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Abnormal mitochondrial dynamics and synaptic degeneration as early events in Alzheimer’s disease: Implications to mitochondria-targeted antioxidant therapeutics
Open accessAbstract
Synaptic pathology and mitochondrial oxidative damage are early events in Alzheimer's disease (AD) progression. Loss of synapses and synaptic damage are the best correlates of cognitive deficits found in AD patients. Recent research on amyloid beta (Aβ) and mitochondria in AD revealed that Aβ accumulates in synapses and synaptic mitochondria, leading to abnormal mitochondrial dynamics and synaptic degeneration in AD neurons. Further, recent studies using live-cell imaging and primary neurons from amyloid beta precursor protein (AβPP) transgenic mice revealed reduced mitochondrial mass, defective axonal transport of mitochondria and synaptic degeneration, indicating that Aβ is responsible for mitochondrial and synaptic deficiencies. Tremendous progress has been made in studying antioxidant approaches in mouse models of AD and clinical trials of AD patients. This article highlights the recent developments made in Aβ-induced abnormal mitochondrial dynamics, defective mitochondrial biogenesis, impaired axonal transport and synaptic deficiencies in AD. This article also focuses on mitochondrial approaches in treating AD, and also discusses latest research on mitochondria-targeted antioxidants in AD. This article is part of a Special Issue entitled: Antioxidants and Antioxidant Treatment in Disease.
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“However, oxidative stress, mitochondrial dysfunction, and glucose hypometabolism have been well documented in MCI and AD brain [8,53,74,75,76].”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [53]
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“As mentioned above, the use of redox proteomics has led to the identification of oxidized proteins, as indexed by carbonylation, nitration, and modification with HNE, in both in vitro and in vivo models of AD in addition to MCI and AD brain.”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [53]
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“Compelling evidence links neurodegeneration to altered brain metabolism and mitochondrial dysfunction, both of which are early hallmarks of AD [21–28].”
From Neuronal Apolipoprotein E4 Expression Results in Proteome-Wide Alterations and Compromises Bioenergetic Capacity by Disrupting Mitochondrial Function (2019) · cites this paper as [27]
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“Consistent with the hypothesis that both oxidative stress and mitochondrial dysfunction are early events in the progression of AD [12,35,53], many of the oxidized proteins identified are mitochondrial proteins involved in metabolism, protein synthesis and folding, ROS scavenging, transport, and apoptosis (Table 1).”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [53]
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“The presence of Aβ oligomers in mitochondrial membranes is consistent with Aβ-induced mitochondrial dysfunction occurring early in the disease progression timeline [34,53].”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [53]
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Cites
Sequence and organization of the human mitochondrial genome
Anderson, S., Bankier, A. T., Barrell, B. G., de Bruijn, M. H. L., Coulson, A. R., Drouin, J., Eperon, I. C., Nierlich, D. P., Roe, B. A., Sanger, F., et al. (1981) · Nature · doi:10.1038/290457a0 · Cited by 9,740
Mitochondrial Dysfunction and Oxidative Stress in Neurodegenerative Diseases
Lin, M. T., & Beal, M. F. (2006) · Nature · doi:10.1038/nature05292 · Cited by 6,455
Mitochondrial diseases in man and mouse
Wallace, D. C. (1999) · Science · doi:10.1126/science.283.5407.1482 · Cited by 3,060
Pathways towards and Away from Alzheimer’s Disease
Mattson, M. P. (2004) · Nature · doi:10.1038/nature02621 · Cited by 3,052
Yang, F., Lim, G. P., Begum, A. N., Ubeda, O. J., Simmons, M. R., Ambegaokar, S. S., Chen, P. P., Kayed, R., Glabe, C. G., Frautschy, S. A., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m404751200 · Cited by 2,336
Vitamin E and Donepezil for the Treatment of Mild Cognitive Impairment
Petersen, R. C., Thomas, R. G., Grundman, M., Bennett, D., Doody, R., Ferris, S., Galasko, D., Jin, S., Kaye, J., Levey, A., et al. (2005) · New England Journal of Medicine · doi:10.1056/nejmoa050151 · Cited by 1,844
Mitochondrial abnormalities in Alzheimer's disease
Hirai, K., Aliev, G., Nunomura, A., Fujioka, H., Russell, R. L., Atwood, C. S., Johnson, A. B., Kress, Y., Vinters, H. V., Tabaton, M., et al. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-09-03017.2001 · Cited by 1,367
Reiman, E. M., Caselli, R. J., Yun, L. S., Chen, K., Bandy, D., Minoshima, S., Thibodeau, S. N., & Osborne, D. (1996) · New England Journal of Medicine · doi:10.1056/nejm199603213341202 · Cited by 1,366
ABAD Directly Links Aß to Mitochondrial Toxicity in Alzheimer's Disease
Lustbader, J. W., Cirilli, M., Lin, C., Xu, H. W., Takuma, K., Wang, N., Caspersen, C., Chen, X., Pollak, S., Chaney, M., et al. (2004) · Science · doi:10.1126/science.1091230 · Cited by 1,303
Impaired Balance of Mitochondrial Fission and Fusion in Alzheimer's Disease
Wang, X., Su, B., Lee, H.-G., Li, X., Perry, G., Smith, M. A., & Zhu, X. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.1357-09.2009 · Cited by 1,224
Flagged first, then by citations
2 of the 104 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Oxidative Stress, Synaptic Dysfunction, and Alzheimer’s Disease
Tönnies, E., & Trushina, E. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-161088 · Cited by 1,750
Bhatti, J. S., Bhatti, G. K., & Reddy, P. H. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.11.010 · Cited by 1,655
Self-citationAgeing and Parkinson's disease: Why is advancing age the biggest risk factor?
Reeve, A. K., Simcox, E. M., & Turnbull, D. M. (2014) · Ageing Research Reviews · doi:10.1016/j.arr.2014.01.004 · Cited by 1,013
Is Alzheimer’s disease a type 3 diabetes? A critical appraisal
Kandimalla, R., Thirumala, V., & Reddy, P. H. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.08.018 · Cited by 621
Self-citationHippocampus and its involvement in Alzheimer’s disease: a review
Rao, Y. L., Ganaraja, B., Murlimanju, B. V., Joy, T., Krıshnamurthy, A., & Agrawal, A. (2022) · 3 Biotech · doi:10.1007/s13205-022-03123-4 · Cited by 646
Verdile, G., Keane, K. N., Cruzat, V. F., Medic, S., Sabale, M., Rowles, J., Wijesekara, N., Martins, R. N., Fraser, P. E., & Newsholme, P. (2015) · Mediators of Inflammation · doi:10.1155/2015/105828 · Cited by 509
Amyloid Beta and Phosphorylated Tau-Induced Defective Autophagy and Mitophagy in Alzheimer’s Disease
Reddy, P. H., & Oliver, D. M. (2019) · Cells · doi:10.3390/cells8050488 · Cited by 496
Self-citationDiverse Roles of Mitochondria in Immune Responses: Novel Insights Into Immuno-Metabolism
Angajala, A., Lim, S., Phillips, J. B., Kim, J. H., Yates, C. C., You, Z., & Tan, M. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01605 · Cited by 469
Trushina, E., Dutta, T., Persson, X.-M. T., Mielke, M. M., & Petersen, R. C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0063644 · Cited by 438
Baltazar, M. T., Dinis‐Oliveira, R. J., Bastos, M. D. L., Tsatsakis, A. M., Duarte, J. A., & Carvalho, F. D. (2014) · Toxicology Letters · doi:10.1016/j.toxlet.2014.01.039 · Cited by 410
Neuroprotective Mechanisms of Resveratrol in Alzheimer’s Disease: Role of SIRT1
Gomes, B. A. Q., Silva, J. P. B., Romeiro, C. F. R., dos Santos, S. M., Rodrigues, C. A., Gonçalves, P. R., Sakai, J. T., Mendes, P. F. S., Varela, E. L. P., & Monteiro, M. C. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/8152373 · Cited by 403
Insulin and Insulin Resistance in Alzheimer’s Disease
Sędzikowska, A., & Szablewski, L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22189987 · Cited by 414
Defective mitophagy in Alzheimer’s disease
Pradeepkiran, J. A., & Reddy, P. H. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101191 · Cited by 367
Self-citationSynaptic basis of Alzheimer’s disease: Focus on synaptic amyloid beta, P-tau and mitochondria
John, A., & Reddy, P. H. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101208 · Cited by 359
Self-citationProtective Effects of Indian Spice Curcumin Against Amyloid-β in Alzheimer’s Disease
Reddy, P. H., Manczak, M., Yin, X., Grady, M. C., Mitchell, A., Tonk, S., Kuruva, C. S., Bhatti, J. S., Kandimalla, R., Vijayan, M., et al. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-170512 · Cited by 354
Self-citationMitochondrial Quality Control and Disease: Insights into Ischemia-Reperfusion Injury
Anzell, A. R., Maizy, R., Przyklenk, K., & Sanderson, T. H. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0503-9 · Cited by 359
PINK1 signalling rescues amyloid pathology and mitochondrial dysfunction in Alzheimer’s disease
Du, F., Yu, Q., Yan, S., Hu, G., Lue, L., Walker, D., Wu, L., Yan, S. F., Tieu, K., & Yan, S. S. (2017) · Brain · doi:10.1093/brain/awx258 · Cited by 308
Molecular Strategies for Targeting Antioxidants to Mitochondria: Therapeutic Implications
Apostolova, N., & Víctor, V. M. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5952 · Cited by 311
Reddy, P. H., Yin, X., Mańczak, M., Kumar, S., Pradeepkiran, J. A., Vijayan, M., & Reddy, A. P. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy154 · Cited by 292
Self-citationMańczak, M., Kandimalla, R. J. L., Yin, X., & Reddy, P. H. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy042 · Cited by 288
Self-citationRetractedVDAC1, mitochondrial dysfunction, and Alzheimer’s disease
Shoshan-Barmatz, V., Nahon-Crystal, E., Shteinfer-Kuzmine, A., & Gupta, R. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.03.010 · Cited by 286
Locus coeruleus cellular and molecular pathology during the progression of Alzheimer’s disease
Kelly, S. C., He, B., Perez, S. E., Ginsberg, S. D., Mufson, E. J., & Counts, S. E. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0411-2 · Cited by 286
The role of type 2 diabetes in neurodegeneration
Verdile, G., Fuller, S. J., & Martins, R. N. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.04.008 · Cited by 290
Mitochondrial Aspects of Synaptic Dysfunction in Alzheimer’s Disease
Cai, Q., & Tammineni, P. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160726 · Cited by 282
Kandimalla, R. J. L., Mańczak, M., Yin, X., Wang, R., & Reddy, P. H. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx381 · Cited by 256
Self-citationRetractedBaek, S. H., Park, S. J., Jeong, J. I., Kim, S. H., Han, J., Kyung, J. W., Baik, S.-H., Choi, Y., Choi, B. Y., Park, J. S., et al. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.2385-16.2017 · Cited by 258
Mitochondrial Dysfunction in Alzheimer’s Disease and the Rationale for Bioenergetics Based Therapies
Onyango, I. G., Dennis, J., & Khan, S. M. (2016) · Aging and Disease · doi:10.14336/ad.2015.1007 · Cited by 260
Goozee, K. G., Shah, T. M., Sohrabi, H. R., Rainey‐Smith, S. R., Brown, B. M., Verdile, G., & Martins, R. N. (2015) · British Journal Of Nutrition · doi:10.1017/s0007114515004687 · Cited by 245
Zhang, Y., Xu, Z., Wang, H., Dong, Y., Shi, H. N., Culley, D. J., Crosby, G. J., Marcantonio, E. R., Tanzi, R. E., & Xie, Z. (2012) · Annals of Neurology · doi:10.1002/ana.23536 · Cited by 239
Inhibition of mitochondrial protein import by mutant huntingtin
Yano, H., Baranov, S. V., Baranova, O. V., Kim, J., Pan, Y., Yablonska, S., Carlisle, D. L., Ferrante, R. J., Kim, A. H., & Friedlander, R. M. (2014) · Nature Neuroscience · doi:10.1038/nn.3721 · Cited by 226
Amyloid precursor protein processing and bioenergetics
Wilkins, H., & Swerdlow, R. H. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.08.009 · Cited by 228
Clemente‐Suárez, V. J., Redondo-Flórez, L., Beltrán-Velasco, A. I., Ramos‐Campo, D. J., Belinchón-deMiguel, P., Martínez‐Guardado, I., Dalamitros, A. A., Sepulveda, R. A. Y., Martín-Rodríguez, A., & Tornero-Aguilera, J. F. (2023) · Biomedicines · doi:10.3390/biomedicines11092488 · Cited by 251
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
Mitochondrial division and fusion in metabolism
Roy, M., Reddy, P. H., Iijima, M., & Sesaki, H. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2015.02.001 · Cited by 215
Self-citationPARK2 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
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Pei, L., & Wallace, D. C. (2017) · Biological Psychiatry · doi:10.1016/j.biopsych.2017.11.018 · Cited by 203
Mitochondrial dynamics and transport in Alzheimer's disease
Flannery, P. J., & Trushina, E. V. (2019) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2019.06.009 · Cited by 203
Oxidative Stress in Alzheimer’s Disease: Are We Connecting the Dots?
Rosini, M., Simoni, E., Milelli, A., Minarini, A., & Melchiorre, C. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400970m · Cited by 202
Wang, D., Li, S., Wu, W., Zhu, X., Wang, Y., & Yuan, H. (2014) · Neurochemical Research · doi:10.1007/s11064-014-1343-x · Cited by 203
Mitochondrial alterations near amyloid plaques in an Alzheimer’s disease mouse model
Xie, H., Guan, J., Borrelli, L. A., Xu, J., Serrano-Pozo, A., & Bacskai, B. J. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.1836-13.2013 · Cited by 185
“An effective treatment will likely include a combination of drugs that protect mitochondrial function (Calkins et al., 2012; Eckert et al., 2012; Reddy et al., 2012) and prevent amyloid accumulation.”
BackgroundKim, D. I., Lee, K. H., Gabr, A. A., Choi, G. E., Kim, J. S., Ko, S. H., & Han, H. J. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.09.003 · Cited by 187
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Serasinghe, M. N., & Chipuk, J. E. (2016) · Handbook of experimental pharmacology · doi:10.1007/164_2016_38 · Cited by 186
Hypoxia, Oxidative Stress, and Inflammation: Three Faces of Neurodegenerative Diseases
Merelli, A., Repetto, M. G., Lazarowski, A., & Auzmendi, J. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-201074 · Cited by 188
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
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Mandal, A., & Drerup, C. M. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00373 · 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
Self-citationMorton, 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
Self-citationWhy 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
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Gowda, P., Reddy, P. H., & Kumar, S. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101529 · Cited by 170
Self-citationFerreiro, 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
Pesticides, cognitive functions and dementia: A review
Aloizou, A., Siokas, V., Vogiatzi, C., Peristeri, E., Docea, A. O., Petrakis, D., Provatas, A., Folia, V., Chalkia, C., Vinceti, M., et al. (2020) · Toxicology Letters · doi:10.1016/j.toxlet.2020.03.005 · Cited by 164
Wáng, Y., Zhang, M., Li, Z., Yue, J., Xu, M., Zhang, Y., Yung, K. K. L., & Li, R. (2018) · Chemosphere · doi:10.1016/j.chemosphere.2018.11.149 · Cited by 149
Genetic reduction of Nrf2 exacerbates cognitive deficits in a mouse model of Alzheimer’s disease
Branca, C., Ferreira, E., Nguyen, T.-V., Doyle, K., Caccamo, A., & Oddo, S. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx361 · Cited by 139
Reddy, P. H. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.06.012 · Cited by 147
Self-citationMultiple 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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Vissers, C. B., Ming, G., & Song, H. (2019) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2019.02.007 · Cited by 146
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Foret, M. K., Lincoln, R., Carmo, S. D., Cuello, A. C., & Cosa, G. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00761 · Cited by 150
Yin, X., Mańczak, M., & Reddy, P. H. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw045 · Cited by 144
Self-citationXu, 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
Aliev, G., Priyadarshini, M., Reddy, V., Grieg, N. H., Kaminsky, Y., Cacabelos, R., Ashraf, G., Jabir, N. R., Kamal, M. A., Nikolenko, V. N., et al. (2014) · Current Medicinal Chemistry · doi:10.2174/0929867321666131227161303 · Cited by 138
Reddy, P. H., Mańczak, M., & Kandimalla, R. J. L. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx052 · Cited by 137
Self-citationReddy, P. H. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-132060 · Cited by 138
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Reddy, P. H., Tonk, S., Kumar, S., Vijayan, M., Kandimalla, R., Kuruva, C. S., & Reddy, A. P. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.08.067 · Cited by 143
Self-citationPaglia, G., Stocchero, M., Cacciatore, S., Lai, S., Angel, P. M., Alam, M. T., Keller, M. A., Ralser, M., & Astarita, G. (2015) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b01020 · Cited by 136
Mastroeni, D., Khdour, O. M., Delvaux, E., Nolz, J., Olsen, G., Berchtold, N. C., Cotman, C. W., Hecht, S. M., & Coleman, P. D. (2016) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2016.09.003 · Cited by 134
Corsetti, V., Florenzano, F., Atlante, A., Bobba, A., Ciotti, M. T., Natale, F., Della Valle, F., Borreca, A., Manca, A., Meli, G., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv059 · Cited by 129
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Mazzanti, G., & Giacomo, S. D. (2016) · Molecules · doi:10.3390/molecules21091243 · Cited by 131
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Eckert, G. P., Renner, K., Eckert, S. H., Eckmann, J., Hagl, S., Abdel-Kader, R. M., Kurz, C., Leuner, K., & Muller, W. E. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8271-z · Cited by 127
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Goldberg, J., Currais, A. J. M., Prior, M., Fischer, W. H., Chiruta, C., Ratliff, E. P., Daugherty, D., Dargusch, R., Finley, K. D., Esparza‐Moltó, P. B., et al. (2018) · Aging Cell · doi:10.1111/acel.12715 · Cited by 131
Aborode, A. T., Pustake, M., Awuah, W. A., Alwerdani, M., Shah, P., Yarlagadda, R., Ahmad, S., Silva Correia, I. F., Chandra, A., Nansubuga, E. P., et al. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/7934442 · Cited by 124
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Oliver, D. M. A., & Reddy, P. H. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190048 · Cited by 120
Self-citationRovira‐Llopis, S., Apostolova, N., Bañuls, C., Muntané, J., Rocha, M., & Víctor, V. M. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7313 · Cited by 123
Wang, X. H., Souders, C. L., Zhao, Y. H., & Martyniuk, C. J. (2017) · Chemosphere · doi:10.1016/j.chemosphere.2017.10.032 · Cited by 118
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García‐Escudero, V., Martín-Maestro, P., Perry, G. L., & Ávila, J. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/162152 · Cited by 120
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Guo, L., Du, H., Yan, S., Wu, X., McKhann, G. M., Chen, J. X., & Yan, S. S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0054914 · Cited by 118
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Metadata
- Authors
- Reddy, P. H., Tripathi, R., Troung, Q., Tirumala, K., Reddy, T. P., Anekonda, V., Shirendeb, U. P., Calkins, M. J., Reddy, A. P., Mao, P., & Manczak, M.
- Affiliations
- Oregon National Primate Research Center (US)
- Corresponding author
- Reddy, P. Hemachandra
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
- Publisher
- Elsevier BV
- Published
- 2012-05
- Volume
- 1822
- Issue
- 5
- Pages
- 639-649
- ISSN
- 0925-4439 (ISSN-L)
- PMC
- PMC3272314
- OpenAlex
- W1996981671
- Cited by
- 394
- References
- 104
- Citations by year
- 2026: 29 · 2025: 17 · 2024: 22 · 2023: 27 · 2022: 30 · 2021: 38 · 2020: 29 · 2019: 30 · 2018: 26 · 2017: 36 · 2016: 31 · 2015: 19 · 2014: 31 · 2013: 18 · 2012: 10
- FWCI
- 2.02
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- NIH
- Alzheimer Association
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- Alzheimer's disease, mitochondrial dynamics, synaptic degeneration, amyloid-beta, mitochondrial oxidative damage, mitochondrial biogenesis, mitochondria-targeted antioxidants, antioxidant therapeutics, synaptic mitochondria
- MeSH terms
- Alzheimer Disease, Animals, Antioxidants, Humans, Mice, Transgenic, Mitochondria, Synapses, Amyloid beta-Protein Precursor, Mice
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