The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
Control of mitochondrial morphology by a human mitofusin
Abstract
Although changes in mitochondrial size and arrangement accompany both cellular differentiation and human disease, the mechanisms that mediate mitochondrial fusion, fission and morphogenesis in mammalian cells are not understood. We have identified two human genes encoding potential mediators of mitochondrial fusion. The mitofusins (Mfn1 and Mfn2) are homologs of the Drosophila protein fuzzy onion (Fzo) that associate with mitochondria and alter mitochondrial morphology when expressed by transient transfection in tissue culture cells. An internal region including a predicted bipartite transmembrane domain (TM) is sufficient to target Mfn2 to mitochondria and requires hydrophobic residues within the TM. Co-expression of Mfn2 with a dominant interfering mutant dynamin-related protein (Drp1K38A) proposed to block mitochondrial fission resulted in long mitochondrial filaments and networks. Formation of mitochondrial filaments and networks required a wild-type Mfn2 GTPase domain, suggesting that the Mfn2 GTPase regulates or mediates mitochondrial fusion and that mitofusins and dynamin related GTPases play opposing roles in mitochondrial fusion and fission in mammals, as in yeast.
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
“Mitofusin-2 (Mfn2) participates in the maintenance of mitochondrial tubules or networks in mammalian cells (23)(24)(25).”
From Expression of Mfn2, the Charcot-Marie-Tooth Neuropathy Type 2A Gene, in Human Skeletal Muscle (2005) · cites this paper as [24]
In the citing paper
“We show that Mfn2 (mitofusin 2), a mitochondrial membrane protein that participates in mitochondrial fusion in mammalian cells, is induced during myogenesis and contributes to the maintenance and operation of the mitochondrial network.”
From Mitofusin-2 Determines Mitochondrial Network Architecture and Mitochondrial Metabolism (2003) · cites this paper as [22]
Citations
Cites
Basic local alignment search tool
Altschul, S. F., Gish, W., Miller, W., Myers, E. W., & Lipman, D. J. (1990) · Journal of Molecular Biology · doi:10.1006/jmbi.1990.9999 · Cited by 98,669
Predicting coiled coils from protein sequences.
Lupas, A., Van Dyke, M., & Stock, J. (1991) · Science · doi:10.1126/science.252.5009.1162 · Cited by 3,953
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
Nakai, K., & Horton, P. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01336-x · Cited by 2,181
Mitochondrial transcription factor A is necessary for mtDNA maintance and embryogenesis in mice
Larsson, N.-G., Wang, J., Wilhelmsson, H., Oldfors, A., Rustin, P., Lewandoski, M., Barsh, G. S., & Clayton, D. A. (1998) · Nature Genetics · doi:10.1038/ng0398-231 · Cited by 1,594
The dynamin-related GTPase Dnm1 regulates mitochondrial fission in yeast
Bleazard, W., McCaffery, J. M., King, E. J., Bale, S., Mozdy, A. D., Tieu, Q., Nunnari, J. M., & Shaw, J. M. (1999) · Nature Cell Biology · doi:10.1038/13014 · Cited by 795
Piperno, G., & Fuller, M. T. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.101.6.2085 · Cited by 758
Self-citationA Human Dynamin-related Protein Controls the Distribution of Mitochondria
Смирнова, Е. А., Shurland, D., Ryazantsev, S. N., & van der Bliek, A. M. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.2.351 · Cited by 734
MultiCoil: A program for predicting two‐and three‐stranded coiled coils
Wolf, E., Kim, P. S., & Berger, B. (1997) · Protein Science · doi:10.1002/pro.5560060606 · Cited by 720
C. elegans Dynamin-Related Protein DRP-1 Controls Severing of the Mitochondrial Outer Membrane
Labrousse, A. M., Zappaterra, M. D., Rube, D. A., & van der Bliek, A. M. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80391-3 · Cited by 670
Cited by
Sorted by citations
Items 701–800 of 999
Kurashima, K., Chae, M. S., Inoue, H., Hatakeyama, S., & Tanaka, S. (2012) · Eukaryotic Cell · doi:10.1128/ec.00226-12 · Cited by 14
Yin, W., Li, R., Feng, X., & Kang, Y. J. (2018) · Cardiovascular Toxicology · doi:10.1007/s12012-018-9447-1 · Cited by 14
Mitochondrial Dynamics: Shaping Metabolic Adaptation
Cantó, C. (2018) · International review of cytology · doi:10.1016/bs.ircmb.2018.05.004 · Cited by 15
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
Andrews, M., & Arredondo, M. (2012) · BioMetals · doi:10.1007/s10534-012-9543-9 · Cited by 14
Yegambaram, M., Sun, X., Flores, A. G., Lü, Q., Soto, J. E., Richards, J., Aggarwal, S., Wang, T., Gu, H., Fineman, J. R., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242417533 · Cited by 14
Inhibitors of Rho/MRTF/SRF Transcription Pathway Regulate Mitochondrial Function
Patyal, P., Zhang, X., Verma, A., Azhar, G., & Wei, J. Y. (2024) · Cells · doi:10.3390/cells13050392 · 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
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
Grx2 Regulates Skeletal Muscle Mitochondrial Structure and Autophagy
Liaghati, A., Pileggi, C. A., Parmar, G., Patten, D. A., Hadžimustafić, N., Cuillerier, A., Menzies, K. J., Burelle, Y., & Harper, M. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.604210 · Cited by 13
Scott, I., & Logan, D. C. (2010) · Springer eBooks · doi:10.1007/978-0-387-89781-3_2 · Cited by 14
Dang, X., Zhang, L., Franco, A., & Dorn, G. W. (2022) · Human Molecular Genetics · doi:10.1093/hmg/ddac287 · Cited by 13
Mitophagy Regulated by the PINK1-Parkin Pathway
Arano, T., & Imai, Y. (2015) · InTech eBooks · doi:10.5772/61284 · Cited by 14
Wang, Y., Huang, Y., Liu, Y., Li, J., Hao, Y., Yin, P., Liu, Z., Chen, J., Wang, Y., Wang, N., et al. (2018) · The FASEB Journal · doi:10.1096/fj.201701143rr · Cited by 13
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
BAX regulates dendritic spine development via mitochondrial fusion
Gu, Q., Duan, K., Petralia, R. S., Wang, Y., & Li, Z. (2022) · Neuroscience Research · doi:10.1016/j.neures.2022.06.002 · Cited by 13
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
Mitochondrial dynamics in vascular remodeling and target-organ damage
Zhu, T., Hu, Q., Yuan, Y., Yao, H., Zhang, J., & Qi, J. (2023) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2023.1067732 · Cited by 12
Death-associated protein 3 in cancer—discrepant roles of DAP3 in tumours and molecular mechanisms
Song, H., Liu, H., Wang, X., Yang, Y., Zhao, X., Jiang, W. G., Sui, L., & Song, X. (2024) · Frontiers in Oncology · doi:10.3389/fonc.2023.1323751 · Cited by 13
Castiglioni, L., Gelosa, P., Muluhie, M., Mercuriali, B., Rzemieniec, J., Gotti, M., Fiordaliso, F., Busca, G. A., & Sironi, L. (2024) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2024.176767 · Cited by 12
Fierro, R. B., Mora, P. H., Zenteno, J. C., & Villarroel, C. E. (2020) · Neuromuscular Disorders · doi:10.1016/j.nmd.2020.10.003 · 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
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
Foster, C. R., Satomi, S., Kato, Y., & Patel, H. H. (2020) · Biochemical Society Transactions · doi:10.1042/bst20190388 · Cited by 12
Iron Dyshomeostasis and Mitochondrial Function in the Failing Heart: A Review of the Literature
Mousavi‐Aghdas, S. A., Farashi, E., & Naderi, N. (2023) · American Journal of Cardiovascular Drugs · doi:10.1007/s40256-023-00619-z · Cited by 12
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
Islam, M. N., Mishra, V. K., Munalisa, R., Parveen, F., Ali, S. F., Akter, K., Ahmed, T., Ho, T., & Huang, C. (2024) · Molecular & Cellular Toxicology · doi:10.1007/s13273-023-00424-4 · Cited by 11
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
Mfn2-dependent fusion pathway of PE-enriched micron-sized vesicles
Peñalva, D. A., Monnappa, A. K., Natale, P., & López‐Montero, I. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2313609121 · Cited by 11
Mitochondrial function in oral health and disease
Morandini, A. C., & Ramos‐Junior, E. S. (2024) · Journal of Immunological Methods · doi:10.1016/j.jim.2024.113729 · Cited by 14
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
Mitofusin2 expression is associated with podocyte injury in IgA nephropathy
Tang, X.-L., Yuan, Y., Liang, X., & Jiang, X. (2023) · European journal of medical research · doi:10.1186/s40001-023-01107-5 · Cited by 11
Ishihara, N., Maeda, M., Ban, T., & Mihara, K. (2017) · The Journal of Biochemistry · doi:10.1093/jb/mvx029 · Cited by 11
dnm1 deletion blocks mitochondrial fragmentation in Δfzo1 cells
Yang, Y., Hu, Y., Wu, L., Zhang, P., & Shang, J. (2020) · Yeast · doi:10.1002/yea.3524 · Cited by 10
Genetics of lipodystrophy syndromes
Jéru, I. (2021) · La Presse Médicale · doi:10.1016/j.lpm.2021.104074 · Cited by 11
Association of Polymorphisms in Mitofusin-2 Gene with Type 2 Diabetes in Han Chinese
Li, P., Zhu, S., Wu, X., Zhu, X., Li, J., Pan, L., Xin, Z., Niu, F., Wu, J., & Liu, Y. (2012) · BioMed Research International · doi:10.1155/2012/205752 · 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
Miro ubiquitination is critical for efficient damage-induced PINK1/Parkin-mediated mitophagyPreprint
López‐Doménech, G., Covill‐Cooke, C., Howden, J. H., Birsa, N., Morfill, C., Brandon, N. J., & Kittler, J. T. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/414664 · Cited by 11
Inagaki, S., Suzuki, Y., Kawasaki, K., Kondo, R., Imaizumi, Y., & Yamamura, H. (2023) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2023.01.044 · Cited by 12
Palacios, B. S., Villares, R., Lucas, P., Rodrı́guez-Frade, J. M., Cayuela, A., Piccirillo, J., Lombardía, M., Gestoso, D. D., Fernández-García, M., Risco, C., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1200259 · Cited by 10
Differentiation in Stem Cell Lineages and in Life
Fuller, M. T. (2016) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2015.11.041 · Cited by 10
Self-citationRapid and quantitative in vitro analysis of mitochondrial fusion and its interplay with apoptosis
Xu, J., Su, L., Han, J., Gao, K., Zhang, M., Wang, S., Chen, C., & Yan, X. (2020) · Talanta · doi:10.1016/j.talanta.2020.121523 · Cited by 10
Sloat, S. R., & Hoppins, S. C. (2022) · Life Science Alliance · doi:10.26508/lsa.202101305 · Cited by 10
Stavropoulos, F., Georgiou, E., Schiza, N., Bell, S., Baloh, R. H., Kleopa, K. A., & Sargiannidou, I. (2023) · Journal of the Peripheral Nervous System · doi:10.1111/jns.12564 · Cited by 10
A novel MFN2 mutation causes variable clinical severity in a multi-generational CMT2 family
Dankwa, L., Richardson, J. M., Motley, W. W., Scavina, M. T., Courel, S. C., Bardakjian, T., Zuchner, S. L., & Scherer, S. S. (2018) · Neuromuscular Disorders · doi:10.1016/j.nmd.2018.12.008 · Cited by 10
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
Effects of mitofusin-2 gene on cell proliferation and chemotherapy sensitivity of MCF-7
Xia, Y. F., Wu, Y., He, X., Gong, J., & Qiu, F. (2008) · Journal of Huazhong University of Science and Technology [Medical Sciences] · doi:10.1007/s11596-008-0218-2 · Cited by 10
Might mammalian mitochondria merge?
Turnbull, D. M., & Lightowlers, R. N. (2001) · Nature Medicine · doi:10.1038/90929 · Cited by 10
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
Li, W., Cai, P., Xu, Y., Tian, W., Jing, L., Lv, Q., Zhao, Y., Wang, H., & Shao, Q. (2024) · Journal of Immunology Research · doi:10.1155/2024/5577506 · Cited by 9
Plant mitochondrial fission and fusion
Arimura, S., & Tsutsumi, N. (2005) · Plant Biotechnology · doi:10.5511/plantbiotechnology.22.415 · Cited by 9
Zhang, Z., Li, M., Cui, B., & Chen, X. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.829686 · Cited by 9
Leigh syndrome caused by mitochondrial DNA-maintenance defects revealed by whole exome sequencing
de Souza, P. V. S., Bortholin, T., Teixeira, C. A. C., Seneor, D. D., Marin, V. D. G. B., Dias, R. B., Farias, I. B., Badia, B. D. M. L., Silva, L. H. L., Pinto, W. B. V. D. R., et al. (2019) · Mitochondrion · doi:10.1016/j.mito.2019.06.008 · Cited by 9
Inagaki, S., Suzuki, Y., Kawasaki, K., Kondo, R., Imaizumi, Y., & Yamamura, H. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00274.2021 · Cited by 11
Czernik, M., Toschi, P., Zacchini, F., Iuso, D., & Ptak, G. (2017) · PLoS ONE · doi:10.1371/journal.pone.0169579 · Cited by 9
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
Mitofusin function is dependent on the distinct tissue and organ specific roles of mitochondria
Sack, M. N. (2011) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2011.09.004 · Cited by 9
Guerra, S. M. V. T. A., de França, L. C. K., da Silva, K. N., Grotto, F. S., & Glaser, V. (2024) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2024.127549 · Cited by 8
Mitochondrial homeostasis in stem cell senescence
Peng, B., & Zhang, H. (2025) · Oral Science and Homeostatic Medicine · doi:10.26599/oshm.2025.9610006 · Cited by 8
A comparison of spermatogenesis between flies and men—conserved processes of male gamete production
Houston, B. J., Cauchi, L. M., Dunleavy, J. E. M., Burke, R., Hime, G. R., & O’Bryan, M. K. (2025) · Human Reproduction Update · doi:10.1093/humupd/dmaf018 · Cited by 8
Intricacy of Mitochondrial Dynamics and Antiviral Response During RNA Virus Infection
Singh, S., Dirani, K., & Kumar, A. (2022) · Frontiers in Virology · doi:10.3389/fviro.2022.918806 · 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
Mitochondrial Proteomes in Neural Cells: A Systematic Review
Nusir, A., Sinclair, P., & Kabbani, N. (2023) · Biomolecules · doi:10.3390/biom13111638 · Cited by 8
He, S., Tian, B., Cao, H., Wang, M., Cai, D., Wu, Y., Yang, Q., Ou, X., Sun, D., Zhang, S., et al. (2024) · Poultry Science · doi:10.1016/j.psj.2024.103446 · Cited by 8
Sharma, V., Arora, A., Bansal, S., Semwal, A., Sharma, M., & Aggarwal, A. (2024) · Cell Biochemistry and Function · doi:10.1002/cbf.3920 · Cited by 8
Tolosa-Díaz, A., Almendro‐Vedia, V. G., Natale, P., & López‐Montero, I. (2020) · Biomolecules · doi:10.3390/biom10071085 · Cited by 8
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
Mitochondrial Genetics and Optic Neuropathy
Wiggs, J. L. (2015) · Annual Review of Vision Science · doi:10.1146/annurev-vision-082114-035651 · 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
Can endogenous gaseous messengers control mitochondrial biogenesis in mammalian cells?
Nisoli, E., Clementi, E., Tonello, C., Moncada, S., & Carruba, M. O. (2004) · Prostaglandins & Other Lipid Mediators · doi:10.1016/j.prostaglandins.2004.01.005 · Cited by 8
Expression of HSG is essential for mouse blastocyst formation
Jiang, G., Pan, L., Huang, X.-Y., Han, M. H., Wen, J., & Sun, F.-Z. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.07.088 · Cited by 8
Yuan, Y., Wu, Y., He, M., & Jiang, X. (2024) · Current Molecular Medicine · doi:10.2174/0115665240310818240531080353 · Cited by 7
Wang, X., He, J., Xie, P., Wu, Y., Dong, L., & An, W. (2024) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2024.101436 · Cited by 7
Regulation of Mitochondrial Quality Control of Intestinal Stem Cells in Homeostasis and Diseases
Lei, X., Xu, Z., Huang, Y., Huang, L., Lang, J., Qu, M., & Liu, D. (2024) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0489 · Cited by 7
Mitostasis in age-associated neurodegeneration
Panda, M., Markaki, M., & Tavernarakis, N. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2024.167547 · Cited by 7
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
Role of human oocyte-enriched factors in somatic cell reprograming
El-Gammal, Z., AlOkda, A., & El‐Badri, N. (2018) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2018.05.009 · Cited by 6
Qu, L., Chen, H., Wang, G., & Wei, J. (2013) · Tumori Journal · doi:10.1177/030089161309900609 · Cited by 7
Cellular role and molecular machinery of mitochondrial fusion
Westermann, B. (2002) · Cited by 7
Mitochondrial Mechanisms in Immunity and Inflammatory Conditions: Beyond Energy Management
Álvarez, S., Vanasco, V., Areán, J. S. A., Magnani, N., & Evelson, P. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0367 · Cited by 6
Zhong, Z., Hou, Y., Zhou, C., Wang, J., Gao, L., Wu, X., Zhou, G., Liu, S., Xu, Y., & Yang, W. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02575-w · Cited by 6
Chen, Y.-A., Lu, W.-N., Li, P., Nie, T., Li, Y., Zeng, R., Lin, S., Gao, M., Hejtmancik, J. F., Hou, L., et al. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.07.025 · Cited by 6
Mitochondrial dynamics and signaling in stem cell differentiation
Verma, R. K., Madan, S., & Rikhy, R. (2026) · Journal of Cell Science · doi:10.1242/jcs.263847 · Cited by 6
Wu, S., Zhao, X., Wu, M., Yang, L., Liu, X., Li, D., Xu, H., Zhao, Y., Su, X., Wei, Z., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231710145 · Cited by 6
Mishra, E., & Thakur, M. K. (2024) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.4c00283 · Cited by 6
Chin, M. Y., Joy, D. A., Samaddar, M., Rana, A., Chow, J., Miyamoto, T., & Calvert, M. (2025) · SLAS DISCOVERY · doi:10.1016/j.slasd.2025.100208 · Cited by 6
Moro, L. (2020) · Biology · doi:10.3390/biology9120479 · Cited by 6
Novel homozygous mutations in Pakistani families with Charcot–Marie–Tooth disease
Kanwal, S., Choi, Y. J., Lim, S.-O., Choi, H.-J., Park, J., Nuzhat, R., Khan, A., Perveen, S., Choi, B.-O., & Chung, K. (2021) · BMC Medical Genomics · doi:10.1186/s12920-021-01019-5 · Cited by 7
The role of mtDNA damage in mitochondrial dysfunction
Furda, A. M. (2011) · D-Scholarship@Pitt (University of Pittsburgh) · Cited by 6
Valproate Disturbs Morphology and Mitochondrial Membrane Potential in Human Neural Cells
da Costa, R. M., Kormann, M. L., Galina, A., & Rehen, S. K. (2015) · Applied In Vitro Toxicology · doi:10.1089/aivt.2015.0016 · Cited by 6
Mitochondrial network of skeletal muscle fiber
Vinogradskaia, I. S., Kuznetsova, T. G., & Александровна, С. Е. (2014) · Moscow University Biological Sciences Bulletin · doi:10.3103/s009639251402014x · Cited by 6
Przygodda, F., Manfredi, L. H., Machado, J., Gonçalves, D. A. P., Zanon, N. M., Bonagamba, L. G. H., Machado, B. H., Kettelhut, Í. D. C., & Navegantes, L. C. C. (2016) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00977.2015 · Cited by 6
Mitochondrial Ubiquitin Ligase in Cardiovascular Disorders
Yu, T., Zhang, Y., & Li, P. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-55330-6_17 · Cited by 6
WangJianju, W., Zhu, L., Zhang, J. W. J., & Zheng, L. (2012) · Cited by 6
Sharma, G., Zaman, M., Sabouny, R., Joel, M., Martino, D., Martino, D., de Koning, A. P. J., Shutt, T. E., & Shutt, T. E. (2021) · F1000Research · doi:10.12688/f1000research.53230.1 · Cited by 23
Nonlinear analysis of local field potentials and motor cortex EEG in spinocerebellar ataxia 3
Yu, Y., He, X., Zhao, Z., Jiang, W., Pan, D., Shi, L., Xu, L., Shi, L., Gu, R., & Wei, J. (2018) · Journal of Clinical Neuroscience · doi:10.1016/j.jocn.2018.10.018 · Cited by 6
Metadata
- Authors
- Santel, A., & Fuller, M. T.
- Affiliations
- Stanford Medicine (US)
- ORCID
- Fuller, Margaret T.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2001-03-01
- Volume
- 114
- Issue
- 5
- Pages
- 867-874
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2144846851
- Cited by
- 1,012
- References
- 33
- Citations by year
- 2026: 14 · 2025: 38 · 2024: 45 · 2023: 50 · 2022: 50 · 2021: 45 · 2020: 68 · 2019: 73 · 2018: 66 · 2017: 52 · 2016: 42 · 2015: 41 · 2014: 39 · 2013: 43 · 2012: 57
- FWCI
- 8.96
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Cell Science (publishedVersion)
- PubMed (publishedVersion)
- HighWire Press Open Archive (submittedVersion)
- Funders
- National Institutes of Health (5r01hd029194-05)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (HD29194)
- 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
- mitofusin 2, mitofusin 1, mitochondrial fusion, mitochondrial fission, mitochondrial morphology, mitochondrial network, mitochondrial targeting, Drp1, dynamin-related GTPase, GTPase domain, mitochondrial morphogenesis
- MeSH terms
- Animals, Cell Line, Fluorescent Antibody Technique, Humans, Mitochondria, Receptors, CXCR4, GTP Phosphohydrolases
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