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

Show all 49 references

Sorted by citations

Items 501–600 of 998

Tumor-selective mitochondrial network collapse induced by atmospheric gas plasma-activated medium
Saito, K., Asai, T., Fujiwara, K., Sahara, J., Koguchi, H., Fukuda, N., Suzuki‐Karasaki, M., Soma, M., & Suzuki‐Karasaki, Y. (2016) · Oncotarget · doi:10.18632/oncotarget.7889 · Cited by 55
Zn2+-transporters ZIP7 and ZnT7 play important role in progression of cardiac dysfunction via affecting sarco(endo)plasmic reticulum-mitochondria coupling in hyperglycemic cardiomyocytes
Tuncay, E., Bitirim, C. V., Olğar, Y., Durak, A. T., Rutter, G. A., & Turan, B. (2018) · Mitochondrion · doi:10.1016/j.mito.2017.12.011 · Cited by 55
Novel insights into the role of mitochondrial fusion and fission in cardiomyocyte apoptosis induced by ischemia/reperfusion
Li, Y., & Liu, X. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.26522 · Cited by 56
Mitochondria focused neurotherapeutics for spinal cord injury
Rabchevsky, A. G., Michael, F. M., & Patel, S. P. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113332 · Cited by 56
Glutamate receptor activation triggers OPA1 release and induces apoptotic cell death in ischemic rat retina.
Ju, W., Lindsey, J. D., Angert, M., Patel, A., & Weinreb, R. N. (2008) · PubMed Central · Cited by 54
Protein tyrosine phosphatase interacting protein 51 (PTPIP51) is a novel mitochondria protein with an N-terminal mitochondrial targeting sequence and induces apoptosis
Lv, B., Yu, C. F., Chen, Y. Y., Lu, Y., Guo, J., Song, Q. S., L., D., Shi, T., & Wang, L. (2006) · APOPTOSIS · doi:10.1007/s10495-006-8882-9 · Cited by 55
Mitochondria in the Pulmonary Vasculature in Health and Disease: Oxygen‐Sensing, Metabolism, and Dynamics
Dasgupta, A., Wu, D., Tian, L., Xiong, P. Y., Dunham‐Snary, K. J., Chen, K., Alizadeh, E., Motamed, M., Potus, F., Hindmarch, C. C. T., et al. (2020) · Comprehensive physiology · doi:10.1002/cphy.c190027 · Cited by 64
The role of mitochondrial dysfunction in Alzheimer's disease: A potential pathway to treatment
Reiss, A. B., Ahmed, S., Dayaramani, C., Glass, A. D., Gomolin, I. H., Pinkhasov, A., Stecker, M. M., Wısnıewskı, T., & Leon, J. D. (2022) · Experimental Gerontology · doi:10.1016/j.exger.2022.111828 · Cited by 55
Transient Contraction of Mitochondria Induces Depolarization through the Inner Membrane Dynamin OPA1 Protein
Lee, H., & Yoon, Y. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.533299 · Cited by 51
Mitochondrial fission determines cisplatin sensitivity in tongue squamous cell carcinoma through the BRCA1-miR-593-5p–MFF axis
Fan, S., Liu, B., Sun, L., Lv, X., Lin, Z., Chen, W., Chen, W., Tang, Q.-L., Wang, Y., Su, Y., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.3659 · Cited by 54
Mitochondria-dependent apoptosis in triptolide-induced hepatotoxicity is associated with the Drp1 activation
Hasnat, M., Yuan, Z., Ullah, A., Naveed, M., Raza, F., Baig, M. M. F. A., Asifullah, K., Xu, D., Su, Y., Sun, L., et al. (2019) · Toxicology Mechanisms and Methods · doi:10.1080/15376516.2019.1669247 · Cited by 54
Astragaloside IV Derivative (LS-102) Alleviated Myocardial Ischemia Reperfusion Injury by Inhibiting Drp1Ser616 Phosphorylation-Mediated Mitochondrial Fission
Chen, L., Chen, X.-Y., Wang, Q.-L., Yang, S., Zhou, H., Ding, L., Qing, L., & Luo, P. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.01083 · Cited by 56
Molecular mechanisms of mitochondrial quality control
Li, W., Gui, Y., Guo, C., Huang, Y.-T., Liu, Y., Yu, X., Zhang, H., Wang, J., Liu, R., Mahaman, Y. A. R., et al. (2025) · Translational Neurodegeneration · doi:10.1186/s40035-025-00505-5 · Cited by 57
Cyclin C mediates stress-induced mitochondrial fission and apoptosis
Wang, K., Yan, R., Cooper, K. F., & Strich, R. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-08-1315 · Cited by 55
Stereoisomer-Specific Anticancer Activities of Ginsenoside Rg3 and Rh2 in HepG2 Cells: Disparity in Cytotoxicity and Autophagy-Inducing Effects Due to 20(S)-Epimers
Cheong, J. H., Kim, H., Hong, M. J., Yang, M. H., Kim, J. W., Yoo, H., Yang, H., Park, J. H., Sung, S. H., Kim, H. P., et al. (2015) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b14-00603 · Cited by 53
Dynamin-1–Like Protein Inhibition Drives Megamitochondria Formation as an Adaptive Response in Alcohol-Induced Hepatotoxicity
Palma, E., Ma, X., Riva, A., Iansante, V., Dhawan, A. K., Wang, S., Ni, H., Sesaki, H., Williams, R. L., Ding, W., et al. (2018) · American Journal Of Pathology · doi:10.1016/j.ajpath.2018.11.008 · Cited by 53
Human papillomavirus infection and expression of ATPase family AAA domain containing 3A, a novel anti-autophagy factor, in uterine cervical cancer
Chow, K. (2011) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2011.743 · Cited by 53
Mitochondrial dynamics and the innate antiviral immune response
Pourcelot, M., & Arnoult, D. (2014) · FEBS Journal · doi:10.1111/febs.12940 · Cited by 50
Oxidative stress by Helicobacter pylori causes apoptosis through mitochondrial pathway in gastric epithelial cells
Calvino-Fernández, M., Martínez, S. B., & Parra-Cid, T. (2008) · APOPTOSIS · doi:10.1007/s10495-008-0255-0 · Cited by 52
VEGF attenuates development from cardiac hypertrophy to heart failure after aortic stenosis through mitochondrial mediated apoptosis and cardiomyocyte proliferation
Xu, X., Xu, J., Xue, L., Cao, H. L., Liu, X., & Chen, Y. J. (2011) · Journal of Cardiothoracic Surgery · doi:10.1186/1749-8090-6-54 · Cited by 52
Toxoplasma gondii Infection Is Associated with Mitochondrial Dysfunction in-Vitro
Syn, G., Anderson, D. R., Blackwell, J. M., & Jamieson, S. E. (2017) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00512 · Cited by 52
The Interplay among PINK1/PARKIN/Dj-1 Network during Mitochondrial Quality Control in Cancer Biology: Protein Interaction Analysis
Salazar, C., Ruiz‐Hincapie, P., & Ruíz, L. M. (2018) · Cells · doi:10.3390/cells7100154 · Cited by 52
Melatonin Affects Mitochondrial Fission/Fusion Dynamics in the Diabetic Retina
Chang, J. Y.-A., Yu, F., Shi, L., Ko, M. L., & Ko, G. Y. ‐. (2019) · Journal of Diabetes Research · doi:10.1155/2019/8463125 · Cited by 55
Epigenetic modifications associated with pathophysiological effects of lead exposure
Khalid, M., & Abdollahi, M. R. (2019) · Journal of Environmental Science and Health Part C · doi:10.1080/10590501.2019.1640581 · Cited by 54
Programmed Cell Death in Fungi
Lu, B. C. (2006) · Springer eBooks · doi:10.1007/3-540-28135-5_9 · Cited by 51
Multi-Parametric Analysis and Modeling of Relationships between Mitochondrial Morphology and Apoptosis
Reis, Y., Bernardo-Faura, M., Richter, D., Wolf, T. A., Brors, B., Hamacher‐Brady, A., Eils, R., & Brady, N. R. (2012) · PLoS ONE · doi:10.1371/journal.pone.0028694 · Cited by 53
Role of mitochondrial fission and fusion in cardiomyocyte contractility
Givvimani, S., Pushpakumar, S. B., Metreveli, N. S., Veeranki, S., Kundu, S., & Tyagi, S. C. (2015) · International Journal of Cardiology · doi:10.1016/j.ijcard.2015.03.352 · Cited by 52
Mitochondrial Dynamics Imbalance: A Strategy for Promoting Viral Infection
Ren, Z., Zhang, X., Ding, T., Zhong, Z., Hu, H., Xu, Z., & Deng, J. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.01992 · Cited by 50
HtrA2/Omi Terminates Cytomegalovirus Infection and Is Controlled by the Viral Mitochondrial Inhibitor of Apoptosis (vMIA)
McCormick, A. L., Roback, L., & Mocarski, E. S. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.1000063 · Cited by 51
Mitochondrial division inhibitor-1 induces mitochondrial hyperfusion and sensitizes human cancer cells to TRAIL-induced apoptosis
Akita, M., Suzuki‐Karasaki, M., Fujiwara, K., Nakagawa, C., Soma, M., Yoshida, Y., Ochiai, T., Tokuhashi, Y., & Suzuki‐Karasaki, Y. (2014) · International Journal of Oncology · doi:10.3892/ijo.2014.2608 · Cited by 50
Mitochondrial Dynamics as a Therapeutic Target for Treating Cardiac Diseases
Ong, S., & Hausenloy, D. J. (2016) · Handbook of experimental pharmacology · doi:10.1007/164_2016_7 · Cited by 50
The mitochondrial inner membrane protein LETM1 modulates cristae organization through its LETM domain
Nakamura, S., Matsui, A., Akabane, S., Tamura, Y., Hatano, A., Miyano, Y., Omote, H., Kajikawa, M., Maenaka, K., Moriyama, Y., et al. (2020) · Communications Biology · doi:10.1038/s42003-020-0832-5 · Cited by 52
Mitochondria and early-life adversity
Zitkovsky, E. K., Daniels, T. E., & Tyrka, A. R. (2021) · Mitochondrion · doi:10.1016/j.mito.2021.01.005 · Cited by 53
hNOA1 Interacts with Complex I and DAP3 and Regulates Mitochondrial Respiration and Apoptosis
Tang, T., Zheng, B., Chen, S., Murphy, A. N., Kudlicka, K., Zhou, H., & Farquhar, M. G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807797200 · Cited by 48
Impaired parkin-mediated mitochondrial targeting to autophagosomes differentially contributes to tissue pathology in lysosomal storage diseases
de Pablo, R., Saide, A., Polishhuck, E. V., Nusco, E., Fraldi, A., & Ballabio, A. (2012) · Human Molecular Genetics · doi:10.1093/hmg/ddr610 · Cited by 50
Inhibition of mitochondrial fusion is an early and critical event in breast cancer cell apoptosis by dietary chemopreventative benzyl isothiocyanate
Sehrawat, A., Croix, C. M. S., Baty, C. J., Watkins, S. C., Tailor, D., Singh, R. P., & Singh, S. V. (2016) · Mitochondrion · doi:10.1016/j.mito.2016.06.006 · Cited by 50
Bcl-2 family proteins and mitochondrial fission/fusion dynamics
Autret, A., & Martin, S. J. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0286-x · Cited by 49
Mitochondrial dynamics in aging and disease
Bereiter-Hahn, J. (2014) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-394625-6.00004-0 · Cited by 48
Homeostatic Functions of BCL-2 Proteins beyond Apoptosis
Danial, N. N., Giménez-Cassina, A., & Tondera, D. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-6706-0_1 · Cited by 48
Melatonin attenuates the mitochondrial translocation of mitochondrial fission proteins and Bax, cytosolic calcium overload and cell death in methamphetamine-induced toxicity in neuroblastoma SH-SY5Y cells
Parameyong, A., Govitrapong, P., & Chetsawang, B. (2015) · Mitochondrion · doi:10.1016/j.mito.2015.07.004 · Cited by 48
Mitochondrial dysfunction is associated with a pro-apoptotic cellular environment in senescent cardiac muscle
Ljubicic, V., Menzies, K. J., & Hood, D. A. (2009) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2009.12.004 · Cited by 48
TNFα induces mitochondrial fragmentation and biogenesis in human airway smooth muscle
Delmotte, P. F., Mathieu, N. M., & Sieck, G. C. (2020) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00305.2020 · Cited by 50
THE ROLE OF MITOCHONDRIA IN THE DEVELOPMENT AND PROGRESSION OF LUNG CANCER
Roberts, E., & Craig, K. J. T. (2013) · Computational and Structural Biotechnology Journal · doi:10.5936/csbj.201303019 · Cited by 50
The novel conserved mitochondrial inner-membrane protein MTGM regulates mitochondrial morphology and cell proliferation
Zhao, J., Liu, T., Jin, S., Tomilin, N. V., Castro, J., Shupliakov, O., Lendahl, U., & Nistér, M. (2009) · Journal of Cell Science · doi:10.1242/jcs.038513 · Cited by 46
The Fruits of Paris polyphylla Inhibit Colorectal Cancer Cell Migration Induced by Fusobacterium nucleatum-Derived Extracellular Vesicles
Lin, L., Shi, Y.-C., Choong, C.-Y., & Tai, C. (2021) · Molecules · doi:10.3390/molecules26134081 · Cited by 48
The dynamic interplay between cardiac mitochondrial health and myocardial structural remodeling in metabolic heart disease, aging, and heart failure
Werbner, B., Tavakoli‐Rouzbehani, O. M., Fatahian, A. N., & Boudina, S. (2023) · The Journal of Cardiovascular Aging · doi:10.20517/jca.2022.42 · Cited by 44
Early Selective Vulnerability of Synapses and Synaptic Mitochondria in the Hippocampal CA1 Region of the Tg2576 Mouse Model of Alzheimer's Disease
Balietti, M., Giorgetti, B., Casoli, T., Solazzi, M., Tamagnini, F., Burattini, C., Aicardi, G., & Fattoretti, P. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-121711 · Cited by 50
Linking mitochondrial dynamics to mitochondrial protein quality control
Haroon, S., & Vermulst, M. (2016) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2016.04.004 · Cited by 46
Splitting up the powerhouse: structural insights into the mechanism of mitochondrial fission
Richter, V., Singh, A. P., Kvansakul, M., Ryan, M. T., & Osellame, L. D. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1950-y · Cited by 48
CED-9 and mitochondrial homeostasis inC. elegansmuscle
Tan, F. J., Husain, M., Manlandro, C. M., Koppenol-Raab, M., Fire, A. Z., & Hill, R. B. (2008) · Journal of Cell Science · doi:10.1242/jcs.032904 · Cited by 44
Mechanisms of Mitochondrial Malfunction in Alzheimer’s Disease: New Therapeutic Hope
Nabi, S. U., Khan, A., Siddiqui, E. M., Rehman, M. U., Alshahrani, S., Arafah, A. M., Mehan, S., Alsaffar, R. M., Alexiou, A. T., & Shen, B. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/4759963 · Cited by 51
Balance is the challenge – The impact of mitochondrial dynamics in Parkinson’s disease
Burbulla, L. F., Krebiehl, G., & Krüger, R. (2010) · European Journal of Clinical Investigation · doi:10.1111/j.1365-2362.2010.02354.x · Cited by 46
The Impact of Mitochondrial Fission-Stimulated ROS Production on Pro-Apoptotic Chemotherapy
Ježek, J., Cooper, K. F., & Strich, R. (2021) · Biology · doi:10.3390/biology10010033 · Cited by 47
Cell Biology of Mitochondrial Dynamics
Kiefel, B. R., Gilson, P. R., & Beech, P. L. (2006) · International review of cytology · doi:10.1016/s0074-7696(06)54004-5 · Cited by 44
Mitochondrial Fragmentation Leads to Intracellular Acidification inCaenorhabditis elegansand Mammalian Cells
Johnson, D., & Nehrke, K. W. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-10-0874 · Cited by 46
Apoptosis and aging in mitochondrial morphology mutants ofS. cerevisiae
Palermo, V., Falcone, C., & Mazzoni, C. (2007) · Folia Microbiologica · doi:10.1007/bf02932107 · Cited by 45
The role of the sirtuin family in cartilage and osteoarthritis: molecular mechanisms and therapeutic targets
Sun, K., Wu, Y., Zeng, Y., Xu, J., Wu, L., Li, M., & Shen, B. (2022) · Arthritis Research & Therapy · doi:10.1186/s13075-022-02983-8 · Cited by 45
Role of Mitochondrial Dysfunctions in Neurodegenerative Disorders: Advances in Mitochondrial Biology
Kathiresan, D. S., Balasubramani, R., Marudhachalam, K., Jaiswal, P., Ramesh, N., Suruthi, G. S., Moorthi, P. V., & Vijayan, M. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04469-x · Cited by 49
Human mitochondrial Fis1 links to cell cycle regulators at G2/M transition
Lee, S.-M., Park, Y., Kim, S., Nguyen, T. K. O., Yoo, Y., Chan, G. K. T., Sun, X., & Cho, H. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1428-8 · Cited by 46
DJ-1 promotes the proteasomal degradation of Fis1: implications of DJ-1 in neuronal protection
Zhang, Q., Wu, J., Wu, R., Ma, J., Du, G., Jiao, R., Tian, Y., Zheng, Z., & Yuan, Z. (2012) · Biochemical Journal · doi:10.1042/bj20120598 · Cited by 44
Time representation of mitochondrial morphology and function after acute spinal cord injury
Lv, G., Jia, Z., Li, G., Zhang, Z.-Y., Li, H.-T., Wang, J.-Q., & Fan, Z. (2016) · Neural Regeneration Research · doi:10.4103/1673-5374.175061 · Cited by 44
Mitochondrial fission protein 1 up-regulation ameliorates senescence-related endothelial dysfunction of human endothelial progenitor cells
Wang, H.-H., Wu, Y., Tseng, Y.-M., Su, C., Hsieh, C., & Yeh, H. (2019) · Angiogenesis · doi:10.1007/s10456-019-09680-2 · Cited by 47
Distinct effects of TRAIL on the mitochondrial network in human cancer cells and normal cells: role of plasma membrane depolarization
Suzuki‐Karasaki, Y., Fujiwara, K., Saito, K., Suzuki‐Karasaki, M., Ochiai, T., & Soma, M. (2015) · Oncotarget · doi:10.18632/oncotarget.4268 · Cited by 43
Inhibition of Drp1 by Mdivi-1 attenuates cerebral ischemic injury via inhibition of the mitochondria-dependent apoptotic pathway after cardiac arrest
Li, Y., Wang, P., Wei, J., Fan, R. Z., Zuo, Y., Shi, M., Wu, H., Zhou, M., Lin, J., Mei-yuan, W., et al. (2015) · Neuroscience · doi:10.1016/j.neuroscience.2015.10.020 · Cited by 43
Cell Cycle Regulators Guide Mitochondrial Activity in Radiation-Induced Adaptive Response
Alexandrou, A. T., & Li, J. J. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5684 · Cited by 42
Interaction between endoplasmic/sarcoplasmic reticulum stress (ER/SR stress), mitochondrial signaling and Ca2+ regulation in airway smooth muscle (ASM)
Delmotte, P. F., & Sieck, G. C. (2014) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/cjpp-2014-0361 · Cited by 43
The Interplay between Oncogenic Signaling Networks and Mitochondrial Dynamics
Nagdas, S., & Kashatus, D. F. (2017) · Antioxidants · doi:10.3390/antiox6020033 · Cited by 46
Microcystin-leucine-arginine induced neurotoxicity by initiating mitochondrial fission in hippocampal neurons
Zhang, C., Wang, J., Zhu, J., Chen, Y., & Han, X. (2019) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2019.134702 · Cited by 44
Mitochondria in Early Forebrain Development: From Neurulation to Mid-Corticogenesis
Fame, R. M., & Lehtinen, M. K. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.780207 · Cited by 47
Ovarian Cancer: A Landscape of Mitochondria with Emphasis on Mitochondrial Dynamics
Rasmo, D. D., Cormio, A., Cormio, G., & Signorile, A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24021224 · Cited by 44
Raft component GD3 associates with tubulin following CD95/Fas ligation
Sorice, M., Matarrese, P., Tinari, A., Giammarioli, A. M., Garofalo, T., Manganelli, V., Ciarlo, L., Gambardella, L., Maccari, G., Botta, M., et al. (2009) · The FASEB Journal · doi:10.1096/fj.08-128140 · Cited by 45
The role of Mitochondrial Fission Proteins in Mitochondrial Dynamics in Kidney Disease
Qin, L., & Xi, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232314725 · Cited by 47
Targeting mitochondrial dynamics proteins for the treatment of doxorubicin-induced cardiotoxicity
Chen, R., Niu, M., Hu, X., & He, Y. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1241225 · Cited by 43
Novel therapeutics for Alzheimer's disease: an update.
Bonda, D., Lee, H. P., Lee, H., Friedlich, A. L., Perry, G. L., Zhu, X., & Smith, M. A. (2010) · PubMed · Cited by 41
Ganglioside GD3 as a Raft Component in Cell Death Regulation
Sorice, M., Garofalo, T., Misasi, R., Manganelli, V., Vona, R., & Malorni, W. (2012) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/187152012800228670 · Cited by 42
Downregulation of Drp1, a fission regulator, is associated with human lung and colon cancers
Kim, Y. Y., Yun, S., & Yun, J. (2017) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmx137 · Cited by 45
OPA1 mutations and mitochondrial DNA damage: keeping the magic circle in shape
Zeviani, M. (2008) · Brain · doi:10.1093/brain/awm339 · Cited by 41
Remote Ischemic Conditioning Influences Mitochondrial Dynamics
Cellier, L., Tamareille, S., Kalakech, H., Guillou, S., Lenaers, G., Prunier, F., & Mirebeau‐Prunier, D. (2015) · Shock · doi:10.1097/shk.0000000000000500 · Cited by 41
The enigma of an interconnected mitochondrial reticulum: new insights into mitochondrial fusion
Mattie, S., Krols, M., & McBride, H. M. (2019) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2019.05.004 · Cited by 42
Fis1 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
The Regulatory Role of Mitochondrial MicroRNAs (MitomiRs) in Breast Cancer: Translational Implications Present and Future
Ortega, M. A., Fraile‐Μartinez, O., Guijarro, L. G., Casanova, C., Coca, S., Álvarez‐Mon, M., Buján, J., García‐Honduvilla, N., & Asúnsolo, Á. (2020) · Cancers · doi:10.3390/cancers12092443 · Cited by 41
Regulation of OPA1-mediated mitochondrial fusion by leucine zipper/EF-hand-containing transmembrane protein-1 plays a role in apoptosis
Piao, L., Li, Y., Kim, S. J., Sohn, K., Yang, K., Park, K. A., Byun, H. S., Won, M., Hong, J. H., Hur, G. M., et al. (2009) · Cellular Signalling · doi:10.1016/j.cellsig.2009.01.020 · Cited by 41
Disruption of the histidine triad nucleotide-binding hint2 gene in mice affects glycemic control and mitochondrial function
Martin, J., Maurhofer, O., Bellancé, N., Bénard, G., Graber, F., Hahn, D., Galinier, A., Hora, C., Gupta, A., Ferrand, G., et al. (2012) · Hepatology · doi:10.1002/hep.26060 · Cited by 42
Proteins That Fuse and Fragment Mitochondria in Apoptosis: Con-Fissing a Deadly Con-Fusion?
Scorrano, L. (2005) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-005-6572-x · Cited by 41
Key Note Lecture
Bredesen, D. E. (2007) · Stroke · doi:10.1161/01.str.0000257802.82826.a7 · Cited by 42
Frataxin deficiency in neonatal rat ventricular myocytes targets mitochondria and lipid metabolism
Òbis, È., Irazusta, V. P., Sanchı́s, D., Ros, J., & Tamarit, J. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.04.016 · Cited by 44
Probing in vivo dynamics of mitochondria and cortical actin networks using high‐speed atomic force/fluorescence microscopy
Yoshida, A., Sakai, N., Uekusa, Y., Deguchi, K., Gilmore, J. L., Kumeta, M., Ito, S., & Takeyasu, K. (2014) · Genes to Cells · doi:10.1111/gtc.12204 · Cited by 39
Cross Talk of Proteostasis and Mitostasis in Cellular Homeodynamics, Ageing, and Disease
Gumeni, S., & Trougakos, I. P. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/4587691 · Cited by 43
Integrating Ultra-Weak Photon Emission Analysis in Mitochondrial Research
Wijk, R. V., Wijk, E. P. A. V., Pang, J., Yang, M., Yan, Y., & Han, J. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00717 · Cited by 44
Carboxy-Terminal Modulator Protein (CTMP) is a mitochondrial protein that sensitizes cells to apoptosis
Parcellier, A., Tintignac, L. A. J., Zhuravleva, E., Cron, P. D., Schenk, S., Bozulic, L., & Hemmings, B. A. (2009) · Cellular Signalling · doi:10.1016/j.cellsig.2009.01.016 · Cited by 38
Applications of phototransformable fluorescent proteins for tracking the dynamics of cellular components
Nemet, I., Ropelewski, P., & Imanishi, Y. (2015) · Photochemical & Photobiological Sciences · doi:10.1039/c5pp00174a · Cited by 39
Decreasing Mitochondrial Fission Prevents Cholestatic Liver Injury
Yu, T., Wang, L., Lee, H., O'Brien, D. K., Bronk, S. F., Gores, G. J., & Yoon, Y. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.588616 · Cited by 41
Mitochondria: Joining forces to thwart cell death
Jahani‐Asl, A., Germain, M., & Slack, R. S. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.09.006 · Cited by 39
Morphological control of mitochondrial bioenergetics
Yoon, Y. (2015) · Frontiers in bioscience · doi:10.2741/4306 · Cited by 41
Mitochondrial oxidative phosphorylation in autosomal dominant optic atrophy
Mayorov, V., Lowrey, A. J., Biousse, V., Newman, N. J., Cline, S. D., & Brown, M. D. (2008) · BMC Biochemistry · doi:10.1186/1471-2091-9-22 · Cited by 42
The permeability transition and BCL-2 family proteins in apoptosis: co-conspirators or independent agents?
Forte, M. A., & Bernardi, P. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401957 · Cited by 40
Mechanisms associated with the dysregulation of mitochondrial function due to lead exposure and possible implications on the development of Alzheimer’s disease
Bandaru, L. J. M., Ayyalasomayajula, N., Murumulla, L., & Challa, S. (2022) · BioMetals · doi:10.1007/s10534-021-00360-7 · Cited by 39
DRP1 mutations associated with EMPF1 encephalopathy alter mitochondrial membrane potential and metabolic programs
Robertson, G. L., Riffle, S., Patel, M., Bodnya, C., Marshall, A. G., Beasley, H. K., Lopez, E. G., Shao, J., Vue, Z., Hinton, A. O., Jr., et al. (2023) · Journal of Cell Science · doi:10.1242/jcs.260370 · Cited by 37
Morphological, molecular and functional differences of adult bone marrow- and adipose-derived stem cells isolated from rats of different ages
Mantovani, C., Raimondo, S., Haneef, M. S., Geuna, S., Terenghi, G., Shawcross, S., & Wiberg, M. (2012) · Experimental Cell Research · doi:10.1016/j.yexcr.2012.05.008 · Cited by 38
Mitochondria and Peripheral Neuropathies
Vital, A., & Vital, C. (2012) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3182764d47 · Cited by 39

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