The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Mitofusin 2 tethers endoplasmic reticulum to mitochondria
Open accessAbstract
Juxtaposition between endoplasmic reticulum (ER) and mitochondria is a common structural feature, providing the physical basis for intercommunication during Ca(2+) signalling; yet, the molecular mechanisms controlling this interaction are unknown. Here we show that mitofusin 2, a mitochondrial dynamin-related protein mutated in the inherited motor neuropathy Charcot-Marie-Tooth type IIa, is enriched at the ER-mitochondria interface. Ablation or silencing of mitofusin 2 in mouse embryonic fibroblasts and HeLa cells disrupts ER morphology and loosens ER-mitochondria interactions, thereby reducing the efficiency of mitochondrial Ca(2+) uptake in response to stimuli that generate inositol-1,4,5-trisphosphate. An in vitro assay as well as genetic and biochemical evidences support a model in which mitofusin 2 on the ER bridges the two organelles by engaging in homotypic and heterotypic complexes with mitofusin 1 or 2 on the surface of mitochondria. Thus, mitofusin 2 tethers ER to mitochondria, a juxtaposition required for efficient mitochondrial Ca(2+) uptake.
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
“Other important MAM tethering proteins are B-cell receptor–associated protein 31, mitochondrial fission 1 protein [96], and mitofusin [97].”
From Neuronal Apolipoprotein E4 Expression Results in Proteome-Wide Alterations and Compromises Bioenergetic Capacity by Disrupting Mitochondrial Function (2019) · cites this paper as [97]
In the citing paper
“Marf/Mfn is a mitochondrial fusion protein with pleiotropic functions [39,40] that is also a target of Parkin-dependent ubiquitination upon stress-induced mitophagy.”
From USP8 Down-Regulation Promotes Parkin-Independent Mitophagy in the Drosophila Brain and in Human Neurons (2023) · cites this paper as [39]
In the citing paper
“MFN2, and not MFN1, is expressed on the mitochondria-associated endoplasmic reticulum membranes (MAM) and, to a lesser extent, to the endoplasmic/sarcoplasmic reticulum (ER/SR) [63, 64].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [63]
In the citing paper
“Indeed, MFN2 bridges mitochondria to ER/SR, facilitating critical processes linked to ER–mitochondria interactions like calcium homeostasis and the modulation of the UPR during ER stress via PERK [63, 65–68].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [63]
In the citing paper
“ER stress is induced by the decrease of the ER–mitochondria tethering protein Mfn2 and the down- and upregulation of the ER chaperones calnexin and Bip/Grp78, respectively [63, 65, 66, 213].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [63]
In the citing paper
“Despite some redundancies in their function, the two proteins possess several distinct properties, suggesting that they fulfill different roles in fusion (de Brito and Scorrano, 2008; Eura et al., 2003; Ishihara et al., 2004).”
From New insights into the role of mitochondria in aging: mitochondrial dynamics and more (2010) · cites this paper as de Brito and Scorrano, 2008
Citations
Cites
Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., & Chan, D. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211046 · Cited by 2,601
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
Measurement of co‐localization of objects in dual‐colour confocal images
Manders, E. M. M., Verbeek, F. J., & Aten, J. A. (1993) · Journal of Microscopy · doi:10.1111/j.1365-2818.1993.tb03313.x · Cited by 2,132
OPA1 Controls Apoptotic Cristae Remodeling Independently from Mitochondrial Fusion
Frezza, C., Cipolat, S., Martins de Brito, O., Micaroni, M., Beznoussenko, G. V., Rudka, T., Bartoli, D., Polishuck, R. S., Danial, N. N., De Strooper, B., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.025 · Cited by 1,673
Self-citationMutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A
Züchner, S., Mersiyanova, I. V., Muglia, M., Bissar-Tadmouri, N., Rochelle, J., Dadali, E. L., Zappia, M., Nelis, E., Patitucci, A., Senderek, J., et al. (2004) · Nature Genetics · doi:10.1038/ng1341 · Cited by 1,572
Organelle-specific initiation of cell death pathways
Ferri, K. F., & Kroemer, G. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-e255 · Cited by 1,455
BAX and BAK Regulation of Endoplasmic Reticulum Ca 2+ : A Control Point for Apoptosis
Scorrano, L., Oakes, S. A., Opferman, J. T., Cheng, E. H. Y., Sorcinelli, M. D., Pozzan, T., & Korsmeyer, S. J. (2003) · Science · doi:10.1126/science.1081208 · Cited by 1,387
Self-citationCsordás, G., Renken, C. W., Várnai, P., Walter, L., Weaver, D., BUTTLE, K. F., Balla, T., Mannella, C. A., & Hajnóczky, G. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200604016 · Cited by 1,377
Disruption of Fusion Results in Mitochondrial Heterogeneity and Dysfunction
Chen, H., Chomyn, A., & Chan, D. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503062200 · Cited by 1,376
OPA1 requires mitofusin 1 to promote mitochondrial fusion
Cipolat, S., de Brito, O. M., Dal Zilio, B., & Scorrano, L. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407043101 · Cited by 1,300
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Items 601–700 of 1,010
Du, F., Yan, S., Yu, Q., Chen, D., & Yan, S. S. (2016) · Scientific Reports · doi:10.1038/srep31462 · Cited by 109
Ramalingam, M., Huh, Y.-J., & Lee, Y. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01028 · Cited by 109
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
The MAMs Structure and Its Role in Cell Death
Wang, N., Wang, C., Zhao, H., He, Y., Lan, B., Sun, L., & Gao, Y. (2021) · Cells · doi:10.3390/cells10030657 · Cited by 110
Ca2+ handling at the mitochondria-ER contact sites in neurodegeneration
Lim, D., Dematteis, G., Tapella, L., Genazzani, A. A., Calí, T., Brini, M., & Verkhratsky, A. (2021) · Cell Calcium · doi:10.1016/j.ceca.2021.102453 · Cited by 109
Li, M., Fu, L., Lv, B.-B., Xiang, Y., Xiang, H.-X., Xu, D., & Zhao, H. (2022) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2022.113595 · Cited by 113
Calcium signaling at ER membrane contact sites
Burgoyne, T., Patel, S., & Eden, E. R. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.01.022 · Cited by 109
Wang, X., Olberding, K. E., White, C., & Li, C. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2010.68 · Cited by 108
Kmiecik, P., Leonardelli, M., & Teige, M. (2016) · Journal of Experimental Botany · doi:10.1093/jxb/erw136 · Cited by 108
Liu, Z., Gu, S., Lu, T., Wu, K., Li, L., Dong, C., & Zhou, Y. (2020) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-020-01646-3 · Cited by 108
Inhibition of mitochondrial fission favours mutant over wild-type mitochondrial DNA
Malena, A., Loro, E., Di Re, M., Holt, I. J., & Vergani, L. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp281 · Cited by 107
Tamura, Y., Onguka, O., Hobbs, A. E. A., Jensen, R. E., Iijima, M., Claypool, S. M., & Sesaki, H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.338665 · Cited by 107
Lee, S., Lee, K., Huh, S., Liu, S., Lee, D.-Y., Hong, S. H., Yu, K., & Lu, B. (2016) · Developmental Cell · doi:10.1016/j.devcel.2016.03.023 · Cited by 107
ER Lipid Defects in Neuropeptidergic Neurons Impair Sleep Patterns in Parkinson’s Disease
Valadas, J. S., Esposito, G., Vandekerkhove, D., Miśkiewicz, K., Deaulmerie, L., Raitano, S., Seibler, P., Klein, C., & Verstreken, P. (2018) · Neuron · doi:10.1016/j.neuron.2018.05.022 · Cited by 107
Lysosomal Regulation of Inter-mitochondrial Contact Fate and Motility in Charcot-Marie-Tooth Type 2
Wong, Y. C., Peng, W., & Krainc, D. (2019) · Developmental Cell · doi:10.1016/j.devcel.2019.05.033 · Cited by 107
Toyofuku, T., Okamoto, Y., Ishikawa, T., Sasawatari, S., & Kumanogoh, A. (2019) · The EMBO Journal · doi:10.15252/embj.2018100875 · Cited by 107
An overview of ferroptosis in non-alcoholic fatty liver disease
Wang, S., Liu, Z., Geng, J., Li, L., & Feng, X. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113374 · Cited by 107
Min, C. K., Yeom, D. R., Lee, K., Kwon, H.-K., Kang, M., Kim, Y.-S., Park, Z., Jeon, H., & Kim, D. H. (2012) · Biochemical Journal · doi:10.1042/bj20120705 · Cited by 107
ATPase family AAA domain-containing 3A is a novel anti-apoptotic factor in lung adenocarcinoma cells
Fang, H., Chang, C.-L., Hsu, S., Huang, K. C., Chiang, S., Chiou, S.-H., Huang, C.-H., Hsiao, Y.-T., Lin, T., Chiang, I., et al. (2010) · Journal of Cell Science · doi:10.1242/jcs.062034 · Cited by 107
Elgass, K., Smith, E. A., LeGros, M., Larabell, C. A., & Ryan, M. T. (2015) · Journal of Cell Science · doi:10.1242/jcs.169136 · Cited by 106
The mitochondrial dynamics in cancer and immune-surveillance
Simula, L., Nazio, F., & Campello, S. (2017) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2017.06.007 · Cited by 106
Metabolic flexibility in melanoma: A potential therapeutic target
Ruocco, M. R., Avagliano, A., Granato, G., Vigliar, E., Masone, S., Montagnani, S., & Arcucci, A. (2019) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2019.07.016 · Cited by 106
Phospholipid ebb and flow makes mitochondria go
Acoba, M. G., Senoo, N., & Claypool, S. M. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.202003131 · Cited by 106
New Insights into the Role of Mitochondria-Associated Endoplasmic Reticulum Membrane
Fujimoto, M., & Hayashi, T. (2011) · International review of cytology · doi:10.1016/b978-0-12-386033-0.00002-5 · Cited by 106
Mitochondrial regulation of β-cell function: Maintaining the momentum for insulin release
Kaufman, B. A., Li, C., & Soleimanpour, S. A. (2015) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2015.01.004 · Cited by 107
Barbero‐Camps, E., Fernández, A., Baulies, A., Martínez-Gili, L., Fernández-Checa, J. C., & Colell, A. (2014) · American Journal Of Pathology · doi:10.1016/j.ajpath.2014.03.014 · Cited by 106
Sullivan, E. M., Pennington, E. R., Green, W. D., Beck, M. A., Brown, D. A., & Shaikh, S. R. (2018) · Advances in Nutrition · doi:10.1093/advances/nmy007 · Cited by 105
Mitochondrial Fission and Fusion in Tumor Progression to Metastasis
Boulton, D. P., & Caino, M. C. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.849962 · Cited by 108
Lei, Y., Gan, M., Qiu, Y., Chen, Q., Wang, X., Liao, T., Zhao, M., Chen, L., Zhang, S., Zhao, Y., et al. (2024) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-024-00572-y · Cited by 111
Mitochondria in heart failure: the emerging role of mitochondrial dynamics
Marín-García, J., Akhmedov, A. T., & Moe, G. W. P. L. (2012) · Heart Failure Reviews · doi:10.1007/s10741-012-9330-2 · 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
Gutiérrez, T., & Simmen, T. (2018) · Cell Calcium · doi:10.1016/j.ceca.2017.05.015 · Cited by 104
East, D. A., & Campanella, M. (2013) · Autophagy · doi:10.4161/auto.25367 · Cited by 105
Norkett, R., Modi, S., Birsa, N., Atkin, T. A., Ivankovic, D., Pathania, M., Trossbach, S. V., Korth, C., Hirst, W. D., & Kittler, J. T. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.699447 · Cited by 104
Madreiter‐Sokolowski, C. T., Gottschalk, B., Parichatikanond, W., Eroğlu, E., Klec, C., Waldeck‐Weiermair, M., Malli, R., & Graier, W. F. (2016) · Cellular Physiology and Biochemistry · doi:10.1159/000447844 · Cited by 104
Highlighting the endoplasmic reticulum-mitochondria connection: Focus on Mitofusin 2
Filadi, R., Greotti, E., & Pizzo, P. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.01.003 · Cited by 104
The role of mitochondrial cardiolipin in heart function and its implication in cardiac disease
Dudek, J., Hartmann, M., & Rehling, P. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.08.025 · Cited by 104
Li, J., Liu, X., Wang, H., Zhang, W., Chan, D. C., & Shi, Y. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1120043109 · Cited by 104
de Oliveira, C. C. F., Busquets, S., Toledo, M., Penna, F., Aylwin, M. P., Sirisi, S., Ventura‐Silva, A. P., Orpí, M., García, A., Sette, A., et al. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.11.009 · Cited by 104
Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity
López-Lluch, G. (2017) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2016.12.005 · Cited by 103
“Mfn2 is also associated in the connection between mitochondria and the endoplasmic reticulum (ER) playing a role in the development of endoplasmic reticulum (ER) stress and fat accumulation in conditions of metabolic stress (de Brito and Scorrano, 2008, 2009).”
BackgroundOrr, A. L., Kim, C., Jimenez-Morales, D., Newton, B. W., Johnson, J. R., Krogan, N. J., Swaney, D. L., & Mahley, R. W. (2019) · Journal of Alzheimer's Disease · doi:10.3233/jad-181184 · Cited by 103
Mitophagy in the pathogenesis and management of disease
Wang, Q., Sun, Y., Li, T. Y., & Auwerx, J. (2026) · Cell Research · doi:10.1038/s41422-025-01203-7 · Cited by 103
Samanta, K., Douglas, S. G., & Parekh, A. B. (2014) · PLoS ONE · doi:10.1371/journal.pone.0101188 · Cited by 103
Organelle plasticity and interactions in cholesterol transport and steroid biosynthesis
Issop, L., Rone, M. B., & Papadopoulos, V. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2012.12.003 · Cited by 103
Mitochondrial-Shaping Proteins in Cardiac Health and Disease – the Long and the Short of It!
Ong, S., Kalkhoran, S. B., Hernández‐Reséndiz, S., Samangouei, P., Ong, S., & Hausenloy, D. J. (2017) · Cardiovascular Drugs and Therapy · doi:10.1007/s10557-016-6710-1 · Cited by 103
Mitochondrial energetics and calcium coupling in the heart
Kohlhaas, M., Nickel, A. G., & Maack, C. (2017) · The Journal of Physiology · doi:10.1113/jp273609 · Cited by 102
Bernard‐Marissal, N., van Hameren, G., Juneja, M., Pellegrino, C., Louhivuori, L. M., Bartesaghi, L., Rochat, C., Mansour, O. E., Médard, J., Croisier, M., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1810932116 · Cited by 103
Restoring mitofusin balance prevents axonal degeneration in a Charcot-Marie-Tooth type 2A model
Zhou, Y., Carmona, S., Muhammad, A. K. M. G., Bell, S., Landeros, J., Vazquez, M., Ho, R., Franco, A., Lü, B., Dorn, G. W., et al. (2019) · Journal of Clinical Investigation · doi:10.1172/jci124194 · Cited by 102
Local Mitochondrial ATP Production Regulates Endothelial Fatty Acid Uptake and Transport
Ibrahim, A., Yucel, N. D., Kim, B., & Arany, Z. P. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.05.018 · Cited by 102
Yuan, M., Gong, M., Zhang, Z., Meng, L., Tse, G., Zhao, Y., Bao, Q., Zhang, Y., Yuan, M., Liu, X., et al. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/6569728 · Cited by 102
Adverse Bioenergetic Consequences of Na + -Ca 2+ Exchanger–Mediated Ca 2+ Influx in Cardiac Myocytes
Kohlhaas, M., & Maack, C. (2010) · Circulation · doi:10.1161/circulationaha.110.968057 · Cited by 102
Hereditary spastic paraplegia‐linked REEP1 modulates endoplasmic reticulum/mitochondria contacts
Lim, Y., Cho, I., Schoel, L. J., Cho, G., & Golden, J. A. (2015) · Annals of Neurology · doi:10.1002/ana.24488 · Cited by 102
Autophagy: an affair of the heart
Gottlieb, R. A., & Mentzer, R. M. (2012) · Heart Failure Reviews · doi:10.1007/s10741-012-9367-2 · Cited by 101
Autophagosome biogenesis and human health
Kawabata, T., & Yoshimori, T. (2020) · Cell Discovery · doi:10.1038/s41421-020-0166-y · Cited by 102
Yang, J., Xing, X., Luo, L., Zhou, X., Feng, J.-X., Huang, K., Liu, H., Jin, S., Liu, Y.-N., Zhang, S.-H., et al. (2023) · Science Immunology · doi:10.1126/sciimmunol.abq2424 · Cited by 101
Anti-Tumor Effects of Mfn2 in Gastric Cancer
Zhang, G., Jin, H., Lin, X.-K., Chen, C., Liu, X., Zhang, Q., & Yu, J. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms140713005 · Cited by 101
Singaravelu, K., Nelson, C., Bakowski, D., de Brito, O. M., Ng, S.-W., Capite, J. L. D., Powell, T., Scorrano, L., & Parekh, A. B. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.174029 · Cited by 101
Self-citationThe Maintenance of Mitochondrial DNA Integrity and Dynamics by Mitochondrial Membranes
Chapman, J., Ng, Y. S., & Nicholls, T. J. J. (2020) · Life · doi:10.3390/life10090164 · Cited by 100
Sidarala, V., Zhu, J., Levi-D’Ancona, E., Pearson, G. L., Reck, E. C., Walker, E. M., Kaufman, B. A., & Soleimanpour, S. A. (2022) · Nature Communications · doi:10.1038/s41467-022-29945-7 · Cited by 100
The ER-mitochondria interface, where Ca2+ and cell death meet
de Ridder, I., Kerkhofs, M., Lemos, F. O., Loncke, J., Bultynck, G., & Parys, J. B. (2023) · Cell Calcium · doi:10.1016/j.ceca.2023.102743 · Cited by 104
Mechanistic perspective of mitochondrial fusion: Tubulation vs. fragmentation
Escobar‐Henriques, M., & den Brave, F. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.07.016 · Cited by 100
Mitochondria-Associated Membranes As Networking Platforms and Regulators of Cancer Cell Fate
Sassano, M. L., van Vliet, A. R., & Agostinis, P. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00174 · Cited by 100
Zhang, M., Bener, M. B., Jiang, Z., Wang, T., Esencan, E., Scott, R., Horváth, T. L., & Seli, E. U. (2019) · Aging · doi:10.18632/aging.102024 · Cited by 99
Unraveling the Link Between Mitochondrial Dynamics and Neuroinflammation
de Oliveira, L. G., Angelo, Y. D. S., Iglesias, A. H., & Peron, J. P. S. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.624919 · Cited by 100
Mitochondrial pathophysiology in Friedreich's ataxia
González‐Cabo, P., & Palau, F. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12303 · Cited by 99
Is Alzheimer's Disease a Disorder of Mitochondria-Associated Membranes?
Schon, E. A., & Área-Gómez, E. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100495 · Cited by 98
Postmortem studies on mitochondria in schizophrenia
Roberts, R. C. (2017) · Schizophrenia Research · doi:10.1016/j.schres.2017.01.056 · Cited by 98
Interorganelle Communication between Mitochondria and the Endolysosomal System
Soto‐Heredero, G., Baixauli, F., & Mittelbrunn, M. (2017) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2017.00095 · Cited by 98
Seipin regulates lipid homeostasis by ensuring calcium‐dependent mitochondrial metabolism
Ding, L., Yang, X. N., Tian, H., Liang, J., Zhang, F., Wang, G., Wang, Y., Ding, M., Shui, G., & Huang, X. (2018) · The EMBO Journal · doi:10.15252/embj.201797572 · Cited by 98
Restelli, L. M., Oettinghaus, B., Halliday, M., Ağca, C., Licci, M., Sironi, L., Savoia, C., Hench, J., Tolnay, M., Neutzner, A., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.07.023 · Cited by 98
Self-citationVeeresh, P., Kaur, H., Sarmah, D., Mounica, L., Verma, G., Kotian, V., Kesharwani, R., Kalia, K., Borah, A., Wang, X., et al. (2019) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.14212 · Cited by 98
Jiang, H., Fu, H., Guo, Y., Hu, P., & Shi, J. (2022) · Biomaterials · doi:10.1016/j.biomaterials.2022.121799 · Cited by 98
Kuo, I. Y., Brill, A. L., Lemos, F. O., Jiang, J., Falcone, J. L., Kimmerling, E. P., Cai, Y., Dong, K., Kaplan, D. L., Wallace, D. P., et al. (2019) · Science Signaling · doi:10.1126/scisignal.aat7397 · Cited by 97
Harnessing Hematopoietic Stem Cell Low Intracellular Calcium Improves Their Maintenance In Vitro
Luchsinger, L. L., Strikoudis, A., Danzl, N. M., Bush, E. C., Finlayson, M. O., Satwani, P., Sykes, M., Yazawa, M., & Snoeck, H. (2019) · Cell stem cell · doi:10.1016/j.stem.2019.05.002 · Cited by 100
ER-mitochondria contact sites; a multifaceted factory for Ca2+ signaling and lipid transport
Sassano, M. L., Felipe‐Abrio, B., & Agostinis, P. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.988014 · Cited by 97
The optic nerve: A “mito-window” on mitochondrial neurodegeneration
Maresca, A., Morgia, C. L., Caporali, L., Valentino, M. L., & Carelli, V. (2012) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2012.08.004 · Cited by 97
Mitochondrial dysfunction in glaucoma: Understanding genetic influences
Lascaratos, G., Garway‐Heath, D. F., Willoughby, C. E., Chau, K., & Schapira, A. H. V. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.11.004 · Cited by 97
Mitochondria in cardiomyocyte Ca2+ signaling
Lukyanenko, V. I., Chikando, A. C., & Lederer, W. J. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.03.011 · Cited by 97
Goizet, C., Depienne, C., Bénard, G., Boukhris, A., Mundwiller, E., Solé, G., Coupry, I., Pilliod, J., Martin‐Négrier, M., Fédirko, E., et al. (2011) · Human Mutation · doi:10.1002/humu.21542 · Cited by 97
Zhang, Y., Yang, L., Yuan-fu, G., Fan, Z., Cai, X., Liu, M., Guo, X., Gao, C., & Xia, Z. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2013.08.004 · Cited by 96
Opening the doors to cytochrome c: Changes in mitochondrial shape and apoptosis
Scorrano, L. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.04.016 · Cited by 96
Self-citationDsbA-L ameliorates high glucose induced tubular damage through maintaining MAM integrity
Yang, M., Zhao, L., Gao, P., Zhu, X., Han, Y., Chen, X., Li, L., Xiao, Y., Wei, L., Li, C., et al. (2019) · EBioMedicine · doi:10.1016/j.ebiom.2019.04.044 · Cited by 96
New insights into targeting mitochondria in ischemic injury
Jia, J., Jin, H., Nan, D., Yu, W., & Huang, Y. (2021) · APOPTOSIS · doi:10.1007/s10495-021-01661-5 · Cited by 97
Scheffer, D. D. L., Garcia, A. A., Lee, L., Mochly‐Rosen, D., & Ferreira, J. C. B. (2022) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0145 · Cited by 96
The SR-mitochondria interaction: a new player in cardiac pathophysiology
Ruiz‐Meana, M., Fernández‐Sanz, C., & García‐Dorado, D. (2010) · Cardiovascular Research · doi:10.1093/cvr/cvq225 · Cited by 96
Current perspective of mitochondrial biology in Parkinson's disease
Kaidery, N. A., & Thomas, B. (2018) · Neurochemistry International · doi:10.1016/j.neuint.2018.03.001 · Cited by 95
Roles for the Endoplasmic Reticulum in Regulation of Neuronal Calcium Homeostasis
Karagas, N. E., & Venkatachalam, K. (2019) · Cells · doi:10.3390/cells8101232 · Cited by 95
Mitochondrial dysfunction: An emerging link in the pathophysiology of polycystic ovary syndrome
Shukla, P., & Mukherjee, S. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.02.006 · Cited by 92
Manganelli, V., Matarrese, P., Antonioli, M., Gambardella, L., Vescovo, T., Gretzmeier, C., Longo, A., Capozzi, A., Recalchi, S., Riitano, G., et al. (2020) · Autophagy · doi:10.1080/15548627.2020.1834207 · Cited by 95
Natural history of Charcot-Marie-Tooth disease type 2A: a large international multicentre study
Pipis, M., Feely, S. M. E., Polke, J. M., Skorupinska, M., Pérez, L., Shy, R. R., Laurá, M., Morrow, J. M., Moroni, I., Pisciotta, C., et al. (2020) · Brain · doi:10.1093/brain/awaa323 · Cited by 95
Stress Responses from the Endoplasmic Reticulum in Cancer
Kato, H., & Nishitoh, H. (2015) · Frontiers in Oncology · doi:10.3389/fonc.2015.00093 · Cited by 95
Williamson, C. D., Wong, D. S., Bozidis, P., Zhang, A., & Colberg‐Poley, A. M. (2015) · Current Protocols in Cell Biology · doi:10.1002/0471143030.cb0327s68 · Cited by 84
ER-mitochondria interactions: Both strength and weakness within cancer cells
Doghman-Bouguerra, M., & Lalli, E. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2019.01.009 · Cited by 94
Structure and function of the N‐terminal domain of the human mitochondrial calcium uniporter
Lee, Y., Min, C. K., Kim, T., Song, H. K., Lim, Y., Kim, D., Shin, K., Kang, M., Kang, J. Y., Youn, H., et al. (2015) · EMBO Reports · doi:10.15252/embr.201540436 · Cited by 94
The mitochondria–endoplasmic reticulum contact sites: a signalling platform for cell death
Prudent, J., & McBride, H. M. (2017) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2017.03.007 · Cited by 94
Martinvalet, D. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0237-7 · Cited by 94
Liu, L., & Li, J. (2019) · Frontiers in Plant Science · doi:10.3389/fpls.2019.00749 · Cited by 96
Vallese, F., Catoni, C., Cieri, D., Barazzuol, L., Ramírez, O. A., Calore, V., Bonora, M., Giamogante, F., Pinton, P., Brini, M., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19892-6 · Cited by 98
Jadiya, P., Garbincius, J. F., & Elrod, J. W. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01224-4 · Cited by 94
Liu, D., Qin, H., Gao, Y., Sun, M., & Wang, M. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107258 · Cited by 94
Metadata
- Authors
- de Brito, O. M., & Scorrano, L.
- Affiliations
- University of Geneva (CH)
- Corresponding author
- Scorrano, Luca
- ORCID
- Scorrano, Luca
- Venue
- Nature
- Published
- 2008-12-01
- Volume
- 456
- Issue
- 7222
- Pages
- 605-610
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2166432730
- Cited by
- 2,442
- References
- 35
- Citations by year
- 2026: 105 · 2025: 142 · 2024: 136 · 2023: 142 · 2022: 139 · 2021: 188 · 2020: 186 · 2019: 148 · 2018: 132 · 2017: 175 · 2016: 129 · 2015: 119 · 2014: 132 · 2013: 133 · 2012: 145
- FWCI
- 39.45
- Type
- journal article
- Language
- en
- Update notices
- correction (2014-09-10)
- Open access
- Licence
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
- RePEc: Research Papers in Economics (submittedVersion)
- Padua Research Archive (University of Padova) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- mitofusin 2, mitochondrial calcium uptake, inositol 1,4,5-trisphosphate, calcium signaling, dynamin-related proteins, ER morphology, calcium homeostasis
- MeSH terms
- Animals, Calcium, Charcot-Marie-Tooth Disease, Endoplasmic Reticulum, Fibroblasts, HeLa Cells, Humans, Membrane Proteins, Mitochondria, Inositol 1,4,5-Trisphosphate, Calcium Signaling, GTP Phosphohydrolases, Mitochondrial Proteins, Mice, Organelle Shape
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
