The DOI matches its Crossref record; 103 of the 103 references it cites were found in a registry or an index.
Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
Abstract
Many lines of evidence suggest that mitochondria have a central role in ageing-related neurodegenerative diseases. Mitochondria are critical regulators of cell death, a key feature of neurodegeneration. Mutations in mitochondrial DNA and oxidative stress both contribute to ageing, which is the greatest risk factor for neurodegenerative diseases. In all major examples of these diseases there is strong evidence that mitochondrial dysfunction occurs early and acts causally in disease pathogenesis. Moreover, an impressive number of disease-specific proteins interact with mitochondria. Thus, therapies targeting basic mitochondrial processes, such as energy metabolism or free-radical generation, or specific interactions of disease-related proteins with mitochondria, hold great promise.
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In the citing paper
“Evidence also suggests that not only does Aβ increase cellular RS but that these RS may in turn increase production of Aβ in a destructive autocatalytic cycle (Misonou et al., 2000; Tamagno et al., 2002, 2005; Lin and Beal, 2006; Quiroz-Baez et al., 2009).”
From The mitochondria-targeted antioxidant MitoQ prevents loss of spatial memory retention and early neuropathology in a transgenic mouse model of Alzheimer’s disease (2011) · cites this paper as Lin and Beal, 2006
In the citing paper
“Aβ appears to enhance production of cellular RS, and these RS in turn may to contribute to Aβ toxicity.”
From The mitochondria-targeted antioxidant MitoQ prevents loss of spatial memory retention and early neuropathology in a transgenic mouse model of Alzheimer’s disease (2011) · cites this paper as Lin and Beal, 2006
In the citing paper
“On the basis of evidence from post-mortem brain tissues from AD patients as well as different AD mouse models, damaged mitochondria and increased oxidative stress are common features of AD (Lin and Beal, 2006; Mattson et al., 2008).”
From NAD+ in Brain Aging and Neurodegenerative Disorders (2019) · cites this paper as Lin and Beal, 2006
In the citing paper
“Due to the content of multiple electron carriers and an extensive antioxidant defence, they represent a key centre for ROS/antioxidant balance regulation [56].”
From The Role of Antioxidants in the Interplay between Oxidative Stress and Senescence (2022) · cites this paper as [56]
In the citing paper
“and the AD brain displays insulin resistance and impaired mitochondrial function (45,46)”
From Altered mitochondrial function in insulin-deficient and insulin-resistant states (2018) · cites this paper as [46]
In the citing paper
“a range of distinct aetologies, which manifest as a variety of different syndromes or diseases, converge at some point on an autocatalytic series of reactions, involving imperfectly liganded iron, in the production of the very damaging hydroxyl radical, that by causing the destruction of appropriate cellular structures and proteins liberates further ‘free’ iron and other reactive oxygen species,”
In the citing paper
“Aging-associated expression changes in genes associated with mitochondrial function, protein metabolism, and immune response have been identified in several tissues (173) and are consistent with some proposed mechanisms for late-onset neurodegenerative diseases (98, 113, 124, 166).”
From Unraveling a Multifactorial Late-Onset Disease: From Genetic Susceptibility to Disease Mechanisms for Age-Related Macular Degeneration (2009) · cites this paper as [98]
In the citing paper
“Mitochondrial dysfunction and oxidative stress, including mitochondrial DNA damage, have been implicated in all three diseases—AD, PD, and AMD (12, 17, 98, 165).”
From Unraveling a Multifactorial Late-Onset Disease: From Genetic Susceptibility to Disease Mechanisms for Age-Related Macular Degeneration (2009) · cites this paper as [98]
In the citing paper
“Numerous studies have demonstrated a central role of mitochondria and energy homeostasis in the pathogenesis of aging-associated neurodegenerative diseases (98, 157, 166).”
From Unraveling a Multifactorial Late-Onset Disease: From Genetic Susceptibility to Disease Mechanisms for Age-Related Macular Degeneration (2009) · cites this paper as [98]
In the citing paper
“Much evidence suggests a role for mitochondrial dysfunction in the pathophysiology of PD, a common age-associated neurodegenerative disease characterized by progressive degeneration of the nigrostriatal dopamine (DA) pathway and presence of the intraneuronal protein inclusions (Lewy bodies)1-3.”
From Mitochondrial Approaches for Neuroprotection (2008) · cites this paper as [2]
In the citing paper
“Several different pathogenic mechanisms have been identified in the CNS and peripheral tissues during the disease course in ALS, but mitochondrial and bioenergetic defects are implicated widely in ALS pathogenesis2.”
From Mitochondrial Approaches for Neuroprotection (2008) · cites this paper as [2]
In the citing paper
“These studies provide compelling evidence for a role of PGC-1α in the pathogenesis of neurodegenerative diseases, and thus it is a promising therapeutic target for neurodegenerative disorders2, 72.”
From Mitochondrial Approaches for Neuroprotection (2008) · cites this paper as [2]
In the citing paper
“Second, high cellular ROS levels are associated with cancer, diabetes, inflammatory diseases, ischemia-related diseases, and neurodegeneration, and are thus commonly thought to contribute to human pathologies and aging 80–83.”
From Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes (2010) · cites this paper as [81]
Citations
Cites
Danial, N. N., & Korsmeyer, S. J. (2004) · Cell · doi:10.1016/s0092-8674(04)00046-7 · Cited by 4,651
Chronic systemic pesticide exposure reproduces features of Parkinson's disease
Betarbet, R. S., Sherer, T., MacKenzie, G. M., Garcia‐Osuna, M., Panov, A. V., & Greenamyre, J. T. (2000) · Nature Neuroscience · doi:10.1038/81834 · Cited by 3,770
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
Wallace, D. C. (2005) · Annual Review of Genetics · doi:10.1146/annurev.genet.39.110304.095751 · Cited by 3,185
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
Direct Activation of Bax by p53 Mediates Mitochondrial Membrane Permeabilization and Apoptosis
Chipuk, J. E., Kuwana, T., Bouchier-Hayes, L., Droin, N. M., Newmeyer, D. D., Schuler, M., & Green, D. R. (2004) · Science · doi:10.1126/science.1092734 · Cited by 2,108
Oxidative Damage Is the Earliest Event in Alzheimer Disease
Nunomura, A., Perry, G., Aliev, G., Hirai, K., Takeda, A., Balraj, E. K., Jones, P. K., Ghanbari, H., Wataya, T., Shimohama, S., et al. (2001) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/60.8.759 · Cited by 1,885
Gene regulation and DNA damage in the ageing human brain
Lu, T., Pan, Y., Kao, S.-Y., Li, C., Kohane, I., Chan, J., & Yankner, B. A. (2004) · Nature · doi:10.1038/nature02661 · Cited by 1,874
MITOCHONDRIAL COMPLEX I DEFICIENCY IN PARKINSON'S DISEASE
Schapira, A. H. V., Cooper, J. A. D., Dexter, D. T., Jenner, P. G., Clark, J. B., & MARSDEN, C. D. (1989) · The Lancet · doi:10.1016/s0140-6736(89)92366-0 · Cited by 1,757
Extension of murine life span by overexpression of catalase targeted to mitochondria
Schriner, S. E., Linford, N. J., Martin, G. M., Treuting, P., Ogburn, C. E., Emond, M., Coskun, P. E., Ladiges, W., Wolf, N., Van Remmen, H., et al. (2005) · Science · doi:10.1126/science.1106653 · Cited by 1,724
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Tan, D. Q., & Suda, T. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7273 · Cited by 183
Retinitis Pigmentosa: Progress in Molecular Pathology and Biotherapeutical Strategies
Liu, W., Liu, S., Li, P., & Yao, K. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094883 · Cited by 192
Neuroprotective Role of Trans-Resveratrol in a Murine Model of Familial Alzheimer's Disease
Porquet, D., Griñán‐Ferré, C., Ferrer, I., Camins, A., Sanfeliu, C., del Valle, J., & Pallàs, M. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-140444 · Cited by 180
Venkateshappa, C., Harish, G., Mythri, R. B., Mahadevan, A., Bharath, M. M. S., & Shankar, S. K. (2011) · Neurochemical Research · doi:10.1007/s11064-011-0619-7 · Cited by 177
Mitochondrial Dysfunction in Parkinson's Disease
Keane, P. C., Kurzawa‐Akanbi, M., Blain, P. G., & Morris, C. M. (2011) · Parkinson s Disease · doi:10.4061/2011/716871 · Cited by 182
Deregulation of mitochondrial F1FO-ATP synthase via OSCP in Alzheimer’s disease
Beck, S. J., Guo, L., Phensy, A. J., Tian, J., Wang, L., Tandon, N., Gauba, E., Lu, L., Pascual, J. M., Kroener, S., et al. (2016) · Nature Communications · doi:10.1038/ncomms11483 · Cited by 178
Han, B., Jiang, W., Liu, H., Wang, J., Zheng, K., Cui, P., Feng, Y., Dang, C., Bu, Y., Wang, Q. M., et al. (2020) · Theranostics · doi:10.7150/thno.37119 · Cited by 179
Mitochondrial dysfunction in epilepsy
Folbergrová, J., & Kunz, W. S. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.04.004 · Cited by 175
Moisoi, N., Klupsch, K., Fedele, V., East, P., Sharma, S., Renton, A. E., Plun‐Favreau, H., Edwards, R., Teismann, P., Esposti, M. D., et al. (2008) · Cell Death and Differentiation · doi:10.1038/cdd.2008.166 · Cited by 179
Quantitative profiling brain proteomes revealed mitochondrial dysfunction in Alzheimer’s disease
Adav, S. S., Park, J. E., & Sze, S. K. (2019) · Molecular Brain · doi:10.1186/s13041-019-0430-y · Cited by 183
Understanding the Physiological Links Between Physical Frailty and Cognitive Decline
Ma, L., & Chan, P. (2020) · Aging and Disease · doi:10.14336/ad.2019.0521 · Cited by 180
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Kawamata, H., & Manfredi, G. (2010) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2010.05.003 · Cited by 187
Jain, P., Luo, Z., & Blanke, S. R. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1105175108 · Cited by 173
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Lee, J., Tran, T. A. T., & Tansey, M. G. (2009) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-009-9176-0 · Cited by 174
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Winter, A. N., & Bickford, P. C. (2019) · Antioxidants · doi:10.3390/antiox8090333 · Cited by 185
Ren, J., Li, C., Yan, X., Qu, Y., Yang, Y., & Guo, Z. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/6643382 · Cited by 176
Rapid cell death is preceded by amyloid plaque-mediated oxidative stress
Xie, H., Hou, S., Jiang, J., Sekutowicz, M., Kelly, J., & Bacskai, B. J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1217938110 · Cited by 172
Glycogen synthase kinase-3 inhibitors: Rescuers of cognitive impairments
King, M. K., Pardo, M., Cheng, Y., Downey, K., Jope, R. S., & Beurel, E. (2013) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2013.07.010 · Cited by 177
Kiryu‐Seo, S., Ohno, N., Kidd, G. J., Komuro, H., & Trapp, B. D. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.5265-09.2010 · Cited by 173
Ferrer, I. (2009) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-009-9243-5 · Cited by 172
Yang, L., Calingasan, N. Y., Thomas, B., Chaturvedi, R. K., Kiaei, M., Wille, E. J., Liby, K. T., Williams, C. R., Royce, D. B., Risingsong, R., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005757 · Cited by 173
Self-citationPaths of Convergence: Sirtuins in Aging and Neurodegeneration
Gan, L., & Mucke, L. (2008) · Neuron · doi:10.1016/j.neuron.2008.03.015 · Cited by 173
Oxr1 Is Essential for Protection against Oxidative Stress-Induced Neurodegeneration
Oliver, P. L., Finelli, M. J., Edwards, B., Bitoun, E., Butts, D. L., Becker, E. B. E., Cheeseman, M. T., Davies, B., & Davies, K. E. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1002338 · Cited by 172
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Sun, Y., Ma, C., Sun, H. J., Wang, H., Wei, P., Zhou, Z., Wang, H., Pi, C., Shi, Y., & He, X. (2020) · Journal of Diabetes Research · doi:10.1155/2020/4981814 · Cited by 181
Petrosillo, G., Matera, M. G., Casanova, G., Ruggiero, F. M., & Paradies, G. (2008) · Neurochemistry International · doi:10.1016/j.neuint.2008.07.001 · Cited by 171
Stack, C., Ho, D. J., Wille, E. J., Calingasan, N. Y., Williams, C. R., Liby, K. T., Sporn, M. B., Dumont, M., & Beal, M. F. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.03.017 · Cited by 175
Self-citationXu, Y., Liu, C., Chen, S., Ye, Y., Guo, M., Ren, Q., Liu, L., Zhang, H., Xu, C., Zhou, Q., et al. (2014) · Cellular Signalling · doi:10.1016/j.cellsig.2014.04.009 · Cited by 170
Caspase-cleaved Tau Expression Induces Mitochondrial Dysfunction in Immortalized Cortical Neurons
Quintanilla, R. A., Matthews-Roberson, T. A., Dolan, P. J., & Johnson, G. V. W. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808908200 · Cited by 170
The Identification of Zebrafish Mutants Showing Alterations in Senescence-Associated Biomarkers
Kishi, S., Bayliss, P. E., Uchiyama, J., Koshimizu, E., Qi, J., Nanjappa, P., Imamura, S., Islam, A., Neuberg, D. S., Amsterdam, A., et al. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000152 · Cited by 173
Kaidery, N. A., Banerjee, R., Yang, L., Smirnova, N. A., Hushpulian, D. M., Liby, K. T., Williams, C. R., Yamamoto, M. P., Kensler, T. W., Ratan, R. R., et al. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4491 · Cited by 172
Self-citationRamar, M., Manikandan, B., Prabhu, N. M., Raman, T., Anjugam, M., Palanisamy, S., Karthick, S., & Arumugam, M. (2014) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2014.12.060 · Cited by 170
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
Diffuse Axonal Injury and Oxidative Stress: A Comprehensive Review
Frati, A., Cerretani, D., Fiaschi, A. I., Frati, P., Gatto, V., Russa, R. L., Pesce, A., Pinchi, E., Santurro, A., Fraschetti, F., et al. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18122600 · Cited by 168
Mańczak, M., Kandimalla, R. J. L., Yin, X., & Reddy, P. H. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy335 · Cited by 170
Yang, L., Zhao, K., Calingasan, N. Y., Luo, G., Szeto, H. H., & Beal, M. F. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2445 · Cited by 168
Self-citationRothfuss, O. C., Gasser, T., & Patenge, N. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp1082 · Cited by 169
Zhang, Z., Li, G., Szeto, S. S. W., Chong, C. M., Quan, Q., Huang, C., Cui, W., Guo, B., Wang, Y., Han, Y., et al. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.02.030 · Cited by 169
The mitochondrial permeability transition in neurologic disease
Norenberg, M. D., & RAO, K. (2007) · Neurochemistry International · doi:10.1016/j.neuint.2007.02.008 · Cited by 168
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
Xie, X., Yang, X., Wu, T., Li, Y., Li, M., Tan, Q., Wang, X., & Tang, B. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b01256 · Cited by 168
Ku, Y., Ng, M., Cheng, S., Lo, A. W.-Y., Xiao, Z., Shin, T.-S., Chung, G., & Lam, H. (2020) · Nutrients · doi:10.3390/nu12061717 · Cited by 168
The Complex Interplay between Mitochondria, ROS and Entire Cellular Metabolism
Kuznetsov, A. V., Margreiter, R., Ausserlechner, M. J., & Hagenbuchner, J. (2022) · Antioxidants · doi:10.3390/antiox11101995 · Cited by 182
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Antico, O., Thompson, P. W., Hertz, N. T., Muqit, M. M. K., & Parton, L. E. (2025) · Nature Reviews Drug Discovery · doi:10.1038/s41573-024-01105-0 · Cited by 187
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Wang, Y., Yang, F., Zhang, H.-X., Zi, X., Pan, X.-H., Chen, F.-H., Luo, W., Li, J.-X., Zhu, H.-Y., & Hu, Y.-P. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.314 · Cited by 166
He, Y., Leung, K. W., Zhang, Y.-H., Duan, S., Zhong, X.-F., Jiang, R.-Z., Peng, Z., Tombran‐Tink, J., & Ge, J. (2008) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.07-1361 · Cited by 166
Sharma, A., Liaw, K., Sharma, R. B., Zhang, Z., Kannan, S., & Kannan, R. M. (2018) · Theranostics · doi:10.7150/thno.29039 · Cited by 164
Lagoa, R., Graziani, I., López‐Sánchez, C., García‐Martínez, V., & Gutiérrez‐Merino, C. (2011) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2011.09.022 · Cited by 168
Klosinski, L. P., Yao, J., Yin, F., Fonteh, A. N., Harrington, M. G., Christensen, T. A., Trushina, E. V., & Brinton, R. D. (2015) · EBioMedicine · doi:10.1016/j.ebiom.2015.11.002 · Cited by 163
Zhao, B., Ren, B., Guo, R., Zhang, W., Ma, S., Yao, Y., Yuan, T., Liu, Z., & Liu, X. (2017) · Food and Chemical Toxicology · doi:10.1016/j.fct.2017.09.050 · Cited by 166
Oliveira, J. M. A. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06741.x · Cited by 163
Mitochondrial membrane permeabilisation by amyloid aggregates and protection by polyphenols
Camilleri, A., Zarb, C., Caruana, M., Ostermeier, U., Ghio, S., Högen, T., Schmidt, F., Giese, A., & Vassallo, N. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.06.026 · Cited by 166
Sang, M., Luo, R., Bai, Y., Dou, J., Zhang, Z., Liu, F., Feng, F., Xu, J., & Liu, W. (2019) · Theranostics · doi:10.7150/thno.36283 · Cited by 163
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Patergnani, S., Bouhamida, E., Leo, S., Pinton, P., & Rimessi, A. (2021) · Biomedicines · doi:10.3390/biomedicines9020216 · Cited by 178
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Tan, W. J. T., & Song, L. (2023) · Hearing Research · doi:10.1016/j.heares.2023.108783 · Cited by 163
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Hood, D. A., Tryon, L. D., Carter, H. N., Kim, Y., & Chen, C. C. W. (2016) · Biochemical Journal · doi:10.1042/bcj20160009 · Cited by 159
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Yadav, U. C. S., & Rani, V. (2014) · Springer eBooks · doi:10.1007/978-81-322-2035-0 · Cited by 163
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Huang, J., Yang, R., Jiao, J., Li, Z., Wang, P., Liu, Y., Li, S., Chen, C., Li, Z., Qu, G., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-43364-2 · Cited by 168
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Angeloni, C., Zambonin, L., & Hrelia, S. (2014) · BioMed Research International · doi:10.1155/2014/238485 · Cited by 165
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Cole, A. R., Astell, A. J., Green, C., & Sutherland, C. D. (2007) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2007.04.004 · Cited by 166
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Reddy, P. H., Mao, P., & Mańczak, M. (2009) · Brain Research Reviews · doi:10.1016/j.brainresrev.2009.04.001 · Cited by 164
Du, F., Min, Y., Zeng, F., Yu, C., & Wu, S. (2013) · Small · doi:10.1002/smll.201302036 · Cited by 162
The Parkinson's disease gene DJ-1 is also a key regulator of stroke-induced damage
Aleyasin, H., Rousseaux, M. W. C., Phillips, M., Kim, R. H., Bland, R. J., Callaghan, S. M., Slack, R. S., During, M. J., Mak, T. W., & Park, D. S. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709379104 · Cited by 160
Santos, R. X., Correia, S. C., Wang, X., Perry, G. L., Smith, M. A., Moreira, P. I., & Zhu, X. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100666 · Cited by 162
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Cai, D., & Liu, T. (2011) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2011.06388.x · Cited by 162
Dumont, M., Kipiani, K., Yu, F., Wille, E. J., Katz, M., Calingasan, N. Y., Gouras, G. K., Lin, M. T. S., & Beal, M. F. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110209 · Cited by 164
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Kwon, H. J., Shin, K., Soh, M., Chang, H., Kim, J., Lee, J., Ko, G., Kim, B. H., Kim, D., & Hyeon, T. (2018) · Advanced Materials · doi:10.1002/adma.201704290 · Cited by 163
Herdy, B., Mayer, C., Varshney, D., Marsico, G., Murat, P., Taylor, C., D’Santos, C. S., Tannahill, D., & Balasubramanian, S. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky861 · Cited by 160
Xiao, L., Wei, F., Zhou, Y., Anderson, G. J., Frazer, D. M., Lim, Y. C., Liu, T., & Xiao, Y. (2019) · Nano Letters · doi:10.1021/acs.nanolett.9b04216 · Cited by 160
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Vanova, K. H., Kraus, M., Neužil, J., & Rohlena, J. (2020) · Redox Report · doi:10.1080/13510002.2020.1752002 · Cited by 166
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Kim, S., Jung, U. J., & Kim, S. R. (2024) · Antioxidants · doi:10.3390/antiox13121462 · Cited by 189
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Supnet, C. B., & Борисович, Б. И. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100306 · Cited by 166
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Niu, J., Yu, M., Wang, C., & Xu, Z. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07809.x · Cited by 166
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Ren, M., Zhou, K., He, L., & Lin, W. (2018) · Journal of Materials Chemistry B · doi:10.1039/c7tb03337k · Cited by 159
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Liu, L., Locascio, L. M., & Doré, S. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00153 · Cited by 160
NAD+metabolism and oxidative stress: the golden nucleotide on a crown of thorns
Massudi, H., Grant, R., Guillemin, G. J., & Braidy, N. (2012) · Redox Report · doi:10.1179/1351000212y.0000000001 · Cited by 158
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Mangialasche, F., Kivipelto, M., Mecocci, P., Rizzuto, D., Palmer, K., Winblad, B. G., & Fratiglioni, L. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-091450 · Cited by 172
Spermidine protects against α-synuclein neurotoxicity
Büttner, S., Broeskamp, F., Sommer, C., Markaki, M., Habernig, L., Alavian‐Ghavanini, A., Carmona‐Gutiérrez, D., Eisenberg, T., Michael, E., Kroemer, G., et al. (2014) · Cell Cycle · doi:10.4161/15384101.2014.973309 · Cited by 157
Masanta, G., Heo, C. H., Lim, C. S., Bae, S. K., Cho, B. R., & Kim, H. M. (2012) · Chemical Communications · doi:10.1039/c2cc00034b · Cited by 158
Liao, W., Chen, L., Ma, X., Jiao, R., Li, X., & Wang, Y. (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.02.045 · Cited by 158
Yang, H. N., Chu, X., Cui, L., Fu, S., Gao, C., Li, Y., & Sun, B. (2020) · Drug Delivery · doi:10.1080/10717544.2020.1745328 · Cited by 163
Antioxidants Targeting Mitochondrial Oxidative Stress: Promising Neuroprotectants for Epilepsy
Yang, N., Guan, Q.-W., Chen, F., Xia, Q., Yin, X., Zhou, H.-H., & Mao, X. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/6687185 · Cited by 161
Structural basis for the phosphorylation of FUNDC1 LIR as a molecular switch of mitophagy
Kuang, Y., Ma, K., Zhou, C., Ding, P., Zhu, Y., Chen, Q., & Xia, B. (2016) · Autophagy · doi:10.1080/15548627.2016.1238552 · Cited by 153
Metabolic syndrome and the role of dietary lifestyles in Alzheimer’s disease
Pasinetti, G. M., & Eberstein, J. A. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05454.x · Cited by 160
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Rana, A., Seinen, E., Siudeja, K., Muntendam, R., Srinivasan, B., van der Want, J. J. L., Hayflick, S. J., Reijngoud, D., Kayser, O., & Sibon, O. C. M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912105107 · Cited by 156
The role of mitochondrial DNA mutation on neurodegenerative diseases
Cha, M.-Y., Kim, D. K., & Mook‐Jung, I. (2015) · Experimental & Molecular Medicine · doi:10.1038/emm.2014.122 · Cited by 157
Jakobsson, E., Argüello‐Miranda, O., Chiu, S.-W., Fazal, Z., Kruczek, J., Núñez-Corrales, S., Pandit, S. A., & Pritchet, L. (2017) · The Journal of Membrane Biology · doi:10.1007/s00232-017-9998-2 · Cited by 165
Brinton, R. D. (2008) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2008.06.003 · Cited by 159
Redox Control of the Survival of Healthy and Diseased Cells
Zhang, Y., Du, Y., Le, W., Wang, K., Kieffer, N., & Zhang, J. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3685 · Cited by 161
Mitochondrial abnormalities in spinal and bulbar muscular atrophy
Ranganathan, S., Harmison, G. G., Meyertholen, K., Pennuto, M., Burnett, B. G., & Fischbeck, K. H. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn310 · Cited by 154
Yang, D., Wang, C.-E., Zhao, B., Li, W., Ouyang, Z., Liu, Z., Yang, H., Fan, P., O’Neill, A., Gu, W., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq313 · Cited by 159
Excessive tubulin polyglutamylation causes neurodegeneration and perturbs neuronal transport
Magiera, M. M., Bodakuntla, S., Žiak, J., Lacomme, S., Sousa, P. M., Leboucher, S., Hausrat, T. J., Bosc, C., Andrieux, A., Kneussel, M., et al. (2018) · The EMBO Journal · doi:10.15252/embj.2018100440 · Cited by 155
Huang, M., Chiang, S., Kalinowski, D. S., Bae, D.-H., Sahni, S., & Richardson, D. R. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/6392763 · Cited by 155
Burtscher, J., Millet, G. P., Place, N., Kayser, B., & Zanou, N. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126479 · Cited by 164
Recent Advancements of Nanomedicine in Neurodegenerative Disorders Theranostics
Mukherjee, S., Madamsetty, V. S., Bhattacharya, D., Roy Chowdhury, S., Paul, M. K., & Mukherjee, A. (2020) · Advanced Functional Materials · doi:10.1002/adfm.202003054 · Cited by 152
Fukui, M., & Zhu, B. T. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.12.024 · Cited by 158
Diabetes drugs and neurological disorders: new views and therapeutic possibilities
Patrone, C., Eriksson, O., & Lindholm, D. (2013) · The Lancet Diabetes & Endocrinology · doi:10.1016/s2213-8587(13)70125-6 · Cited by 151
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
Metadata
- Authors
- Lin, M. T., & Beal, M. F.
- Affiliations
- Cornell University (US)
- Corresponding author
- Beal, M. Flint
- ORCID
- Beal, M. Flint
- Venue
- Nature
- Published
- 2006-10
- Volume
- 443
- Issue
- 7113
- Pages
- 787-795
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2152165298
- Cited by
- 6,455
- References
- 103
- Citations by year
- 2026: 266 · 2025: 386 · 2024: 393 · 2023: 362 · 2022: 408 · 2021: 454 · 2020: 412 · 2019: 366 · 2018: 450 · 2017: 373 · 2016: 356 · 2015: 326 · 2014: 290 · 2013: 296 · 2012: 293
- FWCI
- 13.10
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- American Federation for Aging Research
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- mitochondrial dysfunction, oxidative stress, neurodegenerative diseases, aging, mitochondrial DNA mutations, cell death, energy metabolism, free radicals, pathogenesis, mitochondrial-targeted therapy
- MeSH terms
- Aging, Animals, Humans, Mitochondria, Apoptosis, Oxidative Stress, Neurodegenerative Diseases
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