The DOI matches its Crossref record; 44 of the 45 references it cites were found in a registry or an index.
OPA1 requires mitofusin 1 to promote mitochondrial fusion
Open accessAbstract
The regulated equilibrium between mitochondrial fusion and fission is essential to maintain integrity of the organelle. Mechanisms of mitochondrial fusion are largely uncharacterized in mammalian cells. It is unclear whether OPA1, a dynamin-related protein of the inner membrane mutated in autosomal dominant optic atrophy, participates in fusion or fission. OPA1 promoted the formation of a branched network of elongated mitochondria, requiring the integrity of both its GTPase and C-terminal coiled-coil domain. Stable reduction of OPA1 levels by RNA interference resulted in small, fragmented, and scattered mitochondria. Levels of OPA1 did not affect mitochondrial docking, but they correlated with the extent of fusion as measured by polyethylene glycol mitochondrial fusion assays. A genetic analysis proved that OPA1 was unable to tubulate and fuse mitochondria lacking the outer membrane mitofusin 1 but not mitofusin 2. Our data show that OPA1 functionally requires mitofusin 1 to regulate mitochondrial fusion and reveal a specific functional difference between mitofusin 1 and 2.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“OPA1-dependent mitochondrial fusion needs Mfn1 [73] as well as balanced OPA1S and OPA1L forms.”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [73]
In the citing paper
“OPA1 deletion leads to mitochondrial fragmentation, whereas OPA1 overexpression induces mitochondrial elongation [73].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [73]
In the citing paper
“Opa1 participates in inner mitochondrial membrane fusion and cristae morphogenesis.”
From Mitochondrial DNA and TLR9 drive muscle inflammation upon Opa1 deficiency (2018) · cites this paper as Cipolat et al, 2004
In the citing paper
“which consists in the fusion of the outer and inner mitochondrial membranes orchestrated by mitofusin-1 and mitofusin-2 and optic atrophy protein 1, respectively (Figure 3; Cipolat et al., 2004).”
From Mitochondrial (Dys)function and Insulin Resistance: From Pathophysiological Molecular Mechanisms to the Impact of Diet (2019) · cites this paper as Cipolat et al., 2004
Citations
Cites
Proapoptotic BAX and BAK: A Requisite Gateway to Mitochondrial Dysfunction and Death
Wei, M. C., Zong, W.-X., Cheng, E. H.-Y., Lindsten, T., Panoutsakopoulou, V., Ross, A. J., Roth, K. A., MacGregor, G. R., Thompson, C. B., & Korsmeyer, S. J. (2001) · Science · doi:10.1126/science.1059108 · Cited by 3,988
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
(2001) · PubMed · Cited by 2,381
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
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
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
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
Coiled coils: new structures and new functions
Lupas, A. N. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)10052-9 · Cited by 1,321
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
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
Self-citation
Flagged first, then by citations
1 of the 45 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- Wang, X. (2001) Genes Dev. 15, 2922–2933.11711427
Cited by
Sorted by citations
Items 101–200 of 1,000
Orchestration of lymphocyte chemotaxis by mitochondrial dynamics
Campello, S., Lacalle, R. A., Bettella, M., Mañes, S., Scorrano, L., & Viola, A. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20061877 · Cited by 325
Self-citationThe Metabolic Theory of Pulmonary Arterial Hypertension
Paulin, R., & Michelakis, E. D. (2014) · Circulation Research · doi:10.1161/circresaha.115.301130 · Cited by 328
Neuspiel, M., Zunino, R., Gangaraju, S., Rippstein, P. U., & McBride, H. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501599200 · Cited by 308
Dietrich, M. O., Liu, Z.-W., & Horvath, T. L. (2013) · Cell · doi:10.1016/j.cell.2013.09.004 · Cited by 306
The function of the respiratory supercomplexes: The plasticity model
Acín‐Pérez, R., & Enrı́quez, J. A. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.12.009 · Cited by 319
Molecular Strategies for Targeting Antioxidants to Mitochondria: Therapeutic Implications
Apostolova, N., & Víctor, V. M. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5952 · Cited by 311
Mitochondrial dynamics in cell death and neurodegeneration
Cho, D., Nakamura, T., & Lipton, S. A. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0435-2 · Cited by 306
An intimate liaison: spatial organization of the endoplasmic reticulum–mitochondria relationship
de Brito, O. M., & Scorrano, L. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.177 · Cited by 310
Self-citationMitochondrial fission and fusion mediators, hFis1 and OPA1, modulate cellular senescence
Lee, S., Jeong, S.-Y., Lim, W.-C., Kim, S., Park, Y.-Y., Sun, X., Youle, R. J., & Cho, H. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700679200 · Cited by 298
Mitochondrial shape changes: orchestrating cell pathophysiology
Campello, S., & Scorrano, L. (2010) · EMBO Reports · doi:10.1038/embor.2010.115 · Cited by 307
Self-citationAbnormal mitochondrial dynamics and neurodegenerative diseases
Su, B., Wang, X., Zheng, L., Perry, G. L., Smith, M. A., & Zhu, X. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.09.013 · Cited by 301
Costa, V., Giacomello, M., Hudec, R., Lopreiato, R., Ermak, G., Lim, D., Malorni, W., Davies, K. J. A., Carafoli, E., & Scorrano, L. (2010) · EMBO Molecular Medicine · doi:10.1002/emmm.201000102 · Cited by 293
Self-citationSkeletal muscle insulin resistance: role of mitochondria and other ROS sources
Di Meo, S., Iossa, S., & Venditti, P. (2017) · Journal of Endocrinology · doi:10.1530/joe-16-0598 · Cited by 282
Yu, T., Jhun, B. S., & Yoon, Y. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3284 · Cited by 293
The relationship between mitochondrial shape and function and the cytoskeleton
Anesti, V., & Scorrano, L. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.04.013 · Cited by 286
Self-citationMitochondrial Dynamics: Coupling Mitochondrial Fitness with Healthy Aging
Sebastián, D., Palacı́n, M., & Antonio Zorzano, A. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.01.003 · Cited by 292
The regulation of mitochondrial morphology: Intricate mechanisms and dynamic machinery
Palmer, C. S., Osellame, L. D., Stojanovski, D., & Ryan, M. T. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2011.05.021 · Cited by 300
Alavi, M. V., Bette, S. J., Schimpf, S., Schuettauf, F., Schraermeyer, U., Wehrl, H. F., Rüttiger, L., Beck, S. C., Tonagel, F., Pichler, B. J., et al. (2006) · Brain · doi:10.1093/brain/awm005 · Cited by 278
The role of abnormal mitochondrial dynamics in the pathogenesis of Alzheimer’s disease
Wang, X., Su, B., Zheng, L., Perry, G. L., Smith, M. A., & Zhu, X. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.05867.x · Cited by 284
Lee, J. H., Park, A., Oh, K., Lee, S. C., Kim, W. K., & Bae, K. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20194924 · Cited by 280
Mitochondrial quality control in health and in Parkinson’s disease
Eldeeb, M. A., Thomas, R. A., Ragheb, M. A., Fallahi, A., & Fon, E. A. (2022) · Physiological Reviews · doi:10.1152/physrev.00041.2021 · Cited by 281
Abnormalities in Mitochondrial Structure in Cells from Patients with Bipolar Disorder
Cataldo, A. M., McPhie, D. L., Lange, N. T., Punzell, S., Elmiligy, S., Ye, N., Froimowitz, M. P., Hassinger, L. C., Menesale, E. B., Sargent, L. W., et al. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.081068 · Cited by 279
Mitochondria–endoplasmic reticulum choreography: structure and signaling dynamics
Pizzo, P., & Pozzan, T. (2007) · Trends in Cell Biology · doi:10.1016/j.tcb.2007.07.011 · Cited by 268
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
The SUMO protease SENP5 is required to maintain mitochondrial morphology and function
Zunino, R., Schauss, A. C., Rippstein, P. U., Andrade-Navarro, M. A., & McBride, H. M. (2007) · Journal of Cell Science · doi:10.1242/jcs.03418 · Cited by 262
Stephan, T., Brüser, C., Deckers, M., Steyer, A. M., Balzarotti, F., Barbot, M., Behr, T. S., Heim, G., Hübner, W., Ilgen, P., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2019104105 · Cited by 253
Regulation of mitochondrial fusion and division
Cerveny, K. L., Tamura, Y., Zhang, Z., Jensen, R. E., & Sesaki, H. (2007) · Trends in Cell Biology · doi:10.1016/j.tcb.2007.08.006 · Cited by 271
The Parkinson-associated protein PINK1 interacts with Beclin1 and promotes autophagy
Michiorri, S., Gelmetti, V, Giarda, E., Lombardi, F., Romano, F., Marongiu, R., Nerini-Molteni, S., Sale, P., Vago, R., Arena, G., et al. (2010) · Cell Death & Differentiation · doi:10.1038/cdd.2009.200 · Cited by 260
Moore, A. S., Wong, Y. C., Simpson, C. L., & Holzbaur, E. L. F. (2016) · Nature Communications · doi:10.1038/ncomms12886 · Cited by 264
Mitophagy in Cancer: A Tale of Adaptation
Vara‐Pérez, M., Felipe‐Abrio, B., & Agostinis, P. (2019) · Cells · doi:10.3390/cells8050493 · Cited by 264
Mitochondrial morphology in mitophagy and macroautophagy
Gomes, L. C., & Scorrano, L. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.02.012 · Cited by 259
Self-citationImpairing the Mitochondrial Fission and Fusion Balance: A New Mechanism of Neurodegeneration
Knott, A. B., & Bossy‐Wetzel, E. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1427.030 · Cited by 263
Structure, function, and regulation of mitofusin‐2 in health and disease
Chandhok, G., Lazarou, M., & Neumann, B. (2017) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12378 · Cited by 263
Pyakurel, A., Savoia, C., Hess, D., & Scorrano, L. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.02.021 · Cited by 244
Self-citationPark, Y.-Y., Lee, S., Karbowski, M., Neutzner, A., Youle, R. J., & Cho, H. (2010) · Journal of Cell Science · doi:10.1242/jcs.061481 · Cited by 244
OPA1 Isoforms in the Hierarchical Organization of Mitochondrial Functions
Dotto, V. D., Mishra, P., Vidoni, S., Fogazza, M., Maresca, A., Caporali, L., McCaffery, J. M., Cappelletti, M., Baruffini, E., Lenaers, G., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.05.073 · Cited by 254
High levels of Fis1, a pro-fission mitochondrial protein, trigger autophagy
Gomes, L. C., & Scorrano, L. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.05.442 · Cited by 242
Self-citationThe Association of Tau With Mitochondrial Dysfunction in Alzheimer’s Disease
Cheng, Y., & Bai, F. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00163 · Cited by 239
Skeletal muscle mitochondria as a target to prevent or treat type 2 diabetes mellitus
Hesselink, M. K. C., Schrauwen-Hinderling, V., & Schrauwen, P. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2016.104 · Cited by 242
Iannielli, A., Bido, S., Folladori, L., Segnali, A., Cancellieri, C., Maresca, A., Massimino, L., Rubio, A., Morabito, G., Caporali, L., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.01.089 · Cited by 239
Mitochondrial dynamics and disease, OPA1
Olichon, A., Guillou, E., Delettre, C., Landes, T., Pelloquin, L., Emorine, L. J., Mils, V., Daloyau, M., Hamel, C., Amati‐Bonneau, P., et al. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.04.003 · Cited by 238
Mitochondrial dynamics in the adult cardiomyocytes: which roles for a highly specialized cell?
Piquereau, J., Caffin, F., Novotová, M., Lemaire, C., Veksler, V., Garnier, A., Ventura‐Clapier, R., & Joubert, F. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00102 · Cited by 251
Separate fusion of outer and inner mitochondrial membranes
Malka, F., Guillery, O., Cifuentes-Díaz, C., Guillou, E., Belenguer, P., Lombès, A., & Rojo, M. (2005) · EMBO Reports · doi:10.1038/sj.embor.7400488 · Cited by 233
Grasso, D., Zampieri, L. X., Capelôa, T., de Velde, J. A. V., & Sonveaux, P. (2020) · Cell Stress · doi:10.15698/cst2020.06.221 · Cited by 239
Mitochondrial trafficking and morphology in healthy and injured neurons
Chang, D. T. W., & Reynolds, I. J. (2006) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2006.09.003 · Cited by 235
Mitochondrial diseases: from molecular mechanisms to therapeutic advances
Wen, H., Deng, H., Li, B., Chen, J., Zhu, J., Zhang, X., Yoshida, S., & Zhou, Y. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02044-3 · Cited by 284
Olichon, A., Elachouri, G., Baricault, L., Delettre, C., Belenguer, P., & Lenaers, G. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402048 · Cited by 228
Mitochondrial dynamics and their potential as a therapeutic target
Whitley, B. N., Engelhart, E. A., & Hoppins, S. C. (2019) · Mitochondrion · doi:10.1016/j.mito.2019.06.002 · Cited by 228
Makino, A., Scott, B. T., & Dillmann, W. H. (2010) · Diabetologia · doi:10.1007/s00125-010-1770-4 · Cited by 223
Mitochondrial Structure and Bioenergetics in Normal and Disease Conditions
Protasoni, M., & Zeviani, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020586 · Cited by 243
Opa1 Overexpression Ameliorates the Phenotype of Two Mitochondrial Disease Mouse Models
Civiletto, G., Varanita, T., Cerutti, R., Gorletta, T., Barbaro, S., Marchet, S., Lamperti, C., Viscomi, C., Scorrano, L., & Zeviani, M. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.04.016 · Cited by 216
Self-citationCritical dependence of neurons on mitochondrial dynamics
Chen, H., & Chan, D. C. (2006) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2006.06.004 · Cited by 219
Hyatt, H. W., Deminice, R., Yoshihara, T., & Powers, S. K. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.11.005 · Cited by 226
Mitochondrial Dynamics in Diabetes
Yoon, Y., Galloway, C. A., Jhun, B. S., & Yu, T. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3286 · Cited by 223
Mitochondrial DNA and TLR9 drive muscle inflammation upon Opa1 deficiency
Rodríguez‐Nuevo, A., Díaz‐Ramos, A., Noguera, E., Díaz‐Sáez, F., Duran, X., Muñoz, J. P., Romero, M., Plana, N., Sebastián, D., Tezze, C., et al. (2018) · The EMBO Journal · doi:10.15252/embj.201796553 · Cited by 207
MFN2 mutations cause severe phenotypes in most patients with CMT2A
Feely, S. M. E., Laurá, M., Siskind, C. E., Sottile, S. L., Davis, M. B., Gibbons, V. S., Reilly, M. M., & Shy, M. E. (2011) · Neurology · doi:10.1212/wnl.0b013e31821a441e · Cited by 222
The role of mitochondrial dynamics in cardiovascular diseases
Forte, M., Schirone, L., Ameri, P., Basso, C., Catalucci, D., Modica, J., Chimenti, C., Crotti, L., Frati, G., Rubattu, S. D., et al. (2020) · British Journal of Pharmacology · doi:10.1111/bph.15068 · Cited by 227
Yu, W., Sun, Y., Guo, S., & Lu, B. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr235 · Cited by 219
Yue, W., Chen, Z., Liu, H., Chen, Y., Chen, M., Feng, D., Yan, C., Wu, H., Du, L., Wang, Y., et al. (2014) · Cell Research · doi:10.1038/cr.2014.20 · Cited by 218
Kotiadis, V. N., Duchen, M. R., & Osellame, L. D. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.10.041 · Cited by 216
Regulation of ER-mitochondria contacts by Parkin via Mfn2
Basso, V., Marchesan, E., Peggion, C., Chakraborty, J., von Stockum, S., Giacomello, M., Ottolini, D., Debattisti, V., Caicci, F., Tasca, E., et al. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.09.006 · Cited by 217
Central Role of Mitofusin 2 in Autophagosome-Lysosome Fusion in Cardiomyocytes
Zhao, T. S., Huang, X., Han, L., Wang, X., Cheng, H., Zhao, Y., Chen, Q., Chen, J., Cheng, H., Xiao, R., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.379164 · Cited by 212
Mitochondrial Dynamics in Cardiovascular Health and Disease
Ong, S., Hall, A. R., & Hausenloy, D. J. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4777 · Cited by 213
Regulation of mitophagy by the Gp78 E3 ubiquitin ligase
Fu, M., St-Pierre, P., Shankar, J., Wang, P. T. C., Joshi, B., & Nabi, I. R. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-08-0607 · Cited by 210
Mitochondrial Dynamics in Stem Cells and Differentiation
Seo, B. J., Yoon, S. H., & Tae, J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19123893 · Cited by 208
Givvimani, S., Munjal, C., Tyagi, N., Sen, U., Metreveli, N. S., & Tyagi, S. C. (2012) · PLoS ONE · doi:10.1371/journal.pone.0032388 · Cited by 203
The pathophysiology of mitochondrial disease as modeled in the mousePreprint
Wallace, D. C., & Fan, W. (2009) · Genes & Development · doi:10.1101/gad.1784909 · Cited by 204
Qian, W., Choi, S., Gibson, G. A., Watkins, S. C., Bakkenist, C. J., & Houten, B. V. (2012) · Journal of Cell Science · doi:10.1242/jcs.109769 · Cited by 204
Bhatia, D., Capili, A. M., & Choi, M. E. (2020) · Kidney Research and Clinical Practice · doi:10.23876/j.krcp.20.082 · Cited by 213
Ferreira-da-Silva, A., Valacca, C., Rios, E., Pópulo, H., Soares, P., Sobrinho-Simões, M. A., Scorrano, L., Máximo, V., & Campello, S. (2015) · PLoS ONE · doi:10.1371/journal.pone.0122308 · Cited by 200
Self-citationCoincident Phosphatidic Acid Interaction Restrains Drp1 in Mitochondrial Division
Adachi, Y., Itoh, K., Yamada, T., Cerveny, K. L., Suzuki, T. L., Macdonald, P. J., Frohman, M. A., Ramachandran, R., Iijima, M., & Sesaki, H. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.08.013 · Cited by 206
Romanello, V., & Sandri, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03662-0 · Cited by 197
Mitochondrial fusion proteins: Dual regulators of morphology and metabolism
Antonio Zorzano, A., Liesa, M., Sebastián, D., Segalés, J., & Palacín, M. (2010) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2010.01.002 · Cited by 204
PGC1α-mediated Mitofusin-2 Deficiency in Female Rats and Humans with Pulmonary Arterial Hypertension
Ryan, J. J., Marsboom, G., Fang, Y.-H., Tóth, P. T., Morrow, E., Luo, N., Piao, L. H., Hong, Z., Ericson, K. J., Zhang, H. J., et al. (2013) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201209-1687oc · Cited by 194
Franco-Iborra, S., Vila, M., & Perier, C. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00342 · Cited by 197
Acidosis overrides oxygen deprivation to maintain mitochondrial function and cell survival
Khacho, M., Tarabay, M., Patten, D. A., Khacho, P., MacLaurin, J. G., Guadagno, J., Bergeron, R., Cregan, S. P., Harper, M., Park, D. S., et al. (2014) · Nature Communications · doi:10.1038/ncomms4550 · Cited by 197
Piquereau, J., Caffin, F., Novotová, M., Prola, A., Garnier, A., Matéo, P., Fortin, D., Huynh, L. H., Nicolas, V., Alavi, M. V., et al. (2012) · Cardiovascular Research · doi:10.1093/cvr/cvs117 · Cited by 204
Role for CED-9 and Egl-1 as Regulators of Mitochondrial Fission and Fusion Dynamics
Delivani, P., Adrain, C., Taylor, R. C., Duriez, P. J., & Martin, S. J. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.034 · Cited by 193
Hsu, Y., Wu, Y., Yu, T.-H., & Wei, Y. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.02.011 · Cited by 189
Mitochondrial Dynamics in Mitochondrial Diseases
Suarez-Rivero, J. M., Paz, M. V., de la Cruz‐Ojeda, P., de la Mata, M., Cotán, D., Oropesa-Ávila, M., de Lavera, I., Álvarez-Córdoba, M., Luzón–Hidalgo, R., & Sánchez-Alcázar, J. A. (2016) · Diseases · doi:10.3390/diseases5010001 · Cited by 196
Neutrophil extracellular trap formation requires OPA1-dependent glycolytic ATP production
Amini, P., Stojkov, D., Felser, A., Jackson, C. B., Courage, C., Schaller, A., Gelman, L., Soriano, M. E., Nuoffer, J., Scorrano, L., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05387-y · Cited by 190
Self-citationDysregulated Mitochondrial Dynamics and Metabolism in Obesity, Diabetes, and Cancer
Dai, W., & Jiang, L. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00570 · Cited by 186
The Mitochondrial Dynamism-Mitophagy-Cell Death Interactome
Dorn, G. W., & Kitsis, R. N. (2014) · Circulation Research · doi:10.1161/circresaha.116.303554 · Cited by 193
Mitofusin-2 Is a Major Determinant of Oxidative Stress-mediated Heart Muscle Cell Apoptosis
Shen, T., Zheng, M., Cao, C., Chen, C., Tang, J., Zhang, W., Cheng, H., Chen, K., & Xiao, R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702657200 · Cited by 189
Dimmer, K. S., Navoni, F., Casarin, A., Trevisson, E., Endele, S. U., Winterpacht, A., Salviati, L., & Scorrano, L. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm297 · Cited by 183
Self-citationMitofusin 2 Protects Cerebellar Granule Neurons against Injury-induced Cell Death
Jahani‐Asl, A., Cheung, E. C., Neuspiel, M., MacLaurin, J. G., Fortin, A., Park, D. S., McBride, H. M., & Slack, R. S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703812200 · Cited by 187
The ever-growing complexity of the mitochondrial fission machinery
Pagliuso, A., Cossart, P., & Stavru, F. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2603-0 · Cited by 192
Developmental and Tumor Angiogenesis Requires the Mitochondria-Shaping Protein Opa1
Herkenne, S., Ek, O., Zamberlan, M., Pellattiero, A., Chergova, M., Chivite, Í., Novotná, E., Rigoni, G., Fonseca, T. B., Samardžić, D., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.04.007 · Cited by 185
Self-citationLee, H., Smith, S. B., & Yoon, Y. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.762567 · Cited by 190
Mitochondrial dynamics in the regulation of neurogenesis: From development to the adult brain
Khacho, M., & Slack, R. S. (2017) · Developmental Dynamics · doi:10.1002/dvdy.24538 · Cited by 189
Onoguchi, K., Onomoto, K., Takamatsu, S., Jogi, M., Takemura, A., Morimoto, S., Julkunen, I., Namiki, H., Yoneyama, M., & Fujita, T. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1001012 · Cited by 180
Pathomechanisms of Mutant Proteins in Charcot-Marie-Tooth Disease
Niemann, A., Berger, P., & Suter, U. (2006) · NeuroMolecular Medicine · doi:10.1385/nmm:8:1-2:217 · Cited by 200
Neurodegeneration as a consequence of failed mitochondrial maintenance
Karbowski, M., & Neutzner, A. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0921-0 · Cited by 187
Ge, J., Zhang, C., Sun, Y., Zhang, Q., Lv, M., Guo, K., & Li, J. (2019) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2019.06.405 · Cited by 181
At the right distance: ER-mitochondria juxtaposition in cell life and death
Naon, D., & Scorrano, L. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.05.011 · Cited by 178
Self-citationIs Mitochondrial Dysfunction a Common Root of Noncommunicable Chronic Diseases?
Díaz‐Vegas, A., Sánchez-Aguilera, P., Krycer, J. R., Morales, P. E., Monsalves‐Álvarez, M., Cifuentes, M., Rothermel, B. A., & Lavandero, S. (2020) · Endocrine Reviews · doi:10.1210/endrev/bnaa005 · Cited by 179
Mitochondrial quality control in human health and disease
Liu, B., Xu, C.-Z., Liu, Y., Lu, Z., Fu, T.-L., Li, G., Deng, Y., Luo, G., Ding, S. Z., Li, N., et al. (2024) · Military Medical Research · doi:10.1186/s40779-024-00536-5 · Cited by 211
Mandemakers, W. J., Morais, V. A., & Strooper, B. D. (2007) · Journal of Cell Science · doi:10.1242/jcs.03443 · Cited by 183
Duvezin‐Caubet, S., Koppen, M., Wagener, J., Zick, M., Israel, L., Bernacchia, A., Jagasia, R., Rugarli, E. I., Imhof, A., Neupert, W., et al. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-02-0164 · Cited by 175
Cristae undergo continuous cycles of membrane remodelling in a MICOS‐dependent manner
Kondadi, A. K., Anand, R., Hänsch, S., Urbach, J., Zobel, T., Wolf, D. M., Segawa, M., Liesa, M., Shirihai, O. S., Weidtkamp‐Peters, S., et al. (2020) · EMBO Reports · doi:10.15252/embr.201949776 · Cited by 168
Metadata
- Authors
- Cipolat, S., de Brito, O. M., Dal Zilio, B., & Scorrano, L.
- Affiliations
- Veneto Institute of Molecular Medicine (IT)
- Dulbecco–Telethon Institute, Venetian Institute of Molecular Medicine, Via Orus 2, I-35129 Padua, Italy
- ORCID
- Scorrano, Luca
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2004-10-27
- Volume
- 101
- Issue
- 45
- Pages
- 15927-15932
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC528769
- OpenAlex
- W1989540421
- Cited by
- 1,300
- References
- 45
- Citations by year
- 2026: 46 · 2025: 76 · 2024: 64 · 2023: 74 · 2022: 75 · 2021: 88 · 2020: 90 · 2019: 82 · 2018: 73 · 2017: 59 · 2016: 66 · 2015: 50 · 2014: 58 · 2013: 53 · 2012: 63
- FWCI
- 10.44
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Padua Research Archive (University of Padova) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Keywords
- OPA1, mitofusin 1, mitofusin 2, mitochondrial fusion, mitochondrial fission, dynamin-related proteins, GTPase, coiled-coil domain, mitochondrial outer membrane, mitochondrial tubulation, autosomal dominant optic atrophy, mitochondrial morphology
- MeSH terms
- Animals, Cells, Cultured, Membrane Fusion, Mitochondria, Mice, Knockout, Gene Targeting, GTP Phosphohydrolases, RNA Interference, Mice, In Vitro Techniques
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