The DOI matches its Crossref record; 103 of the 103 references it cites were found in a registry or an index.
Mitochondrial fusion and fission: The fine‐tune balance for cellular homeostasis
Open accessAbstract
Mitochondria are highly dynamic, maternally inherited cytoplasmic organelles, which fulfill cellular energy demand through the oxidative phosphorylation system. Besides, they play an active role in calcium and damage‐associated molecular patterns signaling, amino acid, and lipid metabolism, and apoptosis. Thus, the maintenance of mitochondrial integrity and homeostasis is extremely critical, which is achieved through continual fusion and fission. Mitochondrial fusion allows the transfer of gene products between mitochondria for optimal functioning, especially under metabolic and environmental stress. On the other hand, fission is crucial for mitochondrial division and quality control. The imbalance between these two processes is associated with various ailments such as cancer, neurodegenerative and cardiovascular diseases. This review discusses the molecular mechanisms that control mitochondrial fusion and fission and how the disruption of mitochondrial dynamics manifests into various disease conditions.
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
“Oxidative stress leads to oxidative damage to biomolecules (especially DNA),201 causing endogenous damage-associated molecular patterns (DAMPs) production and cytokine release in the organism.202,203”
From Inflammation and aging: signaling pathways and intervention therapies (2023) · cites this paper as [203]
Experimental — accuracy not yet measuredThe check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“Cytokines activate downstream signaling pathways of pattern recognition receptors,203 causing systemic chronic inflammatory responses in the body.204”
From Inflammation and aging: signaling pathways and intervention therapies (2023) · cites this paper as [203]
Experimental — accuracy not yet measured
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
Endothelial Cell Dysfunction and the Pathobiology of Atherosclerosis
Gimbrone, M. A., & García‐Cardeña, G. (2016) · Circulation Research · doi:10.1161/circresaha.115.306301 · Cited by 3,694
Mitofusin 2 tethers endoplasmic reticulum to mitochondria
de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442
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 fusion and fission in cell life and death
Westermann, B. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3013 · Cited by 2,002
Dynamin-related Protein Drp1 Is Required for Mitochondrial Division in Mammalian Cells
Smirnova, E., Griparić, L., Shurland, D., & van der Bliek, A. M. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.8.2245 · Cited by 1,938
During autophagy mitochondria elongate, are spared from degradation and sustain cell viability
Gomes, L. C., Benedetto, G. D., & Scorrano, L. (2011) · Nature Cell Biology · doi:10.1038/ncb2220 · Cited by 1,735
Mutations 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
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
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 by
Sorted by citations
Inflammation and aging: signaling pathways and intervention therapies
Li, X., Li, C., Zhang, W., Wang, Y., Qian, P., & Huang, H. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01502-8 · Cited by 1,443
“Oxidative stress leads to oxidative damage to biomolecules (especially DNA),(201) causing endogenous damageassociated molecular patterns (DAMPs) production and cytokine release in the organism.(202,203) Cytokines activate downstream signaling pathways of pattern recognition receptors,(203) causing systemic chronic inf…”
BackgroundMitochondria: It is all about energy
Casanova, A., Wevers, A., Ledesma, S. N., & Pruimboom, L. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1114231 · Cited by 350
Pang, B., Dong, G., Pang, T., Sun, X., Liu, X., Nie, Y., & Chang, X. (2024) · Angiogenesis · doi:10.1007/s10456-024-09938-4 · Cited by 282
Mitochondrial Glutathione in Cellular Redox Homeostasis and Disease Manifestation
Chen, T., Wang, H., Chang, C.-J., & Lee, S. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25021314 · Cited by 250
“Unlike mitochondrial fission, which promotes apoptosis, mitochondrial fusion occurs via the interferon-responsive cGAMP interactor 1–mitochondrial fusion 1/2 (MFN1/2) pathway [116].”
BackgroundHong, X., Isern, J., Campanario, S., Perdiguero, E., Ramírez-Pardo, I., Segalés, J., Hernansanz-Agustín, P., Curtabbi, A., Deryagin, O., Pollán, A., et al. (2022) · Cell stem cell · doi:10.1016/j.stem.2022.07.009 · Cited by 213
Chaudhary, M. R., Chaudhary, S., Sharma, Y., Singh, T. A., Mishra, A. K., Sharma, S. G., & Mehdi, M. M. (2023) · Biogerontology · doi:10.1007/s10522-023-10050-1 · Cited by 218
Mitochondrial quality control in human health and disease
Liu, B., Xu, C.-Z., Liu, Y., Lu, Z., Fu, T.-L., Li, G., Deng, Y., Luo, G., Ding, S. Z., Li, N., et al. (2024) · Military Medical Research · doi:10.1186/s40779-024-00536-5 · Cited by 211
Yi, L., Shang, X., Lv, L., Wang, Y., Zhang, J., Quan, C., Shi, Y., Liu, Y., & Zhang, L. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-05364-w · Cited by 136
“Mitochondrial dynamics is associated with various cellular processes, including mitochondrial quality control, metabolic adaptation, regulation of mitophagy and apoptosis [18].”
BackgroundInfluentialThe role of mitochondrial dynamics in cerebral ischemia-reperfusion injury
Huang, J., Chen, L., Yao, Z., Sun, X., Tong, X., & Dong, S. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.114671 · 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
“These mechanisms enable the mitochondrial network to adapt to challenges such as protein misfolding, oxidative stress, and organelle damage [68,69].”
Zhang, X., Zhou, H., & Chang, X. (2023) · Archives of Toxicology · doi:10.1007/s00204-023-03599-w · Cited by 115
“Mitochondrial fusion is involved in the communication of genetic material and metabolic substrates among different mitochondria, thereby maintaining mitochondrial stability and integrity (Adebayo et al. 2021).”
BackgroundMolecular Pathophysiological Mechanisms in Huntington’s Disease
Jurcău, A. (2022) · Biomedicines · doi:10.3390/biomedicines10061432 · Cited by 118
Regulation of the NLRP3 inflammasome by autophagy and mitophagy
Gupta, S., Cassel, S. L., Sutterwala, F. S., & Dagvadorj, J. (2024) · Immunological Reviews · doi:10.1111/imr.13410 · Cited by 116
“112,115 The fusion of the two membranes of the mitochondria are separately regulated; OMM fusion is facilitated by homo-and heterodimers of mitofusins Mfn1 and Mfn2, while the fusion of the IMM is regulated by long and short isomers of optic atrophy gene 1 (OPA1).”
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
“The optimal balance of fission and fusion is critical for mitochondrial homeostasis [8 – 12].”
BackgroundLi, Y., Guo, M., Niu, S., Shang, M., Chang, X., Sun, Z., Zhang, R., Shen, X., & Xue, Y. (2023) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2023.110502 · Cited by 119
Miller, D. M., McCauley, K. F., & Dunham‐Snary, K. J. (2025) · Endocrinology Diabetes & Metabolism · doi:10.1002/edm2.70132 · Cited by 131
“In MASLD, this balance is disrupted, leading to excessive mitochondrial fragmentation or elongation, impacting their function and contributing to disease progression [75] (Figure 5).”
Mitochondrial dysfunction in chronic neuroinflammatory diseases (Review)
Qin, P., Sun, Y., & Li, L. (2024) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2024.5371 · Cited by 106
Wang, Y., Shi, Y., Shao, Y., Lu, X., Zhang, H., & Miao, C. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06849-6 · Cited by 98
“Speci fi cally, fusion allows mitochondria to transfer gene products for optimal function [13], while fi ssion induces the isolation of impaired mitochondria for degradation through mitophagy (a selective form of autophagy) [14].”
BackgroundLiu, D., Qin, H., Gao, Y., Sun, M., & Wang, M. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107258 · Cited by 94
Sun, Y., Yang, Y.-M., Hu, Y.-Y., Ouyang, L., Sun, Z., Yin, X., Li, N., He, Q., & Wang, Y. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102334 · Cited by 91
“The balance of mitochondrial dynamics is a principal procedure to sustain cellular homeostasis [25].”
BackgroundMitochondrial Dysfunction in Metabolic Dysfunction Fatty Liver Disease (MAFLD)
Zhao, Y., Zhou, Y., Wang, D., Huang, Z., Xiao, X., Zheng, Q., Li, S., Long, D., & Feng, L. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242417514 · Cited by 89
“The imbalance between mitochondrial dynamics is key to determining the total mass of mitochondrial cells in the pathogenesis of MAFLD or MASH models [53–59].”
BackgroundMitochondrial dysfunction at the crossroad of cardiovascular diseases and cancer
Rocca, C., Soda, T., Francesco, E. M. D., Fiorillo, M., Moccia, F. D., Viglietto, G., Angelone, T., & Amodio, N. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04498-5 · Cited by 84
“Mitofusin 1 and 2 (MFN1/2) and optic atrophy 1 (OPA1) are responsible for fusion, while dynamin-related protein 1 (DRP1) and dynamin-2 (DNM2) are the primary fission proteins [32–34].”
BackgroundYan, Y., Li, M., Lin, J., Ji, Y., Wang, K., Yan, D., Shen, Y., Wang, W., Huang, Z., Jiang, H., et al. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.947387 · Cited by 84
“Fission is necessary for the creation of new mitochondria, it provides the raw material for new mitochondria and also contributes to quality control by the removal of damaged mitochondria and facilitates apoptosis (Adebayo et al., 2021).”
BackgroundKhatun, J., Gelles, J. D., & Chipuk, J. E. (2024) · Developmental Cell · doi:10.1016/j.devcel.2024.09.004 · Cited by 77
Role of mitochondria in physiological activities, diseases, and therapy
Wang, L., Zhou, X., & Lu, T. (2025) · Molecular Biomedicine · doi:10.1186/s43556-025-00284-5 · Cited by 87
“1a) [49].”
The role of mitochondrial dysfunction in periodontitis: From mechanisms to therapeutic strategy
Jiang, W., Wang, Y., Cao, Z., Chen, Y., Si, C., Sun, X., & Huang, S. (2023) · Journal of Periodontal Research · doi:10.1111/jre.13152 · Cited by 78
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
Yu, T., Wang, L., Zhang, L., & Deuster, P. A. (2023) · Antioxidants · doi:10.3390/antiox12061163 · Cited by 72
“The molecular mechanisms of mitochondrial fusion have been reviewed extensively elsewhere [56,60,63,64].”
BackgroundMitochondria-targeted fluorophore: State of the art and future trends
Ding, Q., Wang, X., Luo, Y., Leng, X., Li, X., Gu, M., & Kim, J. S. (2024) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2024.215772 · Cited by 69
Palabıyık, A. A., & Palabıyık, E. (2025) · Molecular Biology Reports · doi:10.1007/s11033-025-10368-8 · Cited by 76
“5 [31].”
Jurcău, A., & Jurcău, M. C. (2022) · Neural Regeneration Research · doi:10.4103/1673-5374.360289 · Cited by 67
“In depolarized mitochondria, PINK1 stabilizes at the OMM and is no longer imported to the IMM, favouring mitochondrial Parkin translocation (Kazlauskaite et al., 2015).”
BackgroundInfluentialMitochondrial dysfunction in Alzheimer's disease: Guiding the path to targeted therapies
Percy, K. C. M., Liu, Z., & Qi, X. (2025) · Neurotherapeutics · doi:10.1016/j.neurot.2025.e00525 · Cited by 70
Mitochondrial cristae in health and disease
Huang, C., Deng, K., & Wu, M. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.123755 · Cited by 66
Peng, Y., Zhao, L., Hu, K., Yang, Y., Ma, J., Zhai, Y., Jiang, Y., & Zhang, D. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231810920 · Cited by 61
Role of eIF5A in Mitochondrial Function
Barba‐Aliaga, M., & Alepuz, P. M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031284 · Cited by 63
Gu, Y., Zhao, X., Zhang, N., Yang, Y., Yi, Y., Shao, Q.-H., Liu, M.-X., & Zhang, X.-L. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102577 · Cited by 60
The Role of Mitochondria Dysfunction in Inflammatory Bowel Diseases and Colorectal Cancer
Kłos, P., & Dabravolski, S. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111673 · Cited by 57
“Further damaged mitochondria are delivered to lysosomes for disposal, while healthy parts could reincorporate into the mitochondria network [20].”
BackgroundFerretti, G. D. S., Quaas, C. E., Bertolini, I., Zuccotti, A., Saatci, Ö., Kashatus, J. A., Sharmin, S., Lu, D. Y., Poli, A. N. R., Quesnelle, A. F., et al. (2024) · Cell Death and Differentiation · doi:10.1038/s41418-024-01310-9 · Cited by 60
“We found that treatment of mice with AP-4-139B led to a signi fi cant decrease in metastatic potential; this was accompanied by a decrease in lung weights and a decrease in Ki67 staining, a marker of proliferation, in lung metastases of mice treated with AP-4-139B (Fig.”
BackgroundMitochondrial Quality Control: A Pathophysiological Mechanism and Therapeutic Target for Stroke
Yang, M., He, Y. T., Deng, S., Xiao, L., Tian, M., Xin, Y., Lu, C., Zhao, F., & Gong, Y. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.786099 · Cited by 56
Effect of Fluoride on Cytotoxicity Involved in Mitochondrial Dysfunction: A Review of Mechanism
Wei, M., Ye, Y., Ali, M. M., Chamba, Y., Tang, J., & Shang, P. (2022) · Frontiers in Veterinary Science · doi:10.3389/fvets.2022.850771 · Cited by 59
“Fluorosis can cause mitochondrial dysfunction, which is partly due to the disruption of the balance betweenmitochondrial fission and fusion, which leads to changes in the morphology of mitochondria, which in turn leads to mitochondrial dysfunction (122).”
BackgroundMTFR2-dependent mitochondrial fission promotes HCC progression
La, Z., Zhang, X., Liu, H., Yang, C., Yu, J., Zhao, W., Guo, J., Zhou, B., & Jiang, N. (2024) · Journal of Translational Medicine · doi:10.1186/s12967-023-04845-6 · Cited by 58
“The maintenance of mitochondrial integrity and homeostasis is crucial and relies on mitochondrial dynamics [5].”
BackgroundJoshi, D. C., Chavan, M. B., Gurow, K., Gupta, M., Dhaliwal, J. S., & Ming, L. C. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.117827 · Cited by 62
Lu, L., Liu, J., Wang, J., Lian, C.-Y., Wang, Z., & Wang, L. (2022) · Environmental Pollution · doi:10.1016/j.envpol.2022.120314 · Cited by 53
Tang, S., Fuß, A., Fattahi, Z., & Culmsee, C. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-07015-8 · Cited by 53
“…fi ssion process, which is responsible for the subcellular distribution of mitochondria under physiological conditions, for cytochrome C release during apoptosis e.g., in response to oxidative stress, and for mitochondrial quality control through facilitating mitophagy of damaged organelles [5, 6].”
BackgroundReductive stress and mitochondrial dysfunction: The hidden link in chronic disease
Mercola, J. M. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.03.029 · Cited by 56
Mitofusins: from mitochondria to fertility
Zhao, S., Heng, N., Wang, H., Wang, H., Zhang, H., Gong, J., Hu, Z., & Zhu, H. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04386-z · Cited by 53
“It has been established that the impairment of mitochondrial fusion leads to a reduction in glycolysis, OXPHOS, and the Krebs cycle [7, 8].”
BackgroundRecent advances in the pharmacological applications and liver toxicity of triptolide
Cui, D., Xu, D., Yue, S., Yan, C., Liu, W., Fu, R., Ma, W., & Tang, Y. (2023) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2023.110651 · Cited by 49
Standpoints in mitochondrial dysfunction: Underlying mechanisms in search of therapeutic strategies
Videla, L. A., Mariman, A. P., Ramos, B., Silva, M. J., & del Campo, A. (2022) · Mitochondrion · doi:10.1016/j.mito.2021.12.006 · Cited by 54
Molecular basis of the morphogenesis of sperm head and tail in mice
Yogo, K. (2022) · Reproductive Medicine and Biology · doi:10.1002/rmb2.12466 · Cited by 50
Liu, X., Ye, M., & Ma, L. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.1022821 · Cited by 51
“According to the literature, mitochondrial fusion maintains mitochondrial function by enabling the exchange of contents, whereas excessive mitochondrial fission worsens mitochondrial function and is regarded as an indication of dysfunction (Chen and Chan, 2010; Adebayo et al., 2021).”
BackgroundYe, F., Wu, L., Li, H., Peng, X., Xu, Y., Li, W., Wei, Y., Chen, F., Zhang, J., & Liu, Q. (2023) · Environmental Pollution · doi:10.1016/j.envpol.2023.121084 · Cited by 46
Therapeutic Effects of Mesenchymal Stromal Cells Require Mitochondrial Transfer and Quality Control
Mukkala, A. N., Jerkic, M., Khan, Z., Szaszi, K., Kapus, A., & Rotstein, O. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242115788 · Cited by 45
Chen, X., Yang, T., Zhou, Y., Mei, Z., & Zhang, W. (2024) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.14725 · Cited by 46
“51 An imbalance in mitochondrial dy - namics results in an alteration of mitochondrial quantity, morphology, and function, leading to CIRI.”
BackgroundZhao, M., Xie, J., Zhang, J., Zhao, B., Zhang, Y., Xue, J., Zhang, R., Zhang, R., Wang, H., Li, Y., et al. (2024) · Environmental Pollution · doi:10.1016/j.envpol.2024.124935 · Cited by 44
Epidemiology, Genetic Etiology, and Intervention of Premature Ovarian Insufficiency
Guo, T., Liu, H., Xu, B., Qi, Y., Xu, K., Wu, X., He, X., Qin, Y., & Chen, Z. (2025) · Endocrine Reviews · doi:10.1210/endrev/bnaf011 · Cited by 48
HIF-1 signaling: an emerging mechanism for mitochondrial dynamics
Xin, Y., Zhao, L., & Peng, R. (2023) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-023-00966-0 · Cited by 43
“Therefore, abnormal mitochondrial dynamics were thought to be a precursor to axonal degradation and eventually resulted in neurodegenerative disorders [1, 6, 24].”
BackgroundAging promotes an increase in mitochondrial fragmentation in astrocytes
Araujo, A. P. B., Vargas, G., Hayashide, L. D. S., Matias, I., Andrade, C. B. V., de Carvalho, J. J., Gomes, F. C. A., & Diniz, L. P. (2024) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2024.1496163 · Cited by 43
The role of Mitochondrial Fission Proteins in Mitochondrial Dynamics in Kidney Disease
Qin, L., & Xi, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232314725 · Cited by 47
Lysosomes in retinal health and disease
Boya, P., Kaarniranta, K., Handa, J. T., & Sinha, D. (2023) · Trends in Neurosciences · doi:10.1016/j.tins.2023.09.006 · Cited by 44
The role of mitochondrial dynamics in disease
Wang, Y., Dai, X., Li, H., Jiang, H., Zhou, J.-F., Zhang, S., Guo, J., Shen, L., Yang, H., Lin, J. M., et al. (2023) · MedComm · doi:10.1002/mco2.462 · Cited by 41
“8,12,57 For example, mitochondrial with dysfunction fuse with normal mitochondria, mtDNA is reintegrated and renewed, and mitochondrial membrane potential (MMP) returns to normal levels.”
BackgroundResultInfluentialZhao, X., Zhang, J., Li, C., Kuang, W., Deng, J., Tan, X., Li, C., & Li, S. (2024) · Mitochondrion · doi:10.1016/j.mito.2024.101975 · Cited by 47
Kobayashi, H., Imanaka, S., Yoshimoto, C., Matsubara, S., & Shigetomi, H. (2024) · Reproductive Medicine and Biology · doi:10.1002/rmb2.12577 · Cited by 41
“41 Mitochondrial fission is crucial for mitochondrial quality control mechanism that eliminates damaged mitochondria via mitophagy.”
BackgroundInfluentialCheung, C., Tu, S., Feng, Y., Wan, C., Ai, H., & Chen, Z. (2024) · Archives of Gerontology and Geriatrics · doi:10.1016/j.archger.2024.105522 · Cited by 43
Fogo, G. M., Raghunayakula, S., Emaus, K. J., Torres, F. J. T., Wider, J. M., & Sanderson, T. H. (2024) · The FASEB Journal · doi:10.1096/fj.202400313r · Cited by 43
Multiple roles of mitochondrial autophagy receptor FUNDC1 in mitochondrial events and kidney disease
Li, K., Xia, X., & Tong, Y. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1453365 · Cited by 41
Huynh, T. V., Rethi, L., Rethi, L., Chen, C., Chen, Y., & Kao, Y. (2023) · Cells · doi:10.3390/cells12091223 · Cited by 42
“Reduction and escalation of any of these dynamic processes due to pathological or physiological stressors results in an imbalance affecting mitochondrial function, ultimately leading to multiple disorders in cardiovascular, neurodegenerative, metabolic diseases, and cancer [20,21].”
BackgroundA Holistic Perspective on Living Aggregate
He, W., Kwok, R. T. K., Qiu, Z., Zhao, Z., & Tang, B. Z. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.3c09892 · Cited by 43
Recent development of mitochondrial metabolism and dysfunction in osteoarthritis
Guo, P., Alhaskawi, A., Moqbel, S. A. A., & Pan, Z. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1538662 · Cited by 52
Feng, X., Li, C.-Y., Zhang, H., Zhang, P., Shahzad, M., Du, W., & Zhao, X. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25094808 · Cited by 39
“Uninterrupted fission and fusion processes in mitochondria are essential for maintaining optimal mitochondrial activity, integrity and internal homeostasis [99].”
BackgroundZhang, X., Wang, L., Li, B., Shi, J., Xu, J. F., & Yuan, M. (2023) · Pharmaceuticals · doi:10.3390/ph16020277 · Cited by 42
Light and electron microscopy continuum-resolution imaging of 3D cell cultures
D’Imprima, E., Montero, M. G., Gawrzak, S., Ronchi, P., Zagoriy, I., Schwab, Y., Jechlinger, M., & Mahamid, J. (2023) · Developmental Cell · doi:10.1016/j.devcel.2023.03.001 · Cited by 42
Mitochondrial Dysfunction-Associated Mechanisms in the Development of Chronic Liver Diseases
Arumugam, M. K., Gopal, T., Kandy, R. R. K., Boopathy, L. K., Perumal, S. K., Ganesan, M., Rasineni, K., Donohue, T. M., Osna, N. A., & Kharbanda, K. K. (2023) · Biology · doi:10.3390/biology12101311 · Cited by 40
“Mitochondrial fusion and fission help to maintain organelle homeostasis and allow mitochondrial metabolism to be precisely tuned to cellular needs [177].”
BackgroundLiu, Z., Han, X., You, Y., Xin, G., Li, L., Gao, J., Meng, H., Cao, C., Liu, J., Zhang, Y., et al. (2024) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2023.117690 · Cited by 37
The multifaceted roles of natural products in mitochondrial dysfunction
Chen, Q., Ruan, D., Shi, J., Du, D., & Bian, C. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1093038 · Cited by 39
“material exchange in mitochondria to compensate for mitochondrial function, and mitochondrial fission removes damaged mitochondria through mitophagy (Adebayo et al., 2021).”
BackgroundMitochondrion: A bridge linking aging and degenerative diseases
Zhang, L., Wu, J., Zhu, Z., He, Y., & Fang, R. (2023) · Life Sciences · doi:10.1016/j.lfs.2023.121666 · Cited by 38
Riou, M., Enache, I., Sauer, F., Charles, A., & Gény, B. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24119572 · Cited by 38
“Indeed, mitochondria can move, fragment (also called fission) or fuse, and mitochondrial division is crucial to maintain the number and distribution of mitochondria in cells and to transfer gene products between mitochondria [54].”
BackgroundLiu, X., Song, L., Yu, J., Huang, F., Li, Y., & Ma, C. (2022) · PubMed · doi:10.14670/hh-18-443 · Cited by 35
Mitochondrial dysfunction in pulmonary arterial hypertension
Zhang, W., Liu, B., Wang, Y., Zhang, H., He, L., Wang, P., & Dong, M. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.1079989 · Cited by 37
“Mitochondrial division is crucial to maintain the number and proper distribution of mitochondria in daughter cells (Adebayo et al., 2021).”
BackgroundMitochondrial Dysfunction in Systemic Lupus Erythematosus with a Focus on Lupus Nephritis
Halfon, M., Tankeu, A. T., & Ribi, C. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25116162 · Cited by 36
“This process plays a role in inheritance and mitochondrial partitioning during cell division, apoptosis, and mitophagy [29].”
BackgroundBassiouni, W., y Valencia, R. H., Mahmud, Z., Seubert, J. M., & Schulz, R. (2023) · Basic Research in Cardiology · doi:10.1007/s00395-023-00999-y · Cited by 35
“Mfn-2, as an outer mitochondrial membrane fusion protein, mediates the docking and fusion of mitochondria through the oligomerization of the GTPase domains of different Mfn-2 proteins [1].”
Harnessing Mitophagy for Therapeutic Advances in Aging and Chronic Neurodegenerative Diseases
Ghosh, D., & Kumar, A. (2024) · Neuroglia · doi:10.3390/neuroglia5040026 · Cited by 36
“Fusion is vital for preventing the accumulation of mitochondrial damage and supporting biogenesis [28,29].”
Metabolic and Mitochondrial Dysregulations in Diabetic Cardiac Complications
Tashkandi, A. J. A., Gorman, A., Mathers, E. M., Carney, G., Yacoub, A., Setyaningsih, W. A. W., Kuburas, R., & Margariti, A. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26073016 · Cited by 35
“Mitochondria make up roughly 40% of the volume of cardiac cells, which is necessary to keep up with the high demand for cardiac function [203].”
Established and emerging roles for mitochondria in neutrophils
Peng, S., Gao, J., Stojkov, D., Yousefi, S., & Simon, H. (2022) · Immunological Reviews · doi:10.1111/imr.13158 · Cited by 34
Mitochondrial Dysfunction and Metabolic Reprogramming in Obesity and Asthma
Hartsoe, P., Holguín, F., & Chu, H. W. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25052944 · Cited by 36
“Fusion is controlled by GTPase proteins Mitofusin 1 (Mfn1), Mitofusin 2 (Mfn2), and Optic atrophy protein (OPA1) [29].”
BackgroundTurkington, R. E., Hukriede, N. A., Ho, J., Jayasundara, N., & Sanders, A. P. (2025) · Environmental Science and Pollution Research · doi:10.1007/s11356-025-36538-6 · Cited by 33
“Processes such as mitochondrial signaling, biogenesis, fission, fusion, and mitophagy are essential to maintaining mitochondrial function and optimal ATP production (Bhargava and Schnellmann 2017, Popov 2020, Adebayo et al. 2021).”
Kong, Y., Akatsuka, S., Motooka, Y., Zheng, H., Cheng, Z., Shiraki, Y., Mashimo, T., Imaoka, T., & Toyokuni, S. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102356 · Cited by 34
“This was also confirmed by a decrease in the protein levels regulating mitochondrial fusion (Mitofusion1/2 and Opa1) and fission (Drp1) [38] in the MUT kidney at 3 weeks of the carcinogenesis protocol (Figs.”
BackgroundZhou, J., Hao, J., Zhong, Z., Yang, J., Lv, T., Zhao, B., Lin, H., Chi, J., & Guo, H. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0355 · Cited by 32
“Mitochondrial fission is also important for maintaining the proper distribution and quantity of mitochondria in daughter cells and is beneficial in situations where large amounts of energy are required (Adebayo et al., 2021).”
Lyu, Y.-T., Huo, J., Jiang, W., Yang, W., Yang, W., Wang, S., Cheng, Y., Jiang, Z., & Shan, Q. (2023) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2023.175531 · Cited by 33
Sultana, M. A., Hia, R. A., Akinsiku, O., & Hegde, V. K. (2023) · Biology · doi:10.3390/biology12071019 · Cited by 31
“A subtle balance between mitochondrial fusion and fission is essential for cell survival and optimal function [48].”
BackgroundFang, X., Xia, W., Li, S., Qi, Y., Liu, M., Yu, Y., Li, H., Li, M., Tao, C., Wang, Z., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23095013 · Cited by 31
“Mitochondria are interconnecting and highly dynamic cellular organelles whose homeostasis requires a stable equilibrium in a multitude of processes including fission, fusion, and biogenesis [24].”
BackgroundMitochondrial Control in Inflammatory Gastrointestinal Diseases
Sui, G.-Y., Wang, F., Lee, J., & Roh, Y. S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232314890 · Cited by 31
The Journey of Mitochondrial Protein Import and the Roadmap to Follow
Haastrup, M. O., Vikramdeo, K. S., Singh, S., Singh, A. P., & Dasgupta, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032479 · Cited by 33
“(12S and 16S rRNA), and 22 transfer RNAs [6].”
InfluentialSelf-citationHao, W., Cha, R., Wang, M., Li, J., Guo, H., Du, R., Zhou, F., & Jiang, X. (2023) · ACS Nano · doi:10.1021/acsnano.3c01656 · Cited by 30
New therapeutic directions in type II diabetes and its complications: mitochondrial dynamics
Wang, S., Zhao, H., Lin, S., Lv, Y., Lin, Y. N., Liu, Y., Peng, R., & Jin, H. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1230168 · Cited by 33
“Abbreviations: ROS, reactive oxygen species; OS, oxidative stress; Mfn1, mitofusin-1; Mfn2, mitofusin-2; Opa1, optic atrophy 1; Drp1, dynamin related protein 1; Fis1, mitochondrial fission 1; MFF, mitochondrial fission factor; T2D, type II diabetes; OMM, outer mitochondrial membrane; HR1, helix regions 1; HR2, helix r…”
BackgroundInfluentialGao, J., & Hou, T. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.114999 · Cited by 32
Zhou, L., Su, W., Wang, Y., Zhang, Y., Xia, Z., & Lei, S. (2023) · Diabetes Obesity and Metabolism · doi:10.1111/dom.15369 · Cited by 29
“43,44 Fission in mammals is coordinated by a large dynamin-like GTPase, DRP1, which is recruited to the mitochondria by adaptors present on the outer mitochondrial membrane, including MFF, MID49, MID51 and FIS1.”
BackgroundLi, Q., Guo, P., Wang, S., Su, L., Liang, T., Yu, W., Guo, J., Yang, Q., Tang, Z., & Liao, J. (2023) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2023.169642 · Cited by 29
Latino, D., Venditti, M., Falvo, S., Grillo, G., Santillo, A., Messaoudi, I., Rhouma, M. B., Minucci, S., Baccari, G. C., & Fiore, M. M. D. (2024) · Cells · doi:10.3390/cells13060523 · Cited by 30
“In this regard, several proteins are involved in such dynamic activities: Dynamin-associated protein 1 (DRP1) regulates mitochondrial fission, while Mitofusin 1 and 2 (MFN1 and MFN2), dynamin-like GTPases, and the protein optic atrophy 1 (OPA1), are involved in mitochondrial fusion [8].”
BackgroundJeong, I., Cho, E., Yook, J.-S., Choi, Y., Park, D., Kang, J., Lee, S.-H., Seo, D. Y., Jung, S., & Kwak, H. (2024) · Life · doi:10.3390/life14080962 · Cited by 35
“In contrast, mitochondrial fission refers to the process by which a mitochondrion is divided into two separate mitochondria [56].”
BackgroundHypoxia and aging: molecular mechanisms, diseases, and therapeutic targets
Nisar, A., Khan, S., Li, W., Hu, L., Samarawickrama, P. N., Gold, N. M., Zi, M., Mehmood, S. A., Miao, J., & He, Y. (2024) · MedComm · doi:10.1002/mco2.786 · Cited by 33
“19,20 Additionally, hypoxia induces chronic inflammation and cellular senescence, two processes that accelerate the biological aging of tissues.”
Background
Metadata
- Authors
- Adebayo, M., Singh, S., Singh, A. P., & Dasgupta, S.
- Affiliations
- USA Mitchell Cancer Institute (US)
- Corresponding author
- Singh, Ajay Pratap
- Dasgupta, Santanu
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 2021-05-28
- Volume
- 35
- Issue
- 6
- Pages
- e21620-e21620
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- PMC
- PMC8415099
- OpenAlex
- W3164775823
- Cited by
- 733
- References
- 103
- Citations by year
- 2026: 189 · 2025: 235 · 2024: 183 · 2023: 83 · 2022: 38 · 2021: 4
- FWCI
- 8.11
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- The FASEB Journal (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (CA185490, CA224306, CA204801, CA231925)
- 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 fusion, mitochondrial fission, mitochondrial dynamics, mitochondrial homeostasis, mitochondrial quality control, mitochondrial division, oxidative phosphorylation, calcium signaling, damage-associated molecular patterns, apoptosis, mitochondrial metabolism, neurodegenerative diseases, cardiovascular disease, cancer
- MeSH terms
- Animals, Homeostasis, Humans, Mitochondria, 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