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Impaired Balance of Mitochondrial Fission and Fusion in Alzheimer's Disease
Open accessAbstract
Mitochondrial dysfunction is a prominent feature of Alzheimer's disease (AD) neurons. In this study, we explored the involvement of an abnormal mitochondrial dynamics by investigating the changes in the expression of mitochondrial fission and fusion proteins in AD brain and the potential cause and consequence of these changes in neuronal cells. We found that mitochondria were redistributed away from axons in the pyramidal neurons of AD brain. Immunoblot analysis revealed that levels of DLP1 (also referred to as Drp1), OPA1, Mfn1, and Mfn2 were significantly reduced whereas levels of Fis1 were significantly increased in AD. Despite their differential effects on mitochondrial morphology, manipulations of these mitochondrial fission and fusion proteins in neuronal cells to mimic their expressional changes in AD caused a similar abnormal mitochondrial distribution pattern, such that mitochondrial density was reduced in the cell periphery of M17 cells or neuronal process of primary neurons and correlated with reduced spine density in the neurite. Interestingly, oligomeric amyloid-beta-derived diffusible ligands (ADDLs) caused mitochondrial fragmentation and reduced mitochondrial density in neuronal processes. More importantly, ADDL-induced synaptic change (i.e., loss of dendritic spine and postsynaptic density protein 95 puncta) correlated with abnormal mitochondrial distribution. DLP1 overexpression, likely through repopulation of neuronal processes with mitochondria, prevented ADDL-induced synaptic loss, suggesting that abnormal mitochondrial dynamics plays an important role in ADDL-induced synaptic abnormalities. Based on these findings, we suggest that an altered balance in mitochondrial fission and fusion is likely an important mechanism leading to mitochondrial and neuronal dysfunction in AD brain.
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“Increased accumulation of APP and its processed peptides in the mitochondria of AD neurons and their effects on mitochondrial dynamics and mitophagy have been documented (21–24).”
From Alzheimer's Disease–Associated Amyloid-β Precursor Protein Prevents Aging Stress–Induced Mitophagy and Fumarate Depletion to Improve Antitumor Immunity (2025) · cites this paper as [24]
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In the citing paper
“Mitochondrial fission-fusion dynamics through alterations of Drp1, Parkin, and Pink1 functions (23,24), which play essential roles in mitophagy induction and mitochondrial quality control during healthy brain aging, are disrupted in various neurodegenerative diseases, including Parkinson’s disease (PD) and AD (25).”
From Alzheimer's Disease–Associated Amyloid-β Precursor Protein Prevents Aging Stress–Induced Mitophagy and Fumarate Depletion to Improve Antitumor Immunity (2025) · cites this paper as [24]
In the citing paper
“Aβ accumulates in mitochondria in AD brain, which is accompanied by altered mitochondrial structure, decreased mitochondrial respiratory function and ATP production, impaired mitochondrial dynamics, and elevated mitochondria-associated oxidative stress.”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [97]
In the citing paper
“Mitochondrial Aβ levels correlate with abnormalities in mitochondrial structure and function.”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [97]
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“Aβ peptides can induce ROS production from mitochondria, leading to release of cytochrome c and apoptosis-inducing factor, thereby driving mitochondrial dysfunction, cell apoptosis and neuronal loss [97, 100].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [97]
In the citing paper
“Soluble Aβ oligomers disrupted the balance between mitochondrial fission and fusion, leading to significant mitochondrial dysfunction.197,198”
From Amyloid β-based therapy for Alzheimer’s disease: Challenges, successes and future (2023) · cites this paper as [197]
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Cites
Terry, R. D., Masliah, E., Salmon, D. P., Butters, N., DeTeresa, R., Hill, R., Hansen, L. A., & Katzman, R. (1991) · Annals of Neurology · doi:10.1002/ana.410300410 · Cited by 4,397
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291
Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506
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
Synapse loss in frontal cortex biopsies in Alzheimer's disease: Correlation with cognitive severity
DeKosky, S. T., & Scheff, S. W. (1990) · Annals of Neurology · doi:10.1002/ana.410270502 · Cited by 2,376
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
Mucke, L., Masliah, E., Yu, G.-Q., Mallory, M., Rockenstein, E. M., Tatsuno, G., Hu, K., Kholodenko, D., Johnson-Wood, K., & McConlogue, L. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-11-04050.2000 · Cited by 1,856
Natural oligomers of the amyloid-β protein specifically disrupt cognitive function
Cleary, J. P., Walsh, D. M., Hofmeister, J. J., Shankar, G. M., Kuskowski, M. A., Selkoe, D. J., & Ashe, K. H. (2004) · Nature Neuroscience · doi:10.1038/nn1372 · Cited by 1,722
APP Processing and Synaptic Function
Kamenetz, F., Tomita, T., Hsieh, H., Seabrook, G., Borchelt, D., Iwatsubo, T., Sisodia, S., & Malinow, R. (2003) · Neuron · doi:10.1016/s0896-6273(03)00124-7 · Cited by 1,644
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
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Items 101–200 of 1,001
Dysfunctional Mitochondria and Mitophagy as Drivers of Alzheimer’s Disease Pathogenesis
Chakravorty, A., Jetto, C. T., & Manjithaya, R. R. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00311 · Cited by 225
Macdonald, R., Barnes, K., Hastings, C., & Mortiboys, H. (2018) · Biochemical Society Transactions · doi:10.1042/bst20170501 · Cited by 223
Mechanisms and roles of mitophagy in neurodegenerative diseases
Wang, Y., Liu, N., & Lu, B. (2019) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.13140 · Cited by 217
Mitochondrial Dysfunction: a Potential Therapeutic Target to Treat Alzheimer’s Disease
Nand, S., Singh, C., Singh, A., Singh, M. P., & Singh, S. P. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-01945-y · Cited by 217
Mitochondrial dysfunction in microglia: a novel perspective for pathogenesis of Alzheimer’s disease
Li, Y., Xia, X., Wang, Y., & Zheng, J. (2022) · Journal of Neuroinflammation · doi:10.1186/s12974-022-02613-9 · Cited by 231
Mitochondrial Dysfunction and Synaptic Transmission Failure in Alzheimer’s Disease
Guo, L., Tian, J., & Du, H. (2017) · Journal of Alzheimer’s Disease · doi:10.3233/jad-160702 · Cited by 211
Mitochondrial Dysfunction: Different Routes to Alzheimer’s Disease Therapy
Picone, P., Nuzzo, D., Caruana, L., Scafidi, V., & Carlo, M. D. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/780179 · Cited by 219
Mechanism of Neuroprotective Mitochondrial Remodeling by PKA/AKAP1
Merrill, R. A., Dagda, R. K., Dickey, A. S., Cribbs, J. T., Green, S. H., Usachev, Y. M., & Strack, S. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1000612 · Cited by 212
Wang, X., Petrie, T. G., Liu, Y., Liu, J., Fujioka, H., & Zhu, X. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07734.x · Cited by 217
Self-citationCui, M., Tang, X., Christian, W. V., Yoon, Y., & Tieu, K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.066662 · Cited by 210
Müller, W. E., Eckert, A., Kurz, C., Eckert, G. P., & Leuner, K. (2010) · Molecular Neurobiology · doi:10.1007/s12035-010-8141-5 · Cited by 243
Mitochondrial dysfunction in amyotrophic lateral sclerosis
Shi, P., Gál, J., Kwinter, D. M., Liu, X., & Zhu, H. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.08.012 · Cited by 213
Swerdlow, R. H. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4149 · Cited by 206
PARK2 enhancement is able to compensate mitophagy alterations found in sporadic Alzheimer's disease
Martín-Maestro, P., Gargini, R., Perry, G., Avila, J., & García-Escudero, V. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddv616 · Cited by 184
Self-citationA role for tau at the synapse in Alzheimer’s disease pathogenesis
Pooler, A. M., Noble, W., & Hanger, D. P. (2014) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.09.018 · Cited by 203
Rizza, S., Cardaci, S., Montagna, C., Giacomo, G. D., Zio, D. D., Bordi, M., Maiani, E., Campello, S., Borreca, A., Puca, A. A., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1722452115 · Cited by 208
Mitochondrial dysfunction in Alzheimer’s disease
D’Alessandro, M. C. B., Kanaan, S., Geller, M., Praticò, D., & Daher, J. P. L. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102713 · Cited by 240
Zhang, X., Wang, R., Hu, D., Sun, X., Fujioka, H., Lundberg, K., Chan, E. R., Wang, Q., Xu, R., Flanagan, M. E., et al. (2020) · Science Advances · doi:10.1126/sciadv.abb8680 · Cited by 200
An Overview of the Nrf2/ARE Pathway and Its Role in Neurodegenerative Diseases
Zgórzyńska, E., Dziedzic, B., & Walczewska, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179592 · Cited by 215
Zhao, F., Xu, Y., Gao, S., Qin, L., Austria, Q. M., Siedlak, S. L., Pajdzik, K., Dai, Q., He, C., Wang, W., et al. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00484-x · Cited by 199
Self-citationMitochondrial abnormalities in temporal lobe of autistic brain
Tang, G., Gutierrez Rios, P., Kuo, S.-H., Akman, H. O., Rosoklija, G., Tanji, K., Dwork, A., Schon, E. A., DiMauro, S., Goldman, J., et al. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.01.006 · Cited by 194
Mitochondria as a central sensor for axonal degenerative stimuli
Court, F. A., & Coleman, M. P. (2012) · Trends in Neurosciences · doi:10.1016/j.tins.2012.04.001 · Cited by 201
Alzheimer's Disease: Redox Dysregulation As a Common Denominator for Diverse Pathogenic Mechanisms
Rommy von Bernhardi, M., & Eugenín, J. L. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4082 · Cited by 193
Reddy, P. H., & Shirendeb, U. P. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.10.016 · Cited by 188
Mitochondrial Dysfunction in Alzheimers Disease: Opportunities forDrug Development
Bhatia, S., Rawal, R., Sharma, P., Singh, T., Singh, M., & Singh, V. (2021) · Current Neuropharmacology · doi:10.2174/1570159x19666210517114016 · Cited by 209
Girard, M., Larivière, R., Parfitt, D. A., Deane, E. C., Gaudet, R., Nossova, N., Blondeau, F., Prenosil, G. A., Vermeulen, E. G. M., Duchen, M. R., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1113166109 · Cited by 184
Chornenkyy, Y., Wang, W., Wei, A. L., & Nelson, P. T. (2018) · Brain Pathology · doi:10.1111/bpa.12655 · Cited by 189
Role of Mitochondrial Amyloid-β in Alzheimer's Disease
Chen, J. X., & Yan, S. S. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100357 · Cited by 188
Mitochondrial dynamics in the regulation of neurogenesis: From development to the adult brain
Khacho, M., & Slack, R. S. (2017) · Developmental Dynamics · doi:10.1002/dvdy.24538 · Cited by 189
Axonal Degeneration during Aging and Its Functional Role in Neurodegenerative Disorders
Salvadores, N., Sanhueza, M., Manque, P., & Court, F. A. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00451 · Cited by 182
Mitochondrial dysfunction: the missing link between aging and sporadic Alzheimer’s disease
Grimm, A., Friedland, K., & Eckert, A. (2015) · Biogerontology · doi:10.1007/s10522-015-9618-4 · Cited by 188
Mitochondrial Fission in Human Diseases
Serasinghe, M. N., & Chipuk, J. E. (2016) · Handbook of experimental pharmacology · doi:10.1007/164_2016_38 · Cited by 186
Gan, X., Huang, S., Wu, L., Wang, Y., Hu, G., Li, G., Zhang, H., Yu, H., Swerdlow, R. H., Chen, J. X., et al. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.11.009 · Cited by 180
Sanchez, V., Feinstein, S. D., Lunardi, N., Joksovic, P. M., Boscolo, A., Todorovic, S. M., & Jevtović‐Todorović, V. (2011) · Anesthesiology · doi:10.1097/aln.0b013e3182303a63 · Cited by 182
Kandimalla, R. J. L., Mańczak, M., Fry, D., Yeguvapalli, S., Sesaki, H., & Reddy, P. H. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw312 · Cited by 182
The Role of Oxidative Stress, Mitochondrial Function, and Autophagy in Diabetic Polyneuropathy
Sifuentes-Franco, S., Pacheco-Moisés, F. P., Rodríguez-Carrizález, A. D., & Miranda‐Díaz, A. G. (2017) · Journal of Diabetes Research · doi:10.1155/2017/1673081 · Cited by 186
Mańczak, M., Kandimalla, R. J. L., Fry, D., Sesaki, H., & Reddy, P. H. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw330 · Cited by 180
Multiple Defects in Energy Metabolism in Alzheimers Disease
Ferreira, I. L., Resende, R., Ferreiro, E. B., Rego, A. C., & Pereira, C. (2010) · Current Drug Targets · doi:10.2174/1389450111007011193 · Cited by 185
Inhibition of mitochondrial fragmentation protects against Alzheimer’s disease in rodent model
Wang, W., Yin, J., Ma, X., Zhao, F., Siedlak, S. L., Wang, Z., Torres, S., Fujioka, H., Xu, Y., Perry, G., et al. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx299 · Cited by 175
Self-citationMao, P., Mańczak, M., Calkins, M. J., Truong, Q., Reddy, T. P., Reddy, A. P., Shirendeb, U. P., Lo, H., Rabinovitch, P. S., & Reddy, P. H. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds128 · Cited by 176
Filadi, R., Greotti, E., Turacchio, G., Luini, A., Pozzan, T., & Pizzo, P. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.05.013 · Cited by 173
Mańczak, M., Kandimalla, R. J. L., Yin, X., & Reddy, P. H. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy335 · Cited by 170
Morton, H., Kshirsagar, S., Orlov, E., Bunquin, L. E., Sawant, N. A., Boleng, L., George, M., Basu, T., Ramasubramanian, B., Pradeepkiran, J. A., et al. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.07.013 · Cited by 172
Tau reduction prevents Aβ-induced axonal transport deficits by blocking activation of GSK3β
Vossel, K. A., Xu, J. C., Fomenko, V., Miyamoto, T., Suberbielle, E., Knox, J. A., Ho, K., Kim, D. H., Yu, G.-Q., & Mucke, L. (2015) · Journal of Cell Biology · doi:10.1083/jcb.201407065 · Cited by 167
Structural insights of human mitofusin-2 into mitochondrial fusion and CMT2A onset
Li, Y.-J., Cao, Y.-L., Feng, J.-X., Qi, Y., Meng, S., Yang, J., Zhong, Y.-T., Kang, S., Chen, X., Lan, L., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12912-0 · Cited by 182
Aberrant protein S-nitrosylation contributes to the pathophysiology of neurodegenerative diseases
Nakamura, T., Prikhodko, O. A., Pirie, E., Nagar, S., Akhtar, M. W., Oh, C.-K., McKercher, S. R., Ambasudhan, R., Okamoto, S.-I., & Lipton, S. A. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.03.017 · Cited by 165
Why size matters – balancing mitochondrial dynamics in Alzheimer's disease
DuBoff, B., Feany, M. Β., & Götz, J. (2013) · Trends in Neurosciences · doi:10.1016/j.tins.2013.03.002 · Cited by 168
Peng, K.-G., Yang, L.-K., Wang, J., Ye, F., Dan, G., Zhao, Y.-P., Cai, Y., Cui, Z., Ao, L., Liu, J.-Y., et al. (2017) · Molecular Neurobiology · doi:10.1007/s12035-016-9944-9 · Cited by 155
Molecular Mechanisms of Neuroinflammation in Aging and Alzheimer’s Disease Progression
Andronie-Cioară, F. L., Ardelean, A. I., Nistor-Cseppento, C. D., Jurcău, A., Jurcău, M. C., Pașcalău, N., & Marcu, F. M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24031869 · Cited by 170
Mitochondrial dysfunction in the regulation of aging and aging-related diseases
Zhang, X., Gao, Y., Zhang, S., Wang, Y., Pei, X., Chen, Y., Zhang, J., Zhang, Y., Du, Y., Hao, S., et al. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02308-7 · Cited by 192
Mitochondrial respiratory chain dysfunction: Implications in neurodegeneration
Morán, M., Moreno-Lastres, D., Marín-Buera, L., Arenas, J., Martín, M. A., & Ugalde, C. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.05.009 · Cited by 168
Tripathi, M. K., Kartawy, M., & Amal, H. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101567 · Cited by 163
Bossy, B., Petrilli, A. M., Klinglmayr, E., Chen, J., Lütz‐Meindl, U., Knott, A. B., Masliah, E., Schwarzenbacher, R., & Bossy‐Wetzel, E. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100552 · Cited by 165
Xu, S., Pi, H., Chen, Y., Zhang, N., Guo, P., Lu, Y., He, M., Xie, J., Zhong, M., Zhang, Y., et al. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.7 · Cited by 159
Neuronal Calcium Signaling, Mitochondrial Dysfunction, and Alzheimer's Disease
Supnet, C. B., & Борисович, Б. И. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100306 · Cited by 166
Pathak, D., Berthet, A., & Nakamura, K. (2013) · Annals of Neurology · doi:10.1002/ana.24014 · Cited by 162
Pires, M., & Rego, A. C. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24010778 · Cited by 157
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Edwards, J. L., Quattrini, A., Lentz, S. I., Figueroa-Romero, C., Cerri, F., Backus, C., Hong, Y., & Feldman, E. L. (2010) · Diabetologia · doi:10.1007/s00125-009-1553-y · Cited by 156
Targeting drugs to mitochondria
Heller, A., Brockhoff, G., & Göpferich, A. M. (2012) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2012.05.014 · Cited by 156
Ferreiro, E. B., Baldeiras, I., Ferreira, I. L., Costa, R. O., Rego, A. C., Pereira, C., & Oliveira, C. R. (2012) · International Journal of Cell Biology · doi:10.1155/2012/735206 · Cited by 156
Hung, C. H.-L., Cheng, S. S., Cheung, Y.-T., Wuwongse, S., Zhang, N. Q., Ho, J. Y. S., Lee, S. M., & Chang, R. C. (2017) · Redox Biology · doi:10.1016/j.redox.2017.08.010 · Cited by 147
Agnihotri, A., & Aruoma, O. I. (2019) · Journal of the American College of Nutrition · doi:10.1080/07315724.2019.1683379 · Cited by 156
Vincent, A. M., Edwards, J. L., McLean, L. L., Hong, Y., Cerri, F., Lopez, I., Quattrini, A., & Feldman, E. L. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0697-7 · Cited by 152
Role of mitochondrial homeostasis and dynamics in Alzheimer's disease
Selfridge, J. E., E, L., Lu, J., & Swerdlow, R. H. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.12.057 · Cited by 175
Mitochondrial trafficking and the provision of energy and calcium buffering at excitatory synapses
MacAskill, A. F., Atkin, T. A., & Kittler, J. T. (2010) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2010.07345.x · Cited by 163
Xie, W., & Chung, K. K. K. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07769.x · Cited by 151
Synaptic Mitochondrial Pathology in Alzheimer's Disease
Du, H., Guo, L., & Yan, S. S. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4277 · Cited by 154
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Nakamura, T., & Lipton, S. A. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4703 · Cited by 151
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Cabezas-Opazo, F., Vergara-Pulgar, K., Maria Jose Perez, J., Jara, C., Osorio‐Fuentealba, C., & Quintanilla, R. A. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/509654 · Cited by 155
Oxidative Stress and Metabolic Syndrome: Cause or Consequence of Alzheimer's Disease?
Contreras, D. L., Carvajal, K., Toral-Ríos, D., Franco-Bocanegra, D., & Campos‐Peña, V. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/497802 · Cited by 155
Mitochondrial morphology—emerging role in bioenergetics
Galloway, C. A., Lee, H., & Yoon, Y. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.09.035 · Cited by 159
Self-citationInorganic Nanoparticles Applied as Functional Therapeutics
Liu, Q., Kim, Y., Im, G., Zhu, J., Wu, Y., Liu, Y., & Bhang, S. H. (2020) · Advanced Functional Materials · doi:10.1002/adfm.202008171 · Cited by 153
Mitochondrial import and degradation of amyloid-β peptide
Pinho, C. M., Teixeira, P. F., & Glaser, E. G. (2014) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2014.02.007 · Cited by 149
Joshi, A. U., Saw, N. L., Shamloo, M., & Mochly‐Rosen, D. (2017) · Oncotarget · doi:10.18632/oncotarget.23640 · Cited by 150
Smith, H., Bourne, J. N., Cao, G., Chirillo, M. A., Ostroff, L. E., Watson, D. J., & Harris, K. M. (2016) · eLife · doi:10.7554/elife.15275 · Cited by 151
Multiple faces of dynamin-related protein 1 and its role in Alzheimer's disease pathogenesis
Kandimalla, R. J. L., & Reddy, P. H. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.12.018 · Cited by 148
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Li, X., Zhang, X., Ladiwala, A. R. A., Du, D., Yadav, J. K., Tessier, P. M., Wright, P. E., Kelly, J. W., & Buxbaum, J. N. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.2561-13.2013 · Cited by 143
Self-citationAlzheimer's disease: Effects of β-amyloid on mitochondria
Tillement, L., Lecanu, L., & Papadopoulos, V. (2010) · Mitochondrion · doi:10.1016/j.mito.2010.08.009 · Cited by 148
Iijima-Ando, K., Sekiya, M., Maruko-Otake, A., Ohtake, Y., Suzuki, E., Lu, B., & Iijima, K. M. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002918 · Cited by 142
Yin, X., Mańczak, M., & Reddy, P. H. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw045 · Cited by 144
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Li, P., Jiao, J., Gao, G., & Prabhakar, B. S. (2011) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24004 · Cited by 145
Vukotic, M., Nolte, H., König, T., Saita, S., Ananjew, M., Krüger, M., Tatsuta, T., & Langer, T. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.06.013 · Cited by 139
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Spilsbury, A., Miwa, S., Attems, J., & Saretzki, G. (2015) · The Journal of Neuroscience · doi:10.1523/jneurosci.2925-14.2015 · Cited by 140
Xu, S., Pi, H., Zhang, L., Zhang, N.-X., Li, Y., Zhang, H., Tang, J., Li, H., Feng, M., Deng, P., et al. (2016) · Journal of Pineal Research · doi:10.1111/jpi.12310 · Cited by 139
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Reddy, P. H., Mańczak, M., & Kandimalla, R. J. L. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx052 · Cited by 137
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Lee, A., Hirabayashi, Y., Kwon, S., Lewis, T. L., & Polleux, F. (2018) · Current Opinion in Physiology · doi:10.1016/j.cophys.2018.03.009 · Cited by 131
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Reddy, P. H. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-132060 · Cited by 138
Paula-Lima, A. C., Adasme, T., SanMartín, C. D., Sebollela, A. S., Hetz, C. A., Carrasco, M. A., Ferreira, S. T., & Hidalgo, C. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3287 · Cited by 141
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Self-citationBirnbaum, J. H., Wanner, D., Gietl, A. F., Saake, A., Kündig, T. M., Hock, C., Nitsch, R. M., & Tackenberg, C. (2018) · Stem Cell Research · doi:10.1016/j.scr.2018.01.019 · Cited by 135
Yan, T., & Zhao, Y. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101381 · Cited by 141
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Bell, S., Barnes, K., Marco, M. D., Shaw, P. J., Ferraiuolo, L., Blackburn, D. J., Venneri, A., & Mortiboys, H. (2021) · Biomedicines · doi:10.3390/biomedicines9010063 · Cited by 138
Truncated tau and Aβ cooperatively impair mitochondria in primary neurons
Quintanilla, R. A., Dolan, P. J., Jin, Y. N., & Johnson, G. V. W. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.02.007 · Cited by 139
Mitochondrial turnover in the heart
Gottlieb, R. A., & Gustafsson, Å. B. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.11.017 · Cited by 136
Sepulveda-Falla, D., Barrera-Ocampo, A., Hagel, C., Korwitz, A., Vinueza-Veloz, M. F., Zhou, K., Schonewille, M., Zhou, H., Velazquez-Perez, L., Rodriguez-Labrada, R., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci66407 · Cited by 135
Metadata
- Authors
- Wang, X., Su, B., Lee, H.-G., Li, X., Perry, G., Smith, M. A., & Zhu, X.
- Affiliations
- Case Western Reserve University (US)
- The University of Texas at San Antonio (US)
- Venue
- Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2009-07-15
- Volume
- 29
- Issue
- 28
- Pages
- 9090-9103
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC2735241
- OpenAlex
- W2089141103
- Cited by
- 1,224
- References
- 50
- Citations by year
- 2026: 49 · 2025: 82 · 2024: 71 · 2023: 92 · 2022: 77 · 2021: 102 · 2020: 83 · 2019: 71 · 2018: 60 · 2017: 75 · 2016: 67 · 2015: 59 · 2014: 57 · 2013: 58 · 2012: 84
- FWCI
- 29.56
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Neuroscience (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Alzheimer's Association (AG031852, IIRG-07-60196)
- National Institutes of Health (IIRG-07-60196)
- National Institute on Aging (AG 031852, R01AG031852)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- Alzheimer's disease, mitochondrial dynamics, mitochondrial fission, mitochondrial fusion, Drp1, OPA1, Mfn1, mitofusin 2, Fis1, mitochondrial distribution, axons, pyramidal neurons, synaptic loss, dendritic spines, PSD-95, mitochondrial dysfunction
- MeSH terms
- Aged, Aged, 80 and over, Alzheimer Disease, Animals, Antibodies, Monoclonal, Biotin, Cells, Cultured, Embryo, Mammalian, Gene Expression Regulation, Hippocampus, Humans, Membrane Proteins, Microtubule-Associated Proteins, Middle Aged, Mitochondria, Mutation, Neuroblastoma, Neurons, Postmortem Changes, Time Factors, Transfection, Amyloid beta-Peptides, Microscopy, Immunoelectron, Reactive Oxygen Species, GTP Phosphohydrolases, Mitochondrial Proteins, Membrane Transport Proteins, Mitochondrial Membrane Transport Proteins, Dynamins, Green Fluorescent Proteins, Rats, Cyclooxygenase 1
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