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
Flagged first, then by citations
Cited by
Sorted by citations
Items 501–600 of 999
Clinical value of non-coding RNAs in cardiovascular, pulmonary, and muscle diseases
Bonnet, S., Boucherat, O., Paulin, R., Wu, D., Hindmarch, C. C. T., Archer, S. L., Song, R., Moore, J. B., Provencher, S., Zhang, L., et al. (2019) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00078.2019 · Cited by 34
Maternal transmission of mitochondrial diseases
Chiaratti, M. R., Macabelli, C. H., Neto, J. D. A., Grejo, M. P., Pandey, A. K., Perecin, F., & del Collado, M. (2020) · Genetics and Molecular Biology · doi:10.1590/1678-4685-gmb-2019-0095 · Cited by 37
Chan, T., Wu, W., Li, W., Shiao, M., Shiue, Y., & Li, C. (2020) · Theranostics · doi:10.7150/thno.51655 · Cited by 35
Mitochondrial Dynamics and VMP1-Related Selective Mitophagy in Experimental Acute Pancreatitis
Vanasco, V., Ropolo, A., Grasso, D., Ojeda, D. S., Garcia, M. N., Vico, T. A., Orquera, T., Quarleri, J. F., Álvarez, S., & Vaccaro, M. I. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.640094 · Cited by 35
A new non-canonical pathway of Gαq protein regulating mitochondrial dynamics and bioenergetics
Benincá, C., Planagumà, J., Shuck, A. D. F., Acín‐Pérez, R., Muñoz, J. P., de Almeida, M. M., Brown, J. H., Murphy, A. N., Zorzano, A., Enrı́quez, J. A., et al. (2014) · Cellular Signalling · doi:10.1016/j.cellsig.2014.01.009 · Cited by 34
Expression of mitochondria-related genes is elevated in overfeeding-induced goose fatty liver
Osman, R. H., Shao, D., Liu, L., Xia, L., Sun, X., Zheng, Y., Wang, L., Zhang, R., Zhang, Y., Zhang, J., et al. (2015) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2015.11.006 · Cited by 35
Beyond fission and fusion—Diving into the mysteries of mitochondrial shape
Preminger, N., & Schuldiner, M. (2024) · PLoS Biology · doi:10.1371/journal.pbio.3002671 · Cited by 41
A role for the GDAP1 gene in the molecular pathogenesis of Charcot-Marie-Tooth disease
Rzepnikowska, W., & Kochański, A. (2018) · Acta Neurobiologiae Experimentalis · doi:10.21307/ane-2018-002 · Cited by 35
Disturb mitochondrial associated proteostasis: Neurodegeneration and imperfect ageing
Jagtap, Y. A., Kumar, P., Kinger, S., Dubey, A. R., Choudhary, A., Gutti, R. K., Singh, S., Jha, H. C., Poluri, K. M., & Mishra, A. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1146564 · Cited by 36
郡衛, 佐., Uittenbogaard, M., Yoon, J., & Chiaramello, A. (2009) · ASN NEURO · doi:10.1042/an20090036 · Cited by 36
Ma, X., Niu, M., Ni, H., & Ding, W. (2024) · Hepatology · doi:10.1097/hep.0000000000000910 · Cited by 37
Dysfunction of mitochondrial dynamics in the brains of scrapie-infected mice
Choi, H.-S., Choi, Y., Shin, H., Oh, J.-M., Park, J., Kim, J., Carp, R. I., Choi, E., & Kim, Y. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.04.069 · Cited by 33
Targeted-mitochondria antioxidants therapeutic implications in inflammatory bowel disease
Matondo, A., & Kim, S. S. (2017) · Journal of drug targeting · doi:10.1080/1061186x.2017.1339196 · Cited by 34
Pietrangelo, L., Michelucci, A., Ambrogini, P., Sartini, S., Guarnier, F. A., Fusella, A., Zamparo, I., Mammucari, C., Protasi, F., & Boncompagni, S. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.12.017 · Cited by 36
Drp1 Phosphorylation Is Indispensable for Steroidogenesis in Leydig Cells
Park, J.-E., Kim, Y. J., Lee, S. G., Kim, J. Y., Chung, J.-Y., Jeong, S.-Y., Koh, H., Yun, J., Park, H. T., Yoo, Y. H., et al. (2019) · Endocrinology · doi:10.1210/en.2019-00029 · Cited by 34
Bowes, T., & Gupta, R. S. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.08.120 · Cited by 33
Ryu, S., Han, E. C., Yoon, J. W., & Choi, C. (2014) · Molecules and Cells · doi:10.14348/molcells.2015.2285 · Cited by 35
Pathomechanisms of Mutant Proteins in Charcot-Marie-Tooth Disease
Niemann, A., Berger, P., & Suter, U. (2006) · NeuroMolecular Medicine · doi:10.1385/nmm:8:1:217 · Cited by 33
Emerging pathways for hereditary axonopathies
Zuchner, S. L., & Vance, J. M. (2005) · Journal of Molecular Medicine · doi:10.1007/s00109-005-0694-9 · Cited by 33
Mitochondria: A Promising Convergent Target for the Treatment of Amyotrophic Lateral Sclerosis
Cunha‐Oliveira, T., Montezinho, L., Simões, R. F., de Carvalho, M., Ferreiro, E. B., & Silva, F. S. G. (2024) · Cells · doi:10.3390/cells13030248 · Cited by 34
A unified mechanism for mitochondrial damage sensing in PINK1-Parkin–mediated mitophagy
Thayer, J. A., Petersen, J. D., Huang, X., Budet, L. M. G., Hawrot, J., Ramos, D. M., Sekine, S., Li, Y., Ward, M. E., & Narendra, D. P. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00604-z · Cited by 37
Emerging roles of mitochondrial membrane dynamics in health and disease
Schäfer, A., & Reichert, A. S. (2009) · Biological Chemistry · doi:10.1515/bc.2009.086 · Cited by 32
Fusing a lasting relationship between ER tubules
Moss, T. J., Daga, A., & McNew, J. A. (2011) · Trends in Cell Biology · doi:10.1016/j.tcb.2011.03.009 · Cited by 32
The promoter activity of human Mfn2 depends on Sp1 in vascular smooth muscle cells
Sorianello, E. M., Soriano, F. X., Fernández‐Pascual, S., Sancho, A., Naón, D., Vila-Caballer, M., Navarro, H. G., Portugal, J., Andrés, V., Palacı́n, M., et al. (2012) · Cardiovascular Research · doi:10.1093/cvr/cvs006 · Cited by 32
The antiapoptotic OPA1/Parl couple participates in mitochondrial adaptation to heat shock
Szklarz, L. K. S., & Scorrano, L. (2012) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.05.001 · Cited by 32
(Neuro)degenerated Mitochondria-ER contacts
Mario, A. D., Quintana–Cabrera, R., Martinvalet, D., & Giacomello, M. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.07.056 · Cited by 35
Guardia, C. M. A., Pace, R. D., Sen, A., Sarić, A., Jarník, M., Kolin, D. A., Kunwar, A., & Bonifacino, J. S. (2019) · PLoS Biology · doi:10.1371/journal.pbio.3000279 · Cited by 31
Eshima, H. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.758316 · Cited by 31
Involvement of Dynamin-Related Protein 1 in Free Fatty Acid-Induced INS-1-Derived Cell Apoptosis
Peng, L., Men, X., Zhang, W., Wang, H., Xu, S., Fang, Q., Liu, H., Yang, W., & Lou, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0049258 · Cited by 31
Vadnais, M. L., Lin, A. M., & Gerton, G. L. (2014) · Cilia · doi:10.1186/2046-2530-3-5 · Cited by 32
Multiple recycling routes: Canonical vs. non-canonical mitophagy in the heart
Moyzis, A. G., & Gustafsson, Å. B. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.09.034 · Cited by 33
Within the cell: analytical techniques for subcellular analysis
Olson, K. J., Ahmadzadeh, H., & Arriaga, E. A. (2005) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-005-3135-2 · Cited by 32
A human mitofusin 2 mutation can cause mitophagic cardiomyopathy
Franco, A., Li, J., Kelly, D. P., Hershberger, R. E., Marian, A. J., Lewis, R. M., Song, M., Dang, X., Schmidt, A. D., Mathyer, M. E., et al. (2023) · eLife · doi:10.7554/elife.84235 · Cited by 31
Interfaces between mitochondrial dynamics and disease
Mishra, P. (2016) · Cell Calcium · doi:10.1016/j.ceca.2016.05.004 · Cited by 32
Tak, H., Eun, J. W., Kim, J., Park, S. J., Kim, C., Ji, E., Lee, H., Kang, H., Cho, D., Lee, K., et al. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2016.90 · Cited by 31
L‐OPA1 regulates mitoflash biogenesis independently from membrane fusion
Rosselin, M., Domingo, J. S., Bermont, F., Giacomello, M., & Demaurex, N. (2017) · EMBO Reports · doi:10.15252/embr.201642931 · Cited by 30
Free Radical Medicine and Biology
Das, K. K., Das, S. N., Biradar, M. S., Bobbarala, V., & Tata, S. S. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.77829 · Cited by 32
When the Balance Tips: Dysregulation of Mitochondrial Dynamics as a Culprit in Disease
Kyriakoudi, S., Drousiotou, A., & Petrou, P. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094617 · Cited by 33
Oocyte mitophagy is critical for extended reproductive longevity
Cota, V., Sohrabi, S., Kaletsky, R. L., & Murphy, C. T. (2022) · PLoS Genetics · doi:10.1371/journal.pgen.1010400 · Cited by 32
Baker, C., & Ebert, S. N. (2013) · OA Biotechnology · doi:10.13172/2052-0069-2-2-571 · Cited by 30
Precise expression of Fis1 is important for glucose responsiveness of beta cells
Schultz, J., Waterstradt, R., Kantowski, T., Rickmann, A., Reinhardt, F., Sharoyko, V. V., Mulder, H., Tiedge, M., & Baltrusch, S. (2016) · Journal of Endocrinology · doi:10.1530/joe-16-0111 · Cited by 32
The role of circadian clock-controlled mitochondrial dynamics in diabetic cardiomyopathy
Jin, Z., Ji, Y., Su, W., Zhou, L., Wu, X., Gao, L., Guo, J., Liu, Y., Zhang, Y., Wen, X., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1142512 · Cited by 34
Liu, G., Mei, H., Chen, M., Qin, S., Li, K., Zhang, W., & Chen, T. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.04.164 · Cited by 30
Hussain, Y., Khan, H. Z., Efferth, T., & Alam, W. (2022) · Phytomedicine · doi:10.1016/j.phymed.2022.153985 · Cited by 28
Rawat, A. K., Korthikunta, V., Gautam, S., Pal, S., Narender, T., Tamrakar, A. K., & Srivastava, R. (2014) · Fitoterapia · doi:10.1016/j.fitote.2014.10.006 · Cited by 29
Mitochondria and the regulation of hypervirulence in the fatal fungal outbreak on Vancouver Island
Ma, H., & May, R. C. (2010) · Virulence · doi:10.4161/viru.1.3.11053 · Cited by 30
Renkawitz‐Pohl, R., Hempel, L. U., Hollmann, M., & Schäfer, M. (2005) · Elsevier eBooks · doi:10.1016/b0-44-451924-6/00011-9 · Cited by 30
Divide et impera: Ca2+ signals, mitochondrial fission and sensitization to apoptosis
Scorrano, L. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401310 · Cited by 30
A membrane-inserted structural model of the yeast mitofusin Fzo1
Vecchis, D. D., Cavellini, L., Baaden, M., Hénin, J., Cohen, M. M., & Taly, A. (2017) · Scientific Reports · doi:10.1038/s41598-017-10687-2 · Cited by 30
Transcriptional Regulation of ROS Homeostasis by the ERR Subfamily of Nuclear Receptors
Scholtes, C., & Giguère, V. (2021) · Antioxidants · doi:10.3390/antiox10030437 · Cited by 33
Eschenbacher, W. H., Song, M., Chen, Y., Bhandari, P., Zhao, P. Y., Jowdy, C. C., Engelhard, J. T., & Dorn, G. W. (2012) · PLoS ONE · doi:10.1371/journal.pone.0044296 · Cited by 31
Banerjee, S., & Balaji, C. (2014) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2014.05.041 · Cited by 29
Upstream Pathways Controlling Mitochondrial Function in Major Psychosis
Machado, A. K., Pan, A. Y., da Silva, T. M., Duong, A., & Andreazza, A. C. (2016) · The Canadian Journal of Psychiatry · doi:10.1177/0706743716648297 · Cited by 30
Cho, H., Sung, D., Kim, B., & Ki, C. (2007) · Clinical Genetics · doi:10.1111/j.1399-0004.2007.00763.x · Cited by 29
Mitochondria as mediators of systemic inflammation and organ cross talk in acute kidney injury
Hepokoski, M., & Singh, P. (2022) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00372.2021 · Cited by 29
Mitochondrial quality control in the brain: The physiological and pathological roles
Shen, X., Sun, P., Zhang, H., & Yang, H. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.1075141 · Cited by 30
Peng, L., Men, X.-L., Zhang, W.-J., Wang, H.-Y., Xu, S.-Q., Xu, M., Xu, Y., Yang, W., & Lou, J. (2011) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2011.684 · Cited by 33
Mitochondrial Dynamics in the Heart as a Novel Therapeutic Target for Cardioprotection
Hwang, S. J., & Kim, W. (2013) · Chonnam Medical Journal · doi:10.4068/cmj.2013.49.3.101 · Cited by 29
Mukherjee, A., Patra, U., Bhowmick, R., & Chawla‐Sarkar, M. (2018) · Cellular Microbiology · doi:10.1111/cmi.12831 · Cited by 29
Feng, M. H., Wang, L., Chang, S., & Yuan, P. (2018) · European Journal of Pharmaceutical Sciences · doi:10.1016/j.ejps.2018.05.023 · Cited by 28
Cherubini, M., & Ginés, S. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.08.042 · Cited by 28
Li, Y., Dong, W., Shan, X., Hong, H., Liu, Y., Liu, Y., Liu, X., Zhang, X., & Zhang, J. (2018) · Oncology Letters · doi:10.3892/ol.2018.8314 · Cited by 27
Clonorchis sinensis and Clonorchiasis: The Relevance of Exploring Genetic Variation
Wang, D., Young, N. D., Korhonen, P. K., & Gasser, R. B. (2018) · Advances in Parasitology/Advances in parasitology · doi:10.1016/bs.apar.2018.03.006 · Cited by 26
Xue, R., Yang, J., Jia, L., Zhu, X., Wu, J., Zhu, Y., & Meng, Q. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00601 · Cited by 27
Pakpian, N., Phopin, K., Kitidee, K., Govitrapong, P., & Wongchitrat, P. (2020) · Current Alzheimer Research · doi:10.2174/1567205017666201006162538 · Cited by 28
A novel role for kynurenine 3-monooxygenase in mitochondrial dynamics
Maddison, D. C., Alfonso-Núñez, M., Swaih, A. M., Breda, C., Campesan, S., Allcock, N., Straatman-Iwanowska, A. A., Kyriacou, C. P., & Giorgini, F. (2020) · PLoS Genetics · doi:10.1371/journal.pgen.1009129 · Cited by 30
Zhang, X., Wang, C., Song, G., Gan, K., Kong, D., Nie, Q., & Ren, L. (2013) · Journal of Biomedical Science · doi:10.1186/1423-0127-20-45 · Cited by 27
Zebrafish Tg(hb9:MTS-Kaede): a new in vivo tool for studying the axonal movement of mitochondria
Bergamin, G., Cieri, D., Vazza, G., Argenton, F., & Mostacciuolo, M. L. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.03.007 · Cited by 27
van Herpen, R. E. M. A., Ophuis, R. J. A. O., Wijers, M., Bennink, M. B., van de Loo, F. A. J., Fransen, J. A. M., Wieringa, B., & Wansink, D. G. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.4.1402-1414.2005 · Cited by 27
Role of Astrocytic Mitochondria in Limiting Ischemic Brain Injury?
Shih, E. K., & Robinson, M. B. (2018) · Physiology · doi:10.1152/physiol.00038.2017 · Cited by 27
Jilly, R., Khan, N. Z., Aronsson, H., & Schneider, D. (2018) · Frontiers in Plant Science · doi:10.3389/fpls.2018.00206 · Cited by 26
Identifying Plectin Isoform Functions through Animal Models
Castañón, M. J., & Wiche, G. (2021) · Cells · doi:10.3390/cells10092453 · Cited by 26
Franco, A., Dang, X., Zhang, L., Molinoff, P. B., & Dorn, G. W. (2022) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.122.001332 · Cited by 28
Mitofusin-2: Functional switch between mitochondrial function and neurodegeneration
Kulkarni, P. G., Mohire, V. M., Bhaisa, P. K., Joshi, M., Puranik, C. M., Waghmare, P. P., & Banerjee, T. (2023) · Mitochondrion · doi:10.1016/j.mito.2023.02.001 · Cited by 27
Wolf, C., Zimmermann, R., Thaher, O., Bueno, D., Wüllner, V., Schäfer, M. K. E., Albrecht, P., & Methner, A. (2019) · Cells · doi:10.3390/cells8101289 · Cited by 26
Chen, W., Lv, L., Nong, Z., Chen, X., Pan, X., & Chen, C. (2020) · Molecular Medicine Reports · doi:10.3892/mmr.2020.11497 · Cited by 27
Sharpening the Scissors: Mitochondrial Fission With Aid
Yoon, Y. (2004) · Cell Biochemistry and Biophysics · doi:10.1385/cbb:41:2:193 · Cited by 27
Inter-mitochondrial complementation of mtDNA mutations and nuclear context
Attardi, G. M., Enrı́quez, J. A., & Cabezas‐Herrera, J. (2002) · Nature Genetics · doi:10.1038/ng0402-360 · Cited by 26
Alghamdi, A. (2024) · Saudi Pharmaceutical Journal · doi:10.1016/j.jsps.2024.102012 · Cited by 26
Proteomic analysis of mitochondria associated membranes in renal ischemic reperfusion injury
Li, Y., Wang, H., Cao, J., Zhang, W.-J., Wang, H., Xu, C.-H., Li, K., Liu, Y., Wang, J., Ha, H.-L., et al. (2024) · Journal of Translational Medicine · doi:10.1186/s12967-024-05021-0 · Cited by 25
Truong, T. T., Singh, A. A., Bang, N. V., Vu, N. M. H., Na, S., Choi, J., Oh, J., & Mondal, S. (2025) · Membranes · doi:10.3390/membranes15090263 · Cited by 25
Ma, S., Qin, J., Zhang, Y., Luan, J., Sun, N., Hou, G., He, J., Xiao, Y., Zhang, W., & Gao, M. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116234 · Cited by 30
Lee, J. E., Seo, B. J., Han, M. J., Hong, Y. J., Hong, K., Song, H., Lee, J.-W., & Tae, J. (2020) · Stem Cells International · doi:10.1155/2020/9369268 · Cited by 25
Mitochondrial Surveillance by Cdc48/p97: MAD vs. Membrane Fusion
Escobar‐Henriques, M., & Anton, V. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186841 · Cited by 26
Zhang, Y., Fu, X., Li, Y., Li, W., Hong, G., Guo, S., Xiao, Y., Liu, Z., Ding, S., Bi, X., et al. (2022) · Human Molecular Genetics · doi:10.1093/hmg/ddac270 · Cited by 26
Johnson, D., Allman, E. L., & Nehrke, K. W. (2012) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00411.2011 · Cited by 25
Mitochondrial fusion: Reaching the end of mitofusin’s tether
Formosa, L. E., & Ryan, M. T. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201611048 · Cited by 22
Marchi, S., Bonora, M., Patergnani, S., Giorgi, C., & Pinton, P. (2016) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2016.09.080 · Cited by 25
Molecular Basis of Mitochondrial and Peroxisomal Division Machineries
Imoto, Y., Itoh, K., & Fujiki, Y. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155452 · Cited by 27
MacVicar, T. (2013) · Essays in Biochemistry · doi:10.1042/bse0550093 · Cited by 27
Protein misfolding and mitochondrial dysfunction in glaucoma
Venkatesan, A., & Bernstein, A. M. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1595121 · Cited by 24
Control by Ca2+ of mitochondrial structure and function in pancreatic β-cells
Georgiadou, E., & Rutter, G. A. (2020) · Cell Calcium · doi:10.1016/j.ceca.2020.102282 · Cited by 24
Byun, K.-A., Oh, S., Yang, J. Y., Lee, S., Son, K. H., & Byun, K. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113283 · Cited by 24
Wojtyniak, P., Boratyńska-Jasińska, A., Serwach, K., Gruszczynska‐Biegala, J., Zabłocka, B., Jaworski, J., & Kawalec, M. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-02981-6 · Cited by 26
MTCH2 cooperates with MFN2 and lysophosphatidic acid synthesis to sustain mitochondrial fusion
Goldman, A., Mullokandov, M., Zaltsman, Y., Regev, L., Levin‐Zaidman, S., & Gross, A. (2023) · EMBO Reports · doi:10.1038/s44319-023-00009-1 · Cited by 25
Zhao, G., Yao, Y.-M., Lu, Z., Hong, G., Zhu, X.-M., Wu, Y., Wang, D., Dong, N., Yu, Y., & Sheng, Z.-Y. (2012) · Cytokine · doi:10.1016/j.cyto.2012.03.026 · Cited by 24
The ARL2 GTPase regulates mitochondrial fusion from the intermembrane space
Newman, L. E., Schiavon, C. R., Turn, R. E., & Kahn, R. (2017) · Cellular Logistics · doi:10.1080/21592799.2017.1340104 · Cited by 24
Μitochondrial Membrane Dynamics and Inherited Optic Neuropathies
Bagli, E., Zikou, A. K., Agnantis, N. J., & Kitsos, G. (2017) · In Vivo · doi:10.21873/invivo.11090 · Cited by 24
S6 kinase 1 plays a key role in mitochondrial morphology and cellular energy flow
Tran, Q., Jung, J.-H., Park, J., Lee, H., Hong, Y., Cho, H., Kim, M., Park, S. J., Kwon, S.-H., Kim, S., et al. (2018) · Cellular Signalling · doi:10.1016/j.cellsig.2018.04.002 · Cited by 24
Hoebeke, C., Bonello‐Palot, N., Audic, F., Boulay, C., Tufod, D., Attarian, S., & Chabrol, B. (2018) · Archives de Pédiatrie · doi:10.1016/j.arcped.2018.09.006 · Cited by 24
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