The DOI matches its Crossref record; 63 of the 63 references it cites were found in a registry or an index.
Cooperative and independent roles of the Drp1 adaptors Mff, MiD49 and MiD51 in mitochondrial fission
Open accessAbstract
Cytosolic dynamin-related protein 1 (Drp1, also known as DNM1L) is required for both mitochondrial and peroxisomal fission. Drp1-dependent division of these organelles is facilitated by a number of adaptor proteins at mitochondrial and peroxisomal surfaces. To investigate the interplay of these adaptor proteins, we used gene-editing technology to create a suite of cell lines lacking the adaptors MiD49 (also known as MIEF2), MiD51 (also known as MIEF1), Mff and Fis1. Increased mitochondrial connectivity was observed following loss of individual adaptors, and this was further enhanced following the combined loss of MiD51 and Mff. Moreover, loss of adaptors also conferred increased resistance of cells to intrinsic apoptotic stimuli, with MiD49 and MiD51 showing the more prominent role. Using a proximity-based biotin labeling approach, we found close associations between MiD51, Mff and Drp1, but not Fis1. Furthermore, we found that MiD51 can suppress Mff-dependent enhancement of Drp1 GTPase activity. Our data indicates that Mff and MiD51 regulate Drp1 in specific ways to promote mitochondrial fission.
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
“In mammals, there are no orthologues for MDV1 and Cav 4, and recent evidence suggests that Fis1 is not required for fission [89, 90].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [89]
Citations
Cites
NIH Image to ImageJ: 25 years of image analysis
Schneider, C. A., Rasband, W. S., & Eliceiri, K. W. (2012) · Nature Methods · doi:10.1038/nmeth.2089 · Cited by 64,638
Andromeda: A Peptide Search Engine Integrated into the MaxQuant Environment
Cox, J., Neuhauser, N., Michalski, A., Scheltema, R. A., Olsen, J. V., & Mann, M. (2011) · Journal of Proteome Research · doi:10.1021/pr101065j · Cited by 5,520
The BCL-2 protein family: opposing activities that mediate cell death
Youle, R. J., & Strasser, A. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2308 · Cited by 4,806
Rappsilber, J., Mann, M., & Ishihama, Y. (2007) · Nature Protocols · doi:10.1038/nprot.2007.261 · Cited by 4,641
Double nicking by RNA-guided CRISPR Cas9 for enhanced genome editing specificity
Ran, F. A., Hsu, P. D., Lin, C.-Y., Gootenberg, J. S., Konermann, S., Trevino, A. E., Scott, D. A., Inoue, A., Matoba, S., Zhang, Y., et al. (2013) · Cell · doi:10.1016/j.cell.2013.08.021 · Cited by 3,299
The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy
Lazarou, M., Sliter, D. A., Kane, L. A., Sarraf, S. A., Wang, C., Burman, J. L., Sideris, D. P., Fogel, A. I., & Youle, R. J. (2015) · Nature · doi:10.1038/nature14893 · Cited by 2,774
ER Tubules Mark Sites of Mitochondrial Division
Friedman, J. R., Lackner, L. L., West, M., DiBenedetto, J. R., Nunnari, J., & Voeltz, G. K. (2011) · Science · doi:10.1126/science.1207385 · Cited by 2,072
Mitochondrial dynamics-fusion, fission, movement, and mitophagy-in neurodegenerative diseases
Chen, H., & Chan, D. C. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp326 · Cited by 1,506
Mitochondria in Apoptosis: Bcl-2 Family Members and Mitochondrial Dynamics
Martinou, J., & Youle, R. J. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.06.017 · Cited by 1,395
CHOPCHOP: a CRISPR/Cas9 and TALEN web tool for genome editing
Montague, T. G., Cruz, J. M. B. S., Gagnon, J. A., Church, G. M., & Valen, E. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku410 · Cited by 1,246
Cited by
Sorted by citations
The cell biology of mitochondrial membrane dynamics
Giacomello, M., Pyakurel, A., Glytsou, C., & Scorrano, L. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0210-7 · Cited by 1,550
Mitochondrial Dynamics and Its Involvement in Disease
Chan, D. C. (2020) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathmechdis-012419-032711 · Cited by 1,416
Mitochondrial dynamics: overview of molecular mechanisms
Tilokani, L., Nagashima, S., Paupe, V., & Prudent, J. (2018) · Essays in Biochemistry · doi:10.1042/ebc20170104 · Cited by 1,397
Distinct fission signatures predict mitochondrial degradation or biogenesis.
Kleele, T., Rey, T., Winter, J., Zaganelli, S., Mahecic, D., Perreten Lambert, H., Ruberto, F. P., Nemir, M., Wai, T., Pedrazzini, T., et al. (2021) · Nature · doi:10.1038/s41586-021-03510-6 · Cited by 794
The functional universe of membrane contact sites
Prinz, W. A., Toulmay, A., & Balla, T. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0180-9 · Cited by 770
Here, there, and everywhere: The importance of ER membrane contact sites
Wu, H., Carvalho, P., & Voeltz, G. K. (2018) · Science · doi:10.1126/science.aan5835 · Cited by 689
Mitochondrial dynamics in adaptive and maladaptive cellular stress responses
Eisner, V., Picard, M., & Hajnóczky, G. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0133-0 · Cited by 622
Mitochondria in health, disease, and aging
Harrington, J. S., Ryter, S. W., Plataki, M. E., Price, D. R., & Choi, A. M. K. (2023) · Physiological Reviews · doi:10.1152/physrev.00058.2021 · Cited by 641
Ježek, J., Cooper, K. F., & Strich, R. (2018) · Antioxidants · doi:10.3390/antiox7010013 · Cited by 532
Multiple dynamin family members collaborate to drive mitochondrial division
Lee, J. E., Westrate, L. M., Wu, H., Page, C., & Voeltz, G. K. (2016) · Nature · doi:10.1038/nature20555 · Cited by 512
Selective autophagy of intracellular organelles: Recent research advances
Li, W., He, P., Huang, Y., Li, Y.-F., Lu, J., Li, M., Kurihara, H., Luo, Z., Meng, T., Onishi, M., et al. (2020) · Theranostics · doi:10.7150/thno.49860 · Cited by 523
Function and regulation of the divisome for mitochondrial fission
Kraus, F., Roy, K., Pucadyil, T. J., & Ryan, M. T. (2021) · Nature · doi:10.1038/s41586-021-03214-x · Cited by 445
Self-citationQuality control of the mitochondrion
Ng, M. Y. W., Wai, T., & Simonsen, A. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.02.009 · Cited by 468
Molecular mechanisms of mitochondrial dynamics
Tábara, L. C., Segawa, M., & Prudent, J. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00785-1 · Cited by 445
Structural basis of mitochondrial receptor binding and constriction by DRP1
Kalia, R., Wang, R. Y., Yusuf, A., Thomas, P. V., Agard, D. A., Shaw, J. M., & Frost, A. S. (2018) · Nature · doi:10.1038/s41586-018-0211-2 · Cited by 385
Defective mitophagy in Alzheimer’s disease
Pradeepkiran, J. A., & Reddy, P. H. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101191 · Cited by 367
Mitochondrial Functions in Infection and Immunity
Tiku, V., Tan, M., & Đikić, I. (2020) · Trends in Cell Biology · doi:10.1016/j.tcb.2020.01.006 · Cited by 355
Mitochondrial Quality Control and Disease: Insights into Ischemia-Reperfusion Injury
Anzell, A. R., Maizy, R., Przyklenk, K., & Sanderson, T. H. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0503-9 · Cited by 359
CerS6-Derived Sphingolipids Interact with Mff and Promote Mitochondrial Fragmentation in Obesity
Hammerschmidt, P., Ostkotte, D., Nolte, H., Gerl, M. J., Jaïs, A., Brunner, H. L., Sprenger, H., Awazawa, M., Nicholls, H. T., Turpin-Nolan, S. M., et al. (2019) · Cell · doi:10.1016/j.cell.2019.05.008 · Cited by 314
Mitochondrial dynamics in health and disease
Yapa, N. M. B., Lisnyak, V., Reljić, B., & Ryan, M. T. (2021) · FEBS Letters · doi:10.1002/1873-3468.14077 · Cited by 323
Self-citationThe role of mitochondrial fission in cardiovascular health and disease
Quiles, J. M., & Gustafsson, Å. B. (2022) · Nature Reviews Cardiology · doi:10.1038/s41569-022-00703-y · Cited by 315
Hu, C., Huang, Y., & Li, L. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18010144 · Cited by 302
Cellular ATP demand creates metabolically distinct subpopulations of mitochondria
Ryu, K. W., Fung, T. S., Baker, D. C., Saoi, M., Park, J., Febres-Aldana, C. A., Aly, R. G., Cui, R., Sharma, A., Fu, Y., et al. (2024) · Nature · doi:10.1038/s41586-024-08146-w · Cited by 284
MIROs and DRP1 drive mitochondrial-derived vesicle biogenesis and promote quality control
König, T., Nolte, H., Aaltonen, M. J., Tatsuta, T., Krols, M., Stroh, T., Langer, T., & McBride, H. M. (2021) · Nature Cell Biology · doi:10.1038/s41556-021-00798-4 · Cited by 288
Lewis, T. L., Kwon, S.-K., Lee, A., Shaw, R., & Polleux, F. (2018) · Nature Communications · doi:10.1038/s41467-018-07416-2 · Cited by 260
Pleiotropic Mitochondria: The Influence of Mitochondria on Neuronal Development and Disease
Rangaraju, V., Lewis, T. L., Hirabayashi, Y., Bergami, M., Motori, E., Cartoni, R., Kwon, S., & Courchet, J. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.1157-19.2019 · Cited by 271
Human Fis1 regulates mitochondrial dynamics through inhibition of the fusion machinery
Yu, R., Jin, S., Lendahl, U., Nistér, M., & Zhao, J. (2019) · The EMBO Journal · doi:10.15252/embj.201899748 · Cited by 253
Structure, function, and regulation of mitofusin‐2 in health and disease
Chandhok, G., Lazarou, M., & Neumann, B. (2017) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12378 · Cited by 263
Kamerkar, S. C., Kraus, F., Sharpe, A. J., Pucadyil, T. J., & Ryan, M. T. (2018) · Nature Communications · doi:10.1038/s41467-018-07543-w · Cited by 252
Self-citationThe constriction and scission machineries involved in mitochondrial fission
Kraus, F., & Ryan, M. T. (2017) · Journal of Cell Science · doi:10.1242/jcs.199562 · Cited by 244
Self-citationReciprocal Regulation of Mitochondrial Fission and Fusion
Sabouny, R., & Shutt, T. E. (2020) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.03.009 · Cited by 247
Romani, P., Nirchio, N., Arboit, M., Barbieri, V., Tosi, A., Michielin, F., Shibuya, S., Benoist, T., Wu, D., Hindmarch, C. C. T., et al. (2022) · Nature Cell Biology · doi:10.1038/s41556-022-00843-w · Cited by 235
Mitochondrial dynamics and their potential as a therapeutic target
Whitley, B. N., Engelhart, E. A., & Hoppins, S. C. (2019) · Mitochondrion · doi:10.1016/j.mito.2019.06.002 · Cited by 228
mTORC1 as a Regulator of Mitochondrial Functions and a Therapeutic Target in Cancer
de la Cruz-López, K. G., Toledo-Guzmán, M. E., Sánchez, E. O., & Carrancá, A. G. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.01373 · Cited by 223
Causal roles of mitochondrial dynamics in longevity and healthy aging
Sharma, A., Smith, H. J., Yao, P., & Mair, W. B. (2019) · EMBO Reports · doi:10.15252/embr.201948395 · Cited by 222
Mitochondrial Dynamics in Stem Cells and Differentiation
Seo, B. J., Yoon, S. H., & Tae, J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19123893 · Cited by 208
Janer, A., Prudent, J., Paupe, V., Fahiminiya, S., Majewski, J., Sgarioto, N., Rosiers, C. D., Forest, A., Lin, Z., Gingras, A., et al. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201506159 · Cited by 208
Drp1/Fis1 interaction mediates mitochondrial dysfunction in septic cardiomyopathy
Haileselassie, B., Mukherjee, R., Joshi, A. U., Napier, B. A., Massis, L. M., Ostberg, N. P., Queliconi, B. B., Monack, D. M., Bernstein, D., & Mochly‐Rosen, D. (2019) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2019.04.006 · Cited by 201
Mitophagy, Mitochondrial Dynamics, and Homeostasis in Cardiovascular Aging
Wu, N. N., Zhang, Y., & Ren, J. T. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/9825061 · Cited by 199
Romanello, V., & Sandri, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03662-0 · Cited by 197
An, S. L., Yao, Y., Hu, H., Wu, J., Li, J., Li, L., Wu, J., Sun, M., Deng, Z., Zhang, Y., et al. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-05952-4 · Cited by 196
A High-Density Human Mitochondrial Proximity Interaction Network
Antonická, H., Lin, Z., Janer, A., Aaltonen, M. J., Weraarpachai, W., Gingras, A., & Shoubridge, E. A. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.07.017 · Cited by 188
Zerihun, M., Sukumaran, S., & Qvit, N. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24065785 · Cited by 198
The ever-growing complexity of the mitochondrial fission machinery
Pagliuso, A., Cossart, P., & Stavru, F. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2603-0 · Cited by 192
Mitochondrial fission and fusion
Lee, H., & Yoon, Y. (2016) · Biochemical Society Transactions · doi:10.1042/bst20160129 · Cited by 183
Mitochondrial network structure homeostasis and cell death
Xie, L., Shi, F., Tan, Z., Li, Y., Bode, A. M., & Cao, Y. (2018) · Cancer Science · doi:10.1111/cas.13830 · Cited by 179
Inhibition of Drp1/Fis1 interaction slows progression of amyotrophic lateral sclerosis
Joshi, A. U., Saw, N. L., Vogel, H. S., Cunnigham, A. D., Shamloo, M., & Mochly‐Rosen, D. (2018) · EMBO Molecular Medicine · doi:10.15252/emmm.201708166 · Cited by 185
Regulation of Mammalian Mitochondrial Dynamics: Opportunities and Challenges
Yu, R., Lendahl, U., Nistér, M., & Zhao, J. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.00374 · Cited by 183
Chen, K., Dasgupta, A., Lin, J.-H., Potus, F., Bonnet, S., Iremonger, J., Fu, J. M., Mewburn, J. D., Wu, D., Dunham‐Snary, K. J., et al. (2018) · Circulation · doi:10.1161/circulationaha.117.031258 · Cited by 167
Xian, H., & Liou, Y. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-00657-z · Cited by 177
Roles of mitochondrial dynamics modulators in cardiac ischaemia/reperfusion injury
Maneechote, C., Palee, S., Chattipakorn, S. C., & Chattipakorn, N. (2017) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13330 · Cited by 154
Receptor-mediated Drp1 oligomerization on endoplasmic reticulum
Ji, W.-K., Chakrabarti, R., Fan, X., Schoenfeld, L. W., Strack, S., & Higgs, H. N. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201610057 · Cited by 151
Mitochondrial dynamics: Shaping and remodeling an organelle network
Fenton, A. R., Jongens, T. A., & Holzbaur, E. L. F. (2020) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2020.08.014 · Cited by 152
Feng, S., Wang, Z., Yuan, Y., Wang, X., Sun, H., Chen, N., & Zhang, Y. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.104553 · Cited by 146
Structural Insights into the Mechanism of Dynamin Superfamily Proteins
Jimah, J. R., & Hinshaw, J. E. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.11.003 · Cited by 140
Mechanisms and roles of mitochondrial localisation and dynamics in neuronal function
Seager, R., Lee, L. J., Henley, J. M., & Wilkinson, K. A. (2020) · Neuronal Signaling · doi:10.1042/ns20200008 · Cited by 152
Mitochondrial Morphofunction in Mammalian Cells
Bulthuis, E. P., Adjobo-Hermans, M. J. W., Willems, P. H. G. M., & Koopman, W. J. H. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7534 · Cited by 133
Atkins, K., Dasgupta, A., Chen, K., Mewburn, J., & Archer, S. L. (2016) · Clinical Science · doi:10.1042/cs20160030 · Cited by 130
Actin filaments as dynamic reservoirs for Drp1 recruitment
Hatch, A. L., Ji, W.-K., Merrill, R. A., Strack, S., & Higgs, H. N. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-03-0193 · Cited by 129
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
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
Motor proteins at the mitochondria–cytoskeleton interface
Kruppa, A. J., & Buß, F. (2021) · Journal of Cell Science · doi:10.1242/jcs.226084 · Cited by 127
Adaniya, S. M., O‐Uchi, J., Cypress, M. W., Kusakari, Y., & Jhun, B. S. (2019) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00523.2018 · Cited by 123
Ihenacho, U. K., Nolden, K. A., Harwig, M. C., Widlansky, M. E., & Hill, R. B. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.660095 · Cited by 117
Zhao, Y., Sun, X., Hu, D., Prosdocimo, D. A., Hoppel, C. L., Jain, M. K., Ramachandran, R., & Qi, X. (2019) · Nature Communications · doi:10.1038/s41467-019-09291-x · Cited by 111
Self-citationMitochondrial dynamics proteins as emerging drug targets
Zacharioudakis, E., & Gavathiotis, E. (2022) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2022.11.004 · Cited by 115
Mitochondrial Quality Control in Cerebral Ischemia–Reperfusion Injury
Wu, M., Gu, X., & Ma, Z.-L. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02494-8 · Cited by 112
Wang, S., Tan, J., Miao, Y., & Zhang, Q. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.848214 · Cited by 118
Sphingolipids as a Culprit of Mitochondrial Dysfunction in Insulin Resistance and Type 2 Diabetes
Roszczyc-Owsiejczuk, K., & Zabielski, P. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.635175 · Cited by 113
Wang, S., Zhu, H., Li, R., Mui, D., Toan, S., Chang, X., & Zhou, H. (2022) · Science Signaling · doi:10.1126/scisignal.abh1121 · Cited by 110
Kornfeld, O. S., Qvit, N., Haileselassie, B., Shamloo, M., Bernardi, P., & Mochly‐Rosen, D. (2018) · Scientific Reports · doi:10.1038/s41598-018-32228-1 · Cited by 108
Formosa, L. E., Muellner-Wong, L., Reljić, B., Sharpe, A. J., Jackson, T. D., Beilharz, T. H., Stojanovski, D., Lazarou, M., Stroud, D. A., & Ryan, M. T. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107541 · Cited by 106
Self-citationCryo-EM Studies of Drp1 Reveal Cardiolipin Interactions that Activate the Helical Oligomer
Francy, C. A., Clinton, R. W., Fröhlich, C., Murphy, C., & Mears, J. A. (2017) · Scientific Reports · doi:10.1038/s41598-017-11008-3 · Cited by 105
Mitochondrial Dysfunction in Cardiovascular Diseases: Potential Targets for Treatment
Yang, J., Guo, Q., Feng, X., Liu, Y., & Zhou, Y. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.841523 · Cited by 105
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
Mitochondria as central hubs in synaptic modulation
Duarte, F. V., Ciampi, D., & Duarte, C. B. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-04814-8 · Cited by 109
Critical role of mitochondrial dysfunction and impaired mitophagy in diabetic nephropathy
Saxena, S., Mathur, A., & Kakkar, P. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.28712 · Cited by 96
Glucocorticoid impairs mitochondrial quality control in neurons
Choi, G. E., & Han, H. J. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105301 · Cited by 95
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
Wyckelsma, V. L., Levinger, I., McKenna, M. J., Formosa, L. E., Ryan, M. T., Petersen, A. C., Anderson, M. J., & Murphy, R. M. (2017) · The Journal of Physiology · doi:10.1113/jp273950 · Cited by 91
Self-citationRole of mitochondrial quality control in the pathogenesis of nonalcoholic fatty liver disease
Li, R., Toan, S., & Zhou, H. (2020) · Aging · doi:10.18632/aging.102972 · Cited by 89
Kapétanovic, R., Afroz, S. F., Ramnath, D., Lawrence, G. M. E. P., Okada, T., Curson, J. E. B., de Bruin, J., Fairlie, D. P., Schroder, K., John, J. C. S., et al. (2020) · Immunology and Cell Biology · doi:10.1111/imcb.12363 · Cited by 97
Lee, J., & Song, C. (2021) · Antioxidants · doi:10.3390/antiox10060872 · Cited by 91
Yu, R., Liu, T., Jin, S., Ning, F. C., Lendahl, U., Nistér, M., & Zhao, J. (2017) · Scientific Reports · doi:10.1038/s41598-017-00853-x · Cited by 89
Novel tumor therapy strategies targeting endoplasmic reticulum-mitochondria signal pathways
Wu, H., Chen, W., Chen, Z., Li, X., & Wang, M. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101951 · Cited by 83
Mancini, N. L., Goudie, L. J. L., Xu, W., Sabouny, R., Rajeev, S., Wang, A., Esquerre, N., Rajabi, A. A., Jayme, T. S., Bernardes, E. V. T., et al. (2020) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2020.04.004 · Cited by 83
Mitochondrial dynamics: The dynamin superfamily and execution by collusion
Ramachandran, R. (2017) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2017.07.039 · Cited by 81
Self-citationPum2-Mff axis fine-tunes mitochondrial quality control in acute ischemic kidney injury
Wang, J., Zhu, P., Toan, S., Li, R., Ren, J. T., & Zhou, H. (2020) · Cell Biology and Toxicology · doi:10.1007/s10565-020-09513-9 · Cited by 79
Mitochondrial Quality Control: Role in Cardiac Models of Lethal Ischemia-Reperfusion Injury
Kulek, A. R., Anzell, A. R., Wider, J. M., Sanderson, T. H., & Przyklenk, K. (2020) · Cells · doi:10.3390/cells9010214 · Cited by 78
Khatun, J., Gelles, J. D., & Chipuk, J. E. (2024) · Developmental Cell · doi:10.1016/j.devcel.2024.09.004 · Cited by 77
Wang, N., Wang, X. J., Lan, B., Gao, Y., & Cai, Y. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02458-0 · Cited by 84
Rahman, F. A., & Quadrilatero, J. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03807-9 · Cited by 77
Jiang, R.-Q., Li, Q., & Sheng, R. (2023) · Pharmacological Research · doi:10.1016/j.phrs.2023.106761 · Cited by 79
Alterations in mitochondrial morphology as a key driver of immunity and host defence
Cervantes‐Silva, M. P., Cox, S. L., & Curtis, A. M. (2021) · EMBO Reports · doi:10.15252/embr.202153086 · Cited by 73
Ferroptosis triggers mitochondrial fragmentation via Drp1 activation
Pedrera, L., Clemente, L. P., Dahlhaus, A., Nasudivar, S. L., Tishina, S., González, D. O., Stroh, J., Yapici, F. I., Singh, R. P., Grotehans, N., et al. (2025) · Cell Death and Disease · doi:10.1038/s41419-024-07312-2 · Cited by 75
Bezawork‐Geleta, A., Devereux, C. J., Keenan, S. N., Lou, J., Cho, H., Nie, S., Souza, D. P. D., Narayana, V. K., Siddall, N. A., Rodrigues, C. H. M., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-57405-5 · Cited by 72
Self-citationMitochondrial Membrane Dynamics—Functional Positioning of OPA1
Lee, H., & Yoon, Y. (2018) · Antioxidants · doi:10.3390/antiox7120186 · Cited by 73
Regulation of Mitochondrial Dynamics and Autophagy by the Mitochondria-Associated Membrane
Tagaya, M., & Arasaki, K. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-4567-7_3 · Cited by 74
A novel mechanism causing imbalance of mitochondrial fusion and fission in human myopathies
Bartsakoulia, M., Pyle, A., Troncoso-Chandía, D., Vial-Brizzi, J., Paz-Fiblas, M. V., Duff, J., Griffin, H., Boczonadi, V., Lochmüller, H., Kleinle, S., et al. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy033 · Cited by 68
Molecular connectivity of mitochondrial gene expression and OXPHOS biogenesis
Singh, A. P., Salvatori, R., Aftab, W., Kohler, A., Carlström, A., Forne, I., Imhof, A., & Ott, M. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.07.024 · Cited by 65
Self-citation
Metadata
- Authors
- Osellame, L. D., Singh, A. P., Stroud, D. A., Palmer, C. S., Stojanovski, D., Ramachandran, R., & Ryan, M. T.
- Affiliations
- Monash University (AU)
- La Trobe University (AU)
- Burnet Institute (AU)
- The University of Melbourne (AU)
- Case Western Reserve University (US)
- ORCID
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2016-06-01
- Volume
- 129
- Issue
- 11
- Pages
- 2170-2181
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- PMC
- PMC6919635
- OpenAlex
- W2415256624
- Cited by
- 336
- References
- 63
- Citations by year
- 2026: 18 · 2025: 34 · 2024: 28 · 2023: 30 · 2022: 35 · 2021: 48 · 2020: 36 · 2019: 31 · 2018: 37 · 2017: 29 · 2016: 9
- FWCI
- 18.36
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Cell Science (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- HighWire Press Open Archive (submittedVersion)
- Funders
- National Health and Medical Research Council (1049968)
- American Heart Association (13BGIA14810010)
- 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
- mitochondrial fission, Drp1, Mff, MiD51, Fis1, apoptosis resistance, protein-protein interaction
- MeSH terms
- Gene Editing, Animals, Cell Line, Membrane Proteins, Mice, Inbred C57BL, Staining and Labeling, Cell Death, Receptors, Cytoplasmic and Nuclear, Mice, Knockout, Peroxisomes, Mitochondrial Proteins, Dynamins, Mitochondrial Dynamics
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