
Taillandier, D., AUROUSSEAU, E., Combaret, L., Guézennec, C.-Y., & Attaix, D. (2003) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(03)00004-9 · Cited by 69 · see citing works
Is the Laron Mouse an Accurate Model of Laron Syndrome?
Kopchick, J. J., & Laron, Z. (1999) · Molecular Genetics and Metabolism · doi:10.1006/mgme.1999.2890 · Cited by 60 · see citing works
LEPROT and LEPROTL1 cooperatively decrease hepatic growth hormone action in mice
Touvier, T., Conte-Auriol, F., Briand, O., Cudejko, C., Paumelle, R., Caron, S., Baugé, E., Rouillé, Y., Salles, J., Staels, B., et al. (2009) · Journal of Clinical Investigation · doi:10.1172/jci34997 · Cited by 59 · see citing works
Self-citationAlter, J., & Bengal, E. (2011) · PLoS ONE · doi:10.1371/journal.pone.0029498 · Cited by 53 · see citing works
Eley, H. L., Russell, S. T., & Tisdale, M. J. (2007) · British Journal of Cancer · doi:10.1038/sj.bjc.6603704 · Cited by 46 · see citing works
Reeds, P. J., & Fiorotto, M. L. (1990) · Proceedings of The Nutrition Society · doi:10.1079/pns19900048 · Cited by 13 · see citing works
Badaloni, A., Bonanomi, D., Albieri, I., Givogri, M. I., Bongarzone, E. R., Valtorta, F., & Consalez, G. G. (2007) · genesis · doi:10.1002/dvg.20307 · Cited by 13 · see citing works
Mfn2 modulates the unfolded protein response
Muñoz, J. P., & Zorzano, A. (2014) · Cell Cycle · doi:10.4161/cc.27782 · Cited by 5 · see citing works
Ogata (1997) · doi:10.1002/(sici)1097-0185(199706)248:2
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Larsson, L., Degens, H., Li, M., Salviati, L., Lee, Y. I., Thompson, W., Kirkland, J. L., & Sandri, M. (2019) · Physiological Reviews · doi:10.1152/physrev.00061.2017 · Cited by 1,797 · see citing works
Mitochondrial Dynamics and Metabolic Regulation
Wai, T., & Langer, T. (2016) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2015.12.001 · Cited by 1,304 · 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
Role of Cardiolipin in Mitochondrial Signaling Pathways
Dudek, J. (2017) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2017.00090 · Cited by 433 · see citing works
DRP1-mediated mitochondrial shape controls calcium homeostasis and muscle mass
Favaro, G., Romanello, V., Varanita, T., Andrea Desbats, M., Morbidoni, V., Tezze, C., Albiero, M., Canato, M., Gherardi, G., De Stefani, D., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10226-9 · Cited by 398 · see citing works
The role of mitochondrial fission in cardiovascular health and disease
Quiles, J. M., & Gustafsson, Å. B. (2022) · Nature Reviews Cardiology · doi:10.1038/s41569-022-00703-y · Cited by 305 · see citing works
Hu, C., Huang, Y., & Li, L. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18010144 · Cited by 302 · see citing works
Skeletal muscle mitochondrial remodeling in exercise and diseases
Gan, Z., Fu, T., Kelly, D. P., & Vega, R. B. (2018) · Cell Research · doi:10.1038/s41422-018-0078-7 · Cited by 287 · see citing works
Mitochondrial morphology is altered in atrophied skeletal muscle of aged mice
Leduc-Gaudet, J.-P., Picard, M., Pelletier, F. S.-J., Sgarioto, N., Auger, M.-J., Vallée, J., Robitaille, R., St-Pierre, D. H., & Gouspillou, G. (2015) · Oncotarget · doi:10.18632/oncotarget.4235 · Cited by 273 · see citing works
Mitochondrial Dynamics and Mitophagy in Skeletal Muscle Health and Aging
Leduc-Gaudet, J.-P., Hussain, S. N. A., Barreiro, E., & Gouspillou, G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22158179 · Cited by 268 · see citing works
“As mentioned above, overexpression of Drp1 impaired skeletal muscle growth [39], whereas deletion or insufficient expression of Drp1 in skeletal muscle led to 40–50% atrophy [42,43], indicating that Drp1 is a key player in regulating skeletal muscle development and maintenance.”
BackgroundMitochondrial dysfunction in the development and progression of neurodegenerative diseases
Johnson, J., Mercado‐Ayón, E., Mercado-Ayon, Y., Dong, Y., Halawani, S. M., Ngaba, L. V., & Lynch, D. R. (2020) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2020.108698 · Cited by 246 · 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
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Lahera, V., Heras, N. D. L., López-Farré, A. J., Manucha, W. A., & Ferder, L. (2017) · Current Hypertension Reports · doi:10.1007/s11906-017-0710-9 · Cited by 180 · see citing works
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Sprenger, H., & Langer, T. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.08.003 · Cited by 173 · see citing works
Huang, Y., Zhu, X., Chen, K., Lang, H., Zhang, Y., Hou, P., Ran, L., Zhou, M., Zheng, J., Yi, L., et al. (2019) · Aging · doi:10.18632/aging.101910 · Cited by 167 · see citing works
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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 · see citing works
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Kubat, G. B., Bouhamida, E., Ülger, Ö., Türkel, İ., Pedriali, G., Ramaccini, D., Ekinci, Ö., Özerkliğ, B., Atalay, Ö., Patergnani, S., et al. (2023) · Mitochondrion · doi:10.1016/j.mito.2023.07.003 · Cited by 128 · see citing works
Restelli, L. M., Oettinghaus, B., Halliday, M., Ağca, C., Licci, M., Sironi, L., Savoia, C., Hench, J., Tolnay, M., Neutzner, A., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.07.023 · Cited by 96 · see citing works
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Salminen, A., Kaarniranta, K., & Kauppinen, A. (2017) · Cellular Signalling · doi:10.1016/j.cellsig.2017.08.009 · Cited by 97 · see citing works
Dulac, M., Leduc‐Gaudet, J., Reynaud, O., Ayoub, M., Guérin, A., Finkelchtein, M., Hussain, S. N., & Gouspillou, G. (2020) · The Journal of Physiology · doi:10.1113/jp279802 · Cited by 90 · see citing works
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Tanaka, H., Okazaki, T., Aoyama-Ishiwatari, S., Yokota, M., Koike, M., Okada, Y., Fujiki, Y., & Gotoh, Y. (2019) · Journal of Cell Science · doi:10.1242/jcs.224766 · Cited by 81 · see citing works
Mitochondrial dysfunction, mitophagy, and role of dynamin‐related protein 1 in Alzheimer's disease
Medala, V. K., Gollapelli, B., Dewanjee, S., Ogunmokun, G., Kandimalla, R. J. L., & Vallamkondu, J. (2021) · Journal of Neuroscience Research · doi:10.1002/jnr.24781 · Cited by 76 · see citing works
Rahman, F. A., & Quadrilatero, J. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03807-9 · Cited by 76 · see citing works
Lv, J., Li, Y., Shi, S., Xu, X., Wu, H., Zhang, B., & Song, Q. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113833 · Cited by 73 · see citing works
Homeostatic sensing of dietary protein restriction: a case for FGF21
Hill, C. M., Berthoud, H.-R., Münzberg, H., & Morrison, C. D. (2018) · Frontiers in Neuroendocrinology · doi:10.1016/j.yfrne.2018.06.002 · Cited by 68 · see citing works
Bell, M. B., Bush, Z., McGinnis, G. R., & Rowe, G. C. (2019) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00719.2018 · Cited by 62 · see citing works
Mitochondrial dynamics define muscle fiber type by modulating cellular metabolic pathways
Yasuda, T., Ishihara, T., Ichimura, A., & Ishihara, N. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112434 · Cited by 60 · see citing works
Zecchini, S., Giovarelli, M., Perrotta, C., Morisi, F., Touvier, T., Renzo, I. D., Moscheni, C., Bassi, M. T., Cervia, D., Sandri, M., et al. (2018) · Autophagy · doi:10.1080/15548627.2018.1507439 · Cited by 53 · see citing works
Self-citationLi, J., Wang, Z., Li, C., Song, Y., Wang, Y., Hai, B., & Zhang, Y. (2022) · Cells · doi:10.3390/cells11132086 · Cited by 52 · see citing works
The Role of Mitophagy in Skeletal Muscle Damage and Regeneration
Chatzinikita, E., Maridaki, M. D., Palikaras, K., Koutsilieris, M., & Philippou, Α. (2023) · Cells · doi:10.3390/cells12050716 · Cited by 53 · see citing works
Regulation of muscle and mitochondrial health by the mitochondrial fission protein Drp1 in aged mice
Dulac, M., Leduc‐Gaudet, J., Cefis, M., Ayoub, M., Reynaud, O., Shams, A., Moamer, A., Nery Ferreira, M. F., Hussain, S. N., & Gouspillou, G. (2021) · The Journal of Physiology · doi:10.1113/jp281752 · Cited by 51 · see citing works
Molecular Machinery and Pathophysiology of Mitochondrial Dynamics
Chiu, Y., Lin, S., Kuo, C.-H., & Li, C. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.743892 · Cited by 48 · see citing works
Mitochondrial dynamics and metabolic homeostasis
Sebastián, D., & Antonio Zorzano, A. (2018) · Current Opinion in Physiology · doi:10.1016/j.cophys.2018.02.006 · Cited by 46 · see citing works
Giovarelli, M., Zecchini, S., Catarinella, G., Moscheni, C., Sartori, P., Barbieri, C., Roux-Biejat, P., Napoli, A., Vantaggiato, C., Cervia, D., et al. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105751 · Cited by 45 · see citing works
Self-citationImplications 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
Mitochondria: At the crossroads between mechanobiology and cell metabolism
Su, É., Villard, C., & Manneville, J. (2023) · Biology of the Cell · doi:10.1111/boc.202300010 · Cited by 42 · see citing works
MeCP2 Affects Skeletal Muscle Growth and Morphology through Non Cell-Autonomous Mechanisms
Conti, V., Gandaglia, A., Galli, F., Tirone, M., Bellini, E., Campana, L., Kilstrup‐Nielsen, C., Rovere, P. Q., Brunelli, S., & Landsberger, N. (2015) · PLoS ONE · doi:10.1371/journal.pone.0130183 · Cited by 45 · see citing works
Self-citationMitochondrial 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
Giovarelli, M., Zecchini, S., Martini, E., Garrè, M., Barozzi, S., Ripolone, M., Napoli, L., Coazzoli, M., Vantaggiato, C., Roux-Biejat, P., et al. (2020) · Cell Death & Differentiation · doi:10.1038/s41418-020-0510-7 · Cited by 41 · see citing works
Self-citationFis1 deficiencies differentially affect mitochondrial quality in skeletal muscle
Zhang, Z., Sliter, D. A., Bleck, C. K. E., & Ding, S. (2019) · Mitochondrion · doi:10.1016/j.mito.2019.09.005 · Cited by 41 · see citing works
Skeletal muscle mitochondria in health and disease
Mario, A. D., Gherardi, G., Rizzuto, R., & Mammucari, C. (2021) · Cell Calcium · doi:10.1016/j.ceca.2021.102357 · Cited by 40 · see citing works
Shero, J. A., Lindholm, M. E., Sandri, M. F., & Stanford, K. I. (2025) · Circulation Research · doi:10.1161/circresaha.124.325614 · Cited by 43 · see citing works
Regulation of Skeletal Muscle DRP-1 and FIS-1 Protein Expression by IL-6 Signaling
Fix, D. K., Vanderveen, B. N., Counts, B., & Carson, J. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/8908457 · Cited by 36 · see citing works
Targeting the Mitochondria-Proteostasis Axis to Delay Aging
Zimmermann, A., Madreiter‐Sokolowski, C. T., Stryeck, S., & Abdellatif, M. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.656201 · Cited by 40 · see citing works
Modulation of Host Cell Metabolism by Chlamydia trachomatis
Rother, M., da Costa, A. R. T., Zietlow, R., Meyer, T. F., & Rudel, T. (2019) · Microbiology Spectrum · doi:10.1128/microbiolspec.bai-0012-2019 · Cited by 39 · see citing works
Mitochondrial mechanisms in the pathogenesis of chronic inflammatory musculoskeletal disorders
Wu, K., Shieh, J.-S., Qin, L., & Guo, J. J. (2024) · Cell & Bioscience · doi:10.1186/s13578-024-01259-9 · Cited by 36 · see citing works
Molecular Mechanisms Underlying Muscle Wasting in Huntington’s Disease
Bozzi, M., & Sciandra, F. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218314 · Cited by 36 · see citing works
Protein composition of the muscle mitochondrial reticulum during postnatal development
Kim, Y., Yang, D. S., Katti, P., & Glancy, B. C. (2019) · The Journal of Physiology · doi:10.1113/jp277579 · Cited by 35 · see citing works
Natani, S., Dhople, V. M., Parveen, A., Sruthi, K. K., Khilar, P., Bhukya, S., & Ummanni, R. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2021.119085 · Cited by 30 · see citing works
Mao, X., Gu, Y., Sui, X., Shen, L., Han, J. S., Wang, H., Xi, Q., Zhuang, Q., Meng, Q., & Wu, G. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.673618 · Cited by 30 · see citing works
The mitochondrial integrated stress response: A novel approach to anti-aging and pro-longevity
Wang, X., & Zhang, G. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102603 · Cited by 29 · see citing works
Regulation of mitochondrial quality following repeated bouts of hindlimb unloading
Rosa‐Caldwell, M. E., Brown, J. L., Perry, R. A., Shimkus, K. L., Shirazi‐Fard, Y., Brown, L. A., Hogan, H. A., Fluckey, J. D., Washington, T. A., Wiggs, M. P., et al. (2019) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/apnm-2019-0218 · Cited by 30 · see citing works
Jun, L., Tao, Y.-X., Geetha, T., & Babu, J. R. (2024) · Current Nutrition Reports · doi:10.1007/s13668-024-00555-7 · Cited by 27 · see citing works
Cefis, M., Dargegen, M., Marcangeli, V., Taherkhani, S., Dulac, M., Leduc‐Gaudet, J., Mayaki, D., Hussain, S. N. A., & Gouspillou, G. (2024) · Acta Physiologica · doi:10.1111/apha.14119 · Cited by 28 · see citing works
Kugler, B. A., Deng, W., Duguay, A. L., Garcia, J. P., Anderson, M. C., Nguyen, P., Houmard, J. A., & Zou, K. (2021) · Physiological Reports · doi:10.14814/phy2.14808 · Cited by 26 · see citing works
All-Trans Retinoic Acid Increases DRP1 Levels and Promotes Mitochondrial Fission
Chidipi, B., Shah, S. I., Reiser, M. A., Kanithi, M., Garces, A. H., Cha, B. J., Ullah, G., & Noujaim, S. F. (2021) · Cells · doi:10.3390/cells10051202 · Cited by 26 · 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
NovelDNM1Lvariants impair mitochondrial dynamics through divergent mechanisms
Nolden, K. A., Egner, J. M., Collier, J. J., Russell, O. M., Alston, C. L., Harwig, M. C., Widlansky, M. E., Sasorith, S., Barbosa, I. A., Douglas, A. G. L., et al. (2022) · Life Science Alliance · doi:10.26508/lsa.202101284 · Cited by 24 · see citing works
Mitochondrial transplantation as a possible therapeutic option for sarcopenia
Türkel, İ., Özerkliğ, B., Yılmaz, M., Ülger, Ö., Kubat, G. B., & Tuncer, M. (2023) · Journal of Molecular Medicine · doi:10.1007/s00109-023-02326-3 · Cited by 24 · see citing works
Pedrotti, S., Caccia, R., Neguembor, M. V., García-Manteiga, J. M., Ferri, G., Palma, C. D., Canu, T., Giovarelli, M., Marra, P., Fiocchi, A., et al. (2019) · Science Advances · doi:10.1126/sciadv.aav1472 · Cited by 24 · see citing works
Self-citationFrataxin deficiency lowers lean mass and triggers the integrated stress response in skeletal muscle
Vásquez-Trincado, C., Dunn, J., Han, J. I., Hymms, B., Tamaroff, J. G., Patel, M., Nguyen, S., Dedio, A., Wade, K., Enigwe, C., et al. (2022) · JCI Insight · doi:10.1172/jci.insight.155201 · Cited by 23 · see citing works
Drp1 controls complex II assembly and skeletal muscle metabolism by Sdhaf2 action on mitochondria
Zhou, Z., Ma, A., Moore, T. M., Wolf, D. M., Yang, N. L., Tran, P. H., Segawa, M., Strumwasser, A. R., Ren, W., Fu, K., et al. (2024) · Science Advances · doi:10.1126/sciadv.adl0389 · Cited by 22 · see citing works
Mechanisms Responsible for the High Sensitivity of Neural Cells to Vitamin B1 Deficiency
IuM, P., Pavlova, A. S., & Mezhenska, O. A. (2016) · Neurophysiology · doi:10.1007/s11062-017-9620-3 · Cited by 22 · see citing works
Yu, J., Zheng, C., Guo, Q., Yin, Y., Duan, Y., & Li, F. (2024) · Science China Life Sciences · doi:10.1007/s11427-023-2552-7 · Cited by 21 · see citing works
Kugler, B. A., Lourie, J., BERGER, N. J. A., Lin, N., Nguyen, P., DosSantos, E., Ali, A. S., Sesay, A., Rosen, H. G., KALEMBA, B. L., et al. (2023) · Molecular Metabolism · doi:10.1016/j.molmet.2023.101802 · Cited by 20 · see citing works
Fowler, P. C., Byrne, D. J., Blackstone, C. D., & O’Sullivan, N. C. (2020) · Brain Sciences · doi:10.3390/brainsci10090646 · Cited by 20 · see citing works
Neural In Vitro Models for Studying Substances Acting on the Central Nervous System
Fritsche, E., Tigges, J., Hartmann, J., Kapr, J., Serafini, M. M., & Viviani, B. (2020) · Handbook of experimental pharmacology · doi:10.1007/164_2020_367 · Cited by 20 · see citing works
Marini, C., Cossu, V., Bonifacino, T., Bauckneht, M., Torazza, C., Bruno, S., Castellani, P., Ravera, S., Milanese, M., Venturi, C. B., et al. (2020) · EJNMMI Research · doi:10.1186/s13550-020-00666-6 · Cited by 20 · see citing works
Kim, K. W., Baek, M., Yoon, M., & Son, K. H. (2021) · Clinical Nutrition · doi:10.1016/j.clnu.2021.03.009 · Cited by 19 · see citing works
Inhibition of DRP1 Impedes Zygotic Genome Activation and Preimplantation Development in Mice
Li, Y., Mei, N., Cheng, G., Yang, J., & Zhou, L. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.788512 · Cited by 19 · see citing works
Fibroblast Growth Factor 21: A Fascinating Perspective on the Regulation of Muscle Metabolism
Li, S., Chen, J., Wei, P., Zou, T., & You, J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242316951 · Cited by 19 · see citing works
Xu, X., & Wen, Z. (2023) · PubMed Central · Cited by 19 · see citing works
Katti, P., Rai, M., Srivastava, S., D’Silva, P., & Nongthomba, U. (2021) · Experimental Cell Research · doi:10.1016/j.yexcr.2021.112486 · Cited by 17 · see citing works
Mitochondria and endoplasmic reticulum: Targets for a better insulin sensitivity in skeletal muscle?
Boulinguiez, A., Staels, B., Duez, H., & Lancel, S. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2017.05.011 · Cited by 17 · see citing works
Control of mitochondrial dynamics and apoptotic pathways by peroxisomes
Jiang, C., & Okazaki, T. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.938177 · Cited by 16 · see citing works
Huang, D., Yang, L., Guo, Y., Weng, M., Ye, H., Zhang, T., Lin, F., Zhang, K., & Fang, X. (2025) · Communications Biology · doi:10.1038/s42003-025-07654-3 · Cited by 15 · see citing works
Roux-Biejat, P., Coazzoli, M., Marrazzo, P., Zecchini, S., Renzo, I. D., Prata, C., Napoli, A., Moscheni, C., Giovarelli, M., Barbalace, M. C., et al. (2021) · Cells · doi:10.3390/cells10113028 · Cited by 15 · see citing works
Self-citationPatel, B., New, L. E., Griffiths, J. C., Deuchars, J., & Filippi, B. (2020) · Molecular Metabolism · doi:10.1016/j.molmet.2020.101123 · Cited by 15 · see citing works
Mitochondrial Dynamics: Shaping Metabolic Adaptation
Cantó, C. (2018) · International review of cytology · doi:10.1016/bs.ircmb.2018.05.004 · Cited by 14 · see citing works
Noone, J., Damiot, A., Kenny, H., Chery, I., Zahariev, A., Normand, S., Crampes, F., de Glisezinski, I., Rochfort, K. D., Laurens, C., et al. (2023) · The Journal of Physiology · doi:10.1113/jp284734 · Cited by 13 · see citing works
Mitochondrial dynamics: roles in exercise physiology and muscle mass regulation
Djalalvandi, A., & Scorrano, L. (2022) · Current Opinion in Physiology · doi:10.1016/j.cophys.2022.100550 · Cited by 12 · see citing works
Jiwan, N. C., Appell, C. R., WANG, R., Shen, C., & Luk, H. (2022) · In Vivo · doi:10.21873/invivo.12998 · Cited by 12 · see citing works
Rosen, H. G., BERGER, N. J. A., Hodge, S. N., Fujishiro, A. A., Lourie, J., Kapadia, V., Duzz, T., Linden, M. A., Jee, E., Kim, J., et al. (2025) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.01009.2024 · Cited by 10 · see citing works
You, Y., Ni, H., Ma, Q., Jiang, L., Cai, J., He, W., Lin, X., Li, K., Wang, Z., Yan, W., et al. (2025) · Nutrition and Diabetes · doi:10.1038/s41387-025-00391-w · Cited by 10 · see citing works
Seipin deficiency leads to defective parturition in mice†
Zowalaty, A. E. E., & Ye, X. (2017) · Biology of Reproduction · doi:10.1093/biolre/iox088 · Cited by 10 · see citing works
Mitochondrial quality orchestrates muscle-adipose dialog to alleviate dietary obesity
Xu, Z., Fu, T., Guo, Q., Sun, W., & Gan, Z. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.12.020 · Cited by 10 · see citing works
Zhou, G., Liu, A., Bai, J., Liu, H., Zhu, Y., Luo, Y., Zheng, L., Hou, Y., Li, J., & Fu, X. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1431683 · Cited by 9 · see citing works
Drp1 Overexpression Decreases Insulin Content in Pancreatic MIN6 Cells
Kabra, U. D., Moruzzi, N., Berggren, P., & Jastroch, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012338 · Cited by 9 · see citing works
Brenmoehl, J., Ohde, D., Walz, C., Langhammer, M., Schultz, J., & Hoeflich, A. (2020) · Cells · doi:10.3390/cells9122697 · Cited by 9 · see citing works
Mahmoud, S. A., Abdel-Aziz, M. M., Khafaga, R. H. M., Hafez, H. A., Kamel, M. A. E.-N., & Shaker, S. A. (2023) · Molecular Medicine · doi:10.1186/s10020-023-00666-x · Cited by 9 · see citing works
Yang, Z., Liu, J.-P., Bao, B., Li, T., Wu, Q., He, M., Bi, H., & Guo, D. (2023) · International Journal of Ophthalmology · doi:10.18240/ijo.2023.12.05 · Cited by 8 · see citing works
Skeletal Muscle Mitochondrial and Autophagic Dysregulation Are Modifiable in Spinal Muscular Atrophy
Mikhail, A. I., Ng, S. Y., Xhuti, D., Lesinski, M. A., Chhor, J., Deguise, M., Repentigny, Y. D., Nederveen, J. P., Kothary, R., Tarnopolsky, M. A., et al. (2025) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.13701 · Cited by 8 · see citing works
DNM1L-mediated fission governs mitophagy & mitochondrial biogenesis during myogenic differentiation
Rahman, F. A., Yap, J. M. F., Joseph, T. M., Adam, A., Chapman, S. M., & Quadrilatero, J. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02142-x · Cited by 8 · see citing works
Zhang, K., Zhu, Y., Tang, A.-Q., Zhou, Z.-T., Yang, Y., Liu, Z., Li, Y., Liang, X., Feng, Z.-F., Wang, J., et al. (2025) · Translational Oncology · doi:10.1016/j.tranon.2025.102272 · Cited by 7 · see citing works
Esteca, M. V., Divino, I. A., da Silva, A. L. V., Severino, M. B., Braga, R. R., Ropelle, E. R., Simabuco, F. M., & Baptista, I. L. (2024) · Acta Physiologica · doi:10.1111/apha.14111 · Cited by 7 · see citing works
- Authors
- Touvier, T., De Palma, C., Rigamonti, E., Scagliola, A., Incerti, E., Mazelin, L., Thomas, J.-L., D'Antonio, M., Politi, L., Schaeffer, L., Clementi, E., & Brunelli, S.
- Affiliations
- IRCCS Eugenio Medea (IT)
- IRCCS Ospedale San Raffaele (IT)
- École Normale Supérieure de Lyon (FR)
- University of Milan (IT)
- Corresponding author
- Clementi, E
- Brunelli, S
- Venue
- Cell Death & Disease
- Published
- 2015-02-26
- Volume
- 6
- Issue
- 2
- Pages
- e1663-e1663
- ISSN
- 2041-4889 (ISSN-L)
- PMC
- PMC4669802
- OpenAlex
- W2002049655
- Cited by
- 140
- References
- 52
- Citations by year
- 2026: 8 · 2025: 19 · 2024: 14 · 2023: 14 · 2022: 11 · 2021: 22 · 2020: 17 · 2019: 12 · 2018: 11 · 2017: 6 · 2016: 4 · 2015: 2
- FWCI
- 3.33
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Cell Death and Disease (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Archivio Istituzionale della Ricerca (Universita Degli Studi Di Milano) (submittedVersion, cc-by)
- BOA (University of Milano-Bicocca) (submittedVersion, cc-by)
- Funders
- European Commission (241440)
- Ministero della Salute (RC2015, GR–2011–02350544, PRIN 2010-2011)
- Ministero dell’Istruzione, dell’Università e della Ricerca (PRIN 2010-2011 “, (PRIN 2010))
- 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 › Physiology › Adipose Tissue and Metabolism
- Keywords
- Drp1, mitochondrial fission, mitochondrial dynamics, skeletal muscle growth, translational attenuation, PKR, eIF2α, FGF21, myogenesis, mitochondrial DNA, transgenic mouse model, muscle regeneration
- MeSH terms
- Animals, DNA, Mitochondrial, Mice, Transgenic, Oxygen Consumption, Blotting, Western, Muscle, Skeletal, Dynamins, Immunoprecipitation, Mice, Membrane Potential, Mitochondrial
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