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 501–600 of 1,010
Miret‐Casals, L., Sebastián, D., Brea, J. M., Rico-Leo, E. M., Palacín, M., Fernández‐Salguero, P. M., Loza, M. I., Alberício, F., & Antonio Zorzano, A. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.12.001 · Cited by 132
FZL, an FZO-like protein in plants, is a determinant of thylakoid and chloroplast morphology
Gao, H., Sage, T. L., & Osteryoung, K. W. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507287103 · Cited by 129
Yamada, H., Chounan, R., Higashi, Y., Kurihara, N., & Kido, H. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.11.017 · Cited by 129
Control of mitochondria dynamics and oxidative metabolism by cAMP, AKAPs and the proteasome
Carlucci, A., Lignitto, L., & Feliciello, A. (2008) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.09.006 · Cited by 134
Wang, X., Su, B., Liu, W., He, X., Gao, Y., Castellani, R. J., Perry, G. L., Smith, M. A., & Zhu, X. (2011) · Aging Cell · doi:10.1111/j.1474-9726.2011.00721.x · Cited by 134
Mitochondrial Structure, Function and Dynamics Are Temporally Controlled by c-Myc
Graves, J. A., Wang, Y., Sims‐Lucas, S., Cherok, E., Rothermund, K. D., Branca, M. F., Elster, J. D., Beer–Stolz, D., Houten, B. V., Vockley, J. E., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0037699 · Cited by 128
Mitochondrial Dynamics: Functional Link with Apoptosis
Otera, H., & Mihara, K. (2012) · International Journal of Cell Biology · doi:10.1155/2012/821676 · Cited by 131
Mitochondrial translocation of EGFR regulates mitochondria dynamics and promotes metastasis in NSCLC
Che, T.-F., Lin, C.-W., Wu, Y.-Y., Chen, Y., Han, C., Chang, Y., Wu, C., Hsiao, T.-H., Hong, T.-M., & Yang, P. (2015) · Oncotarget · doi:10.18632/oncotarget.5736 · Cited by 129
Neuronal Mitochondria Modulation of LPS-Induced Neuroinflammation
Harland, M., Torres, S. L., Liu, J., & Wang, X. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.2324-19.2020 · Cited by 131
Regulation of mitochondrial fission by intracellular Ca2+ in rat ventricular myocytes
Hom, J., Yu, T., Yoon, Y., Porter, G. A., & Sheu, S. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.03.018 · Cited by 130
Alirol, E., James, D. I., Huber, D., Marchetto, A., Vergani, L., Martinou, J., & Scorrano, L. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-05-0377 · Cited by 128
Mitochondrial Dynamics and Peripheral Neuropathy
Baloh, R. H. (2007) · The Neuroscientist · doi:10.1177/1073858407307354 · Cited by 127
Mitochondrial Function, Morphology, and Axonal Transport in Amyotrophic Lateral Sclerosis
Magrané, J., & Manfredi, G. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2604 · Cited by 127
Modulating mitofusins to control mitochondrial function and signaling
Zacharioudakis, E., Agianian, B., Vasantha Kumar, M. V., Biris, N., Garner, T. P., Rabinovich-Nikitin, I., Ouchida, A. T., Margulets, V., Nordstrøm, L. U., Riley, J. S., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31324-1 · Cited by 137
Park, Y.-Y., Nguyen, T. K. O., Kang, H. C., & Cho, H. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.142 · Cited by 125
Mitochondrial Morphofunction in Mammalian Cells
Bulthuis, E. P., Adjobo-Hermans, M. J. W., Willems, P. H. G. M., & Koopman, W. J. H. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7534 · Cited by 133
Mitochondrial dynamics, a key executioner in neurodegenerative diseases
Panchal, K., & Tiwari, A. K. (2018) · Mitochondrion · doi:10.1016/j.mito.2018.11.002 · Cited by 128
Mitochondrial Fission and Fusion: Molecular Mechanisms, Biological Functions, and Related Disorders
Ojaimi, M. A., Salah, A., & El‐Hattab, A. W. (2022) · Membranes · doi:10.3390/membranes12090893 · Cited by 130
Liu, Y.-N., Yang, J., Huang, D.-J., Ni, H.-H., Zhang, C.-X., Zhang, L., He, J., Gu, J., Chen, H.-X., Mai, H., et al. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01906 · Cited by 125
Self-citationPerumalsamy, L. R., Nagala, M., & Sarin, A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910060107 · Cited by 124
Chou, C., Lin, C., Yang, M., Wei, C., Liao, H.-D., Lin, R.-C., Tu, W., Kao, T.-C., Hsu, C., Cheng, J., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0049112 · Cited by 127
Huang, P., Galloway, C. A., & Yoon, Y. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020655 · Cited by 132
Mitochondria-Associated Endoplasmic Reticulum Membranes in Cardiovascular Diseases
Gao, P., Yan, Z., & Zhu, Z. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.604240 · Cited by 136
Mitochondrial dynamics as a bridge between mitochondrial dysfunction and insulin resistance
Antonio Zorzano, A., Liesa, M., & Palacín, M. (2009) · Archives of Physiology and Biochemistry · doi:10.1080/13813450802676335 · Cited by 128
Shy, M. E., Lupski, J. R., Chance, P. F., Klein, C. J., & Dyck, P. J. (2005) · Elsevier eBooks · doi:10.1016/b978-0-7216-9491-7.50072-7 · Cited by 124
Role of Mitofusin-2 in mitochondrial localization and calcium uptake in skeletal muscle
Ainbinder, A., Boncompagni, S., Protasi, F., & Dirksen, R. T. (2015) · Cell Calcium · doi:10.1016/j.ceca.2014.11.002 · Cited by 122
Mitochondrial dynamics and inherited peripheral nerve diseases
Pareyson, D., Saveri, P., Sagnelli, A., & Piscosquito, G. (2015) · Neuroscience Letters · doi:10.1016/j.neulet.2015.04.001 · Cited by 128
Crosstalk between mitochondria and peroxisomes
Demarquoy, J. (2015) · World Journal of Biological Chemistry · doi:10.4331/wjbc.v6.i4.301 · Cited by 136
Axelrod, C. L., Fealy, C. E., Mulya, A., & Kirwan, J. P. (2018) · Acta Physiologica · doi:10.1111/apha.13216 · Cited by 123
Mitochondrial dynamics regulate genome stability via control of caspase-dependent DNA damage
Cao, K., Riley, J. S., Heilig, R., Montes-Gómez, A. E., Vringer, E., Berthenet, K., Cloix, C., Elmasry, Y., Spiller, D. G., Ichim, G., et al. (2022) · Developmental Cell · doi:10.1016/j.devcel.2022.03.019 · Cited by 124
Huang, P., Yu, T., & Yoon, Y. (2007) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2007.04.002 · Cited by 131
Endurance Exercise and the Regulation of Skeletal Muscle Metabolism
Booth, F. W., Ruegsegger, G. N., Toedebusch, R. G., & Yan, Z. (2015) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2015.07.016 · Cited by 128
Which came first, the cytochrome c release or the mitochondrial fission?
Martinou, J., & Youle, R. J. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401985 · Cited by 122
Fragouli, E. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-816561-4.00009-0 · Cited by 122
Mitochondrial function and lifespan of mice with controlled ubiquinone biosynthesis
Wang, Y., Oxer, D., & Hekimi, S. (2015) · Nature Communications · doi:10.1038/ncomms7393 · Cited by 123
The lncRNA Plscr4 Controls Cardiac Hypertrophy by Regulating miR-214
Lv, L., Li, T., Li, X., Xu, C., Liu, Q., Jiang, H., Li, Y., Liu, Y., Yan, H., Huang, Q., et al. (2017) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2017.12.018 · Cited by 119
N-glycanase NGLY1 regulates mitochondrial homeostasis and inflammation through NRF1
Yang, K., Huang, R. B., Fujihira, H., Suzuki, T., & Yan, N. (2018) · The Journal of Experimental Medicine · doi:10.1084/jem.20180783 · Cited by 122
Disruption of mitochondrial dynamics affects behaviour and lifespan in Caenorhabditis elegans
Byrne, J. J., Soh, M. S., Chandhok, G., Vijayaraghavan, T., Teoh, J.-S., Crawford, S., Cobham, A. E., Yapa, N. M. B., Mirth, C. K., & Neumann, B. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03024-5 · Cited by 119
Functional coordination of alternative splicing in the mammalian central nervous system
Fagnani, M., Barash, Y., Ip, J. Y., Misquitta, C., Pan, Q., Saltzman, A. L., Shai, O., Lee, L., Rozenhek, A., Mohammad, N., et al. (2007) · Genome Biology · doi:10.1186/gb-2007-8-6-r108 · Cited by 120
Ferree, A. W., Trudeau, K. M., Zik, E., Benador, I. Y., Twig, G., Gottlieb, R. A., & Shirihai, O. S. (2013) · Autophagy · doi:10.4161/auto.26503 · Cited by 124
Mitochondrial Biology and Neurological Diseases
Arun, S., Liu, L., & Dönmez, G. (2015) · Current Neuropharmacology · doi:10.2174/1570159x13666150703154541 · Cited by 123
Increasing ovarian NAD+ levels improve mitochondrial functions and reverse ovarian aging
Yang, Q., Cong, L., Wang, Y., Luo, X., Li, H., Wang, H., Zhu, J., Dai, S., Jin, H., Yao, G., et al. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.05.003 · Cited by 120
Mitochondrial Biogenesis, Mitochondrial Dynamics, and Mitophagy in the Maturation of Cardiomyocytes
Ding, Q., Qi, Y., & Tsang, S. Y. (2021) · Cells · doi:10.3390/cells10092463 · Cited by 128
The Balance of MFN2 and OPA1 in Mitochondrial Dynamics, Cellular Homeostasis, and Disease
Zanfardino, P., Amati, A., Perrone, M., & Petruzzella, V. (2025) · Biomolecules · doi:10.3390/biom15030433 · Cited by 129
Alzheimer's disease: diverse aspects of mitochondrial malfunctioning.
Santos, R. X., Correia, S. C., Wang, X., Perry, G. L., Smith, M. A., Moreira, P. I., & Zhu, X. (2010) · Europe PMC (PubMed Central) · Cited by 120
The dynamin GTPase OPA1: More than mitochondria?
Belenguer, P., & Pellegrini, L. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.08.004 · Cited by 125
Palma, C. D., Falcone, S., Pisoni, S., Cipolat, S., Panzeri, M. C., Pambianco, S., Pisconti, A., Allevi, R., Bassi, M. T., Cossu, G., et al. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2010.48 · Cited by 119
The endoplasmic reticulum and junctional membrane communication during calcium signaling
Lam, A. K. M., & Galione, A. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.06.004 · Cited by 121
Mitophagy for cardioprotection
Titus, A. S., Sung, E., Zablocki, D., & Sadoshima, J. (2023) · Basic Research in Cardiology · doi:10.1007/s00395-023-01009-x · Cited by 128
Therapeutic prospects for mitochondrial disease
Schon, E. A., DiMauro, S., Hirano, M., & Gilkerson, R. (2010) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2010.04.007 · Cited by 122
Defending the mitochondria: The pathways of mitophagy and mitochondrial-derived vesicles
Roberts, R. F., Tang, M. Y. H., Fon, E. A., & Durcan, T. M. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.07.020 · Cited by 121
Adaniya, S. M., O‐Uchi, J., Cypress, M. W., Kusakari, Y., & Jhun, B. S. (2019) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00523.2018 · Cited by 123
Ihenacho, U. K., Nolden, K. A., Harwig, M. C., Widlansky, M. E., & Hill, R. B. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.660095 · Cited by 117
WAVE1 controls neuronal activity-induced mitochondrial distribution in dendritic spines
Sung, J. Y., Engmann, O., Teylan, M. A., Nairn, A. C., Greengard, P., & Kim, Y. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0712180105 · Cited by 117
Physical Exercise: A Novel Tool to Protect Mitochondrial Health
Sorriento, D., Di Vaia, E., & Iaccarino, G. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.660068 · Cited by 118
Roles of mitochondria in neuronal development
Son, G., & Han, J. (2018) · BMB Reports · doi:10.5483/bmbrep.2018.51.11.226 · Cited by 121
Kang, T. (2020) · Antioxidants · doi:10.3390/antiox9070617 · Cited by 120
Mitochondrial Dynamics in Adult Cardiomyocytes and Heart Diseases
Li, A., Gao, M., Jiang, W., Qin, Y. H., & Gong, G. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.584800 · Cited by 122
Mitochondrial morphology and distribution in mammalian cells
Frazier, A. E., Kiu, C., Stojanovski, D., Hoogenraad, N. J., & Ryan, M. T. (2006) · Biological Chemistry · doi:10.1515/bc.2006.193 · Cited by 118
Strack, S., Wilson, T. J., & Cribbs, J. T. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201210045 · Cited by 116
Role of mitochondrial lipids in guiding fission and fusion
Frohman, M. A. (2014) · Journal of Molecular Medicine · doi:10.1007/s00109-014-1237-z · Cited by 121
Ye, X., Feng, D., Tao, K. X., Wang, R., Shi, Y., Qin, H., Murphy, M. P., Yang, Q., & Zhao, G. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.05.018 · Cited by 119
Mitochondrial Morphological Features Are Associated with Fission and Fusion Events
Westrate, L. M., Drocco, J. A., Martin, K. R., Hlavacek, W. S., & MacKeigan, J. P. (2014) · PLoS ONE · doi:10.1371/journal.pone.0095265 · Cited by 115
ER as master regulator of membrane trafficking and organelle function
Wenzel, E. M., Elfmark, L. A., Stenmark, H., & Raiborg, C. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202205135 · Cited by 120
Characterization of OPA1 isoforms isolated from mouse tissues
Akepati, V. R., Müller, E., Otto, A., Strauss, H. M., Portwich, M., & Alexander, C. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05401.x · Cited by 114
Eura, Y., Ishihara, N., Oka, T., & Mihara, K. (2006) · Journal of Cell Science · doi:10.1242/jcs.03253 · Cited by 115
Energetic requirements and bioenergetic modulation of mitochondrial morphology and dynamics
Sauvanet, C., Duvezin‐Caubet, S., di Rago, J., & Rojo, M. (2009) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2009.12.006 · Cited by 120
Park, K., Wiederkehr, A., Kirkpatrick, C. L., Mattenberger, Y., Martinou, J., Marchetti, P., Demaurex, N., & Wollheim, C. B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806251200 · Cited by 115
Expression of mitofusin 2R94Q in a transgenic mouse leads to Charcot–Marie–Tooth neuropathy type 2A
Cartoni, R., Arnaud, E., Médard, J., Poirot, O., Courvoisier, D. S., Chrast, R., & Martinou, J. (2010) · Brain · doi:10.1093/brain/awq082 · Cited by 115
Larrea, D., Pera, M., Gonnelli, A., Quintana–Cabrera, R., Akman, H. O., Guardia‐Laguarta, C., VELASCO, K. R., Área-Gómez, E., Bello, F. D., Stefani, D. D., et al. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz008 · Cited by 114
Complex Regulation of Mitochondrial Function During Cardiac Development
Zhao, Q., Sun, Q., Zhou, L., Liu, K., & Jiao, K. (2019) · Journal of the American Heart Association · doi:10.1161/jaha.119.012731 · Cited by 116
Williams, P. A., Morgan, J. E., & Votruba, M. (2010) · Brain · doi:10.1093/brain/awq218 · Cited by 113
Liu, T. Y., Bian, X., Sun, S., Hu, X., Klemm, R. W., Prinz, W. A., Rapoport, T. A., & Hu, J. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1208385109 · Cited by 116
Mfn2 downregulation in excitotoxicity causes mitochondrial dysfunction and delayed neuronal death
Riera, A. M., Segarra‐Mondejar, M., Muñoz, J. P., Ginet, V., Olloquequi, J., Pérez‐Clausell, J., Palacín, M., Reina, M., Puyal, J., Antonio Zorzano, A., et al. (2014) · The EMBO Journal · doi:10.15252/embj.201488327 · Cited by 115
ROS as Regulators of Mitochondrial Dynamics in Neurons
Cid‐Castro, C., Hernández-Espinosa, D. R., & Morán, J. (2018) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-018-0584-7 · Cited by 114
Shen, M., Wang, F., Li, M., Sah, N., Stockton, M. E., Tidei, J. J., Gao, Y., Korabelnikov, T., Kannan, S., Vevea, J., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-019-0338-y · Cited by 111
Mitochondrial dynamics proteins as emerging drug targets
Zacharioudakis, E., & Gavathiotis, E. (2022) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2022.11.004 · Cited by 115
The Role of Impaired Mitochondrial Dynamics in MFN2-Mediated Pathology
Zaman, M., & Shutt, T. E. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.858286 · Cited by 116
Severe early-onset axonal neuropathy with homozygous and compound heterozygous MFN2 mutations
Nicholson, G. A., Magdelaine, C., Zhu, D., Grew, S., Ryan, M. M., Sturtz, F. G., Vallat, J. ‐., & Ouvrier, R. (2008) · Neurology · doi:10.1212/01.wnl.0000311275.89032.22 · Cited by 111
Regulation of plasma membrane calcium fluxes by mitochondria
Demaurex, N., Poburko, D., & Frieden, M. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.12.012 · Cited by 115
Identification of a Novel Mitochondrial Complex Containing Mitofusin 2 and Stomatin-like Protein 2
Hájek, P., Chomyn, A., & Attardi, G. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m608168200 · Cited by 111
Biel, T. G., Lee, S., Flores‐Toro, J., Dean, J. W., Go, K. L., Lee, M.-H., Law, B. K., Law, M. E., Dunn, W. A., Zendejas, I. R., et al. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.96 · Cited by 110
Insights into SGLT2 inhibitor treatment of diabetic cardiomyopathy: focus on the mechanisms
Huang, K., Luo, X., Liao, B., Li, G., & Feng, J. (2023) · Cardiovascular Diabetology · doi:10.1186/s12933-023-01816-5 · Cited by 117
Pokharel, M. D., Flores, A. G., Marciano, D. P., Franco, M. C., Fineman, J. R., Aggarwal, S., Wang, T., & Black, S. M. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103049 · Cited by 124
Amiott, E. A., Lott, P. C., Soto, J. E., Kang, P. B., McCaffery, J. M., DiMauro, S., Abel, E. D., Flanigan, K. M., Lawson, V. H., & Shaw, J. M. (2008) · Experimental Neurology · doi:10.1016/j.expneurol.2008.01.010 · Cited by 114
Rolland, S. G. M., Lu, Y., David, C. N., & Conradt, B. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200905070 · Cited by 108
Mitochondrial Dynamics: The Intersection of Form and Function
Ferree, A. W., & Shirihai, O. S. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-3573-0_2 · Cited by 113
Mitochondrial fission and fusion in secondary brain damage after CNS insults
Balog, J., Mehta, S. L., & Vemuganti, R. (2016) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x16671528 · Cited by 110
Mitofusin 1 is required for female fertility and to maintain ovarian follicular reserve
Zhang, M., Bener, M. B., Jiang, Z., Wang, T., Esencan, E., Scott, R., Horváth, T. L., & Seli, E. U. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1799-3 · Cited by 110
Lugus, J. J., Ngoh, G. A., Bachschmid, M. M., & Walsh, K. X. (2011) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2011.07.023 · Cited by 114
Function Over Form: Modeling Groups of Inherited Neurological Conditions in Zebrafish
Kozol, R. A., Abrams, A. J., James, D. M., Buglo, E., Yan, Q., & Dallman, J. E. (2016) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2016.00055 · Cited by 116
Mitochondrial dysfunction and ovarian aging
Wang, T., Zhang, M., Jiang, Z., & Seli, E. U. (2017) · American Journal of Reproductive Immunology · doi:10.1111/aji.12651 · Cited by 109
Yu, R., Liu, T., Ning, F. C., Tan, F., Jin, S., Lendahl, U., Zhao, J., & Nistér, M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.008202 · Cited by 109
Bcl-2 family interaction with the mitochondrial morphogenesis machinery
Harwig, M. C., Norris, K. L., Karbowski, M., Wang, C., Suen, D., Jiao, S., George, N. M., Luo, X., Li, Z., & Youle, R. J. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2010.89 · Cited by 108
Barbier, V., Lang, D., Valois, S., Rothman, A. L., & Medin, C. L. (2016) · Virology · doi:10.1016/j.virol.2016.10.022 · Cited by 110
Real-time imaging of mitochondria in transgenic zebrafish expressing mitochondrially targeted GFP
Kim, J. M., Kang, K. H., Kim, C., & Choi, S. (2008) · BioTechniques · doi:10.2144/000112909 · Cited by 107
Mitochondrial fusion is required for spermatogonial differentiation and meiosis
Varuzhanyan, G., Rojansky, R. B., Sweredoski, M. J., Graham, R. L., Hess, S. Y., Ladinsky, M. S., & Chan, D. C. (2019) · eLife · doi:10.7554/elife.51601 · Cited by 109
Self-citationMitochondrial Dynamics in Alzheimerʼs Disease
Bonda, D., Wang, X., Perry, G. L., Smith, M. A., & Zhu, X. (2010) · Drugs & Aging · doi:10.2165/11532140-000000000-00000 · Cited by 106
NF-κB pathway controls mitochondrial dynamics
Laforge, M., Rodrigues, V, Silvestre, R., Gautier, C., Weil, R., Corti, O., & Estaquier, J. (2016) · Cell Death & Differentiation · doi:10.1038/cdd.2015.42 · Cited by 105
Viral degradasome hijacks mitochondria to suppress innate immunity
Goswami, R., Majumdar, T., Dhar, J., Chattopadhyay, S., Bandyopadhyay, S. K., Verbovetskaya, V., Sen, G. C., & Barik, S. (2013) · Cell Research · doi:10.1038/cr.2013.98 · Cited by 105
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
