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Mitochondrial dynamics and apoptosis
Open accessAbstract
In healthy cells, mitochondria continually divide and fuse to form a dynamic interconnecting network. The molecular machinery that mediates this organelle fission and fusion is necessary to maintain mitochondrial integrity, perhaps by facilitating DNA or protein quality control. This network disintegrates during apoptosis at the time of cytochrome c release and prior to caspase activation, yielding more numerous and smaller mitochondria. Recent work shows that proteins involved in mitochondrial fission and fusion also actively participate in apoptosis induction. This review will cover the recent advances and presents competing models on how the mitochondrial fission and fusion machinery may intersect apoptosis pathways.
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“The frequencies of fusion and fission events are balanced to maintain the overall morphology of the mitochondrial population (8, 41).”
From Mitochondrial Fission Contributes to Mitochondrial Dysfunction and Insulin Resistance in Skeletal Muscle (2012) · cites this paper as [41]
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Li, P., Nijhawan, D., Budihardjo, I., Srinivasula, S. M., Ahmad, M., Alnemri, E. S., & Wang, X. (1997) · Cell · doi:10.1016/s0092-8674(00)80434-1 · Cited by 7,289
Induction of Apoptotic Program in Cell-Free Extracts: Requirement for dATP and Cytochrome c
Liu, X., Kim, C. N., Yang, J., Jemmerson, R., & Wang, X. (1996) · Cell · doi:10.1016/s0092-8674(00)80085-9 · Cited by 5,167
Prevention of Apoptosis by Bcl-2: Release of Cytochrome c from Mitochondria Blocked
Yang, J., Liu, X., Bhalla, K. N., Kim, C. N., Ibrado, A. M., Cai, J., Peng, T.-I., Jones, D. P., & Wang, X. (1997) · Science · doi:10.1126/science.275.5303.1129 · Cited by 4,913
The BCL-2 protein family: opposing activities that mediate cell death
Youle, R. J., & Strasser, A. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2308 · Cited by 4,806
Self-citationThe Release of Cytochrome c from Mitochondria: A Primary Site for Bcl-2 Regulation of Apoptosis
Kluck, R. M., Bossy‐Wetzel, E., Green, D. R., & Newmeyer, D. D. (1997) · Science · doi:10.1126/science.275.5303.1132 · Cited by 4,715
Bcl-2 gene promotes haemopoietic cell survival and cooperates with c-myc to immortalize pre-B cells
Vaux, D., Cory, S., & Adams, J. (1988) · Nature · doi:10.1038/335440a0 · Cited by 3,355
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
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
The Bcl-2 apoptotic switch in cancer development and therapy
Adams, J. M., & Cory, S. (2007) · Oncogene · doi:10.1038/sj.onc.1210220 · Cited by 2,256
The Role of Mitochondria in Apoptosis
Wang, C., & Youle, R. J. (2009) · Annual Review of Genetics · doi:10.1146/annurev-genet-102108-134850 · Cited by 1,987
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Youle, R. J., & van der Bliek, A. M. (2012) · Science · doi:10.1126/science.1219855 · Cited by 3,674
Self-citationAntioxidants Maintain Cellular Redox Homeostasis by Elimination of Reactive Oxygen Species
He, L., He, T., Farrar, S., Ji, L., Liu, T., & Ma, X. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000485089 · Cited by 2,207
The Role of Mitochondria in Apoptosis
Wang, C., & Youle, R. J. (2009) · Annual Review of Genetics · doi:10.1146/annurev-genet-102108-134850 · Cited by 1,987
Self-citationMitochondrial fusion and fission in cell life and death
Westermann, B. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3013 · Cited by 2,002
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Chen, H., & Chan, D. C. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp326 · Cited by 1,506
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Chen, W., Zhao, H., & Li, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01547-9 · Cited by 1,306
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
Otera, H., Wang, C., Cleland, M. M., Setoguchi, K., Yokota, S., Youle, R. J., & Mihara, K. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201007152 · Cited by 1,110
Self-citationIshihara, N., Nomura, M., Jofuku, A., Kato, H., Suzuki, S. O., Masuda, K., Otera, H., Nakanishi, Y., Nonaka, I., Goto, Y.-I., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1907 · Cited by 1,066
BAK/BAX macropores facilitate mitochondrial herniation and mtDNA efflux during apoptosis
McArthur, K., Whitehead, L. W., Heddleston, J. M., Li, L., Padman, B. S., Oorschot, V., Geoghegan, N. D., Chappaz, S., Davidson, S., San Chin, H., et al. (2018) · Science · doi:10.1126/science.aao6047 · Cited by 1,072
SLP‐2 is required for stress‐induced mitochondrial hyperfusion
Tondera, D., Grandemange, S., Jourdain, A. A., Karbowski, M., Mattenberger, Y., Herzig, S., Cruz, S. D., Clerc, P., Lauria, I., Merkwirth, C., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.89 · Cited by 796
Self-citationMitochondrial dynamics regulates migration and invasion of breast cancer cells
Zhao, J., Zhang, J., Yu, M., Xie, Y., Huang, Y., Wolff, D. W., Abel, P. W., & Tu, Y. (2012) · Oncogene · doi:10.1038/onc.2012.494 · Cited by 783
Regulation of mitochondrial dynamics in acute kidney injury in cell culture and rodent models
Brooks, C., Wei, Q., Cho, S.-G., & Dong, Z. (2009) · Journal of Clinical Investigation · doi:10.1172/jci37829 · Cited by 735
Mitochondrial dysfunction in Parkinson's disease
Winklhofer, K. F., & Haass, C. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.08.013 · Cited by 688
The dynamin-related GTPase Drp1 is required for embryonic and brain development in mice
Wakabayashi, J., Zhang, Z., Wakabayashi, N., Tamura, Y., Fukaya, M., Kensler, T. W., Iijima, M., & Sesaki, H. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200903065 · Cited by 667
Disturbed mitochondrial dynamics and neurodegenerative disorders
Burté, F., Carelli, V., Chinnery, P. F., & Yu‐Wai‐Man, P. (2014) · Nature Reviews Neurology · doi:10.1038/nrneurol.2014.228 · Cited by 686
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
Mitochondria-Targeting Ceria Nanoparticles as Antioxidants for Alzheimer’s Disease
Kwon, H. J., Cha, M.-Y., Kim, D., Kim, D., Soh, M., Shin, K., Hyeon, T., & Mook‐Jung, I. (2016) · ACS Nano · doi:10.1021/acsnano.5b08045 · Cited by 667
Misko, A. L., Jiang, S., Wegorzewska, I., Milbrandt, J., & Baloh, R. H. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.6248-09.2010 · Cited by 653
Mitochondrial optic neuropathies—Disease mechanisms and therapeutic strategies
Yu-Wai-Man, P., Griffiths, P. G., & Chinnery, P. F. (2011) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2010.11.002 · Cited by 633
Mitofusins and OPA1 mediate sequential steps in mitochondrial membrane fusion
Song, Z., Ghochani, M., McCaffery, J. M., Frey, T. G., & Chan, D. C. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-03-0252 · Cited by 623
Roca, F. J., & Ramakrishnan, L. (2013) · Cell · doi:10.1016/j.cell.2013.03.022 · Cited by 592
miR-499 regulates mitochondrial dynamics by targeting calcineurin and dynamin-related protein-1
Wang, J., Jiao, J.-Q., Li, Q., Long, B., Wang, K., Liu, J., Li, Y.-R., & Li, P. (2010) · Nature Medicine · doi:10.1038/nm.2282 · Cited by 582
Endothelial dysfunction in diabetes mellitus: Molecular mechanisms and clinical implications
Tabit, C. E., Chung, W. B., Hamburg, N. M., & Vita, J. A. (2010) · Reviews in Endocrine and Metabolic Disorders · doi:10.1007/s11154-010-9134-4 · Cited by 594
Mitochondria as playmakers of apoptosis, autophagy and senescence
Abate, M., Festa, A., Falco, M., Lombardi, A., Luce, A., Grimaldi, A., Zappavigna, S., Sperlongano, P., Irace, C., Caraglia, M., et al. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.05.022 · Cited by 552
Fis1 and Bap31 bridge the mitochondria–ER interface to establish a platform for apoptosis induction
Iwasawa, R., Mahul‐Mellier, A., Datler, C., Pazarentzos, E., & Grimm, S. (2011) · The EMBO Journal · doi:10.1038/emboj.2010.346 · Cited by 520
Mitochondria and Endothelial Function
Kluge, M. A., Fetterman, J. L., & Vita, J. A. (2013) · Circulation Research · doi:10.1161/circresaha.111.300233 · Cited by 508
Mitochondrial Dysfunction in Cancer
Boland, M. L., Chourasia, A. H., & Macleod, K. F. (2013) · Frontiers in Oncology · doi:10.3389/fonc.2013.00292 · Cited by 521
Terman, A., Kurz, T., Navratil, M., Arriaga, E. A., & Brunk, U. T. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2598 · Cited by 490
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 501
Mitochondrial Ca2+ and apoptosis
Giorgi, C., Baldassari, F., Bononi, A., Bonora, M., Marchi, E. D., Marchi, S., Missiroli, S., Patergnani, S., Rimessi, A., Suski, J. M., et al. (2012) · Cell Calcium · doi:10.1016/j.ceca.2012.02.008 · Cited by 488
Wang, K., Long, B., Zhou, L., Liu, F., Zhou, Q., Liu, C.-Y., Fan, Y.-Y., & Li, P. (2014) · Nature Communications · doi:10.1038/ncomms4596 · Cited by 456
Mitochondrial Dynamics in Regulating the Unique Phenotypes of Cancer and Stem Cells
Chen, H., & Chan, D. C. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.05.016 · Cited by 456
Diverse roles of mitochondria in ischemic stroke
Yang, J., Mukda, S., & Chen, S. (2018) · Redox Biology · doi:10.1016/j.redox.2018.03.002 · Cited by 459
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
The novel regulatory role of lnc RNA ‐mi RNA ‐ mRNA axis in cardiovascular diseases
Huang, Y. (2018) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13866 · Cited by 446
Mitochondrial Regulation of Cell Cycle and Proliferation
Arciuch, V. G. A., Elguero, M. E., Poderoso, J. J., & Carreras, M. C. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4085 · Cited by 449
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Burke, P. J. (2017) · Trends in cancer · doi:10.1016/j.trecan.2017.10.006 · Cited by 434
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Kasahara, A., & Scorrano, L. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.08.005 · Cited by 433
The Mitochondrial Basis of Aging and Age-Related Disorders
Srivastava, S. (2017) · Genes · doi:10.3390/genes8120398 · Cited by 446
Mitochondrial cell death effectors
Brenner, D., & Mak, T. W. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.09.004 · Cited by 414
Melatonin: A Mitochondrial Targeting Molecule Involving Mitochondrial Protection and Dynamics
Tan, D.-X., Manchester, L., Qin, L., & Reiter, R. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17122124 · Cited by 402
Mitochondrial dynamics: regulatory mechanisms and emerging role in renal pathophysiology
Zhan, M., Brooks, C. R., Liu, F., Sun, L., & Dong, Z. (2013) · Kidney International · doi:10.1038/ki.2012.441 · Cited by 401
Mechanisms of Aminoglycoside Ototoxicity and Targets of Hair Cell Protection
Huth, M. E., Ricci, A. J., & Cheng, A. G.-L. (2011) · International Journal of Otolaryngology · doi:10.1155/2011/937861 · Cited by 390
Structural and functional link between the mitochondrial network and the endoplasmic reticulum
Giorgi, C., Stefani, D. D., Bononi, A., Rizzuto, R., & Pinton, P. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.04.010 · Cited by 388
Zhao, J., Liu, T., Jin, S., Wang, X., Qu, M., Uhlén, P., Tomilin, N., Shupliakov, O., Lendahl, U., & Nistér, M. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.198 · Cited by 370
Yu, H., Jin, F., Liu, D., Shu, G., Wang, X., Qi, J., Sun, M., Yang, P., Jiang, S., Ying, X., et al. (2020) · Theranostics · doi:10.7150/thno.40395 · Cited by 370
Wu, W., Lin, C., Wu, K., Jiang, L., Wang, X., Li, W., Zhuang, H., Zhang, X., Chen, H. H., Li, S., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201593102 · Cited by 370
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 371
Luzzo, K. M., Wang, Q., Purcell, S. H., Chi, M. M.-Y., Jimenez, P. T., Grindler, N. M., Schedl, T., & Moley, K. H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0049217 · Cited by 356
Cheng, G., Kong, R., Zhang, L., & Zhang, J. (2012) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2012.02025.x · Cited by 359
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Rambold, A. S., & Pearce, E. L. (2017) · Trends in Immunology · doi:10.1016/j.it.2017.08.006 · Cited by 357
Bonora, M., Wieckowski, M. R., Chinopoulos, C., Kepp, O., Kroemer, G., Galluzzi, L., & Pinton, P. (2015) · Oncogene · doi:10.1038/onc.2014.96 · Cited by 330
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Yan, C., Duanmu, X., Zeng, L., Liu, B., & Song, Z. (2019) · Cells · doi:10.3390/cells8040379 · Cited by 346
Mandal, S., Lindgren, A., Srivastava, A., Clark, A. T., & Banerjee, U. K. (2010) · Stem Cells · doi:10.1002/stem.590 · Cited by 328
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Yuan, L., & Kaplowitz, N. (2013) · Clinics in Liver Disease · doi:10.1016/j.cld.2013.07.002 · Cited by 322
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Peterson, C. M., Johannsen, D. L., & Ravussin, É. (2012) · Journal of Aging Research · doi:10.1155/2012/194821 · Cited by 337
Kim, S., Khan, M. A., Quan, J., Till, A., Subramani, S. E., & Siddiqui, A. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003722 · Cited by 316
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
Live-cell microscopy – tips and tools
Frigault, M. M., Lacoste, J., Swift, J. L., & Brown, C. M. (2009) · Journal of Cell Science · doi:10.1242/jcs.033837 · Cited by 307
Mitochondrial fission and fusion
Scott, I., & Youle, R. J. (2010) · Essays in Biochemistry · doi:10.1042/bse0470085 · Cited by 306
Self-citationMitochondrial dynamics in cell death and neurodegeneration
Cho, D., Nakamura, T., & Lipton, S. A. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0435-2 · Cited by 306
Kim, S., Syed, G. H., Khan, M. A., Chiu, W.-W., Sohail, M. A., Gish, R. G., & Siddiqui, A. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321114111 · Cited by 293
High-Mobility Group Box 1 Is Essential for Mitochondrial Quality Control
Tang, D., Kang, R., Livesey, K. M., Kroemer, G., Billiar, T. R., Houten, B. V., Zeh, H. J., & Lotze, M. T. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.04.008 · Cited by 303
Abnormal mitochondrial dynamics and neurodegenerative diseases
Su, B., Wang, X., Zheng, L., Perry, G. L., Smith, M. A., & Zhu, X. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.09.013 · Cited by 301
Ouali, A., Gagaoua, M., Boudida, Y., Becila, S., Boudjellal, A., Herrera-Méndez, C. H., & Sentandreu, M. Á. (2013) · Meat Science · doi:10.1016/j.meatsci.2013.05.010 · Cited by 291
ATG12 Conjugation to ATG3 Regulates Mitochondrial Homeostasis and Cell Death
Radoshevich, L., Murrow, L., Chen, N., Fernandez, E., Roy, S., Fung, C., & Debnath, J. (2010) · Cell · doi:10.1016/j.cell.2010.07.018 · Cited by 290
Sano, R., Annunziata, I., Patterson, A. E., Moshiach, S., Gomero, E. M., Opferman, J. T., Forte, M. A., & d’Azzo, A. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.10.021 · Cited by 301
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(2020) · Proceedings of the Python in Science Conferences · doi:10.25080/majora-342d178e-02b · Cited by 285
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Zaccolo, M., Zerio, A., & Lobo, M. J. (2020) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000086 · Cited by 281
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He, Z., Ning, N., Zhou, Q., Khoshnam, S. E., & Farzaneh, M. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.11.005 · Cited by 272
Quirós, P. M., Ramsay, A. J., Sala, D., Fernández‐Vizarra, E., Rodríguez, F., Peinado, J. R., Fernández‐García, M. S., Vega, J. A., Enríquez, J. A., Zorzano, A., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.70 · Cited by 269
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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
“Mitochondrial fission is mainly governed by Dynamin-Related Protein 1 (Drp1) (reviewed in [30,31]).”
BackgroundMitochondria, Energetics, Epigenetics, and Cellular Responses to Stress
Shaughnessy, D. T., McAllister, K. A., Worth, L., Haugen, A. C., Meyer, J. N., Domann, F. E., Houten, B. V., Mostoslavsky, R., Bultman, S. J., Baccarelli, A., et al. (2014) · Environmental Health Perspectives · doi:10.1289/ehp.1408418 · Cited by 272
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Elgass, K., Pakay, J. L., Ryan, M. T., & Palmer, C. S. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.05.002 · Cited by 274
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Gao, J., Wang, L., Liu, J., Xie, F., Su, B., & Wang, X. (2017) · Antioxidants · doi:10.3390/antiox6020025 · Cited by 250
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Shoshan‐Barmatz, V., Ben-Hail, D., Admoni, L., Krelin, Y., & Tripathi, S. S. (2014) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2014.10.040 · Cited by 255
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Chandhok, G., Lazarou, M., & Neumann, B. (2017) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12378 · Cited by 263
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Venderová, K., & Park, D. S. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a009365 · Cited by 246
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Senyilmaz, D., Virtue, S., Xu, X., Tan, C. Y., Griffin, J. L., Miller, A. K., Vidal‐Puig, A., & Teleman, A. A. (2015) · Nature · doi:10.1038/nature14601 · Cited by 253
Mitochondrial dynamics during cell cycling
Horbay, R., & Bilyy, R. O. (2016) · APOPTOSIS · doi:10.1007/s10495-016-1295-5 · Cited by 256
Classification of mitocans, anti-cancer drugs acting on mitochondria
Neužil, J., Dong, L., Rohlena, J., Truksa, J., & Ralph, S. J. (2012) · Mitochondrion · doi:10.1016/j.mito.2012.07.112 · Cited by 255
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Kim, H., Scimia, M. C., Wilkinson, D., Díaz-Trelles, R., Wood, M. R., Bowtell, D. D. L., Dillin, A. G., Mercola, M. A., & Ronai, Z. A. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.08.045 · Cited by 247
Retinal ganglion cell neurodegeneration in mitochondrial inherited disorders
Carelli, V., Morgia, C. L., Valentino, M. L., Barboni, P., Ross‐Cisneros, F. N., & Sadun, A. A. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.02.024 · Cited by 238
miR-484 regulates mitochondrial network through targeting Fis1
Wang, K., Long, B., Jiao, J.-Q., Wang, J., Liu, J., Li, Q., & Li, P. (2012) · Nature Communications · doi:10.1038/ncomms1770 · Cited by 230
Hamacher‐Brady, A., Stein, H., Turschner, S., Toegel, I., Mora-Rodríguez, R. A., Jennewein, N., Efferth, T., Eils, R., & Brady, N. R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.210047 · Cited by 233
Drp1-dependent mitochondrial fission via MiD49/51 is essential for apoptotic cristae remodeling
Otera, H., Miyata, N., Kuge, O., & Mihara, K. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201508099 · Cited by 229
Zhou, H., Ma, Q., Zhu, P., Ren, J. T., Reiter, R. J., & Chen, Y. (2018) · Journal of Pineal Research · doi:10.1111/jpi.12471 · Cited by 229
Grasso, D., Zampieri, L. X., Capelôa, T., de Velde, J. A. V., & Sonveaux, P. (2020) · Cell Stress · doi:10.15698/cst2020.06.221 · Cited by 239
Hypoxia and energetic tumour metabolism
Brahimi-Horn, M. C., Bellot, G. L., & Pouysségur, J. (2010) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2010.10.006 · Cited by 247
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Metadata
- Authors
- Suen, D.-F., Norris, K. L., & Youle, R. J.
- Affiliations
- National Institutes of Health (US)
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2008-06-15
- Volume
- 22
- Issue
- 12
- Pages
- 1577-1590
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- PMC
- PMC2732420
- OpenAlex
- W2104954806
- Cited by
- 1,270
- References
- 209
- Citations by year
- 2026: 27 · 2025: 41 · 2024: 62 · 2023: 65 · 2022: 57 · 2021: 84 · 2020: 81 · 2019: 69 · 2018: 82 · 2017: 86 · 2016: 95 · 2015: 79 · 2014: 89 · 2013: 63 · 2012: 75
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- HighWire Press Open Archive (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- mitochondrial dynamics, mitochondrial fission, mitochondrial fusion, apoptosis, cytochrome c release, caspase activation, mitochondrial quality control, mitochondrial network, apoptosis induction
- MeSH terms
- Animals, Cell Division, Cell Fusion, Humans, Membrane Proteins, Mitochondria, Models, Biological, Protein Processing, Post-Translational, Cellular Senescence, Apoptosis, Calcium-Calmodulin-Dependent Protein Kinases, Proto-Oncogene Proteins c-bcl-2, GTP Phosphohydrolases, Mitochondrial Proteins, Drosophila Proteins, Cytochromes c, Adaptor Proteins, Signal Transducing, Apoptosis Regulatory Proteins, Death-Associated Protein Kinases
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