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
Items 501–600 of 734
Neurodegenerative Diseases and Succinate Dehydrogenase: A Therapeutics Avenue for Treatment
Viswalingam, V., & Kumar, D. (2025) · Springer eBooks · doi:10.1007/978-981-96-6831-1_9 · Cited by 1
Shi, Z., Peng, Q., Sun, S., Xiong, M., Zhu, X. L., Wang, H., Liu, S., Li, Z., Wang, L., Li, G., et al. (2025) · International Immunopharmacology · doi:10.1016/j.intimp.2025.115275 · Cited by 1
Zhao, Y., Chen, D., Chen, H., Fan, R., Xu, W., & Jiang, H. (2025) · Journal of Neurology · doi:10.1007/s00415-025-13318-3 · Cited by 1
Tang, J., & Yang, K. (2025) · The FASEB Journal · doi:10.1096/fj.202501731r · Cited by 2
Nakamura, K., Sato, Y., Hashimoto, M., Matsumoto, N., Nitta, S., Okazaki, Y., Miyoshi, Y., & Nagase, H. (2025) · Mitochondrion · doi:10.1016/j.mito.2025.102081 · Cited by 1
Wang, X., Li, H., Dong, Z., Lu, W., Chen, J., Zhang, H., Yuan, Z., Liu, Y., Weng, Q., & Han, Y. (2025) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/j.cbpa.2025.111927 · Cited by 1
Krahel, W. D., Chodkowski, M., Bartak, M., Ostrowska, A., Godlewski, M. M., Adamczyk, M., Krzyżowska, M., & Cymerys, J. (2025) · Cells · doi:10.3390/cells14191493 · Cited by 1
Wang, Y.-P., Liu, P., Chen, Y., Wang, Y., Cong, Y., Wen, H., Liu, M., Guo, X., & Li, D. (2025) · Food Science and Human Wellness · doi:10.26599/fshw.2025.9250802 · Cited by 1
Chen, S., Li, Q., & Zheng, W. (2025) · Frontiers in Oncology · doi:10.3389/fonc.2025.1625797 · Cited by 1
“Mitochondria are constantly changing organelles that meet the needs of the cell (20).”
High-content phenotyping reveals Golgi dynamics and their role in cell cycle regulation
Cao, X., Peng, Y., Yang, M., Gan, M., Zhang, D., Zhou, S., & Takao, D. (2025) · The Journal of Cell Biology · doi:10.1083/jcb.202503083 · Cited by 2
“This approach can also be extended to other organelles exhibiting dynamic behaviors, such as mitochondrial fission–fusion cycles (Wang et al., 2019; Stephan et al., 2019; Yang et al., 2020; Adebayo et al., 2021).”
Assessment of Mitochondrial Fission/Fusion Dynamics in Kidney Proximal Tubular Cells
Awasthi, V., Sharief, S. Q., Bkhache, M., Das, A., & Bouchareb, R. (2025) · Journal of Visualized Experiments · doi:10.3791/69268 · Cited by 1
Zhu, X., Shao, Y., & Wang, J. P. (2025) · Molecular Biology · doi:10.1134/s0026893325700426 · Cited by 1
Arici, M., Bilgehan, A., Qaoud, M. T., & Özhan, G. (2025) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2025.111840 · Cited by 1
Impact of dystrophin deficiency on vascular smooth muscle cell
Xuan, W., Cheng, F., Han, X., Tipparaju, S. M., & Ashraf, M. (2025) · Scientific Reports · doi:10.1038/s41598-025-29484-3 · Cited by 1
“Mitochondrial dynamics, specifically the balance between fission and fusion, are essential for maintaining mitochondrial homeostasis and cellular function 17 .”
Mitochondrial position responds to glucose stimulation in a model of the pancreatic beta cell
Perez, L., Ng, X. W., Mohs, M., Piston, D. W., & Mukherji, S. (2025) · Biophysical Journal · doi:10.1016/j.bpj.2025.11.018 · Cited by 1
Xu, L., Cheng, R., Zhou, K., & Ma, J.-X. (2026) · American Journal Of Pathology · doi:10.1016/j.ajpath.2025.12.006 · Cited by 1
“42,43 In ECs, it has been shown that mitochondrial dysfunction disrupts metabolism, a process known to contribute to cellular senescence.”
Robust mitochondria segmentation and morphological profiling using soft X-ray tomography
Yadav, A., Singh, A., Deshmukh, A., Bharadwaj, P., Baliyan, A., White, K. L., & Singla, J. (2026) · Journal of Structural Biology · doi:10.1016/j.jsb.2026.108291 · Cited by 1
Self-citationMei, Z., Zhong, W., Deng, T., Meng, X., Lv, X., Xiao, J., & Li, Y. (2026) · Translational Stroke Research · doi:10.1007/s12975-025-01401-w · Cited by 1
“Upregulated MMPs degrade the extracellular matrix and downregulate the expression of key tight junction proteins, such as Claudin-5 and Occludin [43, 55]. mtDNA, enzyme complexes), while fission enables quality control via segregating damaged components [57, 58].”
Chen, J., Yang, F., Hu, Y., Zhang, C., Wang, D., Li, Y., Liu, P., Xing, C., Li, H., Cao, H., et al. (2026) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2026.119784 · Cited by 1
Monitoring neuronal mitophagy and locomotion deficits in a C. elegans model of Alzheimer’s disease
Niforos-Garcia, G., Tsakiri, E., & Palikaras, K. (2026) · Methods in cell biology · doi:10.1016/bs.mcb.2025.12.001 · Cited by 1
Malik, A. A., Shah, R. A., Yaqoob, S. H., Gayas, M. A., Handoo, N., Magray, S. N., Fazili, M. R., Dar, M. A., Assad, N. I., Nazir, S., et al. (2026) · Frontiers in Veterinary Science · doi:10.3389/fvets.2026.1737059 · Cited by 1
“Higher MFN2 expression has been consistently linked with better oocyte quality and developmental competence across species (29, 32).”
Transgenerational effects of environmentally relevant concentrations of ibuprofen on Daphnia magna
Xiao, Y., Zhao, W., Duan, C., Gong, W., Zhao, Y., Zhang, H., & Nie, X. (2026) · Aquatic Toxicology · doi:10.1016/j.aquatox.2026.107771 · Cited by 1
Vokacova, K., Danesova, N., Sojka, L., & Vymetalkova, V. P. (2026) · Molecular Diagnosis & Therapy · doi:10.1007/s40291-026-00838-5 · Cited by 1
“Mitochondrial fusion merges two mitochondria, allowing the transfer of proteins between them for maintaining their function, especially under stress conditions [79].”
Atmospherically relevant PM2.5 promotes age-related muscle atrophy in an age-dependent manner
Wang, Z., Liu, W., & Kim, S. H. (2026) · Experimental Gerontology · doi:10.1016/j.exger.2026.113091 · Cited by 1
Pu, X., Yan, Z., Liu, J., Wang, Y., Guan, X., Wu, Q., Zhang, Q., Liu, R., & Chang, X. (2026) · Phytotherapy Research · doi:10.1002/ptr.70201 · Cited by 1
Ashraf, R., Tankay, K., Raina, M., Athira, & Kumar, S. (2026) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-026-01172-4 · Cited by 1
郑凤婷, Zhou, J., Cao, Y., Lin, L., Wang, W., Zhang, L., Li, W., Li, T. Y., & Wang, L. (2026) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-026-01146-6 · Cited by 1
Zhou, M., Tian, Y., & Ye, T. (2026) · Gene · doi:10.1016/j.gene.2026.150119 · Cited by 1
Zeng, B., Jiang, G., Wang, C., Zhou, H., Zhang, Y., Yan, Y., Chen, Z., Zhang, L., Li, X., Xie, M., et al. (2026) · Journal of Molecular Histology · doi:10.1007/s10735-026-10750-1 · Cited by 1
Wang, X., Huang, W., Shen, L., Zheng, L., Gu, L., Lin, L., Li, L., Liu, L., Wang, Y., Li, X., et al. (2026) · Phytomedicine · doi:10.1016/j.phymed.2026.158131 · Cited by 1
Burczyk, G., & Kołaczkowska, E. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1770063 · Cited by 1
Small but mighty: mitochondrial DNA at the centre of retrograde signalling
Harding, E., Bazzani, V., & Vascotto, C. (2026) · Cell Communication and Signaling · doi:10.1186/s12964-026-02858-4 · Cited by 1
“Conversely, when ATP levels increase, mitochondria undergo fusion events to optimise energy efficiency and maintain cellular health by distributing the electrochemical gradient evenly across the fused mitochondria [162, 163].”
Mitochondrial dynamics and cancer: mechanisms and targeted therapy
Wang, A., Ye, X., Zhao, Y., & Zhang, C. (2026) · Cell Biology and Toxicology · doi:10.1007/s10565-026-10174-3 · Cited by 1
“Under physiological conditions, fission and fusion maintain the topological balance of the network, autophagy eliminates damaged components, and trafficking enables the precise spatial distribution of energy (Adebayo et al. 2021; Joaquim And Escobar-Henriques 2020; Spinelli And Haigis 2018).”
Zhang, J., Zhang, Y., Li, M., Gao, L., Zhou, J., Gao, L., & Zhou, J. (2026) · Reproduction · doi:10.1093/reprod/xaag041 · Cited by 1
SARS‐CoV‐2 targets mitochondria, exacerbating COVID‐19 pneumonia
Wu, D., Dasgupta, A., Hora, J. S., Chen, K., Banerjee, A., & Archer, S. (2026) · The Journal of Physiology · doi:10.1113/jp290297 · Cited by 1
Hua, Y., Zou, M., Zhang, L., Chen, L., Rao, X., Wei, G., Wei, J., Wei, M., Wei, Y., & Li, J. (2026) · Poultry Science · doi:10.1016/j.psj.2026.106953 · Cited by 1
“Mitochondrial fusion maintains respiratory function and cellular homeostasis by facilitating the exchange of gene products and metabolites between mitochondria, particularly under metabolic and environmental stress (Adebayo et al., 2021).”
Mitochondrial fission mediates an evolutionarily conserved antibacterial defense response
Kapétanovic, R., Afroz, S. F., Curson, J. E. B., Kirmes, I., Ramnath, D., Nothjunge, S., Liu, J., Atkinson, J. D., Ahier, A., Raven, K. D., et al. (2026) · Science Immunology · doi:10.1126/sciimmunol.aed2623 · Cited by 1
Dai, J., Yuan, K., Huang, K., Sun, Y., Zhou, X., & Zhang, Y. (2026) · Journal of Immunotoxicology · doi:10.1080/1547691x.2026.2665189 · Cited by 1
Xia, C., Chen, H., Zhang, J., Jiang, W., Xue, S., Zhao, C., Zhou, Q., Wang, Y., & Sun, W. (2026) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2026.121847 · Cited by 1
Laye, C. J., & Hubbard, W. B. (2026) · npj Metabolic Health and Disease · doi:10.1038/s44324-026-00111-7 · Cited by 1
“Fission, driven mainly by dynamin-related protein-1 (Drp1) and mitochondrial fi ssion 1 protein (FIS1), segregates damaged mitochondrial segments for subsequent clearance by mitophagy 75 .”
Apatinib Causes Hypertension via Drp1-Mediated Endothelial Mitochondrial Fission
Si, F., Ma, X., Li, C., Wang, Y., Ma, J. H., Feng, C., Liu, Q., & Yu, J. (2026) · Hypertension · doi:10.1161/hypertensionaha.125.26188 · Cited by 1
ROS/SIRT1 signaling mediates mitochondrial dysfunction in hyperoxia-induced BEAS-2B cells injury
Yang, K., He, T., Zhang, R., Zhao, S., Kang, L., Lei, X., & Dong, W. (2026) · Free Radical Research · doi:10.1080/10715762.2026.2672452 · Cited by 1
“…mitochondrial dynamics not only contributes to mitochondrial quantity and mass, but also controls mitochondrial oxidative phosphorylation activity [30]. in turn, mitochondrial dynamics can be influenced by ROs [31]. the present study showed that hyperoxia decreased the expression of OPa1, MFN1…”
Landowski, M., Hagimori, R., Gogoi, P., Shahi, P. K., Oikawa, K., Bhute, V. J., McLellan, G. J., Ikeda, S., Yamada, K., Pattnaik, B. R., et al. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2026.1724328 · Cited by 1
Ma, D., Wang, Z., Ji, C., Wang, Y., Zhang, Y., Qu, L., Shi, L., & Mao, R. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2026.103215 · Cited by 1
Mitochondria as integrative regulators of ferroptosis in the female reproductive system
Yenigün, I., Huner, N. E., & Yaba, A. (2026) · Biology of Reproduction · doi:10.1093/biolre/ioag132 · Cited by 1
“Fission is mediated by dynamin-related protein 1 (DRP1), whereas mitofusin 1/2 (MFN1/2) and optic atrophy 1 (OPA1) promote fusion of the outer and inner mitochondrial membranes, respectively [ 9, 10].”
Tau protein as a regulator of mitochondrial function and dynamics
Tsakiri, E. N., Campos‐Marques, C., Ploumi, C., Skourti, K., Roussos, A., Mytilinaiou, E., Vamvaka-Iakovou, A., Ferreira, I. L., Dioli, C., Gianniou, D. D., et al. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2521642123 · Cited by 1
Yang, X., Cheng, K., Chen, C., Zhang, Y., & Wang, D. W. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27177734 · Cited by 1
Zhao, Y., Liu, Y., Xie, M., Ye, Z., Huang, H., Yao, M., Zhou, F., Zhao, J., & Tang, J. (2026) · Cancer Science · doi:10.1111/cas.70488 · Cited by 1
“Mitochondrial fission and fusion are dynamic processes [35], where fission is coordinated with mitophagy or apoptosis [36], promoting the clearance of damaged mitochondria and the redistribution of mtDNA [37], thereby supporting OXPHOS [25].”
Biosynthetic solutions to mechanical stress: why do mechanical stresses drive altered metabolism?
Lee, A., Sakowicz, I., Minor, C., Block, A. V., Adebowale, K., & Tharp, K. M. (2026) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2026.103694 · Cited by 1
Nouws, J., Siller, S. S., Yang, T., Kim, S., Kim, S.-H., Santofimia‐Castaño, P., Iovanna, J., Herzog, E. L., McDonough, J. E., & Sauler, M. (2026) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00098.2026 · Cited by 2
Jasaputra, D. K., Gunadi, J. W., Sutiono, C. A., & Lesmana, R. (2023) · Jurnal Ilmiah Kedokteran Wijaya Kusuma · doi:10.30742/jikw.v12i1.2637 · Cited by 1
“Mitochondrial fission and fusion are interlinked processes which have critical role in maintaining cellular homeostasis(Adebayo et al., 2021), therefore an increase of fusion and a decrease of fission to its baseline level showed the effect of turmeric and mangosteen in maintaining mitochondrial…”
BackgroundKomarova, E. M., Александровна, Л. Е., Ob’edkova, K. V., Ryzhov, J. R., Gzgzyan, A. M., & Tapilskaya, N. I. (2023) · Russian Journal of Human Reproduction · doi:10.17116/repro20232906157 · Cited by 1
Mitochondrial Pharmacotherapeutics - Advancements and Applications
Vyas, G., Kaur, G., Rana, R., Verma, S., Bhatia, M., & Kumar, R. (2024) · BIO Web of Conferences · doi:10.1051/bioconf/20248601014 · Cited by 1
“Further, the task is demonstrated to promote survival of increased fission with mitochondria and was mediated by increased production of ROS[58, 61].”
BackgroundKim, M., Paik, J. H., Lee, H., Kim, M. J., Eum, S. M., Kim, S. Y., Choi, S., Park, H.-Y., Jeong, H. G., & Jeong, T. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25073743 · Cited by 1
“Mitochondria maintain metabolic homeostasis through the processes of fusion and fission, known as mitochondrial dynamics [9].”
BackgroundF‐actin/DRP1 axis‐mediated mitochondrial fission promotes mitophagy in diabetic submandibular glands
Zhu, H., Wang, Y., Zhang, Q., Wang, K., Huang, Y., & Xiang, R. (2024) · Oral Diseases · doi:10.1111/odi.14983 · Cited by 1
Adhikary, A., Joseph, V. F., Banerjee, R., & Nagotu, S. (2025) · Mitochondrion · doi:10.1016/j.mito.2025.102006 · Cited by 1
Mantey, I., Langerscheidt, F., Cakmak, C., Baba, N., Burghardt, K., Karakaya, M., & Zempel, H. (2025) · Genes · doi:10.3390/genes16020198 · Cited by 2
“The process of mitochondrial fusion is known to facilitate interconnectivity in human cells as it transfers gene products be-tween mitochondria for optimal functioning, especially under metabolic and environmental stress [4].”
Zhu, Z., Li, W., Ding, K., Bastawy, E. M., Kamel, A. M., Kou, X., & Min, L. (2025) · Cryobiology · doi:10.1016/j.cryobiol.2025.105231 · Cited by 1
Dobosz, A. M., Krogulec, E., Stefanowski, N., Kendziorek, M., Lebiedzińska, M., Wieckowski, M. R., Janikiewicz, J., & Dobrzyń, A. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2025.159664 · Cited by 1
Vidyadharan, V. A., Betancourt, A., Smith, C., Blesson, C. S., & Yallampalli, C. (2024) · Research Square · doi:10.21203/rs.3.rs-4103233/v1 · Cited by 1
Liu, S., Chen, S., Jiang, X.-Y., Xiao-yun, S., & Yang, N. (2024) · Research Square · doi:10.21203/rs.3.rs-4188427/v1 · Cited by 1
He, T., Sha, J., Hu, Y., Shao, C., Zhou, Y., Lü, C., Yao, J., & Gao, J. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.13.638057 · Cited by 1
Transcriptomic analysis of mitohormesis associated with lifespan extension in Caenorhabditis elegansPreprint
Kim, J., Dutta, N., Garcia, G., & Higuchi‐Sanabria, R. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.15.648933 · Cited by 1
SFRP1 drives glycolytic activation in astrocytes during neuroinflammationPreprint
Martinez-Baños, M., Miaja, P., Martín‐Bermejo, M. J., Pereyra, G., & Bovolenta, P. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.10.675368 · Cited by 2
“In contrast, LPS-mediated TLR4 activation in microglia promoted initial fission followed by Mfn2 and DRP1 mediated compensatory fusion (Katoh et al., 2017), which maintains metabolic efficiency during stress (Adebayo et al., 2021).”
A neuro-intestinal circuit controls mitochondrial dynamics and stress resistancePreprint
Cornell, R., Cao, W. J., Harradine, B., Handley, A., & Pocock, R. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.06.19.545634
Liu, Y.-J., Li, R., Xiao, D., Yang, C., Li, Y.-L., Chen, J., Wang, Z., Zhao, X., & Shan, Z. (2023) · SSRN Electronic Journal · doi:10.2139/ssrn.4515099
Sun, Z., Jiao, A., Han, T., Zhao, Y., Zhang, H., & Gao, Q. (2024) · SSRN Electronic Journal · doi:10.2139/ssrn.4795969
Wang, Z., Wang, Y., Dong, C., Miao, K., Jiang, B., Zhou, D., Dong, K., Wang, Y., & Zhang, Z. (2024) · SSRN Electronic Journal · doi:10.2139/ssrn.4856708
Yang, K., Wu, Y., Zhang, R., Lei, X., Kang, L., & Dong, W. (2024) · PubMed Central · doi:10.7499/j.issn.1008-8830.2404120
Mitohormesis : la clé de voûte de la résistance thérapeutique des cellules cancéreuses
Boët, E., Saland, E., Skuli, S. J., Griessinger, E., & Sarry, J. (2024) · Comptes Rendus Biologies · doi:10.5802/crbiol.154
Maintenance of Mitochondrial Dynamics for Healthy Brain Ageing
Mishra, E., & Thakur, M. K. (2024) · Healthy ageing and longevity · doi:10.1007/978-3-031-68513-2_10
Nörodejeneratif Hastalıklarda Yeni Bir Yaklaşım: Mitokondri Hedefli Tedavi
Çelik, K., & Taşkıran, D. (2024) · Celal Bayar Üniversitesi Sağlık Bilimleri Enstitüsü Dergisi · doi:10.34087/cbusbed.1281151
Mitochondria as a Key Player in Cancer
Čižmárová, B., Hubková, B., Grešová, A., Kraus, V., & Birková, A. (2024) · Interdisciplinary cancer research · doi:10.1007/16833_2024_387
Siri‐Angkul, N., Chattipakorn, S. C., & Chattipakorn, N. (2024) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9789815223910124090006
Wang, Y., Li, Y., Li, C., Pu, L., Geng, W.-L., Gao, F., & Zhang, Q. (2024) · Inhalation Toxicology · doi:10.1080/08958378.2024.2428163 · Cited by 1
“The dynamic equilibrium of mitochondrial fission and fusion maintains the stability of the mitochondrial internal environment and the stability of an organism’s internal environment (Adebayo et al. 2021).”
Control of mitochondrial dynamics by dPGC1 limits Yorkie-induced oncogenic growth in DrosophilaPreprint
Sew, W. Q. G., Molano-Fernández, M., Li, Z., Lange, A., de Ciriza, N. P., Rasmussen, L. J., & Herranz, H. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.12.02.626378
Impact of Mitochondrial Fission and Fusion on Neuronal Health and Incidence of Dementia
Holt, A. G., & Davies, A. M. (2026) · Clinical bioenergetics · doi:10.3390/clinbioenerg2030012
Advances in inflammaging in liver disease
Xu, Y., Chen, L., Liu, W., & Chen, L. (2025) · Journal of Zhejiang University (Medical Sciences) · doi:10.3724/zdxbyxb-2024-0249 · Cited by 2
Filice, M., Mazza, R., Gattuso, A., Caferro, A., Napolitano, G., Fasciolo, G., Venditti, P., Imbrogno, S., & Cerra, M. C. (2025) · Fish Physiology and Biochemistry · doi:10.1007/s10695-025-01452-8
“Fission and fusion events play a key role in determining mitochondrial shape, and the balance between these two opposite processes maintains organelle number, mtDNA mixing, and function (Adebayo et al. 2021).”
Mitochondrial oxidative stress and liver disease
Васильевна, В. Г., & Хавкин, А. И. (2025) · Экспериментальная и клиническая гастроэнтерология · doi:10.31146/1682-8658-ecg-228-8-143-157
Liao, L., Zheng, Z., Deng, M., Xu, W., Zhang, Q., Wang, Z., Li, C., Li, J., Bian, Y., Wang, K., et al. (2025) · SSRN Electronic Journal · doi:10.2139/ssrn.5122491
Mitochondrial remodeling under hypoxia
Skvortsova, K. A., Baranich, T. I., Omarova, Z. M., Алексеевич, Х. Д., Bicherova, I. A., Glinkina, V. V., & Sukhorukov, V. S. (2024) · Morphology · doi:10.17816/morph.634229
王, 超. (2025) · Advances in Clinical Medicine · doi:10.12677/acm.2025.152379
Loss of nuclear envelope bud formation leads to mitophagy initiation in Drosophila muscles
Guo, Y., Brooks, D. S., Zhao, Z., Biven, E., & Geisbrecht, E. R. (2025) · Autophagy Reports · doi:10.1080/27694127.2025.2471121
“Mitochondrial assembly regulatory factor (Marf) is responsible for mediating outer mitochondrial fusion, while Dynamin-related protein 1 (Drp1) catalyzes the constriction of this organelle towards fission [4].”
Zhang, J., Li, M., Zhang, Y., Gao, L., Zhou, J., Gao, L., & Zhou, J. (2025) · Research Square · doi:10.21203/rs.3.rs-6142175/v1
Barnes, A. M., Mitra, A., Knue, M., Derkyi, A., Do, A. N. D., Dale, R., & Marini, J. C. (2025) · Cells · doi:10.3390/cells14070518
“Mitochondrial fusion occurs in response to cellular stress, such as starvation or inhibition of protein synthesis [45].”
Arévalo, C., Carlosama, C., Rojas, L., Cala, M. P., Hamon, M., Friguet, B., Barreto, A., & Susana Fiorentino, G. (2025) · Molecules · doi:10.3390/molecules30081783
“To evaluate whether activity on mitochondria induced apoptosis, we measured the changes by double staining with annexin V-FITC/PI.”
Drp1 promotes vascular smooth muscle cell death via adverse mitochondrial dynamicsPreprint
Patel, V. B., Jadli, A. S., Meechem, M. B., Gomes, K., Mackay, C. D. A., Edalat, P., & Palma, C. D. (2025) · Research Square · doi:10.21203/rs.3.rs-5968820/v1
Koo, K., Choi, J., Nam, Y.-K., Kim, H. J., Kim, C., Jeong, S.-H., Jang, H., Lim, K., Lim, B.-C., Kim, T.-H., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.16.647364
Siller, S. S., Yang, T., Nouws, J., Kim, S., Kim, S., Santofimia‐Castaño, P., Iovanna, J., McDonough, J. E., & Sauler, M. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.27.650854
Inhibition of PKCγ phosphorylation protects against cerebral ischemia-reperfusion injury
Li, C., Chen, J., Ouyang, X., Duan, R. X., Kuang, Y., He, Y., Tan, J., & Zeng, L. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104221
“Mitochondria are the central organelles for cellular energy metabolism, and the process of maintaining their internal homeostasis is highly complex, involving processes such as fission and fusion [11,12].”
Landowski, M., Hagimori, R., Gogoi, P., Bhute, V. J., Ikeda, S., Takimoto, T., & Ikeda, A. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.21.655403
Metabolic disorders associated with mitochondrial dysfunction
Akash, M. S. H., & Rehman, K. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-36312-2.00011-5
Xu, Y., Sha, Y., Chen, X., Chen, Q., Liu, X., He, Y., Huang, W., He, Y., & Gao, X. (2025) · BioTech · doi:10.3390/biotech14020043
Amin, T., Shishir, M. A., Alam, M. M., Anam, M. B., Bulbul, N., Jime, J. S., & Fakruddin, M. (2025) · Infectious Disorders - Drug Targets · doi:10.2174/0118715265362556250717063603
Adipose tissue: A target for prevention and treatment of metabolic diseases
Souza‐Mello, V. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-27370-4.00003-2
Mahadeo, A., Bammler, T. K., MacDonald, J. W., Zheng, A. R., Yeung, C. K., Himmelfarb, J., & Kelly, E. J. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.08.29.673189
Kumar, R., Chinala, A., Chen, L., Desai, S. P., Garcia, M. A., Blossom, S. J., Campen, M. J., & Gullapalli, R. R. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.13.676023
Babayeva, G. H. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-24836-8.00004-3
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
