Cited by 2,002Mitochondrial Function and PathologyAutophagy in Disease and TherapyCell death mechanisms and regulation

The DOI matches its Crossref record; 135 of the 135 references it cites were found in a registry or an index.

Mitochondrial fusion and fission in cell life and death

Westermann, Benedikt·2010·Nature Reviews Molecular Cell Biology

Open this paper in CoChat — free account

Abstract

Mitochondria are dynamic organelles that constantly fuse and divide. These processes (collectively termed mitochondrial dynamics) are important for mitochondrial inheritance and for the maintenance of mitochondrial functions. The core components of the evolutionarily conserved fusion and fission machineries have now been identified, and mechanistic studies have revealed the first secrets of the complex processes that govern fusion and fission of a double membrane-bound organelle. Mitochondrial dynamics was recently recognized as an important constituent of cellular quality control. Defects have detrimental consequences on bioenergetic supply and contribute to the pathogenesis of neurodegenerative diseases. These findings open exciting new directions to explore mitochondrial biology.

Integrity signals

Registry

Crossref · 10.1038/nrm3013

Cites

135 of 135 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Mitochondria, Oxidants, and Aging
Balaban, R. S., Nemoto, S., & Finkel, T. (2005) · Cell · doi:10.1016/j.cell.2005.02.001 · Cited by 4,388
Regulation mechanisms and signaling pathways of autophagy
He, C., & Klionsky, D. J. (2009) · Annual Review of Genetics · doi:10.1146/annurev-genet-102808-114910 · Cited by 3,609
Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
Twig, G., Elorza, A., Molina, A. J. A., Mohamed, H., Wikstrom, J. D., Walzer, G., Stiles, L., Haigh, S. E., Katz, S., Las, G., et al. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601963 · Cited by 3,082
PINK1 Is Selectively Stabilized on Impaired Mitochondria to Activate Parkin
Narendra, D. P., Jin, S. M., Tanaka, A., Suen, D.-F., Gautier, C. A., Shen, J., Cookson, M. R., & Youle, R. J. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000298 · Cited by 2,944
Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development
Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., & Chan, D. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211046 · Cited by 2,601
Mitofusin 2 tethers endoplasmic reticulum to mitochondria
de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442
PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy
Matsuda, N., Sato, S., Shiba, K., Okatsu, K., Saisho, K., Gautier, C. A., Sou, Y.-S., Saiki, S., Kawajiri, S., Sato, F., et al. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200910140 · Cited by 1,969
The Role of Dynamin-Related Protein 1, a Mediator of Mitochondrial Fission, in Apoptosis
Frank, S., Gaume, B., Bergmann-Leitner, E. S., Leitner, W. W., Robert, E. G., Catez, F., Smith, C. L., & Youle, R. J. (2001) · Developmental Cell · doi:10.1016/s1534-5807(01)00055-7 · Cited by 1,755
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
The importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapses
Li, Z., Okamoto, K.-I., Hayashi, Y., & Sheng, M. (2004) · Cell · doi:10.1016/j.cell.2004.11.003 · Cited by 1,498

Flagged first, then by citations

Show all 135 references

Sorted by citations

Items 601–700 of 1,005

Mitochondrial dynamics: biology and therapy in lung cancer
Lennon, F. E., & Salgia, R. (2014) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2014.899350 · Cited by 55
“ensures optimal mitochondrial function and helps maintain mtDNA distribution [30].”
Background
Miro2 Regulates Inter-Mitochondrial Communication in the Heart and Protects Against TAC-Induced Cardiac Dysfunction
Cao, Y., Xu, C., Ye, J., He, Q., Zhang, X., Shi, J. Y., Qiao, X., Zhang, C., Liu, R., Weng, L., et al. (2019) · Circulation Research · doi:10.1161/circresaha.119.315432 · Cited by 55
Paclitaxel inhibits mRNA transport in axons
Bobylev, I., Joshi, A. R., Barham, M., Ritter, C., Neiss, W. F., Höke, A., & Lehmann, H. C. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.07.006 · Cited by 55
Curcumin, a potential therapeutic candidate for retinal diseases
Wang, L., Sun, Y., Huang, K., & Zheng, L. (2013) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201200718 · Cited by 56
“Mitochondrial dynamics, which consist of the constant fusion and dividing processes, are important for the maintenance of normal functions of mitochondria [77].”
Background
Mitochondrial fission determines cisplatin sensitivity in tongue squamous cell carcinoma through the BRCA1-miR-593-5p–MFF axis
Fan, S., Liu, B., Sun, L., Lv, X., Lin, Z., Chen, W., Chen, W., Tang, Q.-L., Wang, Y., Su, Y., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.3659 · Cited by 54
“However, recent evidence has revealed that certain cell types survive MOMP [7, 8].”
Influential
Exclusion of dysfunctional mitochondria from Balbiani body during early oogenesis of Thermobia
Tworzydlo, W., Kisiel, E., Jankowska, W., Witwicka, A., & Biliński, S. M. (2016) · Cell and Tissue Research · doi:10.1007/s00441-016-2414-x · Cited by 54
“…containing deleterious components and exhibiting decreased membrane potential, are eliminated via autophagy, and that the deleterious components can be sorted inside mitochondria (reviewed by Westermann 2010; Youle and van der Bliek 2012; van der Bliek et al. 2013; Hoitzing et al. 2015).”
Ubiquitination of ERMES components by the E3 ligase Rsp5 is involved in mitophagy
Belgareh‐Touzé, N., Cavellini, L., & Cohen, M. M. (2016) · Autophagy · doi:10.1080/15548627.2016.1252889 · Cited by 54
“Mitochondria are double-membrane-bound organelles organized into dynamic tubular networks with a morphology conditioned by the balance between mitochondrial membrane fusion and fission.(1,2) The predominance of one of these events over the other results in hyperfused or highly fragmented mitochondria, with effects on…”
Background
Acrolein induces mtDNA damages, mitochondrial fission and mitophagy in human lung cells
Wang, H., Lin, J.-H., Yang, C.-H., Haung, C.-H., Weng, C.-W., Lin, A. M.-Y., Lo, Y., Chen, W.-S., & Tang, M.-S. (2017) · Oncotarget · doi:10.18632/oncotarget.19710 · Cited by 59
“Mitochondrial dynamics are regulated by the balance of expression levels between mitochondrial fission (Fis1 and Drp1) and fusion (MFN1, MFN2, and OPA1) proteins [47, 51, 52].”
TLR4 Activation Promotes the Progression of Experimental Autoimmune Myocarditis to Dilated Cardiomyopathy by Inducing Mitochondrial Dynamic Imbalance
Wu, B., Li, J., Ni, H., Zhuang, X., Qi, Z., Chen, Q., Wen, Z., Shi, H., Luo, X., & Jin, B. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/3181278 · Cited by 55
“It has been a new focus of researches that mitochondria are highly dynamic organelles and undergo dynamic balance of mitochondrial fusion and fission to maintain normal mitochondrial morphology and function [12].”
Possible Roles of Mitochondrial Dynamics and the Effects of Pharmacological Interventions in Chemoresistant Ovarian Cancer
Kingnate, C., Charoenkwan, K., Kumfu, S., Chattipakorn, N., & Chattipakorn, S. C. (2018) · EBioMedicine · doi:10.1016/j.ebiom.2018.07.026 · Cited by 53
Physiological and pathological functions of sphingolipids in pregnancy
Fakhr, Y., Brindley, D. N., & Hemmings, D. G. (2021) · Cellular Signalling · doi:10.1016/j.cellsig.2021.110041 · Cited by 56
Rescuing mitochondria in traumatic brain injury and intracerebral hemorrhages - A potential therapeutic approach
Ahluwalia, M., Kumar, M., Ahluwalia, P. K., Rahimi, S. Y., Vender, J. R., Raju, R. P., Hess, D. C., Baban, B., Vale, F. Ĺ., Dhandapani, K. M., et al. (2021) · Neurochemistry International · doi:10.1016/j.neuint.2021.105192 · Cited by 55
Selective vulnerability of hippocampal CA1 and CA3 pyramidal cells: What are possible pathomechanisms and should more attention be paid to the CA3 region in future studies?
Einenkel, A., & Salameh, A. (2023) · Journal of Neuroscience Research · doi:10.1002/jnr.25276 · Cited by 56
“Disturbances in fission/fusion homeostasis are associated with neurological pa - thologies (Westermann, 2010 ), with extensive fissions known to be related to mitochondrial depolarization, cytochrome C release, increased radical production, and apoptosis (Anne Stetler et al., 2013; Knott et al.,…”
Background
Mitochondrial network remodeling of the diabetic heart: implications to ischemia related cardiac dysfunction
Rudokas, M. W., McKay, M., Toksoy, Z., Eisen, J. N., Bögner, M., Young, L. H., & Akar, F. G. (2024) · Cardiovascular Diabetology · doi:10.1186/s12933-024-02357-1 · Cited by 55
“Mitochondrial fission serves multiple purposes that are essential to cellular life, including the regulation of mitochondrial inheritance, the removal of damaged organelles, and the release of pro-apoptotic factors [42].”
Background
Mitochondria unite to survive
Blackstone, C. D., & Chang, C. (2011) · Nature Cell Biology · doi:10.1038/ncb0511-521 · Cited by 53
Cyclin C mediates stress-induced mitochondrial fission and apoptosis
Wang, K., Yan, R., Cooper, K. F., & Strich, R. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-08-1315 · Cited by 55
“Mitochondria are dynamic organelles that undergo fusion and fission cycles that are controlled by conserved molecular machines consisting of dynamin-like GTPases (for review, see Westermann, 2010b).”
Background
Impairment of Mitochondrial Biogenesis and Dynamics Involved in Isoniazid-Induced Apoptosis of HepG2 Cells Was Alleviated by p38 MAPK Pathway
Zhang, T., Ikejima, T., Li, L., Wu, R., Yuan, X., Zhao, J., Wang, Y., & Peng, S. (2017) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00753 · Cited by 53
“Because mitochondrial quality control involved rescue of damage by fusion and elimination of damage by fission (Westermann, 2010; Youle and van der Bliek, 2012; van der Bliek et al., 2013), it was possible that INH introduced mitochondrial toxicity beyond a certain threshold so that rescue of…”
BackgroundInfluential
Impaired mitochondrial dynamics underlie axonal defects in hereditary spastic paraplegias
Denton, K. R., Mou, Y., Xu, C., Shah, D., Chang, J., Blackstone, C. D., & Li, X.-J. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy156 · Cited by 53
Thyroid hormone regulation of neural stem cell fate: From development to ageing
Gothié, J. M., Vancamp, P., DEMENEIX, B. A., & Remaud, S. (2019) · Acta Physiologica · doi:10.1111/apha.13316 · Cited by 54
STIM1 is a core trigger of airway smooth muscle remodeling and hyperresponsiveness in asthma
Johnson, M. T., Xin, P., Benson, J. C., Pathak, T., Walter, V., Emrich, S. M., Yoast, R. E., Zhang, X., Cao, G., Panettieri, R. A., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2114557118 · Cited by 53
“In further support of this finding, the protein expression of mitofusin 2 (MFN2) and OPA1, which are two GTPases important for outer and inner mitochondrial membrane fusion, respectively (70), were significantly increased in shSTIM1#1 and shSTIM1#5 KD HASMCs compared to shScramble HASMCs (Fig.”
Result
The systems biology of mitochondrial fission and fusion and implications for disease and aging
Chauhan, A., Vera, J., & Wolkenhauer, O. (2014) · Biogerontology · doi:10.1007/s10522-013-9474-z · Cited by 52
“ATP consuming process (Westermann 2010).”
BackgroundInfluential
The multifaceted roles of mitochondria at the crossroads of cell life and death in cancer
Fontana, F., & Limonta, P. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.09.024 · Cited by 53
“There is now substantial evidence that fission is strictly associated with mitophagy, the process responsible for the removal of damaged mitochondria [165,166], and with the intrinsic apoptosis pathway, through an increased release of cytochome c form the mitochondria [167].”
Background
Peroxiredoxin 3 has a crucial role in the contractile function of skeletal muscle by regulating mitochondrial homeostasis
Lee, K., Shin, Y. J., Cho, S. C., Lee, S.-M., Bahn, Y. J., Kim, J. Y., Kwon, E., Jeong, D. Y., Park, S. C., Rhee, S. G., et al. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.09.010 · Cited by 52
A role for Mfb1p in region-specific anchorage of high-functioning mitochondria and lifespan in Saccharomyces cerevisiae
Pernice, W. M., Vevea, J., & Pon, L. A. (2016) · Nature Communications · doi:10.1038/ncomms10595 · Cited by 54
Adiponectin is required for maintaining normal body temperature in a cold environment
Wei, Q., Lee, J. H., Wang, H., Bongmba, O. Y. N., Wu, C., Pradhan, G., Sun, Z., Chew, L. A., Bajaj, M., Chan, L., et al. (2017) · BMC Physiology · doi:10.1186/s12899-017-0034-7 · Cited by 52
“Mitochondrial dynamics consist of the processes of the ‘joining event’ of fusion and the ‘dividing event’ of fission; the balance between fusion and fission is essential for the maintenance of normal mitochondrial function [44].”
Background
Vitamin D Attenuates Ischemia/Reperfusion-Induced Cardiac Injury by Reducing Mitochondrial Fission and Mitophagy
Lee, T.-L., Lee, M., Chen, Y., Lee, Y., Lai, T.-C., Lin, H. Y., Hsu, L., Sung, H., Lee, C., & Chen, Y. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.604700 · Cited by 53
“To further investigate how Vit D regulates mitochondrial fission, p-Drp1 and Mff, two regulatory proteins associated with mitochondrial fission, were examined.”
BackgroundInfluential
Noncanonical PDK4 action alters mitochondrial dynamics to affect the cellular respiratory status
Thoudam, T., Chanda, D., Sinam, I. S., Kim, B., Kim, M.-J., Oh, C. J., Lee, J. Y., Kim, M., Park, S. Y., Lee, S. Y., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2120157119 · Cited by 53
“Conversely, unopposed fusion results in a hyperfused mitochondrial network, counteracts metabolic insults to preserve cellular integrity and function, and protect against mitophagy (7, 8).”
Background
Unlocking the Mitochondria for Nanomedicine-based Treatments: Overcoming Biological Barriers, Improving Designs, and Selecting Verification Techniques
Pegoraro, C., Domingo-Ortí, I., Conejos‐Sánchez, I., & Vicent, M. J. (2024) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2024.115195 · Cited by 56
Coupling mitochondrial and cell division
Yamano, K., & Youle, R. J. (2011) · Nature Cell Biology · doi:10.1038/ncb2334 · Cited by 56
Standardized mitochondrial analysis gives new insights into mitochondrial dynamics and OPA1 function
Chevrollier, A., Cassereau, J., Ferré, M., Alban, J., Desquiret‐Dumas, V., Guéguen, N., Amati‐Bonneau, P., Procaccio, V., Bonneau, D., & Reynier, P. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.03.006 · Cited by 59
Drp‐1 , a potential therapeutic target for brain ischaemic stroke
Zuo, W., Yang, P., Chen, J., Zhang, Z., & Chen, N. H. (2016) · British Journal of Pharmacology · doi:10.1111/bph.13468 · Cited by 52
“These observations were in accordance with the opinion that Drp-1 has a role after translocating to the outer membrane of mitochondria (Westermann, 2010).”
Result
Mitochondria in Chronic Obstructive Pulmonary Disease and Lung Cancer: Where are We Now?
Nam, H.-S., Izumchenko, E., Dasgupta, S., & Hoque, M. O. (2017) · Biomarkers in Medicine · doi:10.2217/bmm-2016-0373 · Cited by 52
Anhydrobiosis: Inside yeast cells
Rapoport, A. I., Golovina, E. A., Gervais, P., Dupont, S., & Beney, L. (2018) · Biotechnology Advances · doi:10.1016/j.biotechadv.2018.11.003 · Cited by 53
Myotonic Dystrophy type 1 cells display impaired metabolism and mitochondrial dysfunction that are reversed by metformin
García-Puga, M., Saenz‐Antoñanzas, A., Fernández‐Torrón, R., de Munaín, A. L., & Matheu, A. (2020) · Aging · doi:10.18632/aging.103022 · Cited by 55
“machinery of pro-fusion and -fission proteins, which constitutes an important part of the mitochondria quality control as it facilitates the elimination of damaged mitochondria by mitochondrial selective autophagy (mitophagy) [19].”
Background
Let’s Get Physical: Flavivirus-Host Protein–Protein Interactions in Replication and Pathogenesis
Fishburn, A. T., Pham, O., Kenaston, M. W., Beesabathuni, N. S., & Shah, P. S. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.847588 · Cited by 53
“Fission is mediated by dynamin-related protein 1 (DRP1), which is soluble and recruited to mitochondria by mitochondrial fission protein 1 (FIS1; Westermann, 2010).”
Background
Mitochondrial Division Inhibitor 1 Ameliorates Mitochondrial Injury, Apoptosis, and Motor Dysfunction After Acute Spinal Cord Injury in Rats
Li, G., Jia, Z., Cao, Y., Wang, Y., Li, H., Zhang, Z.-Y., Bi, J., Lv, G., & Fan, Z. (2015) · Neurochemical Research · doi:10.1007/s11064-015-1604-3 · Cited by 50
Evidence to support mitochondrial neuroprotection, in severe traumatic brain injury
Gajavelli, S., Sinha, V. K., Mazzeo, A. T., Spurlock, M. S., Lee, S. W., Ahmed, A. I., Yokobori, S., & Bullock, R. M. (2014) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-014-9589-1 · Cited by 51
Lysosomal Proteolysis Is Associated With Exercise-Induced Improvement of Mitochondrial Quality Control in Aged Hippocampus
Luo, L., Dai, J.-R., Guo, S., Lu, A.-M., Gao, X., Gu, Y., Zhang, X., Xu, H., Wang, Y., Zhu, Z., et al. (2017) · The Journals of Gerontology Series A · doi:10.1093/gerona/glw242 · Cited by 52
Nonalcoholic steatohepatitis severity is defined by a failure in compensatory antioxidant capacity in the setting of mitochondrial dysfunction
Boland, M. L., Oldham, S. N., Boland, B. B., Will, S., Lapointe, J., Guionaud, S., Rhodes, C. J., & Trevaskis, J. L. (2018) · World Journal of Gastroenterology · doi:10.3748/wjg.v24.i16.1748 · Cited by 50
Mitochondrial presequence import: Multiple regulatory knobs fine-tune mitochondrial biogenesis and homeostasis.
Moulin, C., Caumont-Sarcos, A., & Ieva, R. (2019) · Biochimica et biophysica acta. Molecular cell research · doi:10.1016/j.bbamcr.2019.02.012 · Cited by 47
Mitophagy in the Retinal Pigment Epithelium of Dry Age-Related Macular Degeneration Investigated in the NFE2L2/PGC-1α-/- Mouse Model
Gurubaran, I. S., Viiri, J., Koskela, A. K. J., Hyttinen, J. M. T., Paterno, J. J., Kis, G. N., Antal, M., Urtti, A. O., Kauppinen, A., Felszeghy, S., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21061976 · Cited by 52
“Mitochondria undergo constant fission and fusion in order to meet the demands of the cells [46].”
Background
Role of Mitofusins and Mitophagy in Life or Death Decisions
Joaquim, M., & Escobar‐Henriques, M. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.572182 · Cited by 50
“…thanks to its expanding roles in tailored metabolic performance, in quality control responses, but also in inflammatory processes and in cell death (Westermann, 2010; Nunnari and Suomalainen, 2012; Xiong et al., 2014; Angajala et al., 2018; Pickles et al., 2018; Spinelli and Haigis, 2018; Figure…”
Background
The structure and function of deubiquitinases: lessons from budding yeast
Suresh, H. G., Pascoe, N., & Andrews, B. (2020) · Open Biology · doi:10.1098/rsob.200279 · Cited by 53
“guanosine triphosphate (GTP)-binding promotes Fzo1 homodimerization and further oligomerization occurs upon tethering of two mitochondria [127].”
Background
Ergosterol reduction impairs mitochondrial DNA maintenance in S. cerevisiae
Cirigliano, A., Macone, A., Bianchi, M. M., Oliaro‐Bosso, S., Balliano, G., Negri, R., & Rinaldi, T. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2018.12.002 · Cited by 48
“The involvement of ergosterol in maintaining mitochondrial morphology and mitochondrial DNA is of extreme biological significance also because the fragmentation of mitochondrial structure and instability of mtDNA are strictly related to human diseases and apoptosis [90-93].”
Background
Neurotoxicity mechanisms of manganese in the central nervous system
Pajarillo, E. A. B., Nyarko‐Danquah, I., Adinew, G. M., Rizor, A., Aschner, M., & Lee, E.-S. (2021) · Advances in neurotoxicology · doi:10.1016/bs.ant.2020.11.003 · Cited by 54
“Mitochondrial fusion is a well-coordinated and synchronized process of combining adjacent mitochondrion and its components (Westermann, 2010).”
Background
Sulforaphane Attenuates Gentamicin-Induced Nephrotoxicity: Role of Mitochondrial Protection
Negrette-Guzmán, M., Huerta‐Yépez, S., Medina‐Campos, O. N., Zatarain-Barrón, Z. L., Hernández‐Pando, R., Torres, I., Tapia, E., & Pedraza‐Chaverrí, J. (2013) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2013/135314 · Cited by 49
“It has been reported that SFN also induces apoptosis by mitochondrial-dependent pathways in some cancer cell lines, inducing loss ofMMP and activating caspase-9, at concentrations ranging frommoderate (6 𝜇M) to high (25 𝜇M) [39, 40].”
BackgroundInfluential
Noninvasive assessment of mitochondrial organization in three-dimensional tissues reveals changes associated with cancer development
Xylas, J. F., Varone, A., Quinn, K. P., Pouli, D., McLaughlin-Drubin, M. E., Thieu, H.-T. N., Garcia-Moliner, M., House, M. D., Hunter, M., Münger, K., et al. (2014) · International Journal of Cancer · doi:10.1002/ijc.28992 · Cited by 46
“Mitochondria are typically organized as tubular networks that have the ability to change dynamically through fusion and fission.(7,8) The factors that affect mitochondrial organization and their impact on cell function are diverse and not thoroughly understood.”
Background
Altered Mitochondrial Respiration and Other Features of Mitochondrial Function inParkin-Mutant Fibroblasts from Parkinson’s Disease Patients
Haylett, W. L., Swart, C., van der Westhuizen, F. H., Dyk, H. C. V., van der Merwe, L., van der Merwe, C., Loos, B., Carr, J. A., Kinnear, C. J., & Bardien, S. (2016) · Parkinson s Disease · doi:10.1155/2016/1819209 · Cited by 49
“These processes finetune the mitochondrial network in response to changes in the metabolic environment, in order to maintain favorable mitochondrial function duringmetabolic perturbations [20].”
Background
Inhibition of mitochondrial fusion is an early and critical event in breast cancer cell apoptosis by dietary chemopreventative benzyl isothiocyanate
Sehrawat, A., Croix, C. M. S., Baty, C. J., Watkins, S. C., Tailor, D., Singh, R. P., & Singh, S. V. (2016) · Mitochondrion · doi:10.1016/j.mito.2016.06.006 · Cited by 50
“BITC treatment inhibited PEG-induced mitochondrial fusion Mitochondrial fragmentation during apoptosis may be the result of increased fission and/or decreased fusion (Suen et al., 2008; Westermann, 2010; van der Bliek et al., 2013).”
Sonic hedgehog pathway activation increases mitochondrial abundance and activity in hippocampal neurons
Yao, P. J., Manor, U., Petralia, R. S., Brose, R. D., Wu, R. T. Y., Ott, C. M., Wang, Y., Charnoff, A., Lippincott‐Schwartz, J., & Mattson, M. P. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-07-0553 · Cited by 49
“Because Drp1 is recruited to fission sites on the mitochondrial surface (Scott and Youle, 2010; Westermann, 2010), we purified mitochondria from the ShhN-treated neurons and the untreated control neurons and examined Drp1 associated with mitochondria.”
Background
Agent-Based Modeling of Mitochondria Links Sub-Cellular Dynamics to Cellular Homeostasis and Heterogeneity
Dalmasso, G., Zapata, P. A. M., Brady, N. R., & Hamacher‐Brady, A. (2017) · PLoS ONE · doi:10.1371/journal.pone.0168198 · Cited by 47
Mitochondrial functions and melatonin: a tour of the reproductive cancers
Chuffa, L. G. D. A., Seiva, F. R. F., Cucielo, M. S., Silveira, H. S., Reiter, R. J., & Lupi, L. A. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2963-0 · Cited by 52
Abnormal Mitochondria in a Non-human Primate Model of MPTP-induced Parkinson's Disease: Drp1 and CDK5/p25 Signaling
Park, J., Seo, J., Won, J., Yeo, H.-G., Ahn, Y.-J., Kim, K., Jin, Y. B., Koo, B., Lim, K. S., Jeong, K.-J., et al. (2019) · Experimental Neurobiology · doi:10.5607/en.2019.28.3.414 · Cited by 48
Structural insights into G domain dimerization and pathogenic mutation of OPA1
Yu, C., Zhao, J., Yan, L., Qi, Y., Guo, X., Lou, Z., Hu, J., & Rao, Z. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.201907098 · Cited by 49
“Mitochondria are double membrane – bound organelles that frequently fuse and divide (Westermann, 2010).”
Dihydromyricetin attenuates heat stress-induced apoptosis in dairy cow mammary epithelial cells through suppressing mitochondrial dysfunction
Wang, H., Xing, G., Qian, Y., Sun, X.-F., Zhong, J., & Chen, K.-L. (2021) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2021.112078 · Cited by 47
Metabolic targeting of breast cancer cells with the 2-deoxy-D-glucose and the mitochondrial bioenergetics inhibitor MDIVI-1
Lucantoni, F., Dussmann, H., & Prehn, J. H. M. (2018) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2018.00113 · Cited by 47
“The highly mitochondrial plasticity is regulated by enzymatic processes (Westermann, 2010).”
Background
DsbA-L deficiency exacerbates mitochondrial dysfunction of tubular cells in diabetic kidney disease
Gao, P., Yang, M., Chen, X., Xiong, S., Liu, J., & Sun, L. (2020) · Clinical Science · doi:10.1042/cs20200005 · Cited by 48
Mitochondria: the gatekeepers between metabolism and immunity
Trinchese, G., Cimmino, F., Catapano, A., Cavaliere, G., & Mollica, M. P. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1334006 · Cited by 57
From dysfunction to healing: advances in mitochondrial therapy for Osteoarthritis
Zhang, M., Wu, J., Cai, K., Liu, Y., Lu, B., Zhang, J., Xu, J., Gu, C., & Chen, T. (2024) · Journal of Translational Medicine · doi:10.1186/s12967-024-05799-z · Cited by 51
Death-associated Protein 3 Regulates Mitochondrial-encoded Protein Synthesis and Mitochondrial Dynamics
Xiao, L., Xian, H., Lee, K. Y., Xiao, B., Wang, H., Yu, F., Shen, H., & Liou, Y. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.673343 · Cited by 46
“Mitochondrial dynamics refers to the opposing fusion and fission processes that enable cells to respond and adapt to their ever changing physiological conditions (1, 2).”
Background
Mitofusin-Dependent ER Stress Triggers Glial Dysfunction and Nervous System Degeneration in a Drosophila Model of Friedreich’s Ataxia
Edenharter, O., Schneuwly, S., & Navarro, J. A. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00038 · Cited by 44
“Accumulation of Drosophila p62 in Frataxin-Deficient Glial Cells Marf has been extensively described as a mediator of mitochondrial fusion in mammals as well as in Drosophila (Westermann, 2010; Corti et al., 2011) and it has been reported to be a substrate of the ubiquitin ligase Parkin in the mitophagy process (Palla…”
Background
Imaging Mitochondrial Functions: From Fluorescent Dyes to Genetically-Encoded Sensors
Gökerküçük, E. B., Tramier, M., & Bertolin, G. (2020) · Genes · doi:10.3390/genes11020125 · Cited by 47
“These events are the interconnection of the organelles or the fragmentation of them into smaller units, respectively [103].”
Background
The relevance of mitochondrial morphology for human disease
Navaratnarajah, T., Anand, R., Reichert, A. S., & Distelmaier, F. (2021) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2021.105951 · Cited by 49
Altered Mitochondrial Quality Control in Rats with Metabolic Dysfunction-Associated Fatty Liver Disease (MAFLD) Induced by High-Fat Feeding
Cioffi, F., Giacco, A., Petito, G., Matteis, R. D., Senese, R., Lombardi, A., de Lange, P., Moreno, M., Goglia, F., Lanni, A., et al. (2022) · Genes · doi:10.3390/genes13020315 · Cited by 49
Mitochondrial hyperfusion via metabolic sensing of regulatory amino acids
Abdullah, M. O., Zeng, R. X., Margerum, C. L., Papadopoli, D. J., Monnin, C., Punter, K. B., Chu, C., Al-Rofaidi, M., Al‐Tannak, N. F., Berardi, D., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111198 · Cited by 46
“Mitochondria display remarkably dynamic membrane remodeling that reflects their origin as autonomous bacteria (Dyall et al., 2004; Westermann, 2010).”
Background
FBXL4 protects against HFpEF through Drp1-Mediated regulation of mitochondrial dynamics and the downstream SERCA2a
Abudureyimu, M., Luo, X., Jiang, L., Jin, X., Pan, C., Yu, W., Ge, J., Zhang, Y., & Ren, J. T. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103081 · Cited by 47
“Fis1 assemblies fission apparatus resulting in mitochondrial membrane constrictions and division [57].”
Background
SARS-CoV-2 aberrantly elevates mitochondrial bioenergetics to induce robust virus propagation
Shin, H. J., Lee, W., Ku, K. B., Yoon, G. Y., Moon, H.-W., Kim, C., Kim, M.-H., Yi, Y.-S., Jun, S., Kim, B., et al. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01836-x · Cited by 52
“20 Mitochondrial fusion involves mitofusins (MFN1 and 2) and optic atrophy 1 (OPA1).”
Background
Oxidative stress-mediated protein sulfenylation in human diseases: Past, present, and future
Mu, B., Zeng, Y., Luo, L., & Wang, K. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103332 · Cited by 49
“Notably, dynamin-related protein 1 (Drp1) can be recruited to the outer mitochondrial membrane for mitochondrial contraction and division [138,139].”
Background
Mitochondrial Therapeutics for Cardioprotection
Carreira, R., Lee, P. P. W., & Gottlieb, R. A. (2011) · Current Pharmaceutical Design · doi:10.2174/138161211796904777 · Cited by 48
“Inner mitochondrial membrane fusion is directed by OPA1 (for review see [20]).”
Background
Piscidin-1 Induces Apoptosis via Mitochondrial Reactive Oxygen Species-Regulated Mitochondrial Dysfunction in Human Osteosarcoma Cells
Cheng, M., Pan, C., Chen, N., Yang, S., Hsieh, S., Wen, Z., Chen, W.-F., Wang, J., Lu, W.-H., & Kuo, H. (2020) · Scientific Reports · doi:10.1038/s41598-020-61876-5 · Cited by 47
Modulation of mitochondria and NADPH oxidase function by the nitrate-nitrite-NO pathway in metabolic disease with focus on type 2 diabetes
Schiffer, T. A., Lundberg, J. O., Weitzberg, E., & Carlström, M. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.165811 · Cited by 49
Miro (Mitochondrial Rho GTPase), a key player of mitochondrial axonal transport and mitochondrial dynamics in neurodegenerative diseases
Panchal, K., & Tiwari, A. K. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.10.005 · Cited by 49
The Combination of Paraformaldehyde and Glutaraldehyde Is a Potential Fixative for Mitochondria
Qin, Y. H., Jiang, W., Li, A., Gao, M., Liu, H., Gao, Y., Tian, X., & Gong, G. (2021) · Biomolecules · doi:10.3390/biom11050711 · Cited by 47
Overexpression of miR-124 in Motor Neurons Plays a Key Role in ALS Pathological Processes
Vaz, A. R., Vizinha, D., Morais, H. M. M., Colaço, A. R. A., Loch-Neckel, G., Barbosa, M., & Brites, D. M. T. O. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22116128 · Cited by 48
“mSOD1 MNs), therefore sustaining cellular quality control and cell bioenergetics efficiency [41,42].”
Background
Streptozotocin Induces Alzheimer’s Disease-Like Pathology in Hippocampal Neuronal Cells via CDK5/Drp1-Mediated Mitochondrial Fragmentation
Park, J., Won, J., Seo, J., Yeo, H.-G., Kim, K., Kim, Y. G., Jeon, C., Kam, M. K., Kim, Y., Huh, J., et al. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00235 · Cited by 45
“Mitochondrial fusion is regulated by optic atrophy 1 (Opa1), mitofusin 1 (Mfn1), and mitofusin 2 (Mfn2), and mitochondrial fission is regulated by dynamin-1-like protein (Drp1) and mitochondrial fission 1 (Fis1; Knott et al., 2008; Cho et al., 2010; Westermann, 2010).”
Background
ROS-mediated cytoplasmic localization of CARM1 induces mitochondrial fission through DRP1 methylation
Cho, Y., & Kim, Y. K. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103212 · Cited by 48
“Intricate processes, such as biogenesis, fission, fusion, and mitophagy, operate in a tightly coordinated manner to maintain an optimal mitochondrial network that supports the overall cellular health and functionality [3,4].”
Background
From mitochondrial dysfunction to neuroinflammation in Parkinson’s disease: Pathogenesis and mitochondrial therapeutic approaches
Ebadpour, N., Mahmoudi, M., Kheder, R. K., Abavisani, M., Baridjavadi, Z., Abdollahi, N., & Esmaeili, S. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.113015 · Cited by 48
Beta-nodavirus B2 protein induces hydrogen peroxide production, leading to Drp1-recruited mitochondrial fragmentation and cell death via mitochondrial targeting
Su, Y., Chiu, H. W., Hung, J.-C., & Hong, J. (2014) · APOPTOSIS · doi:10.1007/s10495-014-1016-x · Cited by 47
Reactive oxygen species effect PASMCs apoptosis via regulation of dynamin-related protein 1 in hypoxic pulmonary hypertension
Zhang, L., Ma, C., Zhang, C., Ma, M., Zhang, F., Zhang, L., Chen, Y., Cao, F., Li, S., & Zhu, D. (2016) · Histochemistry and Cell Biology · doi:10.1007/s00418-016-1424-9 · Cited by 46
Functionally identifiable apoptosis-insensitive subpopulations determine chemoresistance in acute myeloid leukemia
Bhola, P. D., Mar, B. G., Lindsley, R. C., Ryan, J. A., Hogdal, L. J., Vo, T. T., DeAngelo, D. J., Galinsky, I. A., Ebert, B. L., & Letai, A. G. (2016) · Journal of Clinical Investigation · doi:10.1172/jci82908 · Cited by 46
“Alternatively, the age of individual mitochondria (32) or subcellular localization of mitochondria (33) may affect priming heterogeneity.”
Background
Unraveling the causes of sarcopenia: Roles of neuromuscular junction impairment and mitochondrial dysfunction
Miao, Y., Xie, L., Song, J., Cai, X., Yang, J., Ma, X., Chen, S., & Xie, P. (2024) · Physiological Reports · doi:10.14814/phy2.15917 · Cited by 50
“Mitochondria are highly dynamic organelles with the capacity to modify their function through various mechanisms, including changes in mitochondrial DNA (mtDNA), fusion or fission (Westermann, 2010), and auto-phagy.”
Background
Precise control of microtubule disassembly in living cells
Liu, G. Y., Chen, S., Lee, G., Shaiv, K., Chen, P., Cheng, H., Hong, S., Yang, W., Huang, S., Chang, Y., et al. (2022) · The EMBO Journal · doi:10.15252/embj.2021110472 · Cited by 42
“The balance of fusion and fission is critical for the morphology and activities of mitochondria (Westermann, 2010).”
Understanding the neuronal synapse and challenges associated with the mitochondrial dysfunction in mild cognitive impairment and Alzheimer’s disease
Verma, H., Gangwar, P., Yadav, A., Yadav, B., Rao, R., Kaur, S., Kumar, P., Dhiman, M., Taglialatela, G., & Mantha, A. K. (2023) · Mitochondrion · doi:10.1016/j.mito.2023.09.003 · Cited by 46
Programmed Cell Death Initiation and Execution in Budding Yeast
Strich, R. (2015) · Genetics · doi:10.1534/genetics.115.179150 · Cited by 46
“The equilibrium between fission and fusion is controlled by the activity of conserved molecular machines driven by dynamin-like GTPases (see Westermann 2010 for review).”
Background
Liver-specific deletion of RORα aggravates diet-induced nonalcoholic steatohepatitis by inducing mitochondrial dysfunction
Kim, H., Han, Y., Na, H., Kim, J., Kim, T.-W., Kim, H., Shin, C., Lee, S. E., & Lee, M. (2017) · Scientific Reports · doi:10.1038/s41598-017-16077-y · Cited by 45
Peroxiredoxin 5 prevents iron overload-induced neuronal death by inhibiting mitochondrial fragmentation and endoplasmic reticulum stress in mouse hippocampal HT-22 cells
Lee, D. G., Kam, M. K., Kim, K., Kim, H. S., Kwon, O., Lee, H., & Lee, D.-S. (2018) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2018.06.005 · Cited by 46
Inhibition of DNM1L and mitochondrial fission attenuates inflammatory response in fibroblast‐like synoviocytes of rheumatoid arthritis
Wang, X., Chen, Z., Fan, X., Li, W., Qu, J., Dong, C., Wang, Z., Zhen-wei, J., & Li, Y. (2019) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14837 · Cited by 47
Increased long noncoding RNA maternally expressed gene 3 contributes to podocyte injury induced by high glucose through regulation of mitochondrial fission
Deng, Q., Wen, R., Liu, S., Chen, X., Song, S., Li, X., Su, Z., & Wang, C. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-03022-7 · Cited by 45
Mitochondrial Fission Factor (MFF) Inhibits Mitochondrial Metabolism and Reduces Breast Cancer Stem Cell (CSC) Activity
Sánchez‐Alvarez, R., Francesco, E. M. D., Fiorillo, M., Sotgia, F., & Lisanti, M. P. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.01776 · Cited by 50
“As such, it’s not surprising that alterations in fusion/fission balance may play a key role in the pathogenesis of several diseases, including cancer (16, 25).”
Background
Rapamycin Ameliorates Defects in Mitochondrial Fission and Mitophagy in Glioblastoma Cells
Lenzi, P., Ferese, R., Biagioni, F., Fulceri, F., Busceti, C. L., Falleni, A., Gambardella, S., Frati, A., & Fornai, F. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22105379 · Cited by 46
Mitochondrial fusion and fission are required for proper mitochondrial function and cell proliferation in fission yeast
Dong, F., Zhu, M., Zheng, F., & Fu, C. (2021) · FEBS Journal · doi:10.1111/febs.16138 · Cited by 45
Slt2p phosphorylation induces cyclin C nuclear-to-cytoplasmic translocation in response to oxidative stress
Jin, C., Strich, R., & Cooper, K. F. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-09-0550 · Cited by 45
“We determined the percentage of cells that displayed short tubules (indicative of mitochondrial fission; Westermann , 2010; Youle and van der Bliek, 2012) versus the branched reticular networks observed under normal growing conditions (example given in Figure 4A).”
Mitochondrial Dynamics at Different Levels: From Cristae Dynamics to Interorganellar Cross Talk
Kondadi, A. K., & Reichert, A. S. (2024) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-030822-020736 · Cited by 46
Role of Mitochondrial Dysfunctions in Neurodegenerative Disorders: Advances in Mitochondrial Biology
Kathiresan, D. S., Balasubramani, R., Marudhachalam, K., Jaiswal, P., Ramesh, N., Suruthi, G. S., Moorthi, P. V., & Vijayan, M. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04469-x · Cited by 49
“…cellular proliferation, cell differentiation, ATP production, the citric acid cycle, fatty acid oxidation, innate immunity, iron-sulfur (Fe-S) cluster production, generation and maintenance of reactive oxygen species (ROS), redox signaling, calcium homeostasis, apoptosis, and autophagy [50, 70–77].”
Human mitochondrial Fis1 links to cell cycle regulators at G2/M transition
Lee, S.-M., Park, Y., Kim, S., Nguyen, T. K. O., Yoo, Y., Chan, G. K. T., Sun, X., & Cho, H. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1428-8 · Cited by 46
“Mitochondria are multifunctional organelles that play critical roles in many cellular processes, including energy production, metabolism, apoptosis, and senescence [1, 2].”
Background
Ca2+ and cAMP cross‐talk in mitochondria
Benedetto, G. D., Pendin, D., Greotti, E., Pizzo, P., & Pozzan, T. (2013) · The Journal of Physiology · doi:10.1113/jphysiol.2013.259135 · Cited by 45
“…other roles of Ca2+ in mitochondrial functions, such as regulation of organelle shape and movement (MacAskill & Kittler, 2010), fission/fusion (Westermann, 2010) and autophagy (Cardenas & Foskett, 2012). cAMP signalling In eukaryotes, cAMP is involved in processes as diverse as hormone signal…”
Background
The music of lipids: How lipid composition orchestrates cellular behaviour
Schug, Z. T., Frezza, C., Galbraith, L. C. A., & Gottlieb, E. (2012) · Acta Oncologica · doi:10.3109/0284186x.2011.643823 · Cited by 47
Mediators of mitophagy that regulate mitochondrial quality control play crucial role in diverse pathophysiology
De, R., Mazumder, S., & Bandyopadhyay, U. (2020) · Cell Biology and Toxicology · doi:10.1007/s10565-020-09561-1 · Cited by 47
“While mitofusin 1 (MFN1) and mitofusin 2 (MFN2) mediate outer mitochondrial membrane (OMM) fusion, optic atrophy 1 (OPA1) facilitates inner mitochondrial membrane (IMM) fusion (Westermann 2010).”
Background
MIEF2 over-expression promotes tumor growth and metastasis through reprogramming of glucose metabolism in ovarian cancer
Zhao, S., Zhang, X., Shi, Y., Lu, C., Song, T., Wu, B., Li, J., & Yang, H. (2020) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-020-01802-9 · Cited by 43
Biomarkers of non-communicable chronic disease: an update on contemporary methods
Al‐Hadlaq, S. M., Balto, H. A. G., Hassan, W. M., Marraiki, N., & El-Ansary, A. K. (2022) · PeerJ · doi:10.7717/peerj.12977 · Cited by 54
“These interactions change mitochondrial morphology and consecutively modulate the organelles’ function (Westermann, 2010).”
Background

Authors: Westermann, B.
Affiliations: University of Bayreuth (DE)
Corresponding author: Westermann, Benedikt
ORCID: Westermann, Benedikt
Venue: Nature Reviews Molecular Cell Biology
Publisher: Springer Science and Business Media LLC
Published: 2010-11-23
Volume: 11
Issue: 12
Pages: 872-884
ISSN: 1471-0072 (ISSN-L)
1471-0080
DOI: 10.1038/nrm3013
OpenAlex: W2032234589
Cited by: 2,002
References: 135
Citations by year: 2026: 91 · 2025: 109 · 2024: 158 · 2023: 135 · 2022: 134 · 2021: 192 · 2020: 184 · 2019: 125 · 2018: 113 · 2017: 141 · 2016: 117 · 2015: 119 · 2014: 107 · 2013: 95 · 2012: 118
FWCI: 7.67
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Reviews Molecular Cell Biology (publishedVersion)
PubMed (publishedVersion)
ERef Bayreuth (University of Bayreuth) (submittedVersion)
Funders: Deutsche Forschungsgemeinschaft
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 inheritance, mitochondrial quality control, mitochondrial bioenergetics, neurodegenerative diseases
MeSH terms: Animals, Humans, Membrane Fusion, Mitochondria, Models, Biological, Cell Death, Cytokinesis, Cell Proliferation, Genes, Mitochondrial, Mitochondrial Membranes

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

Mitochondrial fusion and fission in cell life and death

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks