The DOI matches its Crossref record; 53 of the 53 references it cites were found in a registry or an index.
Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development
Open accessAbstract
Mitochondrial morphology is determined by a dynamic equilibrium between organelle fusion and fission, but the significance of these processes in vertebrates is unknown. The mitofusins, Mfn1 and Mfn2, have been shown to affect mitochondrial morphology when overexpressed. We find that mice deficient in either Mfn1 or Mfn2 die in midgestation. However, whereas Mfn2 mutant embryos have a specific and severe disruption of the placental trophoblast giant cell layer, Mfn1-deficient giant cells are normal. Embryonic fibroblasts lacking Mfn1 or Mfn2 display distinct types of fragmented mitochondria, a phenotype we determine to be due to a severe reduction in mitochondrial fusion. Moreover, we find that Mfn1 and Mfn2 form homotypic and heterotypic complexes and show, by rescue of mutant cells, that the homotypic complexes are functional for fusion. We conclude that Mfn1 and Mfn2 have both redundant and distinct functions and act in three separate molecular complexes to promote mitochondrial fusion. Strikingly, a subset of mitochondria in mutant cells lose membrane potential. Therefore, mitochondrial fusion is essential for embryonic development, and by enabling cooperation between mitochondria, has protective effects on the mitochondrial population.
Overview
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
Cites
Statistics
Verification
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?
In the citing paper
“Genetic loss of MFN1 induces a higher degree of mitochondrial fragmentation than MFN2 deletion [60].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [60]
In the citing paper
“Mitochondrial fusion rates correlate with the OXPHOS capacity, higher in oxidative fibers than in glycolytic fibers [60].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [60]
In the citing paper
“The full knockout mice of either Mfn1, Mfn2, or OPA1 result in embryonic lethality of mice, demonstrating the biological importance of mitochondrial fusion in early development [60, 178].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [60]
In the citing paper
“Both Mfn proteins mediate fusion through their active GTPase domains by tethering opposing mitochondrial membranes (Chen et al., 2003; Eura et al., 2003).”
From New insights into the role of mitochondria in aging: mitochondrial dynamics and more (2010) · cites this paper as Chen et al., 2003
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
The GTPase superfamily: conserved structure and molecular mechanism
Bourne, H. R., Sanders, D. A., & McCormick, F. (1991) · Nature · doi:10.1038/349117a0 · Cited by 3,392
Close Contacts with the Endoplasmic Reticulum as Determinants of Mitochondrial Ca 2+ Responses
Rizzuto, R., Pinton, P., Carrington, W., Fay, F. S., Fogarty, K. E., Lifshitz, L. M., Tuft, R. A., & Pozzan, T. (1998) · Science · doi:10.1126/science.280.5370.1763 · Cited by 2,257
Regulation of Rate of Cartilage Differentiation by Indian Hedgehog and PTH-Related Protein
Vortkamp, A., Lee, K., Lanske, B., Segre, G. V., Kronenberg, H. M., & Tabin, C. J. (1996) · Science · doi:10.1126/science.273.5275.613 · Cited by 1,999
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
Promotion of Trophoblast Stem Cell Proliferation by FGF4
Tanaka, S., Kunath, T., Hadjantonakis, A., Nagy, A., & Rossant, J. (1998) · Science · doi:10.1126/science.282.5396.2072 · Cited by 1,370
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
G PROTEIN MECHANISMS: Insights from Structural Analysis
Sprang, S. R. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.639 · Cited by 1,057
Control of mitochondrial morphology by a human mitofusin
Santel, A., & Fuller, M. T. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.5.867 · Cited by 1,012
Bereiter‐Hahn, J., & Vöth, M. (1994) · Microscopy Research and Technique · doi:10.1002/jemt.1070270303 · Cited by 900
Flagged first, then by citations
Research works printed but not linked: 3
- 1981, Eur. J. Cell Biol., 25, 175
- 1986, Mol. Cell. Biol., 6, 1204
- 1998, Mol. Med. Today., 4, 286
Cited by
Sorted by citations
Items 901–1,000 of 1,010
Label-Free Quantification of Intracellular Mitochondrial Dynamics Using Dielectrophoresis
Rohani, A., Moore, J. H., Kashatus, J. A., Sesaki, H., Kashatus, D. F., & Swami, N. S. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.6b04666 · Cited by 63
Mitochondria, Bioenergetics and Excitotoxicity: New Therapeutic Targets in Perinatal Brain Injury
Leaw, B., Nair, S., Lim, R., Thornton, C., Mallard, C. E., & Hagberg, H. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00199 · Cited by 64
Spurlock, B., Tullet, J. M. A., Hartman, J. L., & Mitra, K. (2020) · Experimental Gerontology · doi:10.1016/j.exger.2020.110919 · Cited by 60
Distribution and Apoptotic Function of Outer Membrane Proteins Depend on Mitochondrial Fusion
Weaver, D., Eisner, V., Liu, X., Várnai, P., Hunyady, L., Gross, A., & Hajnóczky, G. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.048 · Cited by 58
Mitochondria-associated membranes: A hub for neurodegenerative diseases
Liu, J., & Yang, J. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.112890 · Cited by 67
Lacombe, A., & Scorrano, L. (2024) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2024.02.001 · Cited by 65
Zhang, X., Ladd, A. C., Dragoescu, E. A., Budd, W. T., Ware, J. L., & Zehner, Z. E. (2009) · Clinical & Experimental Metastasis · doi:10.1007/s10585-009-9287-2 · Cited by 61
Sundararajan, R., Chen, G., Mukherjee, C., & White, E. (2005) · Oncogene · doi:10.1038/sj.onc.1208681 · Cited by 61
Lysine deacetylases and mitochondrial dynamics in neurodegeneration
Guedes-Dias, P., & Oliveira, J. M. A. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.04.005 · Cited by 63
Phenotypic spectrum of MFN2 mutations in the Spanish population
Casasnovas, C., Banchs, I., Cassereau, J., Guéguen, N., Chevrollier, A., Martínez‐Matos, J. A., Bonneau, D., & Volpini, V. (2009) · Journal of Medical Genetics · doi:10.1136/jmg.2009.072488 · Cited by 61
GASZ and mitofusin‐mediated mitochondrial functions are crucial for spermatogenesis
Zhang, J., Wang, Q., Wang, M., Jiang, M., Wang, Y., Sun, Y. W., Wang, J., Xie, T., Tang, C. S., Tang, N., et al. (2015) · EMBO Reports · doi:10.15252/embr.201540846 · Cited by 61
The little big genome the organization of mitochondrial DNA
Gilkerson, R. (2016) · Frontiers in bioscience · doi:10.2741/4511 · Cited by 64
Xu, Y., Mei, Y., Shi, X.-Q., Yi-fang, Z., Wang, X., Guan, L., Wang, Q., & Pan, H. (2019) · Brain Research · doi:10.1016/j.brainres.2019.05.037 · Cited by 61
Mitochondria and heart failure: new insights into an energetic problem.
Chen, L., & Knowlton, A. A. (2010) · PubMed · Cited by 62
Casinelli, G., LaRosa, J., Sharma, M., Cherok, E., Banerjee, S., Branca, M., Edmunds, L., Wang, Y., Sims-Lucas, S., Churley, L., et al. (2016) · Cell Death Discovery · doi:10.1038/cddiscovery.2016.82 · Cited by 52
Mitochondrial Fission Mediated Cigarette Smoke–induced Pulmonary Endothelial Injury
Wang, Z., White, A., Wang, X., Ko, J., Choudhary, G., Lange, T. S., Rounds, S., & Lü, Q. (2020) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2020-0008oc · Cited by 63
Mitochondrial dynamics regulators: implications for therapeutic intervention in cancer
Kumar, S., Ashraf, R., & Aparna, C. K. (2021) · Cell Biology and Toxicology · doi:10.1007/s10565-021-09662-5 · Cited by 61
Liu, Y., Qiao, Y., Pan, S., Chen, J., Mao, Z., Ren, K., Yang, Y., Feng, Q., Liu, D., & Liu, Z. (2023) · International Journal of Biological Sciences · doi:10.7150/ijbs.86608 · Cited by 60
Soriano, M. E., & Scorrano, L. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-6706-0_6 · Cited by 60
Calcium Dynamics Mediated by the Endoplasmic/Sarcoplasmic Reticulum and Related Diseases
Reddish, F. N., Miller, C. L., Gorkhali, R., & Yang, J. J. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18051024 · Cited by 60
Lu, Y., Chen, L., Ye, J., Chen, C., Zhou, Y., Li, K., Zhang, Z., & Peng, M. (2020) · Aging · doi:10.18632/aging.102659 · Cited by 64
Mitochondrial functions and rare diseases
Dard, L., Blanchard, W., Hubert, C., Lacombe, D., & Rossignol, R. (2020) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2019.100842 · Cited by 65
Mitochondrial fission and apoptosis: An ongoing trial
Parone, P. A., & Martinou, J. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.04.005 · Cited by 60
Mitofusin 2-Deficiency Suppresses Cell Proliferation through Disturbance of Autophagy
Ding, Y., Gao, H., Zhao, L., Wang, X., & Zheng, M. (2015) · PLOS ONE · doi:10.1371/journal.pone.0121328 · Cited by 59
Chen, K.-L., Wang, H., Jiang, L.-Z., Qian, Y., Yang, C., Chang, W.-W., Zhong, J., & Xing, G. (2020) · In Vitro Cellular & Developmental Biology - Animal · doi:10.1007/s11626-020-00446-5 · Cited by 61
The Multifaceted Regulation of Mitochondrial Dynamics During Mitosis
Pangou, E., & Sumara, I. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.767221 · Cited by 66
Zika Virus Neuropathogenesis: The Different Brain Cells, Host Factors and Mechanisms Involved
Komarasamy, T. V., Adnan, N. A. A., James, W., & Balasubramaniam, V. R. M. T. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.773191 · Cited by 58
Mitochondrial dynamics define muscle fiber type by modulating cellular metabolic pathways
Yasuda, T., Ishihara, T., Ichimura, A., & Ishihara, N. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112434 · Cited by 64
Mitofusin-2 is a novel direct target of p53
Wang, W., Cheng, X., Lu, J., Wei, J., Fu, G., Zhu, F., Jia, C., Zhou, L., Xie, H., & Zheng, S. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.08.108 · Cited by 60
Arduíno, D. M., Esteves, A. R., & Cardoso, S. M. (2011) · Parkinson s Disease · doi:10.4061/2011/767230 · Cited by 61
Reinventing an Organelle: The Reduced Mitochondrion in Parasitic Protists
Santos, H. J., Makiuchi, T., & Nozaki, T. (2018) · Trends in Parasitology · doi:10.1016/j.pt.2018.08.008 · Cited by 61
The rOX‐stars of inflammation: links between the inflammasome and mitochondrial meltdown
Holley, C. L., & Schroder, K. (2020) · Clinical & Translational Immunology · doi:10.1002/cti2.1109 · Cited by 61
Mitochondrial Protection by PARP Inhibition
Gallyas, F., & Sümegi, B. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21082767 · Cited by 58
Gu, Y., Zhao, X., Zhang, N., Yang, Y., Yi, Y., Shao, Q.-H., Liu, M.-X., & Zhang, X.-L. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102577 · Cited by 60
Mitochondrial changes associated with demyelination: Consequences for axonal integrity
Campbell, G. R., & Mahad, D. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.03.007 · Cited by 60
Mitochondria‐type GPAT is required for mitochondrial fusion
Ohba, Y., Sakuragi, T., Kage‐Nakadai, E., Tomioka, N. H., Kono, N., Imae, R., Inoue, A., Aoki, J., Ishihara, N., Inoué, T., et al. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.77 · Cited by 62
Liu, T., Yu, R., Jin, S., Han, L., Lendahl, U., Zhao, J., & Nistér, M. (2013) · Experimental Cell Research · doi:10.1016/j.yexcr.2013.07.010 · Cited by 58
Gall, J. M., Wang, Z., Bonegio, R. G. B., Havasi, A., Liesa, M., Vemula, P., & Borkan, S. C. (2014) · Journal of the American Society of Nephrology · doi:10.1681/asn.2014010126 · Cited by 57
Kamogashira, T., Hayashi, K., Fujimoto, C., Iwasaki, S., & Yamasoba, T. (2017) · npj Aging and Mechanisms of Disease · doi:10.1038/s41514-017-0002-2 · Cited by 60
Marcu, R., Zheng, Y. Y., & Hawkins, B. J. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-55330-6_21 · Cited by 60
Weatherly, L. M., Nelson, A. J., Shim, J., Riitano, A. M., Gerson, E., Hart, A. J., de Juan‐Sanz, J., Ryan, T. A., Sher, R. B., Hess, S. T., et al. (2018) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2018.04.005 · Cited by 58
Mortal engines: Mitochondrial bioenergetics and dysfunction in neurodegenerative diseases
Joshi, A. U., & Mochly‐Rosen, D. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.08.010 · Cited by 57
Two separate functions of NME3 critical for cell survival underlie a neurodegenerative disorder
Chen, C., Wang, H., Huang, C.-W., Huang, C.-Y., Lim, W. K., Tu, I.-C., Koorapati, A., Hsieh, S., Kan, H., Tzeng, S., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1818629116 · Cited by 56
The Complexity of Making Ubiquinone
Wang, Y., & Hekimi, S. (2019) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2019.08.009 · Cited by 58
The influence of aerobic exercise on mitochondrial quality control in skeletal muscle
Philp, A. M., Saner, N. J., Lazarou, M., Ganley, I. G., & Philp, A. (2020) · The Journal of Physiology · doi:10.1113/jp279411 · Cited by 62
Hiendleder, S., Zakhartchenko, V., & Wolf, E. (2004) · Reproduction Fertility and Development · doi:10.1071/rd04115 · Cited by 58
Interorganelle communication, aging, and neurodegenerationPreprint
Petković, M., O’Brien, C. E., & Jan, Y. N. (2021) · Genes & Development · doi:10.1101/gad.346759.120 · Cited by 58
Gong, Y., Lin, J., Ma, Z., Yu, M., Wang, M., Lai, D., & Fu, G. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119511 · Cited by 58
Wu, H., Wei, H., Sehgal, S. A., Liu, L., & Chen, Q. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.03.030 · Cited by 58
Bifari, F., Dolci, S., Bottani, E., Pino, A., Chio, M. D., Zorzin, S., Ragni, M., Zamfir, R. G., Brunetti, D., Bardelli, D., et al. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.104863 · Cited by 56
Pharmacological inhibition of USP30 activates tissue‐specific mitophagy
Luo, H., Krigman, J., Zhang, R., Yang, M., & Sun, N. (2021) · Acta Physiologica · doi:10.1111/apha.13666 · Cited by 56
Zou, G.-P., Yu, C., Shi, S.-L., Li, Q.-G., Wang, X.-H., Qu, X.-H., Yang, Z., Yao, W.-R., Yan, D., Jiang, L., et al. (2021) · Journal of Cancer · doi:10.7150/jca.61379 · Cited by 57
The Role of Mitochondrial Dynamic Dysfunction in Age-Associated Type 2 Diabetes
Vezza, T., Díaz-Pozo, P., Canet, F., de Marañón, A. M., Abad-Jiménez, Z., García-Gargallo, C., Roldan, I., Solá, E., Bañuls, C., López‐Domènech, S., et al. (2022) · The World Journal of Men s Health · doi:10.5534/wjmh.210146 · Cited by 59
New insights into mitochondrial fusion
Zhang, Y., & Chan, D. C. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.01.095 · Cited by 59
Self-citationAnticancer DNA intercalators cause p53-dependent mitochondrial DNA nucleoid re-modelling
Ashley, N., & Poulton, J. (2009) · Oncogene · doi:10.1038/onc.2009.242 · Cited by 57
Losón, O. C., Meng, S., Ngo, H., Liu, R., Kaiser, J. T., & Chan, D. C. (2015) · Protein Science · doi:10.1002/pro.2629 · Cited by 57
Self-citationAnimal models of inherited neuropathies
zu Hörste, G. M., & Nave, K. (2006) · Current Opinion in Neurology · doi:10.1097/01.wco.0000245369.44199.27 · Cited by 57
Developmental Effects of Sublethal Mitochondrial Injury in Mouse Oocytes1
Thouas, G. A., Trounson, A. O., & Jones, G. M. (2006) · Biology of Reproduction · doi:10.1095/biolreprod.105.048611 · Cited by 57
Mitophagy as a Protective Mechanism against Myocardial Stress
Nah, J., Miyamoto, S., & Sadoshima, J. (2017) · Comprehensive physiology · doi:10.1002/cphy.c170005 · Cited by 60
Mitochondrial Quality Control: A Pathophysiological Mechanism and Therapeutic Target for Stroke
Yang, M., He, Y. T., Deng, S., Xiao, L., Tian, M., Xin, Y., Lu, C., Zhao, F., & Gong, Y. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.786099 · Cited by 56
Targeting mitochondrial shape: at the heart of cardioprotection
Hernández‐Reséndiz, S., Prakash, A., Loo, S. J., Semenzato, M., Chinda, K., Crespo-Avilan, G. E., Dam, L. C., Lu, S., Scorrano, L., & Hausenloy, D. J. (2023) · Basic Research in Cardiology · doi:10.1007/s00395-023-01019-9 · Cited by 57
The Phosphorylation-Dependent Regulation of Mitochondrial Proteins in Stress Responses
Kanamaru, Y., Sekine, S., Ichijo, H., & Takeda, K. (2012) · Journal of Signal Transduction · doi:10.1155/2012/931215 · Cited by 62
Structures of the yeast dynamin-like GTPase Sey1p provide insight into homotypic ER fusion
Yan, L., Sun, S., Wang, W., Shi, J., Hu, X., Wang, S., Su, D., Rao, Z., Hu, J., & Lou, Z. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201502078 · Cited by 56
Update on Charcot–Marie–Tooth disease
Gutmann, L., & Shy, M. E. (2015) · Current Opinion in Neurology · doi:10.1097/wco.0000000000000237 · Cited by 56
Oligomerization of Dynamin Superfamily Proteins in Health and Disease
Faelber, K., Gao, S., Held, M., Posor, Y., Haucke, V., Noé, F., & Daumke, O. (2013) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-386931-9.00015-5 · Cited by 53
Lan, B., He, Y., Sun, H., Zheng, X., Gao, Y., & Li, N. (2019) · Life Sciences · doi:10.1016/j.lfs.2019.116587 · Cited by 58
Therapeutic applications of mitochondrial transplantation
Ülger, Ö., & Kubat, G. B. (2022) · Biochimie · doi:10.1016/j.biochi.2022.01.002 · Cited by 56
Mitochondrial protein quality control in health and disease
Baker, M. J., Palmer, C. S., & Stojanovski, D. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12430 · Cited by 60
Nanoparticle (NP) uptake by type I alveolar epithelial cells and their oxidant stress response
VanWinkle, B., Bentley, K. L. D. M., Malecki, J., Gunter, K. K., Evans, I. M., Elder, A. C. P., Finkelstein, J. N., Oberdörster, G., & Gunter, T. E. (2009) · Nanotoxicology · doi:10.1080/17435390903121949 · Cited by 55
Zhu, M., Li, W., & Lü, C. (2013) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.12217 · Cited by 55
Get the balance right: Mitofusins roles in health and disease
Santel, A. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.02.004 · Cited by 55
Lentz, S. I., Edwards, J. L., Backus, C., McLean, L. L., Haines, K. M., & Feldman, E. L. (2009) · Journal of Histochemistry & Cytochemistry · doi:10.1369/jhc.2009.954701 · Cited by 56
Mitochondrial involvement in cell death of non-mammalian eukaryotes
Abdelwahid, E., Rolland, S. G. M., Teng, X., Conradt, B., Hardwick, J. M., & White, K. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.10.008 · Cited by 57
Mitochondrial dynamics coordinate cell differentiation
Noguchi, M., & Kasahara, A. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.06.094 · Cited by 52
Mitochondrial dynamics, mitophagy and biogenesis in neonatal hypoxic‐ischaemic brain injury
Thornton, C., Jones, A., Nair, S., Aabdien, A., Mallard, C. E., & Hagberg, H. (2017) · FEBS Letters · doi:10.1002/1873-3468.12943 · Cited by 58
Daste, F., Sauvanet, C., Bavdek, A., Baye, J., Pierre, F., Borgne, R. L., David, C., Rojo, M., Fuchs, P., & Tareste, D. C. (2018) · EMBO Reports · doi:10.15252/embr.201643637 · Cited by 54
Wang, L., Gao, J., Liu, J., Siedlak, S. L., Torres, S. L., Fujioka, H., Huntley, M. L., Jiang, Y., Ji, H., Yan, T., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.06.011 · Cited by 55
Deciphering OPA1 mutations pathogenicity by combined analysis of human, mouse and yeast cell models
Dotto, V. D., Fogazza, M., Musiani, F., Maresca, A., Aleo, S. J., Caporali, L., Morgia, C. L., Nolli, C., Lodi, T., Goffrini, P., et al. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.08.004 · Cited by 55
Self-citationWestermann, B. (2003) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(03)00091-0 · Cited by 55
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
Clueless/CLUH regulates mitochondrial fission by promoting recruitment of Drp1 to mitochondria
Yang, H. M., Sibilla, C., Liu, R., Yun, J., Hay, B. A., Blackstone, C. D., Chan, D. C., Harvey, R. J., & Guo, M. (2022) · Nature Communications · doi:10.1038/s41467-022-29071-4 · Cited by 60
Self-citationMfn2 Affects Embryo Development via Mitochondrial Dysfunction and Apoptosis
Zhao, N., Zhang, Y., Liu, Q., & Xiang, W. (2015) · PLoS ONE · doi:10.1371/journal.pone.0125680 · Cited by 54
Rath, E., & Haller, D. (2011) · Inflammatory Bowel Diseases · doi:10.1002/ibd.21944 · Cited by 55
Eschbach, J., Sinniger, J., Bouitbir, J., Fergani, A., Schlagowski, A.-I., Zoll, J., Gény, B., René, F., Larmet, Y., Marion, V., et al. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.05.015 · Cited by 54
Vettori, A., Bergamin, G., Moro, E., Vazza, G., Polo, G., Tiso, N., Argenton, F., & Mostacciuolo, M. L. (2010) · Neuromuscular Disorders · doi:10.1016/j.nmd.2010.09.002 · Cited by 54
Molecular basis of axonal dysfunction and traffic impairments in CMT
Gentil, B. J., & Cooper, L. (2012) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2012.05.003 · Cited by 54
Optimal Dynamics for Quality Control in Spatially Distributed Mitochondrial Networks
Patel, P. K., Shirihai, O. S., & Huang, K. C. (2013) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003108 · Cited by 54
Mitochondrial–nuclear epistasis: Implications for human aging and longevity
Tranah, G. J. (2010) · Ageing Research Reviews · doi:10.1016/j.arr.2010.06.003 · Cited by 55
Junctophilin-1 is a modifier gene of GDAP1-related Charcot–Marie–Tooth disease
Pla‐Martín, D., Calpena, E., Lupo, V., Márquez, C., Rivas, E., Sivera, R., Sevilla, T., Palau, F., & Espinós, C. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu440 · Cited by 57
Activation of Mitofusin2 by Smad2-RIN1 Complex during Mitochondrial Fusion
Kumar, S., Pan, C. C., Shah, N. R., Wheeler, S. E., Hoyt, K. R., Hempel, N., Mythreye, K., & Lee, N. Y. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.04.010 · Cited by 54
Carreras‐Sureda, A., Pihán, P., & Hetz, C. A. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00055 · Cited by 57
Astrocytes Attenuate Mitochondrial Dysfunctions in Human Dopaminergic Neurons Derived from iPSC
Du, F., Yu, Q., Chen, A., Chen, D., & Yan, S. S. (2018) · Stem Cell Reports · doi:10.1016/j.stemcr.2017.12.021 · Cited by 54
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
Ullah, R., Rauf, N., Nabi, G., Shen, Y., Yu-Dong, Z., & Fu, J. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.112012 · Cited by 64
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
Rudokas, M. W., McKay, M., Toksoy, Z., Eisen, J. N., Bögner, M., Young, L. H., & Akar, F. G. (2024) · Cardiovascular Diabetology · doi:10.1186/s12933-024-02357-1 · Cited by 55
BDNF-TrkB Signaling in Mitochondria: Implications for Neurodegenerative Diseases
Soman, S. K., Swain, M., & Dagda, R. K. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04357-4 · Cited by 57
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
Characterization of the mitofusin 2 R94W mutation in a knock‐in mouse model
Strickland, A. V., Rebelo, A. P., Zhang, F., Price, J. H., Bolon, B. N., Silva, J. P., Wen, R., & Zuchner, S. L. (2014) · Journal of the Peripheral Nervous System · doi:10.1111/jns5.12066 · Cited by 53
Khacho, M., & Slack, R. S. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7228 · Cited by 54
Metadata
- Authors
- Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., & Chan, D. C.
- Affiliations
- California Institute of Technology (US)
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2003-01-13
- Volume
- 160
- Issue
- 2
- Pages
- 189-200
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2172648
- OpenAlex
- W2073095545
- Cited by
- 2,601
- References
- 52
- Citations by year
- 2026: 111 · 2025: 132 · 2024: 143 · 2023: 149 · 2022: 173 · 2021: 192 · 2020: 170 · 2019: 149 · 2018: 160 · 2017: 127 · 2016: 121 · 2015: 115 · 2014: 126 · 2013: 103 · 2012: 112
- FWCI
- 14.48
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion, cc-by-nc-sa)
- Warwick Research Archive Portal (University of Warwick) (submittedVersion)
- Funders
- National Institute of General Medical Sciences (1 R01 GM62967-01, R01GM062967, T32GM007616, GM07616)
- 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 › Cell death mechanisms and regulation
- Keywords
- mitofusins, Mfn1, mitofusin 2, mitochondrial fusion, mitochondrial fission, mitochondrial morphology, embryonic development, mitochondrial membrane potential, mitochondrial fragmentation, embryonic fibroblasts, mouse mutants
- MeSH terms
- Animals, Cell Movement, Cells, Cultured, Cytoskeletal Proteins, Embryo, Mammalian, Female, Embryonic and Fetal Development, Fetus, Genes, Lethal, Intracellular Membranes, Male, Membrane Potentials, Membrane Proteins, Mitochondria, Placenta, Trophoblasts, Mice, Knockout, Gene Expression Regulation, Developmental, GTP Phosphohydrolases, Embryo Loss, Mitochondrial Proteins, Membrane Transport Proteins, Mitochondrial Membrane Transport Proteins, Macromolecular Substances, Utrophin, Mice
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
