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
Research works printed but not linked: 1
- Wang, X. (2001) Genes Dev. 15, 2922–2933.11711427
Cited by
Sorted by citations
Items 901–1,000 of 1,000
Colla, A. L., Cámara, C. A., Campisano, S., & Chisari, A. N. (2022) · Nutrition Research Reviews · doi:10.1017/s0954422422000038 · Cited by 14
Characterisation of cold-induced mitochondrial fission in porcine aortic endothelial cells
Quiring, L., Walter, B., Lohaus, N., Schwan, D., Rech, A., Dlugos, A. M., & Rauen, U. (2022) · Molecular Medicine · doi:10.1186/s10020-021-00430-z · Cited by 13
A new role for phosphoinositides in regulating mitochondrial dynamics
Lourdes, S. R., Gurung, R., Giri, S., Mitchell, C. A., & McGrath, M. J. (2023) · Advances in Biological Regulation · doi:10.1016/j.jbior.2023.101001 · Cited by 16
Messina, F., Cecconi, F., & Rodolfo, C. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00271 · Cited by 14
The Effects of Regulatory Lipids on Intracellular Membrane Fusion Mediated by Dynamin-Like GTPases
Moon, Y., & Jun, Y. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00518 · Cited by 14
Insights into mitochondrial quality control pathways and Parkinson’s disease
Lehmann, S., & Martins, L. M. (2013) · Journal of Molecular Medicine · doi:10.1007/s00109-013-1044-y · Cited by 14
High‐throughput detection and quantification of mitochondrial fusion through imaging flow cytometry
Nascimento, A., Lannigan, J. A., & Kashatus, D. F. (2016) · Cytometry Part A · doi:10.1002/cyto.a.22891 · Cited by 14
Takahashi, K., Ohsawa, I., Shirasawa, T., & Takahashi, M. M. (2017) · Experimental Gerontology · doi:10.1016/j.exger.2017.09.002 · Cited by 15
Mitochondrial Dynamics: Shaping Metabolic Adaptation
Cantó, C. (2018) · International review of cytology · doi:10.1016/bs.ircmb.2018.05.004 · Cited by 15
Investigating the role of Sirtuins in cell reprogramming
Shin, J., Kim, J., Park, H., & Kim, J. (2018) · BMB Reports · doi:10.5483/bmbrep.2018.51.10.172 · Cited by 14
Esencan, E., Jiang, Z., Wang, T., Zhang, M., Imamoglu, G., & Seli, E. U. (2020) · Reproductive Sciences · doi:10.1007/s43032-019-00063-y · Cited by 14
Sisalli, M. J., Feliciello, A., Notte, S. D., Martino, R. D., Borzacchiello, D., Annunziato, L., & Scorziello, A. (2020) · Cell Calcium · doi:10.1016/j.ceca.2020.102193 · Cited by 14
Falco, F. D., Gentile, I., Cerino, P., Cutarelli, A., Cătoi, C., & Roperto, S. (2020) · Pathogens · doi:10.3390/pathogens9080621 · Cited by 14
Mitochondrial dynamics reveal potential to facilitate axonal regeneration after spinal cord injury
Wang, K., Chen, X., Liu, M., Li, Y., Zhu, Y., Zhou, T., Tao, W., Ma, Y., Guo, Y., Wang, L., et al. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-025-06611-2 · Cited by 13
Brain Mitochondria as a Therapeutic Target for Carnosic Acid
Infantino, V., Pappalardo, I., Santarsiero, A., Tripathi, S., Singh, G., & de Oliveira, M. R. (2024) · Journal of Integrative Neuroscience · doi:10.31083/j.jin2303053 · Cited by 13
Wang, N., Chen, J., Dang, Y., Zhao, X., Tibenda, J. J., Li, N., Zhu, Y., Wang, X., Zhao, Q., & Sun, L. (2024) · Life Sciences · doi:10.1016/j.lfs.2024.123045 · Cited by 16
Antiviral Mx proteins have an ancient origin and widespread distribution among eukaryotes
Langley, C. A., Dietzen, P. A., Emerman, M., Tenthorey, J. L., & Malik, H. S. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2416811122 · Cited by 13
The Role of N6-Methyladenosine in Mitochondrial Dysfunction and Pathology
Yan, W., Saqirile, Li, K., Li, K., & Wang, C. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26083624 · Cited by 13
Role of mitofusin 2 in cardiovascular oxidative injury
Zheng, M., & Xiao, R. (2010) · Journal of Molecular Medicine · doi:10.1007/s00109-010-0675-5 · Cited by 14
Dexmedetomidine Attenuates Lung Injury by Promoting Mitochondrial Fission and Oxygen Consumption
Zhang, J., Lin, Q., Liang, F.-Q., & Xie, T. (2019) · Medical Science Monitor · doi:10.12659/msm.913239 · Cited by 13
The role of mitochondrial fusion and fission in the process of cardiac oxidative stress.
Yu, F., Abdelwahid, E., Xu, T., Hu, L., Wang, M., Li, Y., Mogharbel, B. F., de Carvalho, K. A. T., Guarita-Souza, L. C., An, Y., et al. (2020) · PubMed · doi:10.14670/hh-18-191 · Cited by 14
On the offense and defense: mitochondrial recovery programs amidst targeted pathogenic assault
Mahmud, S. A., Qureshi, M. A., & Pellegrino, M. W. (2021) · FEBS Journal · doi:10.1111/febs.16126 · Cited by 13
Scott, I., & Logan, D. C. (2010) · Springer eBooks · doi:10.1007/978-0-387-89781-3_2 · Cited by 14
Mitochondrial dynamics in neurodegeneration: from cell death to energetic states
Khacho, M., & Slack, R. S. (2015) · AIMS molecular science · doi:10.3934/molsci.2015.2.161 · Cited by 13
The INs and OUTs of mitofusins
Giacomello, M., & Scorrano, L. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201801042 · Cited by 13
Self-citationRole of GTPases in the regulation of mitochondrial dynamics in Parkinson's disease
Zhang, X., Huang, W., Fan, Y.-Y., Sun, Y. J., & Ge, X. (2019) · Experimental Cell Research · doi:10.1016/j.yexcr.2019.06.005 · Cited by 14
Wu, N.-S., Ma, I.-C., Lin, Y., Ko, H.-J., Loh, J., & Hong, Y. (2023) · Cell Cycle · doi:10.1080/15384101.2023.2289753 · Cited by 14
Engineering Macrophage via Biomaterial-Mediated Mitochondrial Regulation: Mechanisms and Strategies
Li, J., He, M., Wan, S., Wang, S., Liu, N., Xin, L., & Chen, T. (2025) · Research · doi:10.34133/research.0883 · Cited by 14
Kawalec, M., Wojtyniak, P., Bielska, E., Lewczuk, A., Boratyńska-Jasińska, A., Beresewicz, M., Frontczak‐Baniewicz, M., Gewartowska, M., & Zabłocka, B. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2022.166633 · Cited by 13
Lanzillotta, S., Esteve, D., Lanzillotta, C., Tramutola, A., Lloret, A., Forte, E., Pesce, V., Picca, A., Domenico, F. D., Marzia Perluigi, A., et al. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.11.043 · Cited by 14
STAR/STARD1: A mitochondrial intermembrane space cholesterol shuttle degraded through mitophagy
Koganti, P. P., Zhao, A. H., Kern, M. C., Fassinou, A. C. R., & Selvaraj, V. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2508809122 · Cited by 12
del Campo, C. M. Z.-M., Rosas, M., & Guarner‐Lans, V. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19051456 · Cited by 12
Kloth, K., Synofzik, M., Kernstock, C., Schimpf-Linzenbold, S., Schuettauf, F., Neu, A., Wissinger, B., & Weisschuh, N. (2019) · BMC Medical Genetics · doi:10.1186/s12881-019-0795-x · Cited by 9
Mitochondrial Nascent Chain Quality Control Determines Organelle Form and Function
Battersby, B. J., Richter, U., & Safronov, O. (2019) · ACS Chemical Biology · doi:10.1021/acschembio.9b00518 · Cited by 12
Ataxia and spastic paraplegia in mitochondrial disease
Synofzik, M., Rugarli, E. I., Reid, E., & Schüle, R. (2023) · Handbook of clinical neurology · doi:10.1016/b978-0-12-821751-1.00009-9 · Cited by 12
Park, D., Yu, Y., Kim, J.-H., Lee, J., Park, J., Hong, K., Seo, J.-K., Lim, C., & Min, K. (2023) · Molecules and Cells · doi:10.14348/molcells.2023.2181 · Cited by 12
Reguera, D. P., Alán, L., Olejár, T., & Ježek, P. (2015) · International Journal of Oncology · doi:10.3892/ijo.2015.2953 · Cited by 12
Merging mitochondria for neuronal survival
Manfredi, G., & Beal, M. F. (2007) · Nature Medicine · doi:10.1038/nm1007-1140 · Cited by 12
Function and regulation of mitofusin 2 in cardiovascular physiology and pathology
Yu, F., Xu, T., Wang, M., Chang, W., Li, P., & Wang, J. (2018) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2018.07.003 · Cited by 12
Zhu, J., Yang, L., Chen, W.-L., Lin, W., Wang, Y., & Chen, T. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00325 · Cited by 12
Recessive ACO2 variants as a cause of isolated ophthalmologic phenotypes
Gibson, S., Azamian, M. S., Lalani, S. R., Yen, K. G., Sutton, V. R., & Scott, D. A. (2020) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.61634 · Cited by 12
Morphology Remodeling and Selective Autophagy of Intracellular Organelles during Viral Infections
Ren, S., Ding, C., & Sun, Y. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21103689 · Cited by 13
Opa1 Prevents Apoptosis and Cisplatin-Induced Ototoxicity in Murine Cochleae
Dong, T., Zhang, X., Liu, Y., Xu, S., Chang, H., Chen, F., Pan, L., Hu, S., Wang, M., & Lu, M. M. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.744838 · Cited by 12
Uchikado, Y., Ikeda, Y., Sasaki, Y., Iwabayashi, M., Akasaki, Y., & Ohishi, M. (2021) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2021.788655 · Cited by 14
Kumar, N., Singh, V. P., Li, L., Willard, B. B., Tripathi, A. K., & Dutta, R. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2021.779003 · Cited by 14
Diot, A., Guillou, E., Daloyau, M., Pelloquin, L., Emorine, L. J., & Belenguer, P. (2009) · Journal of Cell Science · doi:10.1242/jcs.040139 · Cited by 13
Sharma, A., Raut, S. S., Shukla, A. K., Singh, A. K., & Mishra, A. (2026) · Translational research · doi:10.1016/j.trsl.2026.03.004 · Cited by 14
UCP2 and pancreatic cancer: conscious uncoupling for therapeutic effect
Caggiano, E. G., & Taniguchi, C. M. (2024) · Cancer and Metastasis Reviews · doi:10.1007/s10555-023-10157-4 · Cited by 13
Atg44/Mdi1/mitofissin facilitates Dnm1-mediated mitochondrial fission
Furukawa, K., Hayatsu, M., Okuyama, K., Fukuda, T., Yamashita, S., Inoue, K., Shibata, S., & Kanki, T. (2024) · Autophagy · doi:10.1080/15548627.2024.2360345 · Cited by 12
Aquino, A., & Franzese, O. (2025) · Cancers · doi:10.3390/cancers17091547 · Cited by 13
Abraki, S. B., Karamali, F., & Nasr‐Esfahani, M. H. (2022) · Stem Cell Reviews and Reports · doi:10.1007/s12015-022-10338-8 · Cited by 11
Podinić, T., Werstuck, G. H., & Raha, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241311003 · Cited by 11
Extramitochondrial OPA1 and adrenocortical function
Fülöp, L., Rajki, A., Katona, D., Szanda, G., & Spät, A. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2013.07.021 · Cited by 13
Sihali-Beloui, O., Aroune, D., Benazouz, F., Hadji, A., El-Aoufi, S., & Marco, S. (2019) · Comptes Rendus Biologies · doi:10.1016/j.crvi.2019.04.003 · Cited by 11
Auto-fusion and the shaping of neurons and tubes
Soulavie, F., & Sundaram, M. V. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.07.018 · Cited by 11
Trophoblast Syncytialization: A Metabolic Crossroads
Podinić, T., MacAndrew, A., & Raha, S. (2023) · Results and problems in cell differentiation · doi:10.1007/978-3-031-37936-9_6 · Cited by 10
Teng, T., Zheng, Y., Zhang, M., Sun, G., Li, Z., Shi, B., & Shang, T. (2024) · Environmental Pollution · doi:10.1016/j.envpol.2024.124647 · Cited by 10
Mitochondrial Disorders Due to Nuclear OXPHOS Gene Defects
Ugalde, C., Morán, M., Blázquez, A., Arenas, J., & Martín, M. A. (2009) · Advances in experimental medicine and biology · doi:10.1007/978-90-481-2813-6_7 · Cited by 10
Tributyltin Inhibits Neural Induction of Human Induced Pluripotent Stem Cells
Yamada, S., Kubo, Y., Yamazaki, D., Sekino, Y., Nomura, Y., Yoshida, S., & Kanda, Y. (2018) · Scientific Reports · doi:10.1038/s41598-018-30615-2 · Cited by 10
Wang, B., Gan, W., Han, X., & Li, D. (2020) · Cell Biology International · doi:10.1002/cbin.11366 · Cited by 10
Recirculation and Residency of T Cells and Tregs: Lessons Learnt in Anacapri
Piconese, S., Campello, S., & Natalini, A. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00682 · Cited by 12
MITOCHONDRIA: Mitochondrial dynamics in the regulation of stem cells
Wade, S., & Khacho, M. (2022) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2022.106158 · Cited by 9
Piamsiri, C., Maneechote, C., Jinawong, K., Arunsak, B., Chunchai, T., Nawara, W., Kerdphoo, S., Chattipakorn, S. C., & Chattipakorn, N. (2024) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2024.176736 · Cited by 9
Mitochondrial motility modulators coordinate quality control dynamics to promote neuronal health
Jenkins, J. E., Fazli, M., & Evans, C. S. (2024) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2024.102383 · Cited by 9
Shi, J., Liu, M., Zhao, J. V., Tan, Y., & Jiang, C. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1485831 · Cited by 9
Rigoni, G., Calvo, E., Glytsou, C., Carro-Alvarellos, M., Noguchi, M., Semenzato, M., Quirin, C., Caicci, F., Meneghetti, N., Sturlese, M., et al. (2025) · Cell Metabolism · doi:10.1016/j.cmet.2025.01.017 · Cited by 9
Self-citationYuan, L., Jiang, X.-R., Ren, Y., Ma, B., Ji, Z.-H., Wang, S.-B., Hao, B., Li, C.-W., Li, R., & Liu, F.-P. (2025) · Poultry Science · doi:10.1016/j.psj.2025.105034 · Cited by 9
Liu, X., Ma, Y., Wang, X., Zhang, X. W., Shen, C., Su, Y., Chang, X., Zhou, H., & Liu, J. (2025) · Journal of Advanced Research · doi:10.1016/j.jare.2025.09.046 · Cited by 10
Correlation between polymorphisms in the MFN1 gene and myopia in Chinese population.
Zou, Y., Lei, J.-H., Wang, Y., & Xu, S. (2015) · Europe PMC (PubMed Central) · doi:10.3980/j.issn.2222-3959.2015.06.08 · Cited by 9
Szabo, L., Grimm, A., García‐León, J. A., Verfaillie, C. M., & Eckert, A. (2023) · Cells · doi:10.3390/cells12101385 · Cited by 9
Metabolism and Biological Function of Cardiolipin
Nakagawa, Y. (2013) · YAKUGAKU ZASSHI · doi:10.1248/yakushi.13-00052 · Cited by 9
Liu, Z. F., Wang, H. M., Jiang, M., Wang, L., Lin, L. J., Zhao, Y., Shao, J. J., Zhou, J., Xie, M. J., Li, X., et al. (2021) · PubMed · doi:10.3967/bes2021.001 · Cited by 9
How signaling pathways link extracellular mechano‐environment to proline biosynthesis: A hypothesis
Chen, K., Guo, L., & Wu, C. (2021) · BioEssays · doi:10.1002/bies.202100116 · Cited by 9
Li, L., Yu, Q. Z., & Liang, W. (2014) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2014.10.011 · Cited by 9
Mdivi-1 attenuates sodium azide-induced apoptosis in H9c2 cardiac muscle cells
Xu, X., Luo, C., Zhang, Z., Hu, J., Gao, X., Zuo, Y., Wang, Y., & Zhu, S. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.7359 · Cited by 10
Mitochondrial Dynamics and Apoptosis
Harwig, M. C., & Youle, R. J. (2011) · Springer eBooks · doi:10.1007/978-94-007-1291-1_4 · Cited by 9
Wang, X., Zhu, Z., Jia, H., Lu, X., Zhang, Y., Zhu, Y., Wang, J., Wang, Y., Tan, R., & Yuan, J. (2025) · Chinese Medical Journal · doi:10.1097/cm9.0000000000003704 · Cited by 8
Hu, C., Lin, Y., Zhang, C., Yang, J., Lin, M., Cui, Y., Su, Y. J., Jiang, X., Zhang, W., Xu, J., et al. (2025) · Journal of Controlled Release · doi:10.1016/j.jconrel.2025.114051 · Cited by 8
Hines, T. J., Bailey, J., Liu, H., Guntur, A. R., Seburn, K. L., Pratt, S. L., Funke, J. R., Tarantino, L. M., & Burgess, R. W. (2023) · Biology · doi:10.3390/biology12070953 · Cited by 9
ECSIT: Biological function and involvement in diseases
Zhang, T., Fan, J., Wen, X., & Duan, X. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.113524 · Cited by 8
Mitochondria, Oxidative Stress, Cancer, and Aging
Pecorini, S., Gibellini, L., Biasi, S. D., Bianchini, E., Nasi, M., Cossarizza, A., & Pinti, M. (2020) · Springer eBooks · doi:10.1007/978-3-319-57415-8_80 · Cited by 8
Mitochondria-targeted drug delivery in neurodegenerative diseases
Chidambaram, S. B., Ray, B., Bhat, A., Mahalakshmi, A. M., Sunanda, T., Jagadeeswari, P., Gowrav, M. P., Chandra, R., & Sakharkar, M. K. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-817776-1.00005-5 · Cited by 7
Mitochondrial Membrane Intracellular Communication in Healthy and Diseased Myocardium
Kumar, V. K., Lackey, A. I., Snyder, J. E., Karhadkar, S. S., Rao, A. D., DiCarlo, A., & Sato, P. Y. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.609241 · Cited by 8
Research Progress in the Structure and Functions of Prohibitin
Ou, J., HUANG, S.-F., & Chen, H. (2010) · Chin J Reprod Contracep · doi:10.1016/s1001-7844(10)60020-x · Cited by 8
Autophagy, Mitochondrial Dynamics, and Retinal Diseases
Kaden, T. R., & Li, W. (2013) · Asia-Pacific Journal of Ophthalmology · doi:10.1097/apo.0b013e31829d3e33 · Cited by 8
Mitochondrial shaping proteins as novel treatment targets for cardiomyopathies.
Kalkhoran, S. B., Hernández‐Reséndiz, S., Ong, S., Ramachandra, C. J. A., & Hausenloy, D. J. (2020) · PubMed · Cited by 8
Chen, P., Chang, C., Lin, W., Nagabhushanam, K., Ho, C., & Pan, M. (2022) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.202101077 · Cited by 8
Vanmunster, M., Rojo‐García, A. V., Pacolet, A., Jonkers, I., Koppo, K., Lories, R. J. U., & Suhr, F. (2023) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00204.2023 · Cited by 7
Zhou, J., Xi, Y., Wu, T., Zeng, X., Yuan, J., Peng, L., Fu, H., & Zhou, C. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1506292 · Cited by 10
Carbajal, C., Rodriguez, M., Owens, F., Stone, N., Veeragoni, D., Fan, R. Z., Tieu, K., & El‐Hage, N. (2025) · Pharmaceutics · doi:10.3390/pharmaceutics17030365 · Cited by 7
The role of mitochondria-endoplasmic reticulum crosstalk in colorectal cancer
Xiao, L., Wei, Y., Qin, Y., & Guo, B. (2025) · Genes & Diseases · doi:10.1016/j.gendis.2025.101766 · Cited by 7
Shi, R., Zhu, H., Zou, B., Xiong, Y., Zhang, X., Wu, Y., Zhu, L., Bai, Y., Shang, Y., Liu, J., et al. (2025) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2025.119348 · Cited by 7
Choi, S.-I., Lee, G., Woo, J.-H., Jun, I., & Kim, E. K. (2023) · Genes · doi:10.3390/genes14030566 · Cited by 7
Brandão, S. R., Ferreira, R. M., & Rocha, H. (2019) · Archives of Physiology and Biochemistry · doi:10.1080/13813455.2019.1628065 · Cited by 6
Does mitochondrial fusion require transmembrane potential?
Karavaeva, I. E., Shekhireva, K. V., Severin, F. F., & Кнорре, Д. А. (2015) · Biochemistry (Moscow) · doi:10.1134/s0006297915050053 · Cited by 8
From dynamin related proteins structures and oligomers to membrane fusion mediated by mitofusins
Ozeir, M., & Cohen, M. M. (2022) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2022.148913 · Cited by 7
Research progress on ncRNAs regulation of mitochondrial dynamics in diabetes
Wu, Y., Lan, H., Zhang, D., Hu, Z., Zhang, J., Li, Z., Xia, P., Tang, X., Cai, X., & Yu, P. (2022) · Journal of Cellular Physiology · doi:10.1002/jcp.30878 · Cited by 7
Lysakowski, A., Govindaraju, A. C., & Raphael, R. M. (2022) · Hearing Research · doi:10.1016/j.heares.2022.108612 · Cited by 8
Maculopapillary Bundle Degeneration in Optic Neuropathies
Lambiri, D. W., & Levin, L. A. (2024) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-024-01343-0 · Cited by 7
Mitochondrial Function and Neurodegenerative Diseases
Wilkins, H. M., Weidling, I., Koppel, S., Wang, X., von Schulze, A., & Swerdlow, R. H. (2018) · The Molecular and Cellular Basis of Neurodegenerative Diseases · doi:10.1016/b978-0-12-811304-2.00013-4 · Cited by 2
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