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Mitochondrial defects and oxidative stress in Alzheimer disease and Parkinson disease
Open accessAbstract
Alzheimer disease (AD) and Parkinson disease (PD) are the two most common age-related neurodegenerative diseases characterized by prominent neurodegeneration in selective neural systems. Although a small fraction of AD and PD cases exhibit evidence of heritability, among which many genes have been identified, the majority are sporadic without known causes. Molecular mechanisms underlying neurodegeneration and pathogenesis of these diseases remain elusive. Convincing evidence demonstrates oxidative stress as a prominent feature in AD and PD and links oxidative stress to the development of neuronal death and neural dysfunction, which suggests a key pathogenic role for oxidative stress in both AD and PD. Notably, mitochondrial dysfunction is also a prominent feature in these diseases, which is likely to be of critical importance in the genesis and amplification of reactive oxygen species and the pathophysiology of these diseases. In this review, we focus on changes in mitochondrial DNA and mitochondrial dynamics, two aspects critical to the maintenance of mitochondrial homeostasis and function, in relationship with oxidative stress in the pathogenesis of AD and PD.
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“It has been proposed that ROS, which are considered markers of oxidative stress, are generated in the cytoplasm of neurons and can cause damage to key cellular components, including DNA, proteins, and lipids, leading to neuronal dysfunction and death (56, 59, 60).”
From Molecular Basis for Increased Risk for Late-onset Alzheimer Disease Due to the Naturally Occurring L28P Mutation in Apolipoprotein E4 (2014) · cites this paper as [60]
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“An increasing body of research indicates that ROS generation exacerbates α-synuclein misfolding in the brain, resulting in PD and other synaptic proteinopathies [37,38].”
From Neuroprotective Effects of Bifidobacterium breve CCFM1067 in MPTP-Induced Mouse Models of Parkinson’s Disease (2022) · cites this paper as [37]
In the citing paper
“In clinical studies, probiotics have been shown to lower the development of α-synuclein aggregates by lowering ROS levels, thereby improving the condition of patients with PD [37,39].”
From Neuroprotective Effects of Bifidobacterium breve CCFM1067 in MPTP-Induced Mouse Models of Parkinson’s Disease (2022) · cites this paper as [37]
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Cites
Spillantini, M. G., Schmidt, M. L., Lee, V. M.-Y., Trojanowski, J. Q., Jakes, R., & Goedert, M. (1997) · Nature · doi:10.1038/42166 · Cited by 8,382
Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease
Polymeropoulos, M. H., Lavedan, C., Leroy, E., Ide, S. E., Dehejia, A., Dutra, A., Pike, B., Root, H., Rubenstein, J., Boyer, R., et al. (1997) · Science · doi:10.1126/science.276.5321.2045 · Cited by 8,240
Mitochondrial Dysfunction and Oxidative Stress in Neurodegenerative Diseases
Lin, M. T., & Beal, M. F. (2006) · Nature · doi:10.1038/nature05292 · Cited by 6,455
Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., Yokochi, M., Mizuno, Y., & Shimizu, N. (1998) · Nature · doi:10.1038/33416 · Cited by 5,227
Hereditary Early-Onset Parkinson's Disease Caused by Mutations in PINK1
Valente, E. M., Abou-Sleiman, P. M., Caputo, V., Muqit, M. M. K., Harvey, K., Gispert, S., Ali, Z., Del Turco, D., Bentivoglio, A. R., Healy, D. G., et al. (2004) · Science · doi:10.1126/science.1096284 · Cited by 3,481
Mutations in LRRK2 Cause Autosomal-Dominant Parkinsonism with Pleomorphic Pathology
Zimprich, A. A., Biskup, S., Leitner, P., Lichtner, P., Farrer, M. J., Lincoln, S., Kachergus, J. M., Hulihan, M., Uitti, R. J., Calne, D. B., et al. (2004) · Neuron · doi:10.1016/j.neuron.2004.11.005 · Cited by 3,087
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
Mutations in the DJ-1 Gene Associated with Autosomal Recessive Early-Onset Parkinsonism
Bonifati, V., Rizzu, P., van Baren, M. J., Schaap, O., Breedveld, G. J., Krieger, E., Dekker, M. C. J., Squitieri, F., Ibáñez, P., Joosse, M., et al. (2003) · Science · doi:10.1126/science.1077209 · Cited by 2,854
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
Cloning of the Gene Containing Mutations that Cause PARK8-Linked Parkinson's Disease
Paisán‐Ruiz, C., Jain, S., Evans, E. W., Gilks, W. P., Simón, J., van der Brug, M., de Munaín, A. L., Aparicio, S. F., Gil, A. M., Khan, N. L., et al. (2004) · Neuron · doi:10.1016/j.neuron.2004.10.023 · Cited by 2,453
Research works printed but not linked: 1
- Bonifati, 2003, Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism, Science, 299, 256, 10.1126/science.1077209 · DOI
Cited by
Sorted by citations
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Wang, Y., & Mandelkow, E. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2015.1 · Cited by 2,251
The Role of Oxidative Stress in Parkinson's Disease
Dias, V., Junn, E., & Mouradian, M. M. (2013) · Journal of Parkinson’s Disease · doi:10.3233/jpd-130230 · Cited by 1,845
Mitochondria dysfunction in the pathogenesis of Alzheimer’s disease: Recent advances.
Wang, W., Zhao, F., Ma, X., Perry, G., & Zhu, X. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00376-6 · Cited by 1,274
Self-citationProteasomal and Autophagic Degradation Systems
Đikić, I. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044908 · Cited by 1,217
Role of ROS and Nutritional Antioxidants in Human Diseases
Liu, Z., Ren, Z., Zhang, J., Chuang, C.-C., Kandaswamy, E., Zhou, T., & Zuo, L. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00477 · Cited by 860
Tebay, L. E., Robertson, H., Durant, S. T., Vitale, S. R., Penning, T. M., Dinkova-Kostova, A. T., & Hayes, J. D. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.021 · Cited by 837
Oxidative Stress in Neurodegenerative Diseases: From Molecular Mechanisms to Clinical Applications
Liu, Z., Zhou, T., Ziegler, A. C., Dimitrion, P., & Zuo, L. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/2525967 · Cited by 810
Oxidative stress in Alzheimer’s disease
Chen, Z., & Zhong, C. (2014) · Neuroscience Bulletin · doi:10.1007/s12264-013-1423-y · Cited by 797
The release and trans-synaptic transmission of Tau via exosomes
Wang, Y., Balaji, V., Kaniyappan, S., Krüger, L., Irsen, S., Tepper, K., Chandupatla, R., Maetzler, W., Schneider, A., Mandelkow, E., et al. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0143-y · Cited by 674
Microglia, neuroinflammation, and beta-amyloid protein in Alzheimer’s disease
Cai, Z., Hussain, M. D., & Yan, L.-J. (2014) · International Journal of Neuroscience · doi:10.3109/00207454.2013.833510 · Cited by 583
Microbiome, probiotics and neurodegenerative diseases: deciphering the gut brain axis
Westfall, S., Lomis, N., Kahouli, I., Dia, S. Y., Singh, S. P., & Prakash, S. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2550-9 · Cited by 570
Neuroprotective Effects of Quercetin in Alzheimer’s Disease
Khan, H. Z., Ullah, H., Aschner, M., Cheang, W. S., & Akkol, E. K. (2019) · Biomolecules · doi:10.3390/biom10010059 · Cited by 563
Rutin as a Potent Antioxidant: Implications for Neurodegenerative Disorders
Enogieru, A. B., Haylett, W. L., Hiss, D. C., Bardien, S., & Ekpo, O. E. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/6241017 · Cited by 496
Gómez-Virgilio, L., Silva-Lucero, M.-D.-C., Flores-Morelos, D.-S., Gallardo-Nieto, J., Lopez-Toledo, G., Abarca-Fernandez, A.-M., Zacapala-Gómez, A.-E., Luna-Muñoz, J., Montiel-Sosa, F., Soto-Rojas, L. O., et al. (2022) · Cells · doi:10.3390/cells11152262 · Cited by 431
Yavarpour‐Bali, H., Ghasemi‐Kasman, M., & Pirzadeh, M. (2019) · International Journal of Nanomedicine · doi:10.2147/ijn.s208332 · Cited by 381
Mitochondrial fusion/fission dynamics in neurodegeneration and neuronal plasticity
Bertholet, A. M., Delerue, T., Millet, A. M., Moulis, M. F., David, C., Daloyau, M., Arnauné-Pelloquin, L., Davezac, N., Mils, V., Miquel, M. C., et al. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.10.011 · Cited by 363
Melatonin and its metabolites vs oxidative stress: From individual actions to collective protection
Galano, A., & Reiter, R. J. (2018) · Journal of Pineal Research · doi:10.1111/jpi.12514 · Cited by 365
Mitochondrial 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
Oxidative toxicity in diabetes and Alzheimer’s disease: mechanisms behind ROS/ RNS generation
Ahmad, W., Ijaz, B., Shabbiri, K., Ahmed, F., & Rehman, S. (2017) · Journal of Biomedical Science · doi:10.1186/s12929-017-0379-z · Cited by 341
Wang, W., Wang, X., Fujioka, H., Hoppel, C. L., Whone, A. L., Caldwell, M. A., Cullen, P. J., Liu, J., & Zhu, X. (2015) · Nature Medicine · doi:10.1038/nm.3983 · Cited by 331
Self-citationHaddadi, N., Lin, Y., Travis, G., Simpson, A. M., Nassif, N. T., & McGowan, E. M. (2018) · Molecular Cancer · doi:10.1186/s12943-018-0803-3 · Cited by 321
Liu, Y., Ma, X., Fujioka, H., Liu, J., Chen, S., & Zhu, X. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1906565116 · Cited by 300
Self-citationGalano, A., & Alvarez-Idaboy, J. R. (2018) · International Journal of Quantum Chemistry · doi:10.1002/qua.25665 · Cited by 287
Glycogen synthase kinase-3 beta (GSK-3β) signaling: Implications for Parkinson's disease
Golpich, M., Amini, E., Hemmati, F., Ibrahim, N. M., Rahmani, B., Mohamed, Z., Raymond, A. A., Dargahi, L., Ghasemi, R., & Ahmadiani, A. (2015) · Pharmacological Research · doi:10.1016/j.phrs.2015.03.010 · Cited by 282
Neurotoxin-Induced Animal Models of Parkinson Disease: Pathogenic Mechanism and Assessment
Zeng, X., Geng, W.-S., & Jia, J. (2018) · ASN NEURO · doi:10.1177/1759091418777438 · Cited by 292
Combating oxidative stress disorders with citrus flavonoid: Naringenin
Zaidun, N. H., Thent, Z. C., & Latiff, A. A. (2018) · Life Sciences · doi:10.1016/j.lfs.2018.07.017 · Cited by 266
Oxidative stress and mitochondrial impairment: Key drivers in neurodegenerative disorders
Wen, P., Sun, Z., Gou, F., Wang, J., Fan, Q., Zhao, D., & Yang, L. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102667 · Cited by 253
Oxidative Stress Signaling to Chromatin in Health and Disease
Kreuz, S., & Fischle, W. (2016) · Epigenomics · doi:10.2217/epi-2016-0002 · Cited by 265
Raynes, R., Pomatto, L. C. D., & Davies, K. J. A. (2016) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2016.05.001 · Cited by 234
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
Zilberter, Y., & Zilberter, M. Y. (2017) · Journal of Neuroscience Research · doi:10.1002/jnr.24064 · Cited by 222
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Mármol, I., Sánchez‐de‐Diego, C., Jiménez‐Moreno, N., Ancín‐Azpilicueta, C., & Rodriguez‐Yoldi, M. J. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18061137 · Cited by 221
Oxidative stress factors in Parkinson’s disease
Dorszewska, J., Kowalska, M., Prendecki, M., Piekut, T., Kozłowska, J., & Kozubski, W. P. (2020) · Neural Regeneration Research · doi:10.4103/1673-5374.300980 · Cited by 217
Oxidative Stress-Induced Signaling Pathways Implicated in the Pathogenesis of Parkinson’s Disease
Gaki, G. S., & Papavassiliou, A. G. (2014) · NeuroMolecular Medicine · doi:10.1007/s12017-014-8294-x · Cited by 206
Shared Mechanisms of Neurodegeneration in Alzheimer’s Disease and Parkinson’s Disease
Xie, A., Gao, J., Xu, L., & Meng, D.-M. (2014) · BioMed Research International · doi:10.1155/2014/648740 · Cited by 204
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Zuo, L., & Motherwell, M. S. (2013) · Gene · doi:10.1016/j.gene.2013.07.085 · Cited by 200
Cellular and Molecular Basis of Neurodegeneration in Parkinson Disease
Zeng, X., Geng, W.-S., Jia, J., Chen, L., & Zhang, P.-P. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00109 · Cited by 203
Birth oxidative stress and the development of an antioxidant system in newborn piglets
Yin, J., Ren, W., Liu, G., Duan, J., Yang, G., Wu, L., Li, Y., & Yin, Y. (2013) · Free Radical Research · doi:10.3109/10715762.2013.848277 · Cited by 192
Mitophagy and Oxidative Stress: The Role of Aging
Gaetano, A. D., Gibellini, L., Zanini, G., Nasi, M., Cossarizza, A., & Pinti, M. (2021) · Antioxidants · doi:10.3390/antiox10050794 · Cited by 196
Ashique, S., Mohanto, S., Ahmed, M. G., Mishra, N., Garg, A., Chellappan, D. K., Omara, T., Iqbal, S., & Kahwa, I. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e34092 · Cited by 205
RetractedLacourt, T. E., Vichaya, E. G., Chiu, G. S., Dantzer, R., & Heijnen, C. J. (2018) · Frontiers in Behavioral Neuroscience · doi:10.3389/fnbeh.2018.00078 · Cited by 199
Agarwal, S., Yadav, A., & Chaturvedi, R. K. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.08.043 · Cited by 183
Arab, H. H., Safar, M. M., & Shahin, N. N. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00722 · Cited by 180
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Campanella, C., Pace, A., Bavisotto, C. C., Marzullo, P., Marino, A., Buscemi, S., & Piccionello, A. P. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19092603 · Cited by 177
Ng, L. F., Gruber, J., Cheah, I. K.-M., Goo, C. K., Cheong, W. F., Shui, G., Sit, K. P., Wenk, M. R., & Halliwell, B. B. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.03.003 · Cited by 173
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Hu, X., Tao, C., Gan, Q., Zheng, J., Li, H., & You, C. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/3215391 · Cited by 168
Carboni, E., & Lingor, P. (2015) · Metallomics · doi:10.1039/c4mt00339j · Cited by 170
Baker, N., Patel, J., & Khacho, M. (2019) · Mitochondrion · doi:10.1016/j.mito.2019.06.003 · Cited by 173
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Wang, Z., Liu, J., Li, H., & Yang, H. (2016) · The American Journal of Chinese Medicine · doi:10.1142/s0192415x16500853 · Cited by 161
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Cha, M.-Y., Kim, D. K., & Mook‐Jung, I. (2015) · Experimental & Molecular Medicine · doi:10.1038/emm.2014.122 · Cited by 157
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
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Daniels, T. E., Olsen, E. M., & Tyrka, A. R. (2020) · Annual Review of Clinical Psychology · doi:10.1146/annurev-clinpsy-082719-104030 · Cited by 157
He, J., Zhu, G., Wang, G., & Zhang, F. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/6137521 · Cited by 155
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Liu, Y., Tan, Y., Zhang, Z., Yi, M., Zhu, L., & Peng, W. (2024) · Translational Neurodegeneration · doi:10.1186/s40035-024-00397-x · Cited by 156
Kim, D. S., Choi, H.-I., Wang, Y., Luo, Y., Hoffer, B. J., & Greig, N. H. (2017) · Cell Transplantation · doi:10.1177/0963689717721234 · Cited by 136
Galano, A. (2017) · Journal of the Mexican Chemical Society · doi:10.29356/jmcs.v59i4.81 · Cited by 136
Castañeda‐Arriaga, R., Pérez‐González, A., Reina, M., Alvarez-Idaboy, J. R., & Galano, A. (2018) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.8b03500 · Cited by 136
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Sujkowski, A. L., Hong, L., Wessells, R. J., & Todi, S. V. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101543 · Cited by 142
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Ortega, R. H., Cerezo, A. B., de Pablos, R. M., Krisa, S., Richard, T., García-Parrilla, M. C., & Troncoso, A. M. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00373 · Cited by 136
Denis, M.-C., Desjardins, Y., Fürtös, A., Marcil, V., Dudonné, S., Montoudis, A., Garofalo, C., DELVIN, E. E., Marette, A., & Levy, E. H. (2014) · Clinical Science · doi:10.1042/cs20140210 · Cited by 126
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Maramai, S., Benchekroun, M., Gabr, M. T., & Yahiaoui, S. (2020) · BioMed Research International · doi:10.1155/2020/5120230 · Cited by 121
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Arun, S., Liu, L., & Dönmez, G. (2015) · Current Neuropharmacology · doi:10.2174/1570159x13666150703154541 · Cited by 123
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Froger, N., Moutsimilli, L., Cadetti, L., Jammoul, F., Wang, Q., Fan, Y., Gaucher, D., Rosolen, S. G., Neveux, N., Cynober, L., et al. (2014) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2014.03.001 · Cited by 127
Zuo, L., Hemmelgarn, B. T., Chuang, C., & Best, T. M. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/604658 · Cited by 122
Khan, M. S., Misra, S. K., Wang, Z., Daza, E., Schwartz‐Duval, A. S., Kus, J., Pan, D., & Pan, D. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.6b04769 · Cited by 121
Qi, G., Mi, Y., Wang, Y., Li, R., Huang, S., Li, X., & Liu, X. (2017) · Food & Function · doi:10.1039/c7fo00991g · Cited by 118
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Ferreiro, M. J., Pérez, C., Marchesano, M., Ruiz, S., Caputi, A. A., Aguilera, P. A., Barrio, R., & Cantera, R. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00732 · Cited by 111
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Bonda, D., Wang, X., Lee, H., Smith, M. A., Perry, G. L., & Zhu, X. (2014) · Neuroscience Bulletin · doi:10.1007/s12264-013-1424-x · Cited by 114
Self-citationZhang, B., Davidson, M. M., Zhou, H., Wang, C., Walker, W. F., & Hei, T. K. (2013) · Cancer Research · doi:10.1158/0008-5472.can-13-1411 · Cited by 112
Molecular Chaperonin HSP60: Current Understanding and Future Prospects
Singh, M. K., Shin, Y., Han, S., Ha, J., Tiwari, P. K., Kim, S. S., & Kang, I. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25105483 · Cited by 111
Li, B., Liu, J., Gu, G., Han, X., Zhang, Q., & Zhang, W. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15001 · Cited by 110
Balakrishnan, R., Azam, S., Cho, D.-Y., Su-Kim, I., & Choi, D. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/6680935 · Cited by 117
ERK1/2-mediated activation of DRP1 regulates mitochondrial dynamics and apoptosis in chondrocytes
Ansari, M. Y., Novak, K. L., & Haqqi, T. M. (2021) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2021.11.003 · Cited by 109
Song, Q., Peng, S., & Zhu, X. (2021) · NeuroToxicology · doi:10.1016/j.neuro.2021.10.003 · Cited by 108
Self-citationJi, W., Wei, S., Hao, P., Xing, J., Yuan, Q., Wang, J., Xu, F., & Chen, Y. (2016) · Frontiers in Pharmacology · doi:10.3389/fphar.2016.00101 · Cited by 106
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Lauer, A. A., Grimm, H. S., Apel, B., Golobrodska, N., Kruse, L., Ratanski, E., Schulten, N., Schwarze, L., Slawik, T., Sperlich, S., et al. (2022) · Biomolecules · doi:10.3390/biom12010129 · Cited by 121
Liu, X., & Secombe, J. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.11.007 · Cited by 101
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Scheff, S. W., Ansari, M. A., & Mufson, E. J. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.02.030 · Cited by 100
Meng, X., Wang, M., Sun, G., Ye, J., Zhou, Y., Dong, X., Wang, T., Lu, S., & Sun, X. (2014) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2014.03.026 · Cited by 100
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Simmons, E. C., Scholpa, N. E., & Schnellmann, R. G. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113309 · Cited by 100
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Metadata
- Authors
- Yan, M. H., Wang, X., & Zhu, X.
- Affiliations
- Case Western Reserve University (US)
- Corresponding author
- Wang, Xinglong
- Zhu, Xiongwei
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2013-09
- Volume
- 62
- Pages
- 90-101
- ISSN
- 0891-5849 (ISSN-L)
- PMC
- PMC3744189
- OpenAlex
- W2027783468
- Cited by
- 718
- References
- 209
- Citations by year
- 2026: 14 · 2025: 34 · 2024: 73 · 2023: 56 · 2022: 69 · 2021: 67 · 2020: 53 · 2019: 47 · 2018: 53 · 2017: 71 · 2016: 54 · 2015: 49 · 2014: 48 · 2013: 30
- FWCI
- 16.31
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- the National Institutes of Health (AG031852, NS071184)
- Alzheimer's Association (IIRG-10–173358)
- 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
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Keywords
- Alzheimer's disease, Parkinson's disease, mitochondrial dysfunction, oxidative stress, mitochondrial DNA, mitochondrial dynamics, reactive oxygen species, neurodegeneration, mitochondrial homeostasis
- MeSH terms
- Alzheimer Disease, Humans, Mitochondria, Nerve Degeneration, Neurons, Parkinson Disease, Amyloid beta-Peptides, Cell Death, Reactive Oxygen Species, Oxidative Stress
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