The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.
Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
Open accessAbstract
Accumulation of depolarized mitochondria within beta-cells has been associated with oxidative damage and development of diabetes. To determine the source and fate of depolarized mitochondria, individual mitochondria were photolabeled and tracked through fusion and fission. Mitochondria were found to go through frequent cycles of fusion and fission in a 'kiss and run' pattern. Fission events often generated uneven daughter units: one daughter exhibited increased membrane potential (delta psi(m)) and a high probability of subsequent fusion, while the other had decreased membrane potential and a reduced probability for a fusion event. Together, this pattern generated a subpopulation of non-fusing mitochondria that were found to have reduced delta psi(m) and decreased levels of the fusion protein OPA1. Inhibition of the fission machinery through DRP1(K38A) or FIS1 RNAi decreased mitochondrial autophagy and resulted in the accumulation of oxidized mitochondrial proteins, reduced respiration and impaired insulin secretion. Pulse chase and arrest of autophagy at the pre-proteolysis stage reveal that before autophagy mitochondria lose delta psi(m) and OPA1, and that overexpression of OPA1 decreases mitochondrial autophagy. Together, these findings suggest that fission followed by selective fusion segregates dysfunctional mitochondria and permits their removal by autophagy.
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Fission segregates components of the network that are irreversibly damaged or unnecessary for subsequent removal (Twig et al., 2008).”
From Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity (2017) · cites this paper as Twig et al., 2008
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Dysfunctional mitochondrial dynamics, as observed here, particularly excessive mitochondrial fission, have been associated with oxidative stress, mitochondrial DNA damage, and cellular senescence in various cell types (Twig et al., 2008; Miwa et al., 2022).”
From Aging promotes an increase in mitochondrial fragmentation in astrocytes (2024) · cites this paper as Twig et al., 2008
Experimental — accuracy not yet measuredIn the citing paper
“Besides, the fusion between healthy and damaged organelles allows to dilute the damaged material into the healthy network, avoids the accumulation of dysfunctional mitochondria, and maintains their overall function [58].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [58]
In the citing paper
“Impairment of fission leads to the disruption of selective mitochondrial autophagic degradation, followed by dysfunctional organelles accumulation [58, 196–200].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [58]
In the citing paper
“Mitochondrial fusion in mammalian cells is regulated by the proteins mitofusin 1 and mitofusin 2 (Mfn1 and Mfn2) and optic atrophy 1 (Opa1).”
From Mitochondrial DNA and TLR9 drive muscle inflammation upon Opa1 deficiency (2018) · cites this paper as Twig et al, 2008
In the citing paper
“These facts highlight the importance of a functional fission machinery to discard damaged mitochondria by autophagy or mitophagy (Gomes and Scorrano, 2008; Twig et al., 2008).”
From Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity (2017) · cites this paper as Twig et al., 2008
In the citing paper
“The fragmentation of mitochondria is a prerequisite for autophagy (Twig et al., 2008), which might be physiologically favorable: smaller mitochondria might be autophagocytosed more easily than larger ones and require less energy.”
From New insights into the role of mitochondria in aging: mitochondrial dynamics and more (2010) · cites this paper as Twig et al., 2008
In the citing paper
“Intriguingly, in response to oxidant-induced damage, mitochondrial fission generates daughter mitochondria with different Δψm, whereby mitochondria with a lower Δψm can be targeted for degradation by autophagy, whereas parent mitochondria remain intact (Gomes and Scorrano, 2008; Twig et al., 2008).”
From New insights into the role of mitochondria in aging: mitochondrial dynamics and more (2010) · cites this paper as Twig et al., 2008
In the citing paper
“The link between fission proteins and mitochondrial turnover has also been illustrated in neuronal cells, in which Fis1 was shown to activate autophagy and the selective degradation of depolarized mitochondria (Twig et al., 2008).”
From New insights into the role of mitochondria in aging: mitochondrial dynamics and more (2010) · cites this paper as Twig et al., 2008
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 role of autophagy during the early neonatal starvation period
Kuma, A., Hatano, M., Matsui, M., Yamamoto, A., Nakaya, H., Yoshimori, T., Ohsumi, Y., Tokuhisa, T., & Mizushima, N. (2004) · Nature · doi:10.1038/nature03029 · Cited by 2,865
Impairment of starvation-induced and constitutive autophagy in Atg7 -deficient mice
Komatsu, M., Waguri, S., Ueno, T., Iwata, J., Murata, S., Tanida, I., Ezaki, J., Mizushima, N., Ohsumi, Y., Uchiyama, Y., et al. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200412022 · Cited by 2,331
Mitochondrial dysfunction and type 2 diabetes
Lowell, B. B., & Shulman, G. I. (2005) · Science · doi:10.1126/science.1104343 · Cited by 2,070
Mitochondria: Dynamic Organelles in Disease, Aging, and Development
Chan, D. C. (2006) · Cell · doi:10.1016/j.cell.2006.06.010 · Cited by 1,987
Autophagy in cell death: an innocent convict?
Levine, B. (2005) · Journal of Clinical Investigation · doi:10.1172/jci26390 · Cited by 1,694
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 · cited 6×
“Conversely, Dcm is influenced when fusion is inhibited (Olichon et al, 2003; Chen et al, 2005), suggesting that reduced fusion capacity could be either the cause or the result of Dcm depolarization.”
BackgroundResultInfluentialOPA1 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
Olichon, A., Baricault, L., Gas, N., Guillou, E., Valette, A., Belenguer, P., & Lenaers, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200677200 · Cited by 1,168
Wu, M., Neilson, A., Swift, A. L., Moran, R., Tamagnine, J., Parslow, D., Armistead, S., Lemire, K., Orrell, J., Teich, J., et al. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00247.2006 · Cited by 927
Self-citationHohmeier, H. E., Mulder, H., Chen, G., Henkel-Rieger, R., Prentki, M., & Newgard, C. B. (2000) · Diabetes · doi:10.2337/diabetes.49.3.424 · Cited by 922
Cited by
Sorted by citations
Items 601–700 of 1,035
Mitochondrial dysfunction and skeletal muscle atrophy: Causes, mechanisms, and treatment strategies
Kubat, G. B., Bouhamida, E., Ülger, Ö., Türkel, İ., Pedriali, G., Ramaccini, D., Ekinci, Ö., Özerkliğ, B., Atalay, Ö., Patergnani, S., et al. (2023) · Mitochondrion · doi:10.1016/j.mito.2023.07.003 · Cited by 134
Molecular and cellular basis of lysosomal transmembrane protein dysfunction
Ruivo, R., Anne, C., Sagné, C., & Gasnier, B. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.12.008 · Cited by 133
The free‐radical theory of ageing – older, wiser and still alive
Kirkwood, T. B. L., & Kowald, A. (2012) · BioEssays · doi:10.1002/bies.201200014 · Cited by 135
Mitochondrial function and insulin secretion
Maechler, P. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2013.06.019 · Cited by 125
Pancreatic β-Cell Failure Mediated by mTORC1 Hyperactivity and Autophagic Impairment
Bartolomé, A., Kimura-Koyanagi, M., Asahara, S., Guillén, C., Inoue, H., Teruyama, K., Shimizu, S., Kanno, A., García-Aguilar, A., Koike, M., et al. (2014) · Diabetes · doi:10.2337/db13-0970 · Cited by 125
The critical roles of mitophagy in cerebral ischemia
Tang, Y., Tian, H.-X., Yi, T., & Chen, H. (2016) · Protein & Cell · doi:10.1007/s13238-016-0307-0 · Cited by 134
Atkins, K., Dasgupta, A., Chen, K., Mewburn, J., & Archer, S. L. (2016) · Clinical Science · doi:10.1042/cs20160030 · Cited by 130
Ježek, P., Holendová, B., Garlid, K., & Jabůrek, M. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7225 · Cited by 131
SGLT2 Inhibitors Play a Salutary Role in Heart Failure via Modulation of the Mitochondrial Function
Maejima, Y. (2020) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2019.00186 · Cited by 133
Orchestration of selective autophagy by cargo receptors
Adriaenssens, E., Ferrari, L., & Martens, S. (2022) · Current Biology · doi:10.1016/j.cub.2022.11.002 · Cited by 122
Nicotinamide enhances mitochondria quality through autophagy activation in human cells
Kang, H. T., & Hwang, E. S. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00487.x · Cited by 128
Mao, X., Gonzalez, P., Li, C., Meng, G., Jiang, A., Wang, H., Gao, Q., Debatin, K., Beltinger, C. P., & Wei, J. (2014) · Journal of Virology · doi:10.1128/jvi.03851-13 · Cited by 129
Ikeda, Y., Sciarretta, S., Nagarajan, N., Rubattu, S., Volpe, M., Frati, G., & Sadoshima, J. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/210934 · Cited by 126
Swiader, A., Nahapetyan, H., Faccini, J., D’Angelo, R., Mucher, E., Elbaz, M., Boya, P., & Vindis, C. (2016) · Oncotarget · doi:10.18632/oncotarget.8936 · Cited by 129
Grel, H., Woźnica, D., Ratajczak, K., Kalwarczyk, E., Anchimowicz, J., Świtlik, W. Z., Olejnik, P., Zielonka, P., Stobiecka, M., & Jakieła, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241713033 · Cited by 140
Xie, R., Nguyen, S., McKeehan, K. A., Wang, F., McKeehan, W. L., & Leyuan, L. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.206532 · Cited by 124
Laar, V. S. V., Roy, N., Liu, A., Rajprohat, S., Arnold, B. A., Dukes, A. A., Holbein, C. D., & Berman, S. B. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.11.015 · Cited by 121
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
Intracellular and microenvironmental regulation of mitochondrial membrane potential in cancer cells
Begum, H. M., & Shen, K. (2023) · WIREs Mechanisms of Disease · doi:10.1002/wsbm.1595 · Cited by 126
Yu, X., Li, B., Yan, J., Li, W., Tian, H., Wang, G., Zhou, S., & Dai, Y. (2024) · Biomaterials · doi:10.1016/j.biomaterials.2024.122512 · Cited by 125
Cardiolipin remodeling by TAZ/tafazzin is selectively required for the initiation of mitophagy
Hsu, P., Liu, X., Zhang, J., Wang, H., Ye, J.-M., & Shi, Y. (2015) · Autophagy · doi:10.1080/15548627.2015.1023984 · Cited by 124
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
Defects in calcium homeostasis and mitochondria can be reversed in Pompe disease
Lim, J., Li, L., Kakhlon, O., Myerowitz, R., & Raben, N. (2015) · Autophagy · doi:10.1080/15548627.2015.1009779 · Cited by 131
Abeliovich, H., Zarei, M., Rigbolt, K. T. G., Youle, R. J., & Dengjel, J. (2013) · Nature Communications · doi:10.1038/ncomms3789 · Cited by 114
Mitophagy in neurodegeneration and aging
Palikaras, K., & Tavernarakis, N. (2012) · Frontiers in Genetics · doi:10.3389/fgene.2012.00297 · Cited by 126
Mammalian mitophagy – from in vitro molecules to in vivo models
Rodger, C. E., McWilliams, T. G., & Ganley, I. G. (2017) · FEBS Journal · doi:10.1111/febs.14336 · Cited by 127
Aryaman, J., Johnston, I. G., & Jones, N. S. (2019) · Frontiers in Genetics · doi:10.3389/fgene.2018.00718 · Cited by 123
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
Mitophagy and cGAS–STING crosstalk in neuroinflammation
Zhou, X., Wang, J., Yu, L., Qiao, G., Qin, D., Yuen-Kwan Law, B., Ren, F., Wu, J., & Wu, A. (2024) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2024.05.012 · Cited by 131
Hypoxia Activation of Mitophagy and Its Role in Disease Pathogenesis
Wu, H., & Chen, Q. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6204 · Cited by 119
Multi-site control and regulation of mitochondrial energy production
Bénard, G., Bellancé, N., José, C., Melser, S., Nouette‐Gaulain, K., & Rossignol, R. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.02.030 · Cited by 126
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 molecular mechanism of mitochondria autophagy in yeast
Kanki, T., & Klionsky, D. J. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.07035.x · Cited by 142
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
AMPK Regulates ER Morphology and Function in Stressed Pancreatic β-Cells via Phosphorylation of DRP1
Wikström, J. D., Israeli, T., Bachar-Wikström, E., Swisa, A., Ariav, Y., Waiss, M., Kaganovich, D., Dor, Y., Cerasi, E., & Leibowitz, G. (2013) · Molecular Endocrinology · doi:10.1210/me.2013-1109 · Cited by 123
Sabouny, R., Fraunberger, E. A., Geoffrion, M., Ng, A. C., Baird, S. D., Screaton, R. A., Milne, R. W., McBride, H. M., & Shutt, T. E. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6855 · Cited by 119
Human Cachexia Induces Changes in Mitochondria, Autophagy and Apoptosis in the Skeletal Muscle
de Castro, G. S., Simoes, E., Lima, J. D. C. C., Ortiz‐Silva, M., Festuccia, W. T., Tokeshi, F., de Alcântara, P. S. M., Otoch, J. P., Coletti, D., & Seelaender, M. C. L. (2019) · Cancers · doi:10.3390/cancers11091264 · Cited by 118
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
Bolaños, J. P., Moro, M. Á., Lizasoaín, I., & Almeida, Á. (2009) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2009.05.009 · Cited by 120
Inhibition of BMI1 induces autophagy-mediated necroptosis
Dey, A., Mustafi, S. B., Saha, S., Kumar Dhar Dwivedi, S., Mukherjee, P., & Bhattacharya, R. (2016) · Autophagy · doi:10.1080/15548627.2016.1147670 · Cited by 97
Mitochondrial quality control: Easy come, easy go
Stotland, A. B., & Gottlieb, R. A. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.12.041 · 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
Event-driven acquisition for content-enriched microscopy
Mahečić, D., Stepp, W. L., Zhang, C., Griffié, J., WEIGERT, M. G., & Manley, S. (2022) · Nature Methods · doi:10.1038/s41592-022-01589-x · Cited by 118
Joseph, A.-M., Joanisse, D. R., Baillot, R. G., & Hood, D. A. (2011) · Experimental Diabetes Research · doi:10.1155/2012/642038 · Cited by 119
Wu, Q., Gao, C., Wang, H., Zhang, X., Li, Q., Gu, Z., Shi, X., Cui, Y., Wang, T., Chen, X., et al. (2017) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2017.11.007 · Cited by 117
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
Vázquez‐Martín, A., Cufí, S., Corominas-Faja, B., Oliveras‐Ferraros, C., Vellón, L., & Menéndez, J. A. (2012) · Aging · doi:10.18632/aging.100465 · Cited by 116
Fujimoto, K., Hanson, P. T., Tran, H. D., Ford, E. L., Han, Z., Johnson, J. D., Schmidt, R. E., Green, K. G., Wice, B. M., & Polonsky, K. S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.041616 · Cited by 116
The multifaceted role of mitochondria in autism spectrum disorder
Khaliulin, I., Hamoudi, W., & Amal, H. (2024) · Molecular Psychiatry · doi:10.1038/s41380-024-02725-z · Cited by 128
Redox Activity Within the Lysosomal Compartment: Implications for Aging and Apoptosis
Kurz, T., Eaton, J. W., & Brunk, U. T. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.3005 · Cited by 121
Cytoplasmic dynein in neurodegeneration
Eschbach, J., & Dupuis, L. (2011) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2011.03.004 · Cited by 117
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
Alysandratos, K., Russo, S. J., Petcherski, A., Taddeo, E. P., Acín‐Pérez, R., Villacorta-Martín, C., Jean, J., Mulugeta, S., Rodríguez, L. R., Blum, B. C., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109636 · Cited by 116
Self-citationThe multiple links between actin and mitochondria
Fung, T. S., Chakrabarti, R., & Higgs, H. N. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00613-y · Cited by 112
Song, S. B., Jang, S.-Y., Kang, H. T., Wei, B., Jeoun, U.-W., Yoon, G. S., & Hwang, E. S. (2017) · Molecules and Cells · doi:10.14348/molcells.2017.0081 · Cited by 114
Neuronal failure in Alzheimer’s disease: a view through the oxidative stress looking-glass
Bonda, D., Wang, X., Lee, H., Smith, M. A., Perry, G. L., & Zhu, X. (2014) · Neuroscience Bulletin · doi:10.1007/s12264-013-1424-x · Cited by 114
Mitochondria-Associated Membranes and ER Stress
van Vliet, A. R., & Agostinis, P. (2017) · Current topics in microbiology and immunology · doi:10.1007/82_2017_2 · Cited by 116
Optic neuropathies: the tip of the neurodegeneration iceberg
Carelli, V., Morgia, C. L., Ross‐Cisneros, F. N., & Sadun, A. A. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx273 · Cited by 116
Polyphenols as Caloric-Restriction Mimetics and Autophagy Inducers in Aging Research
Yessenkyzy, A., Saliev, T. M., Zhanaliyeva, M., Masoud, A., Umbayev, B. A., Sergazy, S., Кривых, Е. А., Gulyayev, A., & Nurgozhin, T. S. (2020) · Nutrients · doi:10.3390/nu12051344 · Cited by 119
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
What can mitochondrial heterogeneity tell us about mitochondrial dynamics and autophagy?
Wikström, J. D., Twig, G., & Shirihai, O. S. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.06.006 · Cited by 114
Self-citationDeceleration of Fusion–Fission Cycles Improves Mitochondrial Quality Control during Aging
Figge, M. T., Reichert, A. S., Meyer‐Hermann, M., & Osiewacz, H. D. (2012) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002576 · Cited by 114
FRIENDLY Regulates Mitochondrial Distribution, Fusion, and Quality Control in Arabidopsis
Zawily, A. M. E., Schwarzländer, M., Finkemeier, I., Johnston, I. G., Benamar, A., Cao, Y., Gissot, C., Meyer, A. J., Wilson, K., Datla, R. S. S., et al. (2014) · PLANT PHYSIOLOGY · doi:10.1104/pp.114.243824 · Cited by 113
Mitochondrial dysfunction – Silent killer in cerebral ischemia
Pramila, B., & Shanmugam, P. S. T. (2017) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2017.02.043 · Cited by 113
Cardiolipin-Dependent Mitophagy Guides Outcome after Traumatic Brain Injury
Chao, H., Lin, C., Zuo, Q., Liu, Y., Xiao, M., Xu, X., Li, Z., Bao, Z., Chen, H., You, Y., et al. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.3415-17.2018 · Cited by 116
Linking the Metabolic State and Mitochondrial DNA in Chronic Disease, Health, and Aging
Picard, M. A., & Turnbull, D. M. (2013) · Diabetes · doi:10.2337/db12-1203 · Cited by 119
Williams, P. A., Morgan, J. E., & Votruba, M. (2010) · Brain · doi:10.1093/brain/awq218 · Cited by 113
Mending a broken heart: the role of mitophagy in cardioprotection
Moyzis, A. G., Sadoshima, J., & Gustafsson, Å. B. (2014) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00708.2014 · Cited by 114
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
USP14 inhibition corrects an in vivo model of impaired mitophagy
Chakraborty, J., von Stockum, S., Marchesan, E., Caicci, F., Ferrari, V., Raković, A., Klein, C., Antonini, A., Bubacco, L., & Ziviani, E. (2018) · EMBO Molecular Medicine · doi:10.15252/emmm.201809014 · Cited by 114
Zhang, B., Davidson, M. M., Zhou, H., Wang, C., Walker, W. F., & Hei, T. K. (2013) · Cancer Research · doi:10.1158/0008-5472.can-13-1411 · Cited by 112
Yan, J., Feng, Z., Liu, J., Shen, W., Wang, Y., Wertz, K., Weber, P., Long, J., & Liu, J. (2012) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2011.03.014 · Cited by 114
Shields, L. Y., Kim, H., Zhu, L., Haddad, D., Berthet, A., Pathak, D., Lam, M., Ponnusamy, R., Diaz‐Ramirez, L. G., Gill, T. M., et al. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.94 · Cited by 113
Wang, Y., Zhao, H., Shao, Y., Liu, J., Li, J., Luo, L., & Xing, M. (2018) · Chemosphere · doi:10.1016/j.chemosphere.2018.05.013 · Cited by 111
Zhou, Z., Moore, T. M., Drew, B. G., Ribas, V., Wanagat, J., Civelek, M., Segawa, M., Wolf, D. M., Norheim, F., Seldin, M. M., et al. (2020) · Science Translational Medicine · doi:10.1126/scitranslmed.aax8096 · Cited by 109
Self-citationExercise preserves physical fitness during aging through AMPK and mitochondrial dynamics
Campos, J. C., Bozi, L. H. M., Krum, B. N., Bechara, L. R. G., Ferreira, N. D., Arini, G. S., Albuquerque, R. P. E., Traa, A., Ogawa, T., van der Bliek, A. M., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2204750120 · Cited by 121
A short linear motif in BNIP3L (NIX) mediates mitochondrial clearance in reticulocytes
Zhang, J., Loyd, M. R., Randall, M. S., Waddell, M. B., Kriwacki, R. W., & Ney, P. A. (2012) · Autophagy · doi:10.4161/auto.20764 · Cited by 121
UPRmt-mediated cytoprotection and organismal aging
Schulz, A. M., & Haynes, C. M. (2015) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2015.03.008 · Cited by 113
Impaired quality control of mitochondria: Aging from a new perspective
Weber, T. A., & Reichert, A. S. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.03.018 · Cited by 112
Chowdhury, S. R., Reimer, A., Sharan, M., Kozjak‐Pavlovic, V., Eulálio, A., Prusty, B. K., Fraunholz, M. J., Rajeeve, K., & Rudel, T. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201608063 · Cited by 108
Mechanisms of obesity-induced metabolic and vascular dysfunctions
Caldwell, R. W. (2019) · Frontiers in bioscience · doi:10.2741/4758 · Cited by 112
Havird, J. C., Forsythe, E. S., Williams, A. M., Werren, J. H., Dowling, D. K., & Sloan, D. B. (2019) · Current Biology · doi:10.1016/j.cub.2019.03.020 · Cited by 112
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
Mitochondrial dysfunction in pancreatic β-cells in Type 2 Diabetes
Mulder, H., & Ling, C. (2008) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2008.05.015 · Cited by 115
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
Self-citationGeisler, S., Vollmer, S., Golombek, S., & Kahle, P. J. (2014) · Journal of Cell Science · doi:10.1242/jcs.146035 · Cited by 111
Keeping mitochondria in shape: a matter of life and death
Scorrano, L. (2013) · European Journal of Clinical Investigation · doi:10.1111/eci.12135 · Cited by 116
Zhuang, Y., & Miskimins, W. K. (2011) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-10-0343 · 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
The Interrelation between Reactive Oxygen Species and Autophagy in Neurological Disorders
Fang, C., Gu, L., Smerin, D., Mao, S., & Xiong, X. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/8495160 · Cited by 114
Geto, Z., Molla, M. D., Challa, F., Belay, Y., & Getahun, T. (2020) · Journal of Inflammation Research · doi:10.2147/jir.s232009 · Cited by 116
Ježek, P., Jabůrek, M., Holendová, B., Engstová, H., & Dlasková, A. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2022.0173 · Cited by 117
Hao, T., Yu, J., Wu, Z., Jiang, J., Gong, L., Wang, B., Guo, H., Zhao, H., Lü, B., Engelender, S., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-39811-9 · Cited by 115
The Impact of Mitochondrial Fusion and Fission Modulation in Sporadic Parkinson’s Disease
Santos, D., Esteves, A. R., Silva, D. F., Januário, C., & Cardoso, S. M. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8893-4 · Cited by 117
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
Parkin is required for exercise-induced mitophagy in muscle: Impact of aging
Chen, C. C. W., Erlich, A. T., Crilly, M. J., & Hood, D. A. (2018) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00391.2017 · Cited by 108
Bori, Z., Zhao, Z., Koltai, E., Fatouros, I. G., Jamurtas, A. Z., Douroudos, I. I., Terzis, G., Chatzinikolaou, A., Sovatzidis, A., Draganidis, D., et al. (2012) · Experimental Gerontology · doi:10.1016/j.exger.2012.03.004 · Cited by 108
Mitophagy plays a central role in mitochondrial ageing
Diot, A., Morten, K., & Poulton, J. (2016) · Mammalian Genome · doi:10.1007/s00335-016-9651-x · Cited by 112
Metadata
- Authors
- Twig, G., Elorza, A., Molina, A. J. A., Mohamed, H., Wikstrom, J. D., Walzer, G., Stiles, L., Haigh, S. E., Katz, S., Las, G., Alroy, J., Wu, M., Py, B. F., Yuan, J., Deeney, J. T., Corkey, B. E., & Shirihai, O. S.
- Affiliations
- Tufts University (US)
- Boston University (US)
- Billerica Public Library (US)
- Harvard University (US)
- Corresponding author
- Shirihai, Orian S
- ORCID
- Venue
- The EMBO Journal
- Published
- 2008-01-17
- Volume
- 27
- Issue
- 2
- Pages
- 433-446
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC2234339
- OpenAlex
- W2139636031
- Cited by
- 3,082
- References
- 39
- Citations by year
- 2026: 107 · 2025: 144 · 2024: 207 · 2023: 167 · 2022: 186 · 2021: 217 · 2020: 204 · 2019: 176 · 2018: 194 · 2017: 193 · 2016: 188 · 2015: 185 · 2014: 165 · 2013: 171 · 2012: 202
- FWCI
- 91.10
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Funders
- National Science Foundation (0215829)
- National Institutes of Health
- National Heart, Lung, and Blood Institute (R01HL071629)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK074778)
- National Center for Research Resources (P41RR001395)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- mitochondrial fission, mitochondrial fusion, kiss-and-run, mitophagy, OPA1, Drp1, Fis1, pancreatic beta cells, insulin secretion, mitochondrial membrane potential, oxidative stress, diabetes mellitus, mitochondrial segregation
- MeSH terms
- Autophagy-Related Protein 5, Insulin Secretion, Animals, Autophagy, Cell Line, Genotype, Insulin, Male, Mice, Inbred C57BL, Microtubule-Associated Proteins, Mitochondria, Models, Biological, Mutation, Reactive Oxygen Species, Microscopy, Confocal, GTP Phosphohydrolases, Mitochondrial Proteins, Green Fluorescent Proteins, Insulin-Secreting Cells, Mice, Membrane Potential, Mitochondrial
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
