Loss of OPA1 Perturbates the Mitochondrial Inner Membrane Structure and Integrity, Leading to Cytochrome c Release and Apoptosis

Mitochondria as the central control point of apoptosis

Desagher, S., & Martinou, J. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01803-1 · Cited by 1,935

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

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

Analysis of gene function in somatic mammalian cells using small interfering RNAs

Elbashir, S. M. (2002) · Methods · doi:10.1016/s1046-2023(02)00023-3 · Cited by 1,099

A Distinct Pathway Remodels Mitochondrial Cristae and Mobilizes Cytochrome c during Apoptosis

Scorrano, L., Ashiya, M., Buttle, K., Weiler, S., Oakes, S. A., Mannella, C. A., & Korsmeyer, S. J. (2002) · Developmental Cell · doi:10.1016/s1534-5807(01)00116-2 · Cited by 1,072

The dynamin-related GTPase Dnm1 regulates mitochondrial fission in yeast

Bleazard, W., McCaffery, J. M., King, E. J., Bale, S., Mozdy, A. D., Tieu, Q., Nunnari, J. M., & Shaw, J. M. (1999) · Nature Cell Biology · doi:10.1038/13014 · Cited by 795

A Human Dynamin-related Protein Controls the Distribution of Mitochondria

Смирнова, Е. А., Shurland, D., Ryazantsev, S. N., & van der Bliek, A. M. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.2.351 · Cited by 734

Mitochondrial Fusion in Human Cells Is Efficient, Requires the Inner Membrane Potential, and Is Mediated by Mitofusins

Legros, F., Lombès, A., Frachon, P., & Rojo, M. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-06-0330 · Cited by 676

The human dynamin‐related protein OPA1 is anchored to the mitochondrial inner membrane facing the inter‐membrane space

Olichon, A., Emorine, L. J., Descoins, E., Pelloquin, L., Brichese, L., Gas, N., Guillou, E., Delettre, C., Valette, A., Hamel, C., et al. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02985-x · Cited by 430

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

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

Improved Locus-Specific Database forOPA1Mutations Allows Inclusion of Advanced Clinical Data

Ferré, M., Caignard, A., Miléa, D., Leruez, S., Cassereau, J., Chevrollier, A., Amati‐Bonneau, P., Verny, C., Bonneau, D., Procaccio, V., et al. (2014) · Human Mutation · doi:10.1002/humu.22703 · Cited by 54

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

miR-634 Activates the Mitochondrial Apoptosis Pathway and Enhances Chemotherapy-Induced Cytotoxicity

Fujiwara, N., Inoue, J., Kawano, T., Tanimoto, K., Kozaki, K., & Inazawa, J. (2015) · Cancer Research · doi:10.1158/0008-5472.can-15-0257 · Cited by 54

A threshold of transmembrane potential is required for mitochondrial dynamic balance mediated by DRP1 and OMA1

Jones, E., Gaytan, N., Garcia, I., Herrera, A., Ramos, M., Agarwala, D., Rana, M., Innis‐Whitehouse, W., Schuenzel, E. L., & Gilkerson, R. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2421-9 · Cited by 57

Evaluation of the neuroprotective effect of EGCG: a potential mechanism of mitochondrial dysfunction and mitochondrial dynamics after subarachnoid hemorrhage

Chen, Y., Chen, J., Sun, X., Shi, X., Wang, L., Huang, L., & Zhou, W. (2018) · Food & Function · doi:10.1039/c8fo01497c · Cited by 53

Current Understanding of the Pivotal Role of Mitochondrial Dynamics in Cardiovascular Diseases and Senescence

Uchikado, Y., Ikeda, Y., & Ohishi, M. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.905072 · Cited by 53

A Comprehensive Approach to Sample Preparation for Electron Microscopy and the Assessment of Mitochondrial Morphology in Tissue and Cultured Cells

Hinton, A. O., Jr., Katti, P., Christensen, T. A., Mungai, M., Shao, J., Zhang, L., Trushin, S., Alghanem, A. F., Jaspersen, A. L., Geroux, R. E., et al. (2023) · Advanced Biology · doi:10.1002/adbi.202200202 · Cited by 62

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

Mitochondrial Dynamics: An Emerging Paradigm in Ischemia-Reperfusion Injury

Calo, L., Dong, Y., Kumar, R., Przyklenk, K., & Sanderson, T. H. (2013) · Current Pharmaceutical Design · doi:10.2174/138161281939131127110701 · Cited by 53

Impaired mitochondrial dynamics underlie axonal defects in hereditary spastic paraplegias

Denton, K. R., Mou, Y., Xu, C., Shah, D., Chang, J., Blackstone, C. D., & Li, X.-J. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy156 · Cited by 53

Mitochondrial disorders

Zeviani, M., & Carelli, V. (2003) · Current Opinion in Neurology · doi:10.1097/00019052-200310000-00004 · Cited by 53

DRP1: At the Crossroads of Dysregulated Mitochondrial Dynamics and Altered Cell Signaling in Cancer Cells

Adhikary, A., Mukherjee, A., Banerjee, R., & Nagotu, S. (2023) · ACS Omega · doi:10.1021/acsomega.3c06547 · Cited by 60

Possible Role of Mitochondrial Remodelling on Cellular Triacylglycerol Accumulation

Kita, T., Nishida, H., Shibata, H., Niimi, S., Higuti, T., & Arakaki, N. (2009) · The Journal of Biochemistry · doi:10.1093/jb/mvp124 · Cited by 55

Changes in mitochondrial morphology induced by calcium or rotenone in primary astrocytes occur predominantly through ros‐mediated remodeling

Deheshi, S., Dabiri, B., Fan, S., Tsang, M., & Rintoul, G. L. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13090 · Cited by 52

Mitochondrial dynamics and the innate antiviral immune response

Pourcelot, M., & Arnoult, D. (2014) · FEBS Journal · doi:10.1111/febs.12940 · Cited by 50

Exercise Pretreatment Promotes Mitochondrial Dynamic Protein OPA1 Expression after Cerebral Ischemia in Rats

Zhang, L., He, Z., Zhang, Q., Wu, Y., Yang, X., Niu, W., Hu, Y., & Jia, J. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms15034453 · Cited by 52

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

Completion of BAX recruitment correlates with mitochondrial fission during apoptosis

Maes, M. E., Grosser, J. A., Fehrman, R. L., Schlamp, C. L., & Nickells, R. W. (2019) · Scientific Reports · doi:10.1038/s41598-019-53049-w · Cited by 57

Subtle neurological and metabolic abnormalities in an Opa1 mouse model of autosomal dominant optic atrophy

Alavi, M. V., Fuhrmann, N., Nguyen, H. P., Yu‐Wai‐Man, P., Heiduschka, P., Chinnery, P. F., & Wissinger, B. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.09.026 · Cited by 52

Bax/Bak-dependent, Drp1-independent Targeting of X-linked Inhibitor of Apoptosis Protein (XIAP) into Inner Mitochondrial Compartments Counteracts Smac/DIABLO-dependent Effector Caspase Activation

Hamacher‐Brady, A., & Brady, N. R. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.643064 · Cited by 50

Why Mitochondria Must Fuse to Maintain Their Genome Integrity

Vidoni, S., Zanna, C., Rugolo, M., Sarzi, E., & Lenaers, G. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4800 · Cited by 50

Autophagy controls the pathogenicity of OPA 1 mutations in dominant optic atrophy

Kane, M. S., Alban, J., Desquiret‐Dumas, V., Guéguen, N., Ishak, L., Ferré, M., Amati‐Bonneau, P., Procaccio, V., Bonneau, D., Lenaers, G., et al. (2017) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13149 · Cited by 51

Mitochondrial Membrane Remodeling

Yang, Z., Wang, L., Yang, C., Pu, S., Guo, Z., Wu, Q., Zhou, Z., & Zhao, H. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2021.786806 · Cited by 54

Opa1 and Drp1 reciprocally regulate cristae morphology, ETC function, and NAD+ regeneration in KRas-mutant lung adenocarcinoma

Sessions, D. T., Kim, K., Kashatus, J. A., Churchill, N., Park, K.-S., Mayo, M. W., Sesaki, H., & Kashatus, D. F. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111818 · Cited by 49

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

Mitochondrial alterations in Parkinson's disease human samples and cellular models

Zilocchi, M., Finzi, G., Lualdi, M., Sessa, F., Fasano, M., & Alberio, T. (2018) · Neurochemistry International · doi:10.1016/j.neuint.2018.04.013 · Cited by 50

UCP2‐dependent improvement of mitochondrial dynamics protects against acute kidney injury

Qin, N., Cai, T., Ke, Q., Yuan, Q., Luo, J., Mao, X., Jiang, L., Cao, H., Wen, P., Zen, K., et al. (2018) · The Journal of Pathology · doi:10.1002/path.5198 · Cited by 50

Role of PGC-1α in Mitochondrial Quality Control in Neurodegenerative Diseases

Zhang, Q., Lei, Y.-H., Zhou, J.-P., Hou, Y.-Y., Wan, Z., Wang, H., & Meng, H. (2019) · Neurochemical Research · doi:10.1007/s11064-019-02858-6 · Cited by 53

OPA1 , the Disease Gene for Autosomal Dominant Optic Atrophy, Is Specifically Expressed in Ganglion Cells and Intrinsic Neurons of the Retina

Pesch, U. E. A., Fries, J. E., Bette, S. J., Kalbacher, H., Wissinger, B., Alexander, C., & Köhler, K. (2004) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.03-1261 · Cited by 50

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

A novel mutation of AFG3L2 might cause dominant optic atrophy in patients with mild intellectual disability

Charif, M., Roubertie, A., Salime, S., Mamouni, S., Goizet, C., Hamel, C., & Lenaers, G. (2015) · Frontiers in Genetics · doi:10.3389/fgene.2015.00311 · Cited by 49

Chaperone-mediated autophagy controls the turnover of E3 ubiquitin ligase MARCHF5 and regulates mitochondrial dynamics

Nie, T., Tao, K., Zhu, L., Huang, L. H., Hu, S., Yang, R., Xu, P., Mao, Z., & Yang, Q. (2020) · Autophagy · doi:10.1080/15548627.2020.1848128 · Cited by 51

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

Mitochondrial movers and shapers: Recent insights into regulators of fission, fusion and transport

Fatima, N. U., & Ananthanarayanan, V. (2022) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2022.102150 · Cited by 48

Prohibitin 2 Regulates the Proliferation and Lineage-Specific Differentiation of Mouse Embryonic Stem Cells in Mitochondria

Kowno, M., Watanabe-Susaki, K., Ishimine, H., Komazaki, S., Enomoto, K., Seki, Y., Wang, Y. Y., Ishigaki, Y., Ninomiya, N., Noguchi, T.-A. K., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0081552 · Cited by 51

Cell death: Insights into the ultrastructure of mitochondria

Ulivieri, C. (2010) · Tissue and Cell · doi:10.1016/j.tice.2010.10.004 · Cited by 50

A novel ADOA-associated OPA1 mutation alters the mitochondrial function, membrane potential, ROS production and apoptosis

Zhang, J., Liu, X., Liang, X., Lu, Y., Zhu, L., Fu, R., Ji, Y., Fan, W., Chen, J., Lin, B., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-05571-y · Cited by 48

Cerebrovascular function and mitochondrial bioenergetics after ischemia-reperfusion in male rats

Rutkai, I., Merdžo, I., Wunnava, S. V., Curtin, G., Katakam, P. V. G., & Busija, D. W. (2017) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x17745028 · Cited by 48

The relevance of mitochondrial morphology for human disease

Navaratnarajah, T., Anand, R., Reichert, A. S., & Distelmaier, F. (2021) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2021.105951 · Cited by 49

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

Is mitochondrial morphology important for cellular physiology?

Wai, T. (2024) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2024.05.005 · 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

Key Role of Mitochondria in Alzheimer’s Disease Synaptic Dysfunction

Cavallucci, V., Ferraina, C., & D’Amelio, M. (2013) · Current Pharmaceutical Design · doi:10.2174/1381612811319360005 · Cited by 47

Sequences flanking the transmembrane segments facilitate mitochondrial localization and membrane fusion by mitofusin

Huang, X., Zhou, X., Hu, X., Joshi, A. S., Guo, X., Zhu, Y., Chen, Q., Prinz, W. A., & Hu, J. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1708782114 · Cited by 52

Tracking intra‐ and inter‐organelle signaling of mitochondria

Madreiter‐Sokolowski, C. T., Ramadani‐Muja, J., Ziomek, G., Burgstaller, S., Bischof, H., Koshenov, Z., Gottschalk, B., Malli, R., & Graier, W. F. (2019) · FEBS Journal · doi:10.1111/febs.15103 · Cited by 45

Effects of doxorubicin on cardiac muscle subsarcolemmal and intermyofibrillar mitochondria

Kavazis, A. N., Morton, A. B., Hall, S. E., & Smuder, A. J. (2016) · Mitochondrion · doi:10.1016/j.mito.2016.10.008 · Cited by 45

Meta-analysis of genotype-phenotype analysis of OPA1 mutations in autosomal dominant optic atrophy

Ham, M., Han, J., Osann, K., Smith, M., & Kimonis, V. E. (2018) · Mitochondrion · doi:10.1016/j.mito.2018.07.006 · Cited by 45

Regulation of neuronal bioenergetics as a therapeutic strategy in neurodegenerative diseases

Onyango, I. G., Bennett, J. P., & Stokin, G. B. (2021) · Neural Regeneration Research · doi:10.4103/1673-5374.303007 · Cited by 45

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

The new role of F1Fo ATP synthase in mitochondria-mediated neurodegeneration and neuroprotection

Mnatsakanyan, N., & Jonas, E. A. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113400 · Cited by 44

Molecular machineries shaping the mitochondrial inner membrane

Daumke, O., & van der Laan, M. (2025) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-025-00854-z · Cited by 51

Mitochondria as Crucial Players in Demyelinated Axons: Lessons from Neuropathology and Experimental Demyelination

Campbell, G. R., & Mahad, D. (2011) · Autoimmune Diseases · doi:10.4061/2011/262847 · Cited by 46

Protective effect of Homer 1a against hydrogen peroxide-induced oxidative stress in PC12 cells

Luo, P., Chen, T., Zhao, Y., Xu, H., Huo, K., Zhao, M., Yang, Y., & Fei, Z. (2012) · Free Radical Research · doi:10.3109/10715762.2012.678340 · 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

Loss of functional OPA 1 unbalances redox state: implications in dominant optic atrophy pathogenesis

Millet, A. M. C., Bertholet, A. M., Daloyau, M., Reynier, P., Galinier, A., Devin, A., Wissinguer, B., Belenguer, P., & Davezac, N. (2016) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.305 · Cited by 44

Genetically determined optic neuropathies

Miléa, D., Amati‐Bonneau, P., Reynier, P., & Bonneau, D. (2009) · Current Opinion in Neurology · doi:10.1097/wco.0b013e3283347b27 · Cited by 44

Defective Mitochondrial Adenosine Triphosphate Production in Skeletal Muscle From Patients With Dominant Optic Atrophy Due to OPA1 Mutations

Lodi, R., Tonon, C., Valentino, M. L., Manners, D. N., Testa, C. M., Malucelli, E., Morgia, C. L., Barboni, P., Carbonelli, M., Schimpf, S., et al. (2010) · Archives of Neurology · doi:10.1001/archneurol.2010.228 · Cited by 44

Yeast models of human mitochondrial diseases: from molecular mechanisms to drug screening

Schwimmer, C., Rak, M., Lefebvre‐Legendre, L., Duvezin‐Caubet, S., Plane, G., & di Rago, J. (2006) · Biotechnology Journal · doi:10.1002/biot.200500053 · Cited by 49

Modeling autosomal dominant optic atrophy using induced pluripotent stem cells and identifying potential therapeutic targets

Chen, J., Riazifar, H., Guan, M., & Huang, T. (2016) · Stem Cell Research & Therapy · doi:10.1186/s13287-015-0264-1 · Cited by 42

The Interplay between Oncogenic Signaling Networks and Mitochondrial Dynamics

Nagdas, S., & Kashatus, D. F. (2017) · Antioxidants · doi:10.3390/antiox6020033 · Cited by 46

Protective role of the mitochondrial fusion protein OPA1 in hypertension

Robert, P., Nguyen, P. M. C., Richard, A., Grenier, C., Chevrollier, A., Munier, M., Grimaud, L., Proux, C., Champin, T., Lelièvre, E., et al. (2021) · The FASEB Journal · doi:10.1096/fj.202000238rrr · Cited by 42

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

Acute and late-onset optic atrophy due to a novel OPA1 mutation leading to a mitochondrial coupling defect.

Nochez, Y., Arsène, S., Guéguen, N., Chevrollier, A., Ferré, M., Guillet, V., Desquiret‐Dumas, V., Toutain, A., Bonneau, D., Procaccio, V., et al. (2009) · PubMed Central · Cited by 42

Human Misato regulates mitochondrial distribution and morphology

Kimura, M., & Okano, Y. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.02.004 · Cited by 44

Mitochondrial dynamics as an underlying mechanism involved in aerobic exercise training-induced cardioprotection against ischemia-reperfusion injury

Ghahremani, R., Damirchi, A., Salehi, I., Komaki‬, A., & Esposito, F. (2018) · Life Sciences · doi:10.1016/j.lfs.2018.10.035 · Cited by 44

OPA1 mutations and mitochondrial DNA damage: keeping the magic circle in shape

Zeviani, M. (2008) · Brain · doi:10.1093/brain/awm339 · Cited by 41

Reversible optic neuropathy with OPA1 exon 5b mutation

Cornille, K., Miléa, D., Amati‐Bonneau, P., Procaccio, V., Zazoun, L., Guillet, V., Elachouri, G., Delettre, C., Guéguen, N., Loiseau, D., et al. (2008) · Annals of Neurology · doi:10.1002/ana.21376 · Cited by 41

Distinct types of protease systems are involved in homeostasis regulation of mitochondrial morphology via balanced fusion and fission

Saita, S., Ishihara, T., Maeda, M., Iemura, S., Natsume, T., Mihara, K., & Ishihara, N. (2016) · Genes to Cells · doi:10.1111/gtc.12351 · Cited by 43

Resveratrol protects retinal ganglion cells against ischemia induced damage by increasing Opa1 expression

Pang, Y., Qin, M., Hu, P., Ji, K., Xiao, R., Sun, N., Pan, X., & Zhang, X. (2020) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2020.4711 · Cited by 43

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

Quantitative proteomics for identifying biomarkers for Rabies

Venugopal, A. K., Ghantasala, S., Selvan, L. D. N., Mahadevan, A., Renuse, S., Kumar, P., Pawar, H., Sahasrabhuddhe, N. A., Suja, M. S., Lakshmikantha, R. Y., et al. (2013) · Clinical Proteomics · doi:10.1186/1559-0275-10-3 · Cited by 40

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

Mitochondrial dynamics is affected by 17β-estradiol in the MCF-7 breast cancer cell line. Effects on fusion and fission related genes

Sastre-Serra, J., Nadal-Serrano, M., Pons, D. G., Roca, P., & Oliver, J. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.07.012 · Cited by 40

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

Testosterone induces up-regulation of mitochondrial gene expression in murine C2C12 skeletal muscle cells accompanied by an increase of nuclear respiratory factor-1 and its downstream effectors

Pronsato, L., Milanesi, L. M., & Vasconsuelo, A. (2019) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2019.110631 · Cited by 41

OPA1 Modulates Mitochondrial Ca2+ Uptake Through ER-Mitochondria Coupling

Cartes-Saavedra, B., Macuada, J., Lagos, D., Arancibia, D., Andrés, M. E., Yu‐Wai‐Man, P., Hajnóczky, G., & Eisner, V. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.774108 · Cited by 40

Stage-specific enhanced expression of mitochondrial fusion and fission factors during spermatogenesis in rat testis

Honda, S., & Hirose, S. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.10.008 · Cited by 40

Optic atrophy and sensorineural hearing loss in a family caused by an R445H OPA1 mutation

Li, C., Kosmorsky, G. S., Zhang, K., Katz, B. J., Ge, J., & Traboulsi, E. I. (2005) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.30794 · Cited by 40

Tensile Forces and Shape Entropy Explain Observed Crista Structure in Mitochondria

Ghochani, M., Nulton, J., Salamon, P., Frey, T., Rabinovitch, A., & Baljon, A. R. C. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.09.038 · Cited by 40

A missense mutation in the murine Opa3 gene models human Costeff syndrome

Davies, V., Powell, K. A., White, K., Yip, W., Hogan, V. E., Hollins, A. J., Davies, J. R., Piechota, M. J., Brownstein, D. G., Moat, S. J., et al. (2008) · Brain · doi:10.1093/brain/awm333 · Cited by 40

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

Mitochondrial fragmentation and network architecture in degenerative diseases

Shah, S. I., Paine, J. G., Perez, C., & Ullah, G. (2019) · PLoS ONE · doi:10.1371/journal.pone.0223014 · Cited by 40

Cellular Organelles Reorganization During Zika Virus Infection of Human Cells

García, C. C., Vázquez, C., Giovannoni, F., Russo, C., Cordo, S. M., Alaimo, A., & Damonte, E. B. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.01558 · Cited by 40

Role of Mitochondria-Cytoskeleton Interactions in the Regulation of Mitochondrial Structure and Function in Cancer Stem Cells

Kim, J., & Cheong, J. (2020) · Cells · doi:10.3390/cells9071691 · Cited by 40

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

Overexpression of optic atrophy 1 protein increases cisplatin resistance via inactivation of caspase-dependent apoptosis in lung adenocarcinoma cells

Fang, H., Chen, C.-Y., Chiou, S.-H., Wang, Y., Lin, T., Chang, H., Chiang, I., Lan, K.-J., & Chow, K. (2011) · Human Pathology · doi:10.1016/j.humpath.2011.04.012 · Cited by 38

A novel heterozygous OPA3 mutation located in the mitochondrial target sequence results in altered steady-state levels and fragmented mitochondrial network

Grau, T., Burbulla, L. F., Engl, G., Delettre, C., Delprat, B., Oexle, K., Leo‐Kottler, B., Roscioli, T., Krüger, R., Rapaport, D., et al. (2013) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2013-101774 · Cited by 39

Targeting Mitochondrial Dysfunction in Neurodegenerative Diseases: Expanding the Therapeutic Approaches by Plant-Derived Natural Products

Zhang, X., Wang, L., Li, B., Shi, J., Xu, J. F., & Yuan, M. (2023) · Pharmaceuticals · doi:10.3390/ph16020277 · Cited by 42

Mitochondrial Dynamics and Insulin Secretion

Kabra, U. D., & Jastroch, M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241813782 · Cited by 40

Significance of Mitochondrial Protein Post-translational Modifications in Pathophysiology of Brain Injury

Klimova, N., Long, A., & Kristián, T. (2017) · Translational Stroke Research · doi:10.1007/s12975-017-0569-8 · Cited by 36

Acetyl ‐l‐ carnitine protects yeast cells from apoptosis and aging and inhibits mitochondrial fission

Palermo, V., Falcone, C., Calvani, M., & Mazzoni, C. (2010) · Aging Cell · doi:10.1111/j.1474-9726.2010.00587.x · Cited by 39

The role of PTEN-induced kinase 1 in mitochondrial dysfunction and dynamics

Craig, K. J. T., & Cookson, M. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.02.018 · Cited by 37

A novel prohibitin-binding compound induces the mitochondrial apoptotic pathway through NOXA and BIM upregulation

Moncunill‐Massaguer, C., Saura‐Esteller, J., Pérez‐Perarnau, A., Palmeri, C. M., Núñez‐Vázquez, S., Cosialls, A. M., González‐Gironès, D. M., Pomares, H., Korwitz, A., Preciado, S., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.6154 · Cited by 39

mtDNA Maintenance and Alterations in the Pathogenesis of Neurodegenerative Diseases

Shang, D., Huang, M., Wang, B., Yan, X., Wu, Z., & Zhang, X. (2022) · Current Neuropharmacology · doi:10.2174/1570159x20666220810114644 · Cited by 44

HDAC6 maintains mitochondrial connectivity under hypoxic stress by suppressing MARCH5/MITOL dependent MFN2 degradation

Kim, H.-J., Nagano, Y., Choi, S. J., Park, S. Y., Kim, H., Yao, T., & Lee, J. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.07.111 · Cited by 37

OPA 1 and Its Clinical Implications

Trevisson, E., Salviati, L., & Scorrano, L. (2009) · Encyclopedia of Life Sciences · doi:10.1002/9780470015902.a0021785 · Cited by 1

OPA1 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

OPA1-dependent cristae remodeling disassembles respiratory chain supercomplexes, triggering apoptotic mitochondrial dysfunction

Cogliati, S. (2011) · Padua Research Archive (University of Padova) · Cited by 1

Identification and functional characterization of components of the OPA1 complexes targeted during apoptotic cristae remodeling

Glytsou, C. (2016) · Padua@research (University of Padova)

Release of OPA1 during Apoptosis Participates in the Rapid and Complete Release of Cytochrome c and Subsequent Mitochondrial Fragmentation

Arnoult, D., Grodet, A., Lee, Y.-J., Estaquier, J., & Blackstone, C. D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505970200 · Cited by 265