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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
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
Flagged first, then by citations
Cited by
Sorted by citations
Items 301–400 of 1,096
Yamada, Y., & Harashima, H. (2008) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2008.04.016 · Cited by 260
Quality Control of Mitochondrial ProteostasisPreprint
Baker, M. J., Tatsuta, T., & Langer, T. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a007559 · Cited by 271
Alonso‐Álvarez, C., BERTRAND, S., Faivre, B., & Sorci, G. (2007) · Functional Ecology · doi:10.1111/j.1365-2435.2007.01300.x · Cited by 258
Wnt signaling regulates mitochondrial physiology and insulin sensitivityPreprint
Yoon, J. C., Ng, A., Kim, B. H., Bianco, A. C., Xavier, R. J., & Elledge, S. J. (2010) · Genes & Development · doi:10.1101/gad.1924910 · Cited by 259
Fang, J., Nakamura, T., Cho, D., Gu, Z., & Lipton, S. A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705904104 · Cited by 257
Direct Activation of Bax Protein for Cancer Therapy
Liu, Z., Ding, Y., Ye, N., Wild, C., Chen, H., & Zhou, J. (2015) · Medicinal Research Reviews · doi:10.1002/med.21379 · Cited by 260
Rekatsina, M., Paladini, A., Piroli, A., Zis, P., Pergolizzi, J. V., & Varrassi, G. (2019) · Advances in Therapy · doi:10.1007/s12325-019-01148-5 · Cited by 262
Di Domenico, F., Tramutola, A., & Butterfield, D. A. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.10.490 · Cited by 253
Protein Degradation within Mitochondria: Versatile Activities of AAA Proteases and Other Peptidases
Koppen, M., & Langer, T. (2007) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230701380452 · Cited by 252
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
ERRα: a metabolic function for the oldest orphan
Villena, J. A., & Kralli, A. (2008) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2008.07.005 · Cited by 252
“Mitochondrial dysfunction and/or decreased PGC-1α/β levels have been associated with insulin resistance, type 2 diabetes, cardiovascular disease and neurodegenerative disorders [61-65].”
BackgroundImpairing the Mitochondrial Fission and Fusion Balance: A New Mechanism of Neurodegeneration
Knott, A. B., & Bossy‐Wetzel, E. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1427.030 · Cited by 263
Redox Proteomics: Chemical Principles, Methodological Approaches and Biological/Biomedical Promises
Bachi, A., Dalle‐Donne, I., & Scaloni, A. (2012) · Chemical Reviews · doi:10.1021/cr300073p · Cited by 265
Fukui, H., & Moraes, C. T. (2008) · Trends in Neurosciences · doi:10.1016/j.tins.2008.02.008 · Cited by 250
Mick, E., Titov, D. V., Skinner, O. S., Sharma, R., Jourdain, A. A., & Mootha, V. K. (2020) · eLife · doi:10.7554/elife.49178 · Cited by 252
Abnormalities of Mitochondrial Dynamics in Neurodegenerative Diseases
Gao, J., Wang, L., Liu, J., Xie, F., Su, B., & Wang, X. (2017) · Antioxidants · doi:10.3390/antiox6020025 · Cited by 250
Physiology and Pathology of Calcium Signaling in the Brain
Kawamoto, E. M., Vivar, C., & Camandola, S. (2012) · Frontiers in Pharmacology · doi:10.3389/fphar.2012.00061 · Cited by 264
Emerging Applications of Nanotechnology in Healthcare Systems: Grand Challenges and Perspectives
Anjum, S., Ishaque, S., Fatima, H., Farooq, W., Hano, C., Abbasi, B. H., & Anjum, I. (2021) · Pharmaceuticals · doi:10.3390/ph14080707 · Cited by 273
In-depth proteomic analysis of mammalian mitochondria-associated membranes (MAM)
Poston, C. N., Krishnan, S. C., & Bazemore‐Walker, C. R. (2013) · Journal of Proteomics · doi:10.1016/j.jprot.2012.12.018 · Cited by 255
Mitochondrial Energy Metabolism and Redox Signaling in Brain Aging and Neurodegeneration
Yin, F., Boveris, A., & Cadenas, E. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4774 · Cited by 251
Sun, Y., Vashisht, A. A., Tchieu, J. H., Wohlschlegel, J. A., & Dreier, L. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.419721 · Cited by 255
Chemical Design of Activatable Photoacoustic Probes for Precise Biomedical Applications
Liu, Y., Teng, L., Yin, B., Meng, H., Yin, X., Huan, S., Song, G., & Zhang, X. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00875 · Cited by 250
Dual control of mitochondrial biogenesis by sirtuin 1 and sirtuin 3
Brenmoehl, J., & Hoeflich, A. (2013) · Mitochondrion · doi:10.1016/j.mito.2013.04.002 · Cited by 248
Reddy, P. H., Mańczak, M., Mao, P., Calkins, M. J., Reddy, A. P., & Shirendeb, U. P. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100504 · Cited by 247
“Therapeutic uses of natural astaxanthin: An evidence-based review focused on human clinical trials”
Donoso, A., González-Durán, J., Agurto-Muñoz, A., González, P. A., & Agurto-Muñoz, C. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105479 · Cited by 252
Potential Role of Olive Oil Phenolic Compounds in the Prevention of Neurodegenerative Diseases
Rodríguez-Morató, J., Xicota, L., Fitó, M., Farré, M., Dierssen, M., & de la Torre, R. (2015) · Molecules · doi:10.3390/molecules20034655 · Cited by 249
Gasset-Rosa, F., Chillón-Marinas, C., Goginashvili, A., Atwal, R. S., Artates, J. W., Tabet, R., Wheeler, V. C., Bang, A. G., Cleveland, D. W., & Lagier‐Tourenne, C. (2017) · Neuron · doi:10.1016/j.neuron.2017.03.027 · Cited by 233
Alzheimer’s Disease: From Firing Instability to Homeostasis Network Collapse
Frère, S. G. A., & Slutsky, I. (2018) · Neuron · doi:10.1016/j.neuron.2017.11.028 · Cited by 242
Jamwal, S., Blackburn, J. K., & Elsworth, J. D. (2021) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107705 · Cited by 236
Danger-associated molecular patterns in Alzheimer’s disease
Venegas, C., & Heneka, M. T. (2017) · Journal of Leukocyte Biology · doi:10.1189/jlb.3mr0416-204r · Cited by 236
Maternal family history of Alzheimer's disease predisposes to reduced brain glucose metabolism
Mosconi, L., Brys, M., Switalski, R., Mistur, R., Glodzik, L., Pirraglia, E., Tsui, W., De Santi, S., & de Leon, M. J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705036104 · Cited by 237
Mitochondrial Medicine: Pharmacological targeting of mitochondria in disease
Armstrong, J. S. (2007) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0707288 · Cited by 239
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
The Role of Mitochondria in Inflammation: From Cancer to Neurodegenerative Disorders
Missiroli, S., Genovese, I., Perrone, M., Vezzani, B., Vitto, V. A. M., & Giorgi, C. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9030740 · Cited by 235
PINK1-PRKN mediated mitophagy: differences between in vitro and in vivo models
Han, R., Liu, Y., Li, S., Li, X., & Yang, W. (2022) · Autophagy · doi:10.1080/15548627.2022.2139080 · Cited by 247
Mitochondrial dysfunction: A potential link between neuroinflammation and neurodegeneration?
Witte, M. E., Geurts, J. J. G., de Vries, H. E., van der Valk, P., & van Horssen, J. (2010) · Mitochondrion · doi:10.1016/j.mito.2010.05.014 · Cited by 239
Oxidative stress in pregnancy and reproduction
Duhig, K. E., Chappell, L. C., & Shennan, A. H. (2016) · Obstetric Medicine · doi:10.1177/1753495x16648495 · Cited by 235
Venkateshappa, C., Harish, G., Mahadevan, A., Srinivas Bharath, M. M., & Shankar, S. K. (2012) · Neurochemical Research · doi:10.1007/s11064-012-0755-8 · Cited by 232
Cha, M.-Y., Han, S.-H., Son, S. M., Hong, H., Choi, Y.-J., Byun, J., & Mook‐Jung, I. (2012) · PLoS ONE · doi:10.1371/journal.pone.0034929 · Cited by 236
Cudkowicz, M., van den Berg, L. H., Shefner, J. M., Mitsumoto, H., Mora, J. S., Ludolph, A. C., Hardiman, O. M., Bozik, M. E., Ingersoll, E. W., Archibald, D., et al. (2013) · The Lancet Neurology · doi:10.1016/s1474-4422(13)70221-7 · Cited by 232
Biomimetic Design of Mitochondria‐Targeted Hybrid Nanozymes as Superoxide Scavengers
Zhang, Y., Khalique, A., Du, X., Gao, Z., Wu, J., Zhang, X., Zhang, R., Sun, Z., Liu, Q., Xu, Z., et al. (2021) · Advanced Materials · doi:10.1002/adma.202006570 · Cited by 233
Soluble forms of tau are toxic in Alzheimer's disease
Kopeikina, K., Hyman, B., & Spires-Jones, T. (2012) · Translational Neuroscience · doi:10.2478/s13380-012-0032-y · Cited by 232
Is Caffeine a Good Scavenger of Oxygenated Free Radicals?
León‐Carmona, J. R., & Galano, A. (2011) · The Journal of Physical Chemistry B · doi:10.1021/jp201383y · Cited by 232
Role of sigma-1 receptors in neurodegenerative diseases
Nguyen, L., Lucke-Wold, B. P., Mookerjee, S. A., Cavendish, J. Z., Robson, M. J., Scandinaro, A. L., & Matsumoto, R. R. (2014) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2014.12.005 · Cited by 236
Yang, L., Calingasan, N. Y., Wille, E. J., Cormier, K., Smith, K., Ferrante, R. J., & Beal, M. F. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06074.x · Cited by 237
Self-citationCalcium signaling in Alzheimer's disease & therapies
Tong, B. C., Wu, A. J., Li, M., & Cheung, K. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2018.07.018 · Cited by 243
Mitochondrial Medicine for Aging and Neurodegenerative Diseases
Reddy, P. H. (2008) · NeuroMolecular Medicine · doi:10.1007/s12017-008-8044-z · Cited by 230
Is There a Link between Mitochondrial Reserve Respiratory Capacity and Aging?
Desler, C., Hansen, T. L., Frederiksen, J. H., Espersen, M. L. M., Singh, K. K., & Rasmussen, L. J. (2012) · Journal of Aging Research · doi:10.1155/2012/192503 · Cited by 237
Sarcopenia and Muscle Aging: A Brief Overview
Dao, T., Green, A. E., Kim, Y.-A., Bae, S., Ha, K., Gariani, K., Lee, M.-R., Menzies, K. J., & Ryu, D. (2020) · Endocrinology and Metabolism · doi:10.3803/enm.2020.405 · Cited by 249
Peroxisomal alterations in Alzheimer’s disease
Kou, J., Kovacs, G. G., Höftberger, R., Kulik, W., Brodde, A., Forss-Petter, S., Hönigschnabl, S., Gleiss, A., Brügger, B., Wanders, R., et al. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0836-9 · Cited by 227
“Agebased metabolic changes may lead to an imbalance of metabolites and/or second messengers promoting mitochondrial, endosomal–lysosomal and peroxisomal dysfunctions, which might be involved in the initiation of neuropathological events in AD [26, 32].”
BackgroundMitochondria as a Therapeutic Target for Aging and Neurodegenerative Diseases
Reddy, P. H., & Reddy, T. P. (2011) · Current Alzheimer Research · doi:10.2174/156720511795745401 · Cited by 233
On the Neuroprotective Role of Astaxanthin: New Perspectives?
Galasso, C., Orefice, I., Pellone, P., Cirino, P., Miele, R., Ianora, A., Brunet, C., & Sansone, C. (2018) · Marine Drugs · doi:10.3390/md16080247 · Cited by 231
Marchesi, V. T. (2011) · The FASEB Journal · doi:10.1096/fj.11-0102ufm · Cited by 232
Calí, T., Ottolini, D., Negro, A., & Brini, M. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.01.004 · Cited by 231
Mechanisms of Mitochondrial Dysfunction in Alzheimer’s Disease
Cadonic, C., Sabbir, M. G., & Albensi, B. C. (2016) · Molecular Neurobiology · doi:10.1007/s12035-015-9515-5 · Cited by 226
He, C., Wang, J., Zhang, Z., Yang, M., Li, Y., Tian, X., Ma, T., Tao, J., Zhu, K., Song, Y., et al. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17060939 · Cited by 226
Metabolic Methanol: Molecular Pathways and Physiological Roles
Dorokhov, Y. L., Shindyapina, A. V., Sheshukova, E. V., & Komarova, T. V. (2015) · Physiological Reviews · doi:10.1152/physrev.00034.2014 · Cited by 235
Alpha-Synuclein Function and Dysfunction on Cellular Membranes
Snead, D., & Eliezer, D. (2014) · Experimental Neurobiology · doi:10.5607/en.2014.23.4.292 · Cited by 229
Trichloroethylene: Parkinsonism and complex 1 mitochondrial neurotoxicity
Gash, D. M., Rutland, K., Hudson, N. L., Sullivan, P. G., Bing, G., Cass, W. A., Pandya, J. D., Liu, M., Choi, D. Y., Hunter, R. L., et al. (2007) · Annals of Neurology · doi:10.1002/ana.21288 · Cited by 223
Jiwaji, Z., Tiwari, S. S., Avilés-Reyes, R. X., Hooley, M., Hampton, D., Torvell, M., Johnson, D. A., McQueen, J., Baxter, P., Sabari-Sankar, K., et al. (2022) · Nature Communications · doi:10.1038/s41467-021-27702-w · Cited by 223
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
The neurochemical profile quantified by in vivo 1H NMR spectroscopy
Duarte, J. M. N., Lei, H., Mlynárik, V., & Rolf Gruetter, A. (2011) · NeuroImage · doi:10.1016/j.neuroimage.2011.12.038 · Cited by 230
Diseases caused by defects of mitochondrial carriers: A review
Palmieri, F. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.03.008 · Cited by 229
Molecular Hydrogen as a Novel Antioxidant
Ohta, S. (2015) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2014.11.038 · Cited by 226
Challenging microalgal vitamins for human health
Del Mondo, A., Smerilli, A., Sané, E., Sansone, C., & Brunet, C. (2020) · Microbial Cell Factories · doi:10.1186/s12934-020-01459-1 · Cited by 220
Germline Energetics, Aging, and Female Infertility
Tilly, J. L., & Sinclair, D. A. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.05.007 · Cited by 223
Dumont, M., Wille, E., Stack, C., Calingasan, N. Y., Beal, M. F., & Lin, M. T. (2009) · The FASEB Journal · doi:10.1096/fj.09-132928 · Cited by 221
Self-citationDysfunctional Mitochondria and Mitophagy as Drivers of Alzheimer’s Disease Pathogenesis
Chakravorty, A., Jetto, C. T., & Manjithaya, R. R. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00311 · Cited by 225
Wang, L., Yuan, L., Zeng, X. L., Peng, J., Ni, Y. Z., Er, J. C., Wang, X., Agrawalla, B. K., Su, D., Kim, B., et al. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201510003 · Cited by 219
Dong, B., Song, X., Kong, X., Wang, C., Tang, Y., Liu, Y., & Lin, W. (2016) · Advanced Materials · doi:10.1002/adma.201602939 · Cited by 217
The Metallothionein/Thionein System: An Oxidoreductive Metabolic Zinc Link
Bell, S. G., & Vallée, B. L. (2008) · ChemBioChem · doi:10.1002/cbic.200800511 · Cited by 219
Age-Related Accumulation of Somatic Mitochondrial DNA Mutations in Adult-Derived Human iPSCs
Kang, E., Wang, X., Tippner-Hedges, R., Ma, H., Folmes, C. D. L., Gutiérrez, N. M., Lee, Y., Dyken, C. V., Ahmed, R., Li, Y., et al. (2016) · Cell stem cell · doi:10.1016/j.stem.2016.02.005 · Cited by 216
Astaxanthin: A Potential Mitochondrial-Targeted Antioxidant Treatment in Diseases and with Aging
Sztretye, M. T., Dienes, B., Gönczi, M., Czirják, T., Csernoch, L. J., László, A., Szentesi, P., & Keller-Pintér, A. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/3849692 · Cited by 224
Jauhari, A., Baranov, S. V., Suofu, Y., Kim, J., Singh, T., Yablonska, S., Li, F., Wang, X., Oberly, P. J., Minnigh, M. B., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci135026 · Cited by 215
Early oxidative damage underlying neurodegeneration in X-adrenoleukodystrophy
Fourcade, S., Lopez-Erauskin, J., Galino, J., Duval, C., Naudi, A., Jove, M., Kemp, S., Villarroya, F., Ferrer, I., Pamplona, R., et al. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn085 · Cited by 214
Outstanding Questions in Mitophagy: What We Do and Do Not Know
Montava‐Garriga, L., & Ganley, I. G. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.06.032 · Cited by 218
Spaas, J., van Veggel, L., Schepers, M., Tiane, A., van Horssen, J., Wilson, D. M., Moya, P. R., Piccart, E., Hellings, N., Eijnde, B. O., et al. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03802-0 · Cited by 224
Reactive Oxygen Species in Photodynamic Therapy: Mechanisms of Their Generation and Potentiation
Dąbrowski, J. M. (2017) · Advances in inorganic chemistry · doi:10.1016/bs.adioch.2017.03.002 · Cited by 223
Zhang, Z., Huang, Q., Zhao, D., Lian, F., Li, X., & Qi, W. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1112363 · Cited by 236
Maharjan, S., Oku, M., Tsuda, M., Hoseki, J., & Sakai, Y. (2014) · Scientific Reports · doi:10.1038/srep05896 · Cited by 212
Smoking-induced Skeletal Muscle Dysfunction. From Evidence to Mechanisms
Degens, H., Gayan‐Ramirez, G., & van Hees, H. W. H. (2015) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201410-1830pp · Cited by 227
Mercury Involvement in Neuronal Damage and in Neurodegenerative Diseases
Cariccio, V. L., Samà, A., Bramanti, P., & Mazzon, E. (2018) · Biological Trace Element Research · doi:10.1007/s12011-018-1380-4 · Cited by 246
Mitochondrial dysfunction in microglia: a novel perspective for pathogenesis of Alzheimer’s disease
Li, Y., Xia, X., Wang, Y., & Zheng, J. (2022) · Journal of Neuroinflammation · doi:10.1186/s12974-022-02613-9 · Cited by 231
Mitochondrial Dysfunction and Synaptic Transmission Failure in Alzheimer’s Disease
Guo, L., Tian, J., & Du, H. (2017) · Journal of Alzheimer’s Disease · doi:10.3233/jad-160702 · Cited by 211
Bosch, M., Marı́, M., Herms, A., Fernández, A. M. C., Fajardo, A., Kassan, A., Giralt, A., Colell, A., Balgoma, D., Barbero, E., et al. (2011) · Current Biology · doi:10.1016/j.cub.2011.03.030 · Cited by 211
Tan, K., Li, C., Li, Y., Fei, J., Yang, B., Fu, Y., & Li, F. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.6b04020 · Cited by 211
Huntington disease models and human neuropathology: similarities and differences
Vonsattel, J. P. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0306-6 · Cited by 210
Transglutaminase 2 inhibitors and their therapeutic role in disease states
Siegel, M., & Khosla, C. (2007) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2007.05.003 · Cited by 210
Chen, H.-K., Ji, Z.-S., Dodson, S. E., Miranda, R. D., Rosenblum, C. I., Reynolds, I. J., Freedman, S. B., Weisgraber, K. H., Huang, Y., & Mahley, R. W. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.151084 · Cited by 209
Berberine and neurodegeneration: A review of literature
Ahmed, T., Gilani, A. H., Abdollahi, M. R., Daglia, M., Nabavi, S. F., & Nabavi, S. M. (2015) · Pharmacological Reports · doi:10.1016/j.pharep.2015.03.002 · Cited by 212
Nand, S., Yadav, S. K., Singh, D., & Singh, S. P. (2015) · Journal of Chemical Neuroanatomy · doi:10.1016/j.jchemneu.2015.12.002 · Cited by 210
Connolly, N. M. C., Theurey, P., Ádám‐Vizi, V., Bazan, N. G., Bernardi, P., Bolaños, J. P., Culmsee, C., Dawson, V. L., Deshmukh, M., Duchen, M. R., et al. (2017) · Cell Death and Differentiation · doi:10.1038/s41418-017-0020-4 · Cited by 218
Suppressors of superoxide production from mitochondrial complex III
Orr, A. L., Vargas, L., Turk, C. N., Baaten, J., Matzen, J., Dardov, V. J., Attle, S. J., Li, J., Quackenbush, D., Goncalves, R. L. S., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1910 · Cited by 207
Parihar, M. S., Parihar, A., Fujita, M., Hashimoto, M., & Ghafourifar, P. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.05.008 · Cited by 217
The disulfide relay system of mitochondria is connected to the respiratory chain
Bihlmaier, K., Mesecke, N., Terziyska, N., Bien, M., Hell, K., & Herrmann, J. M. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200707123 · Cited by 210
Neurons express hemoglobin α‐ and β‐chains in rat and human brains
Richter, F., Meurers, B. H., Zhu, C., Medvedeva, V. P., & Chesselet, M. (2009) · The Journal of Comparative Neurology · doi:10.1002/cne.22062 · Cited by 202
Gollihue, J. L., Patel, S. P., Eldahan, K. C., Cox, D. H., Donahue, R. R., Taylor, B. K., Sullivan, P. G., & Rabchevsky, A. G. (2018) · Journal of Neurotrauma · doi:10.1089/neu.2017.5605 · Cited by 209
Resveratrol Improves Motoneuron Function and Extends Survival in SOD1G93A ALS Mice
Mancuso, R., del Valle, J., Mòdol, L., Martínez‐Muriana, A., Granado‐Serrano, A. B., Ramírez‐Núñez, O., Pallàs, M., Portero‐Otín, M., Osta, R., & Navarro, X. (2014) · Neurotherapeutics · doi:10.1007/s13311-013-0253-y · Cited by 212
Fluorescent Diagnostic Probes in Neurodegenerative Diseases
Zhou, J., Jangili, P., Son, S., Ji, M. S., Won, M., & Kim, J. S. (2020) · Advanced Materials · doi:10.1002/adma.202001945 · Cited by 204
Bridges, R., Lutgen, V., Lobner, D., & Baker, D. A. (2012) · Pharmacological Reviews · doi:10.1124/pr.110.003889 · Cited by 205
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
