The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.
Mitofusins and OPA1 Mediate Sequential Steps in Mitochondrial Membrane Fusion
Open accessAbstract
Mitochondrial fusion requires the coordinated fusion of the outer and inner membranes. Three large GTPases--OPA1 and the mitofusins Mfn1 and Mfn2--are essential for the fusion of mammalian mitochondria. OPA1 is mutated in dominant optic atrophy, a neurodegenerative disease of the optic nerve. In yeast, the OPA1 ortholog Mgm1 is required for inner membrane fusion in vitro; nevertheless, yeast lacking Mgm1 show neither outer nor inner membrane fusion in vivo, because of the tight coupling between these two processes. We find that outer membrane fusion can be readily visualized in OPA1-null mouse cells in vivo, but these events do not progress to inner membrane fusion. Similar defects are found in cells lacking prohibitins, which are required for proper OPA1 processing. In contrast, double Mfn-null cells show neither outer nor inner membrane fusion. Mitochondria in OPA1-null cells often contain multiple matrix compartments bounded together by a single outer membrane, consistent with uncoupling of outer versus inner membrane fusion. In addition, unlike mitofusins and yeast Mgm1, OPA1 is not required on adjacent mitochondria to mediate membrane fusion. These results indicate that mammalian mitofusins and OPA1 mediate distinct sequential fusion steps that are readily uncoupled, in contrast to the situation in yeast.
Overview
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
Verification
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?
In the citing paper
“Depletion of any of one these proteins results in severe dysfunction in respiratory capacity and fragmentation of mitochondria (Chen et al., 2005; Chen et al., 2010; Song et al., 2009)”
From Role of the mitochondrial DNA replication machinery in mitochondrial DNA mutagenesis, aging and age-related diseases (2017) · cites this paper as Song et al., 2009
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
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
Self-citationOPA1 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
A Photoactivatable GFP for Selective Photolabeling of Proteins and Cells
Patterson, G. H., & Lippincott‐Schwartz, J. (2002) · Science · doi:10.1126/science.1074952 · Cited by 1,612
Mutations 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
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
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
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
Self-citationAlexander, C., Votruba, M., Pesch, U. E. A., Thiselton, D. L., Mayer, S., Moore, A., Rodriguez, M., Kellner, U., Leo-Kottler, B., Auburger, G., et al. (2000) · Nature Genetics · doi:10.1038/79944 · Cited by 1,330
OPA1 requires mitofusin 1 to promote mitochondrial fusion
Cipolat, S., de Brito, O. M., Dal Zilio, B., & Scorrano, L. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407043101 · Cited by 1,300
Mitochondrial dynamics and apoptosis
Suen, D.-F., Norris, K. L., & Youle, R. J. (2008) · Genes & Development · doi:10.1101/gad.1658508 · Cited by 1,270
Cited by
Sorted by citations
ER Tubules Mark Sites of Mitochondrial Division
Friedman, J. R., Lackner, L. L., West, M., DiBenedetto, J. R., Nunnari, J., & Voeltz, G. K. (2011) · Science · doi:10.1126/science.1207385 · Cited by 2,072
Mitochondrial Dynamics and Its Involvement in Disease
Chan, D. C. (2020) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathmechdis-012419-032711 · Cited by 1,416
Mitochondrial dynamics-fusion, fission, movement, and mitophagy-in neurodegenerative diseases
Chen, H., & Chan, D. C. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp326 · Cited by 1,506
Mitochondrial dynamics: overview of molecular mechanisms
Tilokani, L., Nagashima, S., Paupe, V., & Prudent, J. (2018) · Essays in Biochemistry · doi:10.1042/ebc20170104 · Cited by 1,397
Mitochondrial dynamics and apoptosis
Suen, D.-F., Norris, K. L., & Youle, R. J. (2008) · Genes & Development · doi:10.1101/gad.1658508 · Cited by 1,270
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
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
Mitochondrial dynamics and inheritance during cell division, development and disease
Mishra, P., & Chan, D. C. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3877 · Cited by 1,076
Pernas, L. F., & Scorrano, L. (2015) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021115-105011 · Cited by 845
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
Mitochondria in health, disease, and aging
Harrington, J. S., Ryter, S. W., Plataki, M. E., Price, D. R., & Choi, A. M. K. (2023) · Physiological Reviews · doi:10.1152/physrev.00058.2021 · Cited by 641
Mitochondrial fusion, fission, and mitochondrial toxicity
Meyer, J. N., Leuthner, T. C., & Luz, A. L. (2017) · Toxicology · doi:10.1016/j.tox.2017.07.019 · Cited by 535
Mitofusins, from Mitochondria to Metabolism
Schrepfer, E., & Scorrano, L. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.02.022 · Cited by 504
Bannwarth, S., Ait-El-Mkadem, S., Chaussenot, A., Genin, E. C., Lacas‐Gervais, S., Fragaki, K., Berg-Alonso, L., Kageyama, Y., Serre, V., Moore, D. G., et al. (2014) · Brain · doi:10.1093/brain/awu138 · Cited by 507
Mishra, P., Carelli, V., Manfredi, G., & Chan, D. C. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.03.011 · Cited by 473
Hoppins, S. C., Collins, S. R., Cassidy-Stone, A., Hummel, E., DeVay, R. M., Lackner, L. L., Westermann, B., Schuldiner, M., Weissman, J. S., & Nunnari, J. M. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201107053 · Cited by 489
Mitochondrial dynamics in neurodegeneration
Itoh, K., Nakamura, K., Iijima, M., & Sesaki, H. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.10.006 · Cited by 486
SIRT3 Deacetylates and Activates OPA1 To Regulate Mitochondrial Dynamics during Stress
Samant, S. A., Zhang, H. J., Hong, Z., Pillai, V. B., Sundaresan, N. R., Wolfgeher, D., Archer, S. L., Chan, D. C., & Gupta, M. P. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01483-13 · Cited by 446
Molecular basis of selective mitochondrial fusion by heterotypic action between OPA1 and cardiolipin
Ban, T., Ishihara, T., Kohno, H., Saita, S., Ichimura, A., Maenaka, K., Oka, T., Mihara, K., & Ishihara, N. (2017) · Nature Cell Biology · doi:10.1038/ncb3560 · Cited by 410
Mitochondrial quality control: a matter of life and death for neurons
Rugarli, E. I., & Langer, T. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.38 · Cited by 423
ER sliding dynamics and ER-mitochondrial contacts occur on acetylated microtubules
Friedman, J. R., Webster, B. M., Mastronarde, D. N., Verhey, K. J., & Voeltz, G. K. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200911024 · Cited by 393
Mitochondrial Fusion: The Machineries In and Out
Gao, S., & Hu, J. (2020) · Trends in Cell Biology · doi:10.1016/j.tcb.2020.09.008 · Cited by 396
Mitochondrial fusion/fission dynamics in neurodegeneration and neuronal plasticity
Bertholet, A. M., Delerue, T., Millet, A. M., Moulis, M. F., David, C., Daloyau, M., Arnauné-Pelloquin, L., Davezac, N., Mils, V., Miquel, M. C., et al. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.10.011 · Cited by 363
Determinants and outcomes of mitochondrial dynamics
Quintana–Cabrera, R., & Scorrano, L. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.02.012 · Cited by 362
Baker, M. J., Lampe, P., Stojanovski, D., Korwitz, A., Anand, R., Tatsuta, T., & Langer, T. (2014) · The EMBO Journal · doi:10.1002/embj.201386474 · Cited by 367
Elfawy, H. A., & Das, B. B. (2018) · Life Sciences · doi:10.1016/j.lfs.2018.12.029 · Cited by 348
Liu, Y. J., McIntyre, R. L., Janssens, G. E., & Houtkooper, R. H. (2020) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2020.111212 · Cited by 347
Mitochondrial DNA: Distribution, Mutations, and Elimination
Yan, C., Duanmu, X., Zeng, L., Liu, B., & Song, Z. (2019) · Cells · doi:10.3390/cells8040379 · Cited by 346
Mitochondrial morphology transitions and functions: implications for retrograde signaling?
Picard, M. A., Shirihai, O. S., Gentil, B. J., & Burelle, Y. (2013) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00584.2012 · Cited by 335
Determinants and Functions of Mitochondrial Behavior
Labbè, K., Murley, A., & Nunnari, J. M. (2014) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-101011-155756 · Cited by 324
How mitochondrial dynamism orchestrates mitophagy
Shirihai, O. S., Song, M., & Dorn, G. W. (2015) · Circulation Research · doi:10.1161/circresaha.116.306374 · Cited by 311
Dietrich, M. O., Liu, Z.-W., & Horvath, T. L. (2013) · Cell · doi:10.1016/j.cell.2013.09.004 · Cited by 306
Hall, A. R., Burke, N., Dongworth, R. K., & Hausenloy, D. J. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12516 · Cited by 294
The regulation of mitochondrial morphology: Intricate mechanisms and dynamic machinery
Palmer, C. S., Osellame, L. D., Stojanovski, D., & Ryan, M. T. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2011.05.021 · Cited by 300
Nair, S., Sobotka, K. S., Joshi, P., Gressèns, P., Fleiss, B., Thornton, C., Mallard, C. E., & Hagberg, H. (2019) · Glia · doi:10.1002/glia.23587 · Cited by 285
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
Lee, J. H., Park, A., Oh, K., Lee, S. C., Kim, W. K., & Bae, K. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20194924 · Cited by 280
Fission and fusion machineries converge at ER contact sites to regulate mitochondrial morphology
Abrisch, R. G., Gumbin, S. C., Wisniewski, B. T., Lackner, L. L., & Voeltz, G. K. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.201911122 · Cited by 273
Energy matters: presynaptic metabolism and the maintenance of synaptic transmission
Li, S., & Sheng, Z. (2021) · Nature reviews. Neuroscience · doi:10.1038/s41583-021-00535-8 · Cited by 285
Phosphatidic Acid and Cardiolipin Coordinate Mitochondrial Dynamics
Kameoka, S., Adachi, Y., Okamoto, K., Iijima, M., & Sesaki, H. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.08.011 · Cited by 275
Picard, M. A., White, K., & Turnbull, D. M. (2012) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01096.2012 · Cited by 273
Mitophagy in Cancer: A Tale of Adaptation
Vara‐Pérez, M., Felipe‐Abrio, B., & Agostinis, P. (2019) · Cells · doi:10.3390/cells8050493 · Cited by 264
Programming axonal mitochondrial maintenance and bioenergetics in neurodegeneration and regeneration
Cheng, X., Huang, N., & Sheng, Z. (2022) · Neuron · doi:10.1016/j.neuron.2022.03.015 · Cited by 257
Mitochondrial Energy Metabolism and Redox Signaling in Brain Aging and Neurodegeneration
Yin, F., Boveris, A., & Cadenas, E. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4774 · Cited by 251
PKM2 coordinates glycolysis with mitochondrial fusion and oxidative phosphorylation
Li, T., Han, J., Jia, L., Hu, X., Chen, L., & Wang, Y. (2019) · Protein & Cell · doi:10.1007/s13238-019-0618-z · Cited by 251
The Soluble Form of Bax Regulates Mitochondrial Fusion via MFN2 Homotypic Complexes
Hoppins, S. C., Edlich, F., Harwig, M. C., Banerjee, S., McCaffery, J. M., Youle, R. J., & Nunnari, J. M. (2011) · Molecular Cell · doi:10.1016/j.molcel.2010.11.030 · Cited by 253
The MFN2 gene is responsible for mitochondrial DNA instability and optic atrophy 'plus' phenotype
Rouzier, C., Bannwarth, S., Chaussenot, A., Chevrollier, A., Verschueren, A., Bonello‐Palot, N., Fragaki, K., Caño, A., Pouget, J., Pellissier, J., et al. (2011) · Brain · doi:10.1093/brain/awr323 · Cited by 243
OPA1 Isoforms in the Hierarchical Organization of Mitochondrial Functions
Dotto, V. D., Mishra, P., Vidoni, S., Fogazza, M., Maresca, A., Caporali, L., McCaffery, J. M., Cappelletti, M., Baruffini, E., Lenaers, G., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.05.073 · Cited by 254
Ban, T., Heymann, J. A. W., Song, Z., Hinshaw, J. E., & Chan, D. C. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq088 · Cited by 239
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 231
Alterations in Mitochondrial Quality Control in Alzheimer’s Disease
Cai, Q., & Tammineni, P. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2016.00024 · Cited by 226
Parra, V., Verdejo, H., Iglewski, M., del Campo, A., Troncoso, R., Jones, D., Zhu, Y., Kuzmicic, J., Pennanen, C., López‐Crisosto, C., et al. (2013) · Diabetes · doi:10.2337/db13-0340 · Cited by 224
Mitochondrial Dynamics in Diabetes
Yoon, Y., Galloway, C. A., Jhun, B. S., & Yu, T. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3286 · Cited by 223
Song, W., Song, Y., Kincaid, B., Bossy, B., & Bossy‐Wetzel, E. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.07.004 · Cited by 220
Martin, O. J., Lai, L., Soundarapandian, M. M., Leone, T. C., Antonio Zorzano, A., Keller, M. P., Attie, A., Muoio, D. M., & Kelly, D. P. (2013) · Circulation Research · doi:10.1161/circresaha.114.302562 · Cited by 218
Mutations in SLC25A46, encoding a UGO1-like protein, cause an optic atrophy spectrum disorder
Abrams, A. J., Hufnagel, R. B., Rebelo, A. P., Zanna, C., Patel, N., Gonzalez, M., Campeanu, I. J., Griffin, L. B., Groenewald, S., Strickland, A. V., et al. (2015) · Nature Genetics · doi:10.1038/ng.3354 · Cited by 215
Mitochondrial Dynamics in Stem Cells and Differentiation
Seo, B. J., Yoon, S. H., & Tae, J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19123893 · Cited by 208
Qian, W., Choi, S., Gibson, G. A., Watkins, S. C., Bakkenist, C. J., & Houten, B. V. (2012) · Journal of Cell Science · doi:10.1242/jcs.109769 · Cited by 204
Mitochondrial dynamics and viral infections: A close nexus
Khan, M. A., Syed, G. H., Kim, S., & Siddiqui, A. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.12.040 · Cited by 195
Mitochondrial quality control mechanisms as molecular targets in diabetic heart
Chang, X., Li, Y., Cai, C., Wu, F., He, J., Zhang, Y., Zhong, J., Tan, Y., Liu, R., Zhu, H., et al. (2022) · Metabolism · doi:10.1016/j.metabol.2022.155313 · Cited by 193
Dysregulated Mitochondrial Dynamics and Metabolism in Obesity, Diabetes, and Cancer
Dai, W., & Jiang, L. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00570 · Cited by 186
The Mitochondrial Dynamism-Mitophagy-Cell Death Interactome
Dorn, G. W., & Kitsis, R. N. (2014) · Circulation Research · doi:10.1161/circresaha.116.303554 · Cited by 193
The ever-growing complexity of the mitochondrial fission machinery
Pagliuso, A., Cossart, P., & Stavru, F. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2603-0 · Cited by 192
Lee, H., Smith, S. B., & Yoon, Y. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.762567 · Cited by 190
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 196
Mitochondrial fission and fusion
Lee, H., & Yoon, Y. (2016) · Biochemical Society Transactions · doi:10.1042/bst20160129 · Cited by 183
Mitochondrial dynamics in the regulation of neurogenesis: From development to the adult brain
Khacho, M., & Slack, R. S. (2017) · Developmental Dynamics · doi:10.1002/dvdy.24538 · Cited by 189
Mitochondrial network structure homeostasis and cell death
Xie, L., Shi, F., Tan, Z., Li, Y., Bode, A. M., & Cao, Y. (2018) · Cancer Science · doi:10.1111/cas.13830 · Cited by 179
DeBalsi, K. L., Hoff, K. E., & Copeland, W. C. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2016.04.006 · Cited by 180
Mitochondrial Biogenesis in Neurons: How and Where
Cardanho‐Ramos, C., & Morais, V. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222313059 · Cited by 189
Mitochondrial dynamics in Parkinson's disease: a role for α-synuclein?
Devoto, V. M. P., & Falzone, T. L. (2017) · Disease Models & Mechanisms · doi:10.1242/dmm.026294 · Cited by 184
Is Mitochondrial Dysfunction a Common Root of Noncommunicable Chronic Diseases?
Díaz‐Vegas, A., Sánchez-Aguilera, P., Krycer, J. R., Morales, P. E., Monsalves‐Álvarez, M., Cifuentes, M., Rothermel, B. A., & Lavandero, S. (2020) · Endocrine Reviews · doi:10.1210/endrev/bnaa005 · Cited by 179
Li, H., Ruan, Y., Zhang, K., Jian, F., Hu, C., Miao, L., Gong, L., Sun, L., Zhang, X., Chen, S., et al. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.102 · Cited by 171
Specific Interaction with Cardiolipin Triggers Functional Activation of Dynamin-Related Protein 1
Bustillo-Zabalbeitia, I., Montessuit, S., Raemy, E., Basañez, G., Terrones, O., & Martinou, J.-C. (2014) · PLoS ONE · doi:10.1371/journal.pone.0102738 · Cited by 162
Zhang, Z., Wakabayashi, N., Wakabayashi, J., Tamura, Y., Song, W., Sereda, S., Clerc, P., Polster, B. M., Aja, S. M., Pletnikov, M. V., et al. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-12-0933 · Cited by 172
Cannavino, J., Brocca, L., Sandri, M., Grassi, B., Bottinelli, R., & Pellegrino, M. A. (2015) · The Journal of Physiology · doi:10.1113/jphysiol.2014.286740 · Cited by 166
Why size matters – balancing mitochondrial dynamics in Alzheimer's disease
DuBoff, B., Feany, M. Β., & Götz, J. (2013) · Trends in Neurosciences · doi:10.1016/j.tins.2013.03.002 · Cited by 168
Xian, H., & Liou, Y. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-00657-z · Cited by 177
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 165
Unravelling the mechanisms regulating muscle mitochondrial biogenesis
Hood, D. A., Tryon, L. D., Carter, H. N., Kim, Y., & Chen, C. C. W. (2016) · Biochemical Journal · doi:10.1042/bcj20160009 · Cited by 159
Mitochondrial dynamics in heart disease
Dorn, G. W. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.03.008 · Cited by 167
Redox homeostasis, oxidative stress and mitophagy
Garza-Lombó, C., Pappa, A., Panayiotidis, M. I., & Franco, R. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.01.002 · Cited by 168
Membrane depolarization activates the mitochondrial protease OMA1 by stimulating self‐cleavage
Zhang, K., Li, H., & Song, Z. (2014) · EMBO Reports · doi:10.1002/embr.201338240 · Cited by 159
Pennanen, C., Parra, V., López‐Crisosto, C., Morales, P. E., del Campo, A., Gutiérrez, T., Rivera-Mejías, P., Kuzmicic, J., Chiong, M., Antonio Zorzano, A., et al. (2014) · Journal of Cell Science · doi:10.1242/jcs.139394 · Cited by 166
Mitochondrial Dynamics and Mitochondrial Dysfunction in Diabetes.
Wada, J., & Nakatsuka, A. (2016) · PubMed · doi:10.18926/amo/54413 · Cited by 161
Contribution of Tau Pathology to Mitochondrial Impairment in Neurodegeneration
Maria Jose Perez, J., Jara, C., & Quintanilla, R. A. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00441 · Cited by 157
Mitochondrial dynamics and cell death in heart failure
Marín-García, J., & Akhmedov, A. T. (2016) · Heart Failure Reviews · doi:10.1007/s10741-016-9530-2 · Cited by 160
Functional and morphological impact of ER stress on mitochondria
Vannuvel, K., Renard, P., Raes, M. J., & Arnould, T. (2013) · Journal of Cellular Physiology · doi:10.1002/jcp.24360 · Cited by 161
Shaping the dynamic mitochondrial network
Lackner, L. L. (2014) · BMC Biology · doi:10.1186/1741-7007-12-35 · Cited by 156
Mitochondrial Dysfunction Contributes to the Pathogenesis of Alzheimer’s Disease
Cabezas-Opazo, F., Vergara-Pulgar, K., Maria Jose Perez, J., Jara, C., Osorio‐Fuentealba, C., & Quintanilla, R. A. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/509654 · Cited by 155
Acute exercise remodels mitochondrial membrane interactions in mouse skeletal muscle
Picard, M. A., Gentil, B. J., McManus, M. J., White, K., Louis, K. S., Gartside, S. E., Wallace, D. C., & Turnbull, D. M. (2013) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00819.2013 · Cited by 145
Mitochondrial dynamism and heart disease: changing shape and shaping change
Dorn, G. W. (2015) · EMBO Molecular Medicine · doi:10.15252/emmm.201404575 · Cited by 157
OPA1 and MICOS Regulate mitochondrial crista dynamics and formation
Hu, C., Shu, L., Huang, X., Yu, J., Li, L., Gong, L., Yang, M., Wu, Z., Gao, Z. Y., Zhao, Y., et al. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-03152-y · Cited by 142
Fealy, C. E., Mulya, A., Lai, N., & Kirwan, J. P. (2014) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01064.2013 · Cited by 140
Structural Insights into the Mechanism of Dynamin Superfamily Proteins
Jimah, J. R., & Hinshaw, J. E. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.11.003 · Cited by 140
Madhu, V., Boneski, P. K., Silagi, E. S., Qiu, Y., Kurland, I. J., Guntur, A. R., Shapiro, I. M., & Risbud, M. V. (2020) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.4019 · Cited by 137
Slower Dynamics and Aged Mitochondria in Sporadic Alzheimer’s Disease
Martín-Maestro, P., Gargini, R., García, E., Perry, G. L., Ávila, J., & García‐Escudero, V. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/9302761 · Cited by 135
Exercise and mitochondrial dynamics: keeping in shape with ROS and AMPK
Trewin, A., Berry, B., & Wojtovich, A. (2018) · Antioxidants · doi:10.3390/antiox7010007 · Cited by 129
Mitoconfusion: Noncanonical Functioning of Dynamism Factors in Static Mitochondria of the Heart
Song, M., & Dorn, G. W. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2014.12.019 · Cited by 128
Rosenfeld, M., Brenner-Lavie, H., Gal-Ben-Ari, S., Kavushansky, A., & Ben‐Shachar, D. (2011) · Biological Psychiatry · doi:10.1016/j.biopsych.2011.01.010 · Cited by 132
Metadata
- Authors
- Song, Z., Ghochani, M., McCaffery, J. M., Frey, T. G., & Chan, D. C.
- Affiliations
- California Institute of Technology (US)
- Departments of ‡Physics and
- Johns Hopkins University (US)
- San Diego State University (US)
- Venue
- Molecular Biology of the Cell
- Published
- 2009-08
- Volume
- 20
- Issue
- 15
- Pages
- 3525-3532
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- PMC
- PMC2719570
- OpenAlex
- W2164886443
- Cited by
- 623
- References
- 38
- Citations by year
- 2026: 32 · 2025: 45 · 2024: 46 · 2023: 39 · 2022: 62 · 2021: 41 · 2020: 41 · 2019: 35 · 2018: 36 · 2017: 36 · 2016: 31 · 2015: 33 · 2014: 33 · 2013: 38 · 2012: 31
- FWCI
- 9.79
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular Biology of the Cell (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion, cc-by-nc-sa)
- Funders
- California Institute of Technology
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM062967, GM062967)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Keywords
- mitochondrial fusion, mitofusins, Mfn1, mitofusin 2, OPA1, prohibitin, autosomal dominant optic atrophy, GTPase
- MeSH terms
- Animals, Cell Fusion, Cells, Cultured, Fibroblasts, Hybrid Cells, Membrane Fusion, Membrane Proteins, Microscopy, Electron, Polyethylene Glycols, Mice, Knockout, Microscopy, Confocal, GTP Phosphohydrolases, Mitochondrial Proteins, Adaptor Proteins, Signal Transducing, Green Fluorescent Proteins, Mitochondrial Membranes, Mice
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