Mitochondrial Dysfunction and Oxidative Stress in Neurodegenerative Diseases

Lin, Michael T.; Beal, M. Flint

doi:10.1038/nature05292

Cited by 6,455Mitochondrial Function and PathologyParkinson's Disease Mechanisms and TreatmentsAutophagy in Disease and Therapy

Mitochondrial Dysfunction and Oxidative Stress in Neurodegenerative Diseases

Lin, Michael T., Beal, M. Flint·2006·Nature

DOI 10.1038/nature05292

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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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Aβ increases cellular RS, and these RS may in turn increase production of Aβ in a destructive autocatalytic cycle.
“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
Aβ enhances production of cellular RS, and these RS contribute to Aβ toxicity.
“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
On the basis of evidence from post-mortem brain tissues from Alzheimer's disease patients and different AD mouse models, damaged mitochondria and increased oxidative stress are common features of Alzheimer's disease.
“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
Mitochondria represent a key centre for ROS/antioxidant balance regulation due to their content of multiple electron carriers and an extensive antioxidant defence.
“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]
The Alzheimer's disease brain displays insulin resistance and impaired mitochondrial function.
“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]

A range of distinct aetiologies converge on an autocatalytic series of reactions involving imperfectly liganded iron producing hydroxyl radical, which causes destruction of cellular structures and proteins, liberates further free iron and reactive oxygen species, and effects positive feedback leading to further damage.
“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,”
From Towards a unifying, systems biology understanding of large-scale cellular death and destruction caused by poorly liganded iron: Parkinson’s, Huntington’s, Alzheimer’s, prions, bactericides, chemical toxicology and others as examples (2010) · cites this paper as Lin and Beal 2006
Aging-associated expression changes in genes associated with mitochondrial function, protein metabolism, and immune response have been identified in several tissues and are consistent with some proposed mechanisms for late-onset neurodegenerative diseases.
“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]
Mitochondrial dysfunction and oxidative stress, including mitochondrial DNA damage, have been implicated in AD, PD, and AMD.
“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]
Numerous studies have demonstrated a central role of mitochondria and energy homeostasis in the pathogenesis of aging-associated neurodegenerative diseases.
“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]
Mitochondrial dysfunction plays a role in the pathophysiology of Parkinson's disease.
“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]
Mitochondrial and bioenergetic defects are implicated widely in ALS pathogenesis.
“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]
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 disorders.
“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]
High cellular ROS levels are associated with cancer, diabetes, inflammatory diseases, ischemia-related diseases, and neurodegeneration.
“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]

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Reddy, P. H., McWeeney, S. K., Park, B. S., Mańczak, M., Gutala, R. V., Partovi, D., Jung, Y., Yau, V., Searles, R. P., Mori, M., et al. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh140 · Cited by 327 · see citing works
β‐Site APP cleaving enzyme up‐regulation induced by 4‐hydroxynonenal is mediated by stress‐activated protein kinases pathways
Tamagno, E., Parola, M., Bardini, P., Piccini, A., Borghi, R., Guglielmotto, M., Santoro, G., Davit, A., Danni, O., Smith, M. A., et al. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02895.x · Cited by 324 · see citing works
Enhanced substantia nigra mitochondrial pathology in human α-synuclein transgenic mice after treatment with MPTP111-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine.
Song, D. D., Shults, C. W., Sisk, A., Rockenstein, E. M., & Masliah, E. (2003) · Experimental Neurology · doi:10.1016/s0014-4886(03)00342-x · Cited by 294 · see citing works
Increased plaque burden in brains of APP mutant MnSOD heterozygous knockout mice
Li, F., Calingasan, N. Y., Yu, F., Mauck, W. M., Toidze, M., Almeida, C. G., Takahashi, R. H., Carlson, G. A., Beal, M. F., Lin, M. T. S., et al. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02455.x · Cited by 276 · see citing works
Self-citation
Cybrids in Alzheimer's disease: a cellular model of the disease?
Swerdlow, R. H., Parks, J. K., Cassarino, D. S., Maguire, D. J., Maguire, R. S., Bennett, J. P., Davis, R. E., & Parker, W. D. (1997) · Neurology · doi:10.1212/wnl.49.4.918 · Cited by 272 · see citing works
CuZn superoxide dismutase (SOD1) accumulates in vacuolated mitochondria in transgenic mice expressing amyotrophic lateral sclerosis-linked SOD1 mutations
Jaarsma, D., Rognoni, F., van Duijn, W., Verspaget, H. W., Haasdijk, E. D., & Holstege, J. C. (2001) · Acta Neuropathologica · doi:10.1007/s004010100399 · Cited by 271 · see citing works
Parkin enhances mitochondrial biogenesis in proliferating cells
Kuroda, Y., Mitsui, T., Kunishige, M., Shono, M., Akaike, M., Azuma, H., & Matsumoto, T. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl006 · Cited by 268 · see citing works
ALS-associated mutant SOD1G93A causes mitochondrial vacuolation by expansion of the intermembrane space and by involvement of SOD1 aggregation and peroxisomes
Higgins, C. M. J., Jung, C., & Xu, Z. (2003) · BMC Neuroscience · doi:10.1186/1471-2202-4-16 · Cited by 262 · see citing works
Cybrids in Alzheimer's disease: A cellular model of the disease?
Swerdlow, R. H., & Parker, D. W. (1998) · Neurology · doi:10.1212/wnl.51.1.326-a · Cited by 260 · see citing works
Mitochondrial Respiration and ATP Production Are Significantly Impaired in Striatal Cells Expressing Mutant Huntingtin
Milakovic, T., & Johnson, G. V. W. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504749200 · Cited by 259 · see citing works
Nicastrin, Presenilin, APH-1, and PEN-2 Form Active γ-Secretase Complexes in Mitochondria
Hansson, C. A., Frykman, S., Farmery, M. R., Tjernberg, L. O., Nilsberth, C., Pursglove, S. E., Ito, A., Winblad, B., Cowburn, R. F., Thyberg, J., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404500200 · Cited by 256 · see citing works
Oxidative modification and down-regulation of Pin1 in Alzheimer's disease hippocampus: A redox proteomics analysis
Rukhsana Sultana, A., Debra Boyd-kimball, A., Poon, H. F., Cai, J., Pierce, W. M. J., Klein, J. B., Markesbery, W. R., Zhou, X. Z., Lu, K. P., & Butterfield, D. A. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.05.005 · Cited by 255 · see citing works
Energy Inhibition Elevates β-Secretase Levels and Activity and Is Potentially Amyloidogenic in APP Transgenic Mice: Possible Early Events in Alzheimer's Disease Pathogenesis
Velliquette, R. A., O'Connor, T., & Vassar, R. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.2350-05.2005 · Cited by 254 · see citing works
Mutant Superoxide Dismutase 1 Forms Aggregates in the Brain Mitochondrial Matrix of Amyotrophic Lateral Sclerosis Mice
Vijayvergiya, C., Beal, M. F., Buck, J., & Manfredi, G. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.4385-04.2005 · Cited by 251 · see citing works
Self-citation
Involvement of Mitochondrial Complex II Defects in Neuronal Death Produced by N-Terminus Fragment of Mutated Huntingtin
Benchoua, A., Trioulier, Y., Zala, D., Gaillard, M., Lefort, N., Dufour, N., Saudou, F., Elalouf, J., Hirsch, É. C., Hantraye, P., et al. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-07-0607 · Cited by 248 · see citing works
Neural mitochondrial Ca 2+ capacity impairment precedes the onset of motor symptoms in G93A Cu/Zn‐superoxide dismutase mutant mice
Damiano, M. G., Starkov, A. A., Petri, S., Kipiani, K., Kiaei, M., Mattiazzi, M., Beal, M. F., & Manfredi, G. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03619.x · Cited by 247 · see citing works
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Amyotrophic lateral sclerosis: A proposed mechanism
Okado‐Matsumoto, A., & Fridovich, I. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.132260399 · Cited by 247 · see citing works
Association of DJ-1 and parkin mediated by pathogenic DJ-1 mutations and oxidative stress
Moore, D. J., Zhang, L., Troncoso, J. C., Lee, M. K., Hattori, N., Mizuno, Y., Dawson, T. M., & Dawson, V. L. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddi007 · Cited by 245 · see citing works
Mitochondrial complex I and IV activities in leukocytes from patients with parkin mutations
Müftüoğlu, M., Elibol, B., Dalmızrak, Ö., Ercan, A., Kulaksiz-Erkmen, G., Öğüş, İ. H., Dalkara, T., & Özer, N. (2003) · Movement Disorders · doi:10.1002/mds.10695 · Cited by 237 · see citing works
Mutational analysis of DJ-1 in Drosophila implicates functional inactivation by oxidative damage and aging
Meulener, M. C., Xu, K., Thomson, L., Ischiropoulos, H., & Bonini, N. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601891103 · Cited by 230 · see citing works
Mice lacking alpha-synuclein are resistant to mitochondrial toxins
Klivènyi, P., Siwek, D. F., Gardian, G., Yang, L., Starkov, A. A., Cléren, C., Ferrante, R. J., Kowall, N. W., Abeliovich, A., & Beal, M. F. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.08.018 · Cited by 213 · see citing works
Self-citation
Association of PINK1 and DJ-1 confers digenic inheritance of early-onset Parkinson's disease
Tang, B., Xiong, H., Sun, P., Zhang, Y., Wang, D., Hu, Z., Zhu, Z.-H., Ma, H., Pan, Q., Xia, J., et al. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl104 · Cited by 213 · see citing works
Induction of hyperphosphorylated tau in primary rat cortical neuron cultures mediated by oxidative stress and glycogen synthase kinase-3
Lovell, M., Xiong, S., Xie, C.-S., Davies, P., & Markesbery, W. (2005) · Journal of Alzheimer's Disease · doi:10.3233/jad-2004-6610 · Cited by 207 · see citing works
Chronic mitochondrial energy impairment produces selective striatal degeneration and abnormal choreiform movements in primates
Brouillet, M. (1995) · Medical Entomology and Zoology · Cited by 190 · see citing works
Mitochondrial DNA haplogroup cluster UKJT reduces the risk of PD
Pyle, A., Foltynie, T., Tiangyou, W., Lambert, C., Keers, S. M., Allcock, L. M., Davison, J., Lewis, S. J. G., Perry, R. H., Barker, R. A., et al. (2005) · Annals of Neurology · doi:10.1002/ana.20417 · Cited by 176 · see citing works
Strikingly higher frequency in centenarians and twins of mtDNA mutation causing remodeling of replication origin in leukocytes
Zhang, J., Asin-Cayuela, J., Fish, J. L., Michikawa, Y., Bonafè, M., Olivieri, F., Passarino, G., Benedictis, G. D., Franceschi, C., & Attardi, G. M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.242719399 · Cited by 166 · see citing works
Mitochondrial Localization of Mutant Superoxide Dismutase 1 Triggers Caspase-dependent Cell Death in a Cellular Model of Familial Amyotrophic Lateral Sclerosis*
Takeuchi, H., Kobayashi, Y., Ishigaki, S., Doyu, M., & Sobue, G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m209356200 · Cited by 154 · see citing works
Human brain contains high levels of heteroplasmy in the noncoding regions of mitochondrial DNA.
JAZIN, E. E., Cavelier, L. B., Eriksson, I., Oreland, L., & Gyllensten, U. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.22.12382 · Cited by 144 · see citing works
Familial multisystem degeneration with parkinsonism associated with the 11778 mitochondrial DNA mutation
Simon, D. K., Pulst, S. M., Sutton, J. P., Browne, S. E., Beal, M. F., & Johns, D. R. (1999) · Neurology · doi:10.1212/wnl.53.8.1787 · Cited by 141 · see citing works
Self-citation
Somatic mitochondrial DNA mutations in cortex and substantia nigra in aging and Parkinson’s disease
Simon, D. K., Lin, M. T., Zheng, L., Liu, G.-J., Ahn, C. H., Kim, L. M., Mauck, W. M., Twu, F., Beal, M. F., & Johns, D. R. (2004) · Neurobiology of Aging · doi:10.1016/s0197-4580(03)00037-x · Cited by 118 · see citing works
Self-citation
Mitochondrial DNA and ageing
Trifunović, A. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.03.003 · Cited by 110 · see citing works
Does the mitochondrial genome play a role in the etiology of Alzheimer’s disease?
Elson, J. L., Herrnstadt, C., Preston, G., Thal, L. J., Morris, C. M., Edwardson, J. A., Beal, M. F., Turnbull, D. M., & Howell, N. (2006) · Human Genetics · doi:10.1007/s00439-005-0123-8 · Cited by 100 · see citing works
Self-citation
Point Mutations of the mtDNA Control Region in Normal and Neurodegenerative Human Brains
Chinnery, P. F., Taylor, G. A., Howell, N., Brown, D. T., Parsons, T. J., & Turnbull, D. M. (2001) · The American Journal of Human Genetics · doi:10.1086/318204 · Cited by 88 · see citing works
Sequence Analysis of the Entire Mitochondrial Genome in Parkinson's Disease
Vives-Bauzá, C., Andreu, A. L., Manfredi, G., Beal, M. F., Janetzky, B., Gruenewald, T. H., & Lin, M. T. S. (2002) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2002.6388 · Cited by 73 · see citing works
Self-citation
DJ‐1 is present in a large molecular complex in human brain tissue and interacts with α‐synuclein
Meulener, M. C., Graves, C. L., Sampathu, D. M., Armstrong‐Gold, C. E., Bonini, N. M., & Giasson, B. I. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03145.x · Cited by 71 · see citing works
Selective increase in cellular Aβ42 is related to apoptosis but not necrosis
Ohyagi, Y., Yamada, T., Nishioka, K., Clarke, N. J., Tomlinson, A. J., Naylor, S., Nakabeppu, Y., Kira, J., & Younkin, S. G. (2000) · Neuroreport · doi:10.1097/00001756-200001170-00033 · Cited by 69 · see citing works
Alzheimer's disease-associated amyloid beta interacts with the human serine protease HtrA2/Omi
Park, H., Seong, Y.-M., Choi, J.-Y., Kang, S., & Rhim, H. (2004) · Neuroscience Letters · doi:10.1016/j.neulet.2003.11.068 · Cited by 67 · see citing works
Mechanisms of transcriptional dysregulation in Huntington's disease
Luthi‐Carter, R., & Cha, J.-H. J. (2003) · Clinical Neuroscience Research · doi:10.1016/s1566-2772(03)00059-8 · Cited by 56 · see citing works
Erratum: The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-β production
Pastorino, L., Sun, A., Lu, P., Zhou, X., Balaštík, M., Finn, G., Wulf, G. M., Lim, J., Li, S., Li, X., et al. (2007) · Nature · doi:10.1038/nature05606 · Cited by 55 · see citing works
Low Mutational Burden of Individual Acquired Mitochondrial DNA Mutations in Brain
Simon, D. K., Lin, M. T. S., Ahn, C., Liu, G.-J., Gibson, G. E., Beal, M. F., & Johns, D. R. (2001) · Genomics · doi:10.1006/geno.2001.6515 · Cited by 34 · see citing works
Self-citation
Progressive Loss of Striatal Neurons Causes Motor Dysfunction in MND2 Mutant Mice and Is Not Prevented by Bcl-2
Rathke‐Hartlieb, S., Schlomann, U., Heimann, P., Meisler, M. H., Jockusch, H., & Bartsch, J. W. (2002) · Experimental Neurology · doi:10.1006/exnr.2002.7868 · Cited by 33 · see citing works
Mitochondrial genotypes and cytochrome b variants associated with longevity or Parkinson's disease
Tanaka, M. (2002) · Journal of Neurology · doi:10.1007/s00415-002-1203-5 · Cited by 28 · see citing works

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Regulation of cancer cell metabolism
Cairns, R. A., Harris, I. S., & Mak, T. W. (2011) · Nature Reviews Cancer · doi:10.1038/nrc2981 · Cited by 4,744 · see citing works
Pathological roles of MAPK signaling pathways in human diseases
Kim, E. K., & Choi, E.-J. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.12.009 · Cited by 2,472 · see citing works
Molecular mechanisms of necroptosis: an ordered cellular explosion
Vandenabeele, P., Galluzzi, L., Vanden Berghe, T., & Kroemer, G. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2970 · Cited by 2,382 · see citing works
Signal transduction by reactive oxygen species
Finkel, T. (2011) · Journal of Cell Biology · doi:10.1083/jcb.201102095 · Cited by 2,322 · see citing works
Protein Phase Separation: A New Phase in Cell Biology
Boeynaems, S., Alberti, S., Fawzi, N. L., Mittag, T., Polymenidou, M., Rousseau, F., Schymkowitz, J. W. H., Shorter, J., Wolozin, B. L., Bosch, L. V. D., et al. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.02.004 · Cited by 1,954 · see citing works
The Role of Oxidative Stress in Parkinson's Disease
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Hallmarks of neurodegenerative diseases
Wilson, D. M., Cookson, M. R., Van Den Bosch, L., Zetterberg, H., Holtzman, D. M., & Dewachter, I. (2023) · Cell · doi:10.1016/j.cell.2022.12.032 · Cited by 1,789 · see citing works
Synaptic Energy Use and Supply
Harris, J. J., Jolivet, R., & Attwell, D. (2012) · Neuron · doi:10.1016/j.neuron.2012.08.019 · Cited by 1,747 · see citing works
Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia-induced mitophagy in mammalian cells
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Mitochondria-Targeted Triphenylphosphonium-Based Compounds: Syntheses, Mechanisms of Action, and Therapeutic and Diagnostic Applications
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Mitochondrial dysfunction and oxidative stress in metabolic disorders - A step towards mitochondria based therapeutic strategies
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 · see citing works
Glutathione Peroxidase 4 Senses and Translates Oxidative Stress into 12/15-Lipoxygenase Dependent- and AIF-Mediated Cell Death
Seiler, A., Schneider, M., Förster, H., Roth, S., Wirth, E. K., Culmsee, C., Plesnila, N., Kremmer, E., Rådmark, O., Wurst, W., et al. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.07.005 · Cited by 1,470 · see citing works
PGC-1α mediates mitochondrial biogenesis and oxidative phosphorylation in cancer cells to promote metastasis
LeBleu, V. S., O’Connell, J. T., Herrera, K. N. G., Wikman, H., Pantel, K., Haigis, M. C., de Carvalho, F. M., Damascena, A. S., Chinen, L. T. D., Rocha, R. M., et al. (2014) · Nature Cell Biology · doi:10.1038/ncb3039 · Cited by 1,412 · see citing works
Trinucleotide Repeat Disorders
Orr, H. T., & Zoghbi, H. Y. (2007) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.29.051605.113042 · Cited by 1,365 · see citing works
The role of oxidative stress in neurodegenerative diseases
Kim, G. H., Kim, J. E., Rhie, S. J., & Yoon, S. (2015) · Experimental Neurobiology · doi:10.5607/en.2015.24.4.325 · Cited by 1,355 · see citing works
Oxidative stress, mitochondrial damage and neurodegenerative diseases.
Guo, C., Sun, L., Chen, X., & Zhang, D. (2013) · PubMed Central · doi:10.3969/j.issn.1673-5374.2013.21.009 · Cited by 1,308 · see citing works
Pesticides and human chronic diseases: Evidences, mechanisms, and perspectives
Mostafalou, S., & Abdollahi, M. R. (2013) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2013.01.025 · Cited by 1,266 · see citing works
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 · see citing works
Spermidine in health and disease
Madeo, F., Eisenberg, T., Pietrocola, F., & Kroemer, G. (2018) · Science · doi:10.1126/science.aan2788 · Cited by 1,154 · see citing works
Multi-target-Directed Ligands To Combat Neurodegenerative Diseases
Cavalli, A., Bolognesi, M. L., Minarini, A., Rosini, M., Tumiatti, V., Recanatini, M., & Melchiorre, C. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm7009364 · Cited by 1,152 · see citing works
Mitochondrial Import and Accumulation of α-Synuclein Impair Complex I in Human Dopaminergic Neuronal Cultures and Parkinson Disease Brain
Devi, L., Raghavendran, V., Prabhu, B. M., Avadhani, N. G., & Anandatheerthavarada, H. K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m710012200 · Cited by 1,087 · see citing works
Mechanisms of Age-Related Macular Degeneration
Ambati, J., & Fowler, B. J. (2012) · Neuron · doi:10.1016/j.neuron.2012.06.018 · Cited by 1,029 · see citing works
Oxidative Stress, Mitochondrial Dysfunction, and Aging
Cui, H., Kong, Y., & Zhang, H. (2011) · Journal of Signal Transduction · doi:10.1155/2012/646354 · Cited by 1,036 · see citing works
Compromised MAPK signaling in human diseases: an update
Kim, E., & Choi, E. (2015) · Archives of Toxicology · doi:10.1007/s00204-015-1472-2 · Cited by 1,017 · see citing works
Mitochondrial fragmentation in neurodegeneration.
Knott, A. B., Perkins, G., Schwarzenbacher, R., & Bossy-Wetzel, E. (2008) · Nature Reviews Neuroscience · doi:10.1038/nrn2417 · Cited by 1,002 · see citing works
Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes
Hamanaka, R. B., & Chandel, N. S. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.04.002 · Cited by 1,011 · see citing works
Assessment of mitochondrial respiratory chain enzymatic activities on tissues and cultured cells
Spinazzi, M., Casarin, A., Pertegato, V., Salviati, L., & Angelini, C. I. (2012) · Nature Protocols · doi:10.1038/nprot.2012.058 · Cited by 989 · see citing works
Mitochondrial Glutathione, a Key Survival Antioxidant
Marı́, M., Morales, A., Colell, A., García‐Ruiz, C., & Fernández-Checa, J. C. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2695 · Cited by 986 · see citing works
Amyloid beta, mitochondrial dysfunction and synaptic damage: Implications for cognitive decline in aging and Alzheimer’s disease
Reddy, P. H., & Beal, M. F. (2008) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2007.12.002 · Cited by 975 · see citing works
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Mechanism of Oxidative Stress in Neurodegeneration
Gandhi, S., & Abramov, A. Y. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/428010 · Cited by 964 · see citing works
Identification of miRNA changes in Alzheimer's disease brain and CSF yields putative biomarkers and insights into disease pathways
Cogswell, J. P., Ward, J., Taylor, I. A., Waters, M., Shi, Y., Cannon, B., Kelnar, K., Kemppainen, J., Brown, D., Chen, C., et al. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-14103 · Cited by 943 · see citing works
Oxidative Stress in Human Pathology and Aging: Molecular Mechanisms and Perspectives
Hajam, Y. A., Rani, R., Ganie, S. Y., Sheikh, T. A., Javaid, D., Qadri, S. S., Pramodh, S., Alsulimani, A., Alkhanani, M. F., Harakeh, S., et al. (2022) · Cells · doi:10.3390/cells11030552 · Cited by 915 · see citing works
Predicting Age Using Neuroimaging: Innovative Brain Ageing Biomarkers
Cole, J. H., & Franke, K. (2017) · Trends in Neurosciences · doi:10.1016/j.tins.2017.10.001 · Cited by 911 · see citing works
The secret life of NAD+: an old metabolite controlling new metabolic signaling pathways
Houtkooper, R. H., Cantó, C., Wanders, R. J., & Auwerx, J. (2010) · Endocrine Reviews · doi:10.1210/er.2009-0026 · Cited by 899 · see citing works
Glial Lipid Droplets and ROS Induced by Mitochondrial Defects Promote Neurodegeneration
Liu, L., Zhang, K., Sandoval, H., Yamamoto, S., Jaiswal, M., Sanz, E., Li, Z., Hui, J., Graham, B. H., Quintana, A., et al. (2015) · Cell · doi:10.1016/j.cell.2014.12.019 · Cited by 876 · see citing works
Oxidative Stress and Neurotoxicity
Sayre, L. M., Perry, G. L., & Smith, M. A. (2007) · Chemical Research in Toxicology · doi:10.1021/tx700210j · Cited by 868 · see citing works
The apoptotic effect of nanosilver is mediated by a ROS- and JNK-dependent mechanism involving the mitochondrial pathway in NIH3T3 cells
Hsin, Y.-H., Chen, C.-F., Huang, S., Shih, T., Lai, P., & Chueh, P. J. (2008) · Toxicology Letters · doi:10.1016/j.toxlet.2008.04.015 · Cited by 865 · see citing works
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 · see citing works
Mitochondria in oxidative stress, inflammation and aging: from mechanisms to therapeutic advances
Xu, X., Pang, Y., & Fan, X. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02253-4 · Cited by 939 · see citing works
Mitochondrial dysfunction in Parkinson's disease
Bose, A., & Beal, M. F. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13731 · Cited by 598 · see citing works
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The role of mitochondria in reactive oxygen species metabolism and signaling
Starkov, A. A. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1427.015 · Cited by 846 · see citing works
Mechanistic explanations how cell-mediated immune activation, inflammation and oxidative and nitrosative stress pathways and their sequels and concomitants play a role in the pathophysiology of unipolar depression
Leonard, B., & Maes, M. (2012) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2011.12.005 · Cited by 805 · see citing works
Discerning the Chemistry in Individual Organelles with Small‐Molecule Fluorescent Probes
Xu, W., Zeng, Z., Jiang, J., Chang, Y., & Yuan, L. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201510721 · Cited by 806 · see citing works
Oxidative Stress in Neurodegenerative Diseases: From Molecular Mechanisms to Clinical Applications
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Authors: Lin, M. T., & Beal, M. F.
Affiliations: Cornell University (US)
Corresponding author: Beal, M. Flint
ORCID: Beal, M. Flint
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2006-10
Volume: 443
Issue: 7113
Pages: 787-795
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature05292
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 › Neurology › Parkinson's Disease Mechanisms and Treatments
Health Sciences › Medicine › Epidemiology › 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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Mitochondrial Dysfunction and Oxidative Stress in Neurodegenerative Diseases

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