Cited by 1,042Mitochondrial Function and PathologyCell death mechanisms and regulationAutophagy in Disease and Therapy

The DOI matches its Crossref record; 49 of the 49 references it cites were found in a registry or an index.

Roles of the Mammalian Mitochondrial Fission and Fusion Mediators Fis1, Drp1, and Opa1 in Apoptosis

Open access

Lee, Yang-ja, Jeong, Seon-Yong, Karbowski, Mariusz, Smith, Carolyn L., Youle, Richard J.·2004·Molecular Biology of the Cell

DOI 10.1091/mbc.e04-04-0294PMC PMC524759

Open this paper in CoChat — free account

Abstract

During apoptosis, the mitochondrial network fragments. Using short hairpin RNAs for RNA interference, we manipulated the expression levels of the proteins hFis1, Drp1, and Opa1 that are involved in mitochondrial fission and fusion in mammalian cells, and we characterized their functions in mitochondrial morphology and apoptosis. Down-regulation of hFis1 powerfully inhibits cell death to an extent significantly greater than down-regulation of Drp1 and at a stage of apoptosis distinct from that induced by Drp1 inhibition. Cells depleted of Opa1 are extremely sensitive to exogenous apoptosis induction, and some die spontaneously by a process that requires hFis1 expression. Wild-type Opa1 may function normally as an antiapoptotic protein, keeping spontaneous apoptosis in check. However, if hFis1 is down-regulated, cells do not require Opa1 to prevent apoptosis, suggesting that Opa1 may be normally counteracting the proapoptotic action of hFis1. We also demonstrate in this study that mitochondrial fragmentation per se does not result in apoptosis. However, we provide further evidence that multiple components of the mitochondrial morphogenesis machinery can positively and negatively regulate apoptosis.

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

Crossref · 10.1091/mbc.e04-04-0294

Cites

49 of 49 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

The 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
Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development
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
Dynamin-related Protein Drp1 Is Required for Mitochondrial Division in Mammalian Cells
Smirnova, E., Griparić, L., Shurland, D., & van der Bliek, A. M. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.8.2245 · Cited by 1,938
Movement of Bax from the Cytosol to Mitochondria during Apoptosis
Wolter, K. G., Hsu, Y., Smith, C. L., Nechushtan, A., Xi, X., & Youle, R. J. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.139.5.1281 · Cited by 1,809
The Role of Dynamin-Related Protein 1, a Mediator of Mitochondrial Fission, in Apoptosis
Frank, S., Gaume, B., Bergmann-Leitner, E. S., Leitner, W. W., Robert, E. G., Catez, F., Smith, C. L., & Youle, R. J. (2001) · Developmental Cell · doi:10.1016/s1534-5807(01)00055-7 · Cited by 1,755
Short hairpin RNAs (shRNAs) induce sequence-specific silencing in mammalian cellsPreprint
Paddison, P. J., Caudy, A. A., Bernstein, E., Hannon, G. J., & Conklin, D. S. (2002) · Genes & Development · doi:10.1101/gad.981002 · Cited by 1,571
Nuclear gene OPA1, encoding a mitochondrial dynamin-related protein, is mutated in dominant optic atrophy
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
OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28
Alexander, 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
Bid-induced Conformational Change of Bax Is Responsible for Mitochondrial Cytochrome c Release during Apoptosis
Desagher, S., Osen‐Sand, A., Nichols, A. C., Eskes, R., Montessuit, S., Lauper, S., Maundrell, K., Antonsson, B. E., & Martinou, J. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.144.5.891 · Cited by 1,260
Loss of OPA1 Perturbates the Mitochondrial Inner Membrane Structure and Integrity, Leading to Cytochrome c Release and Apoptosis
Olichon, A., Baricault, L., Gas, N., Guillou, E., Valette, A., Belenguer, P., & Lenaers, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200677200 · Cited by 1,168

Flagged first, then by citations

Show all 49 references

Sorted by citations

Items 301–400 of 998

Mitochondrial fission and fusion in secondary brain damage after CNS insults
Balog, J., Mehta, S. L., & Vemuganti, R. (2016) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x16671528 · Cited by 110
DNA-PKcs interacts with and phosphorylates Fis1 to induce mitochondrial fragmentation in tubular cells during acute kidney injury
Wang, S., Zhu, H., Li, R., Mui, D., Toan, S., Chang, X., & Zhou, H. (2022) · Science Signaling · doi:10.1126/scisignal.abh1121 · Cited by 110
Inhibition of mitochondrial fission favours mutant over wild-type mitochondrial DNA
Malena, A., Loro, E., Di Re, M., Holt, I. J., & Vergani, L. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp281 · Cited by 107
p53 Is Required for Cisplatin-induced Processing of the Mitochondrial Fusion Protein L-Opa1 That Is Mediated by the Mitochondrial Metallopeptidase Oma1 in Gynecologic Cancers
Kong, B., Wang, Q., Fung, E., Xue, K., & Tsang, B. K. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.594812 · Cited by 108
The role of SIRT3-mediated mitochondrial homeostasis in osteoarthritis
He, Y., Wu, Z., Xu, L., Xu, K., Chen, Z., Ran, J., & Wu, L. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03497-9 · Cited by 106
Dynamin-related Protein 1 Inhibition Mitigates Bisphenol A-mediated Alterations in Mitochondrial Dynamics and Neural Stem Cell Proliferation and Differentiation
Agarwal, S., Yadav, A., Tiwari, S. K., Seth, B., Chauhan, L. K. S., Khare, P., Ray, R. S., & Chaturvedi, R. K. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.709493 · Cited by 109
Drp1 Loss-of-function Reduces Cardiomyocyte Oxygen Dependence Protecting the Heart From Ischemia-reperfusion Injury
Zepeda, R. J., Kuzmicic, J., Parra, V., Troncoso, R., Pennanen, C., Riquelme, J. A., Pedrozo, Z., Chiong, M., Sánchez, G., & Lavandero, S. (2014) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0000000000000071 · Cited by 106
The MAMs Structure and Its Role in Cell Death
Wang, N., Wang, C., Zhao, H., He, Y., Lan, B., Sun, L., & Gao, Y. (2021) · Cells · doi:10.3390/cells10030657 · Cited by 110
Mitochondrial Dynamics in Alzheimerʼs Disease
Bonda, D., Wang, X., Perry, G. L., Smith, M. A., & Zhu, X. (2010) · Drugs & Aging · doi:10.2165/11532140-000000000-00000 · Cited by 106
Drp1 levels constitutively regulate mitochondrial dynamics and cell survival in cortical neurons
Uo, T., Dworzak, J., Kinoshita, C., Inman, D. M., Kinoshita, Y., Horner, P. J., & Morrison, R. S. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.05.010 · Cited by 106
Structure and Function of Mitochondria‐Associated Endoplasmic Reticulum Membranes (MAMs) and Their Role in Cardiovascular Diseases
Luan, Y., Luan, Y., Yuan, R., Feng, Q., Chen, X., & Yang, Y. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/4578809 · Cited by 115
Role of apoptotic and necrotic cell death under physiologic conditions
Han, S. I., Kim, Y.-S., & Kim, T. (2008) · BMB Reports · doi:10.5483/bmbrep.2008.41.1.001 · Cited by 106
Cyclin-dependent kinase 5 is an upstream regulator of mitochondrial fission during neuronal apoptosis
Meuer, K., Suppanz, I., Lingor, P., Planchamp, V., Göricke, B., Fichtner, L., Braus, G. H., Dietz, G. P. H., Jakobs, S., Bähr, M., et al. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402087 · Cited by 105
Optic atrophy 1 mediates mitochondria remodeling and dopaminergic neurodegeneration linked to complex I deficiency
Ramonet, D., Perier, C., Recasens, A., Dehay, B., Bové, J., Costa, V., Scorrano, L., & Vila, M. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.95 · Cited by 108
Drp1 Mediates Caspase-Independent Type III Cell Death in Normal and Leukemic Cells
Bras, M., Yuste, V. J., Roué, G., Barbier, S., Sancho, P., Virely, C., Rubio, M., Baudet, S., Esquerda, J. E., Merle‐Béral, H., et al. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02116-06 · Cited by 103
The emerging role of skeletal muscle oxidative metabolism as a biological target and cellular regulator of cancer-induced muscle wasting
Carson, J. A., Hardee, J. P., & VanderVeen, B. N. (2015) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2015.11.005 · Cited by 109
Piceatannol Enhances Cisplatin Sensitivity in Ovarian Cancer via Modulation of p53, X-linked Inhibitor of Apoptosis Protein (XIAP), and Mitochondrial Fission
Farrand, L., Byun, S., Kim, J. Y., Im-Aram, A., Lee, J. H., Lim, S., Lee, K. W., Suh, J., Lee, H. J., & Tsang, B. K. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.487686 · Cited by 103
Mitochondrial membrane dynamics, cristae remodelling and apoptosis
Heath-Engel, H. M., & Shore, G. C. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.02.006 · Cited by 104
Regulation of mitochondrial dynamics: convergences and divergences between yeast and vertebrates
Zhao, J., Lendahl, U., & Nistér, M. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1066-6 · Cited by 105
Mitochondria in heart failure: the emerging role of mitochondrial dynamics
Marín-García, J., Akhmedov, A. T., & Moe, G. W. P. L. (2012) · Heart Failure Reviews · doi:10.1007/s10741-012-9330-2 · Cited by 105
Glucocorticoid impairs mitochondrial quality control in neurons
Choi, G. E., & Han, H. J. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105301 · Cited by 95
Small Molecule Inhibitors of Mitochondrial Division: Tools that Translate Basic Biological Research into Medicine
Lackner, L. L., & Nunnari, J. M. (2010) · Chemistry & Biology · doi:10.1016/j.chembiol.2010.05.016 · Cited by 101
Organelle plasticity and interactions in cholesterol transport and steroid biosynthesis
Issop, L., Rone, M. B., & Papadopoulos, V. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2012.12.003 · Cited by 103
Role of Dynamin-Related Protein 1 (Drp1)-Mediated Mitochondrial Fission in Oxygen Sensing and Constriction of the Ductus Arteriosus
Hong, Z., Kutty, S., Tóth, P. T., Marsboom, G., Hammel, J. M., Chamberlain, C., Ryan, J. J., Zhang, H. J., Sharp, W. W., Morrow, E., et al. (2013) · Circulation Research · doi:10.1161/circresaha.111.300285 · Cited by 100
Drp1-associated mitochondrial dysfunction and mitochondrial autophagy: a novel mechanism in triptolide-induced hepatotoxicity
Hasnat, M., Yuan, Z., Naveed, M., Asifullah, K., Raza, F., Xu, D., Ullah, A., Sun, L., Zhang, L., & Jiang, Z. (2018) · Cell Biology and Toxicology · doi:10.1007/s10565-018-9447-8 · Cited by 100
Mitochondrial division: molecular machinery and physiological functions
Kageyama, Y., Zhang, Z., & Sesaki, H. (2011) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2011.04.009 · Cited by 101
Heart Failure and Mitochondrial Dysfunction
Knowlton, A. A., Chen, L., & Malik, Z. A. (2013) · Journal of Cardiovascular Pharmacology · doi:10.1097/01.fjc.0000432861.55968.a6 · Cited by 100
Aurora kinase A localises to mitochondria to control organelle dynamics and energy production
Bertolin, G., Bulteau, A., Alves‐Guerra, M., Burel, A., Lavault, M.-T., Gavard, O., Bras, S. L., Gagné, J., Poirier, G. G., Borgne, R. L., et al. (2018) · eLife · doi:10.7554/elife.38111 · Cited by 98
Memantine Blocks Mitochondrial OPA1 and Cytochrome c Release and Subsequent Apoptotic Cell Death in Glaucomatous Retina
Ju, W., Keun-young Kim, A., Angert, M., Duong‐Polk, K., Lindsey, J. D., Ellisman, M. H., & Weinreb, R. N. (2009) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.08-2499 · Cited by 98
Menadione-Induced DNA Damage Leads to Mitochondrial Dysfunction and Fragmentation During Rosette Formation in Fuchs Endothelial Corneal Dystrophy
Halilovic, A., Schmedt, T., Benischke, A., Hamill, C. E., Chen, Y., Santos, J. H., & Jurkunas, U. V. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6532 · Cited by 96
Modulation of mitochondrial functions by the indirect antioxidant sulforaphane: A seemingly contradictory dual role and an integrative hypothesis
Negrette-Guzmán, M., Huerta‐Yépez, S., Tapia, E., & Pedraza‐Chaverrí, J. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.08.182 · Cited by 95
Mitochondrial Protein Quality Control: The Mechanisms Guarding Mitochondrial Health
Bohovych, I., Chan, S. S. L., & Khalimonchuk, O. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6199 · Cited by 98
Resveratrol Induces Cancer Cell Apoptosis through MiR-326/PKM2-Mediated ER Stress and Mitochondrial Fission
Wu, H., Wang, Y., Wu, C., Yang, P., Li, H., & Li, Z. (2016) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.6b04549 · Cited by 96
Neuroprotection by estrogen in the brain: the mitochondrial compartment as presumed therapeutic target
Arnold, S., & Beyer, C. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06133.x · Cited by 97
Opening the doors to cytochrome c: Changes in mitochondrial shape and apoptosis
Scorrano, L. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.04.016 · Cited by 96
OPA1 functionally interacts with MIC60 but is dispensable for crista junction formation
Barrera, M., Koob, S., Dikov, D., Vogel, F., & Reichert, A. S. (2016) · FEBS Letters · doi:10.1002/1873-3468.12384 · Cited by 94
Viruses activate a genetically conserved cell death pathway in a unicellular organism
Ivanovska, I., & Hardwick, J. M. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200503069 · Cited by 95
Mechanistic perspective of mitochondrial fusion: Tubulation vs. fragmentation
Escobar‐Henriques, M., & den Brave, F. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.07.016 · Cited by 100
Novel regulatory roles of Mff and Drp1 in E3 ubiquitin ligase MARCH5–dependent degradation of MiD49 and Mcl1 and control of mitochondrial dynamics
Cherok, E., Xu, S., Li, S., Das, S., Meltzer, W. A., Zalzman, M., Wang, C., & Karbowski, M. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-04-0208 · Cited by 94
Genistein Modulates Proliferation and Mitochondrial Functionality in Breast Cancer Cells Depending on ERalpha/ERbeta Ratio
Pons, D. G., Nadal‐Serrano, M., Blanquer-Rosselló, M. D. M., Sastre‐Serra, J., Oliver, J., & Roca, P. (2013) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24737 · Cited by 93
The mitochondria–endoplasmic reticulum contact sites: a signalling platform for cell death
Prudent, J., & McBride, H. M. (2017) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2017.03.007 · Cited by 94
Ultrastructural mitochondrial pathology in human astrocytic tumors: potentials implications pro-therapeutics strategies
Arismendi-Morillo, G., & Castellano-Ramírez, A. (2007) · Journal of Electron Microscopy · doi:10.1093/jmicro/dfm038 · Cited by 93
Bax Activation Initiates the Assembly of a Multimeric Catalyst that Facilitates Bax Pore Formation in Mitochondrial Outer Membranes
Kushnareva, Y., Andreyev, A. Y., Kuwana, T., & Newmeyer, D. D. (2012) · PLoS Biology · doi:10.1371/journal.pbio.1001394 · Cited by 94
Dynamin-Related Protein 1 at the Crossroads of Cancer
Lima, A. R., Santos, L., Correia, M., Soares, P., Sobrinho-Simões, M. A., Melo, M., & Máximo, V. (2018) · Genes · doi:10.3390/genes9020115 · Cited by 96
Mitochondrial Fusion, Fission, and Mitophagy in Cardiac Diseases: Challenges and Therapeutic Opportunities
Scheffer, D. D. L., Garcia, A. A., Lee, L., Mochly‐Rosen, D., & Ferreira, J. C. B. (2022) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0145 · Cited by 96
Larger than life: Mitochondria and the Bcl-2 family
Skommer, J., Włodkowic, D., & Deptała, A. (2006) · Leukemia Research · doi:10.1016/j.leukres.2006.06.027 · Cited by 94
Expression of mitochondrial fusion–fission proteins during post-infarction remodeling: the effect of NHE-1 inhibition
Javadov, S. A., Rajapurohitam, V., Kilić, A., Hunter, J. C., Zeidan, A., Faruq, N. S., Escobales, N., & Karmazyn, M. (2010) · Basic Research in Cardiology · doi:10.1007/s00395-010-0122-3 · Cited by 93
The HIV Protein gp120 Alters Mitochondrial Dynamics in Neurons
Avdoshina, V., Fields, J. A., Castellano, P., Dedoni, S., Palchik, G. A., Trejo, M., Adame, A., Rockenstein, E. M., Eugenín, E. A., Masliah, E., et al. (2016) · Neurotoxicity Research · doi:10.1007/s12640-016-9608-6 · Cited by 91
Involvement of mitochondrial aggregation in arsenic trioxide (As2O3)‐induced apoptosis in human glioblastoma cells
Haga, N., Fujita, N., & Tsuruo, T. (2005) · Cancer Science · doi:10.1111/j.1349-7006.2005.00114.x · Cited by 91
The Role of HSP70 and Its Co-chaperones in Protein Misfolding, Aggregation and Disease
Duncan, E. J., Cheetham, M. E., Chapple, J. P., & van der Spuy, J. (2014) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-319-11731-7_12 · Cited by 96
On the mechanism underlying ethanol-induced mitochondrial dynamic disruption and autophagy response
Bonet‐Ponce, L., Sáez-Atiénzar, S., da Casa, C., Flores‐Bellver, M., Barcia, J. M., Sancho-Pellúz, J., Romero, F. J., Jordán, J., & Galindo, M. F. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.03.006 · Cited by 90
The pathogenetic role of β-cell mitochondria in type 2 diabetes
Fex, M., Nicholas, L. M., Vishnu, N., Medina, A., Sharoyko, V. V., Nicholls, D. G., Spégel, P., & Mulder, H. (2018) · Journal of Endocrinology · doi:10.1530/joe-17-0367 · Cited by 93
Structural implications of mitochondrial dynamics
Bereiter‐Hahn, J., Vöth, M., Mai, S., & Jendrach, M. (2008) · Biotechnology Journal · doi:10.1002/biot.200800024 · Cited by 92
Genome-wide association studies in Asians confirm the involvement of ATOH7 and TGFBR3, and further identify CARD10 as a novel locus influencing optic disc area
Khor, C. C., Ramdas, W. D., Vithana, E. N., Cornes, B. K., Sim, X., Tay, W.-T., Saw, S., Zheng, Y., Lavanya, R., Wu, R., et al. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr060 · Cited by 89
The role of the mitochondria and the endoplasmic reticulum contact sites in the development of the immune responses
Martinvalet, D. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0237-7 · Cited by 94
Instability of the Mitofusin Fzo1 Regulates Mitochondrial Morphology during the Mating Response of the Yeast Saccharomyces cerevisiae
Neutzner, A., & Youle, R. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500807200 · Cited by 89
Ketamine Induces Toxicity in Human Neurons Differentiated from Embryonic Stem Cells via Mitochondrial Apoptosis Pathway
Bosnjak, Z. J., Yan, Y., Canfield, S. G., Muravyeva, M., Kikuchi, C., Wells, C. W., Corbett, J. A., & Bai, X. (2012) · Current Drug Safety · doi:10.2174/157488612802715663 · Cited by 88
miR-483-5p determines mitochondrial fission and cisplatin sensitivity in tongue squamous cell carcinoma by targeting FIS1
Fan, S., Chen, W.-X., Lv, X., Tang, Q.-L., Sun, L., Liu, B., Zhong, J., Lin, Z., Wang, Y., Li, Q., et al. (2015) · Cancer Letters · doi:10.1016/j.canlet.2015.03.045 · Cited by 87
Regulation of autophagy by mitochondrial phospholipids in health and diseases
Hsu, P., & Shi, Y. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.08.003 · Cited by 86
Numb Depletion Promotes Drp1-Mediated Mitochondrial Fission and Exacerbates Mitochondrial Fragmentation and Dysfunction in Acute Kidney Injury
Liu, Z., Li, H., Su, J., Xu, S., Zhu, F., Ai, J., Hu, Z. M., Zhou, M., Tian, J., Su, Z., et al. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7432 · Cited by 81
Mitochondrial dynamics, cell death and the pathogenesis of Parkinson’s disease
Büeler, H. (2010) · APOPTOSIS · doi:10.1007/s10495-010-0465-0 · Cited by 87
Mitofusin 2 as a Driver That Controls Energy Metabolism and Insulin Signaling
Antonio Zorzano, A., Hernández‐Álvarez, M. I., Sebastián, D., & Muñoz, J. P. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6208 · Cited by 83
Structure–Activity Relationship Study of Vitamin K Derivatives Yields Highly Potent Neuroprotective Agents
Josey, B. J., Inks, E. S., Wen, X., & Chou, C. J. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm301485d · Cited by 84
Information from cochlear potentials and genetic mutations helps localize the lesion site in auditory neuropathy
Santarelli, R. (2010) · Genome Medicine · doi:10.1186/gm212 · Cited by 83
Mechanical ventilation triggers abnormal mitochondrial dynamics and morphology in the diaphragm
Picard, M. A., Azuelos, I., Jung, B., Giordano, C., Matecki, S., Hussain, S. N. A., White, K., Li, T., Liang, F., Benedetti, A., et al. (2015) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00873.2014 · Cited by 86
The role of Fis1p–Mdv1p interactions in mitochondrial fission complex assembly
Karren, M. A., Coonrod, E. M., Anderson, T. K., & Shaw, J. M. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200506158 · Cited by 84
Mitochondrial dynamics altered by oxidative stress in cancer
Kim, B., & Song, Y. S. (2016) · Free Radical Research · doi:10.1080/10715762.2016.1210141 · Cited by 88
Toxic effect of serial perfluorosulfonic and perfluorocarboxylic acids on the membrane system of a freshwater alga measured by flow cytometry
Liu, W., Chen, S., Quan, X., & Jin, Y. (2008) · Environmental Toxicology and Chemistry · doi:10.1897/07-459.1 · Cited by 84
Multi-Target Drug Candidates for Multifactorial Alzheimer’s Disease: AChE and NMDAR as Molecular Targets
Uddin, M. S., Al Mamun, A., Kabir, M. T., Ashraf, G. M., Bin-Jumah, M. N., & Abdel-Daim, M. M. (2021) · Molecular Neurobiology · doi:10.1007/s12035-020-02116-9 · Cited by 86
Perturbations in the apoptotic pathway and mitochondrial network dynamics in peripheral blood mononuclear cells from bipolar disorder patients
Scaini, G., Fries, G. R., Valvassori, S. S., Zeni, C., Zunta‐Soares, G. B., Berk, M., Soares, J. C., & Quevedo, J. (2017) · Translational Psychiatry · doi:10.1038/tp.2017.83 · Cited by 88
Cyclosporine A-induced apoptosis in renal tubular cells is related to oxidative damage and mitochondrial fission
de Arriba, G., Calvino, M., Martínez, S. B., & Parra, T. (2013) · Toxicology Letters · doi:10.1016/j.toxlet.2013.01.007 · Cited by 85
Mitochondria on Guard: Role of Mitochondrial Fusion and Fission in the Regulation of Apoptosis
Karbowski, M. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-6706-0_8 · Cited by 83
Increased Drp1-Mediated Mitochondrial Fission Promotes Proliferation and Collagen Production by Right Ventricular Fibroblasts in Experimental Pulmonary Arterial Hypertension
Tian, L., Potus, F., Wu, D., Dasgupta, A., Chen, K., Mewburn, J. D., Lima, P., & Archer, S. L. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00828 · Cited by 82
Axin-2 knockdown promote mitochondrial biogenesis and dopaminergic neurogenesis by regulating Wnt/β-catenin signaling in rat model of Parkinson's disease
Singh, S., Mishra, A., Mohanbhai, S. J., Tiwari, V., Chaturvedi, R. K., Khurana, S., & Shukla, S. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.08.033 · Cited by 82
Role of inner mitochondrial protein OPA1 in mitochondrial dysfunction by tobacco smoking and in the pathogenesis of COPD
Maremanda, K. P., Sundar, I. K., & Rahman, I. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102055 · Cited by 82
Abnormal Mitochondrial Dynamics—A Novel Therapeutic Target for Alzheimer's Disease?
Su, B., Wang, X., Bonda, D., Perry, G. L., Smith, M. A., & Zhu, X. (2010) · Molecular Neurobiology · doi:10.1007/s12035-009-8095-7 · Cited by 85
Differential temporal inhibition of mitochondrial fission by Mdivi-1 exerts effective cardioprotection in cardiac ischemia/reperfusion injury
Maneechote, C., Palee, S., Kerdphoo, S., Jaiwongkam, T., Chattipakorn, S. C., & Chattipakorn, N. (2018) · Clinical Science · doi:10.1042/cs20180510 · Cited by 83
Retracted
A mitochondrial delicacy: dynamin-related protein 1 and mitochondrial dynamics
Breitzig, M., Alleyn, M. D., Lockey, R. F., & Kolliputi, N. (2018) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00042.2018 · Cited by 81
Mitochondrial dynamics involves molecular and mechanical events in motility, fusion and fission
Green, A., Hossain, T., & Eckmann, D. M. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.1010232 · Cited by 86
Two Close, Too Close
Dorn, G. W., & Scorrano, L. (2010) · Circulation Research · doi:10.1161/circresaha.110.225714 · Cited by 82
The Alterations in Mitochondrial Dynamics Following Cerebral Ischemia/Reperfusion Injury
Vongsfak, J., Pratchayasakul, W., Apaijai, N., Vaniyapong, T., Chattipakorn, N., & Chattipakorn, S. C. (2021) · Antioxidants · doi:10.3390/antiox10091384 · Cited by 82
Mitochondrial Fragmentation Is Involved in Methamphetamine-Induced Cell Death in Rat Hippocampal Neural Progenitor Cells
Tian, C., Murrin, L. C., & Zheng, J. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005546 · Cited by 80
Effects of Chlorpyrifos and Chlorpyrifos-Oxon on the Dynamics and Movement of Mitochondria in Rat Cortical Neurons
Risher, M., Adam, B.-L., Lambert, N. A., & Terry, A. V. (2011) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.111.184762 · Cited by 80
Mitochondrial Dynamics and Parkinson's Disease: Focus on Parkin
Lim, K.-L., Ng, X.-H., Grace, L. G.-Y., & Yao, T.-P. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4105 · Cited by 64
Implications of mitochondrial dynamics on neurodegeneration and on hypothalamic dysfunction
Antonio Zorzano, A., & Claret, M. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00101 · Cited by 83
Mitochondrial Optic Neuropathies: How Two Genomes may Kill the Same Cell Type?
Carelli, V., Morgia, C. L., Iommarini, L., Carroccia, R., Mattiazzi, M., Sangiorgi, S., Farne', S., Maresca, A., Foscarini, B., Lanzi, L., et al. (2007) · Bioscience Reports · doi:10.1007/s10540-007-9045-0 · Cited by 79
DRP1-dependent apoptotic mitochondrial fission occurs independently of BAX, BAK and APAF1 to amplify cell death by BID and oxidative stress
Oettinghaus, B., D’Alonzo, D., Barbieri, E., Restelli, L. M., Savoia, C., Licci, M., Tolnay, M., Frank, S., & Scorrano, L. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.03.016 · Cited by 81
PIM kinases alter mitochondrial dynamics and chemosensitivity in lung cancer
Chauhan, S. S., Toth, R. K., Jensen, C. C., Casillas, A. L., Kashatus, D. F., & Warfel, N. A. (2020) · Oncogene · doi:10.1038/s41388-020-1168-9 · Cited by 78
SENP5, a SUMO isopeptidase, induces apoptosis and cardiomyopathy
Kim, E. Y., Zhang, Y., Beketaev, I., Segura, A. M., Yu, W., Xi, Y. T., Chang, J., & Wang, J. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.08.003 · Cited by 81
Baicalein resensitizes tamoxifen‐resistant breast cancer cells by reducing aerobic glycolysis and reversing mitochondrial dysfunction via inhibition of hypoxia‐inducible factor‐1α
Chen, Y., Zhang, J., Zhang, M., Song, Y., Zhang, Y., Fan, S., Ren, S., Fu, L., Zhang, N., Hui, H., et al. (2021) · Clinical and Translational Medicine · doi:10.1002/ctm2.577 · Cited by 82
Identification of a Novel Protein MICS1 that is Involved in Maintenance of Mitochondrial Morphology and Apoptotic Release of Cytochrome c
Oka, T., Sayano, T., Tamai, S., Yokota, S., Kato, H., Fujii, G., & Mihara, K. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-12-1205 · Cited by 76
Mitochondrial Quality Control: Role in Cardiac Models of Lethal Ischemia-Reperfusion Injury
Kulek, A. R., Anzell, A. R., Wider, J. M., Sanderson, T. H., & Przyklenk, K. (2020) · Cells · doi:10.3390/cells9010214 · Cited by 78
New insights into mitochondrial structure during cell death
Perkins, G. A., Bossy‐Wetzel, E., & Ellisman, M. H. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.05.021 · Cited by 79
Targeting metabolism in cellular senescence, a role for intervention
Nacarelli, T., & Sell, C. (2016) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2016.08.049 · Cited by 79
Organellar vs cellular control of mitochondrial dynamics
Hyde, B. B., Twig, G., & Shirihai, O. S. (2010) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2010.01.003 · Cited by 81
ASS234, As a New Multi-Target Directed Propargylamine for Alzheimer's Disease Therapy
Marco, J. L., Unzeta, M., Bolea, I., Esteban, G., Ramsay, R. R., Romero, A., Martínez‐Murillo, R., Carreiras, M. C., & Ismaïli, L. (2016) · Frontiers in Neuroscience · doi:10.3389/fnins.2016.00294 · Cited by 75
Mitochondria: Insights into Crucial Features to Overcome Cancer Chemoresistance
Genovese, I., Carinci, M., Modesti, L., Aguiari, G., Pinton, P., & Giorgi, C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094770 · Cited by 77
Too much death can kill you: inhibiting intrinsic apoptosis to treat disease
Li, K., van Delft, M. F., & Dewson, G. (2021) · The EMBO Journal · doi:10.15252/embj.2020107341 · Cited by 78
DRP1, fission and apoptosis
Wang, N., Wang, X. J., Lan, B., Gao, Y., & Cai, Y. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02458-0 · Cited by 84
New components of the necroptotic pathway
Zhou, Z., Han, V. K. M., & Han, J. (2012) · Protein & Cell · doi:10.1007/s13238-012-2083-9 · Cited by 75

Authors: Lee, Y.-J., Jeong, S.-Y., Karbowski, M., Smith, C. L., & Youle, R. J.
Affiliations: National Institutes of Health (US)
ORCID: Jeong, Seon-Yong
Karbowski, Mariusz
Smith, Carolyn L.
Youle, Richard J.
Venue: Molecular Biology of the Cell
Publisher: American Society for Cell Biology (ASCB)
Published: 2004-11
Volume: 15
Issue: 11
Pages: 5001-5011
ISSN: 1059-1524 (ISSN-L)
1939-4586
DOI: 10.1091/mbc.e04-04-0294
PMC: PMC524759
OpenAlex: W1970248089
Cited by: 1,042
References: 49
Citations by year: 2026: 15 · 2025: 20 · 2024: 41 · 2023: 39 · 2022: 43 · 2021: 50 · 2020: 52 · 2019: 36 · 2018: 54 · 2017: 40 · 2016: 72 · 2015: 55 · 2014: 47 · 2013: 50 · 2012: 74
FWCI: 14.83
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)
AJOU Open Repository (Ajou University) (submittedVersion)
Funders: National Institutes of Health
National Heart, Lung, and Blood Institute
National Institute of Neurological Disorders and Stroke
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: apoptosis, mitochondrial fission, mitochondrial fusion, Fis1, Drp1, OPA1, mitochondrial morphology, mitochondrial fragmentation, anti-apoptotic proteins, spontaneous apoptosis, mitochondrial morphogenesis
MeSH terms: HeLa Cells, Humans, Immunohistochemistry, Membrane Proteins, Microtubule-Associated Proteins, Mitochondria, Poly(ADP-ribose) Polymerases, RNA, Subcellular Fractions, Time Factors, Immunoblotting, Down-Regulation, Apoptosis, Microscopy, Confocal, GTP Phosphohydrolases, Mitochondrial Proteins, Dynamins, RNA Interference

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

Roles of the Mammalian Mitochondrial Fission and Fusion Mediators Fis1, Drp1, and Opa1 in Apoptosis

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks