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 801–900 of 1,096
A Boronate-Caged [18F]FLT Probe for Hydrogen Peroxide Detection Using Positron Emission Tomography
Carroll, V., Michel, B. W., Blecha, J. E., VanBrocklin, H. F., Keshari, K. R., Wilson, D. M., & Chang, C. J. (2014) · Journal of the American Chemical Society · doi:10.1021/ja509198w · Cited by 125
Prospects for therapeutic mitochondrial transplantation
Gollihue, J. L., & Rabchevsky, A. G. (2017) · Mitochondrion · doi:10.1016/j.mito.2017.05.007 · Cited by 125
Chen, J., Liu, X., Li, Z., Qi, A., Yao, P., Zhou, Z., Dong, T. T.-X., & Tsim, K. W. K. (2017) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2017/3019568 · Cited by 124
Li, X., Jiang, M., Lam, J. W. Y., Tang, B. Z., & Qu, J. Y. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b06273 · Cited by 124
Members, E. W. E., Terron, A., Bal-Price, A., Paini, A., Monnet-Tschudi, F., Bennekou, S. H., Leist, M., & Schildknecht, S. (2018) · Archives of Toxicology · doi:10.1007/s00204-017-2133-4 · Cited by 124
Autophagy in Age-Associated Neurodegeneration
Metaxakis, A., Ploumi, C., & Tavernarakis, N. (2018) · Cells · doi:10.3390/cells7050037 · Cited by 127
Aborode, A. T., Pustake, M., Awuah, W. A., Alwerdani, M., Shah, P., Yarlagadda, R., Ahmad, S., Silva Correia, I. F., Chandra, A., Nansubuga, E. P., et al. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/7934442 · Cited by 124
Klotho, Oxidative Stress, and Mitochondrial Damage in Kidney Disease
Donate‐Correa, J., Martín-Carro, B., Cannata-Andía, J. B., Fernández, C. M., & Navarro‐González, J. F. (2023) · Antioxidants · doi:10.3390/antiox12020239 · Cited by 137
Carotenoids can act as antioxidants by oxidizing the superoxideradical anion
Galano, A., Vargas, R., & Martı́nez, A. (2009) · Physical Chemistry Chemical Physics · doi:10.1039/b917636e · Cited by 126
Zeviani, M., & Carelli, V. (2007) · Current Opinion in Neurology · doi:10.1097/wco.0b013e3282ef58cd · Cited by 128
Gray, N. E., Harris, C. J., Quinn, J. F., & Soumyanath, A. (2016) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2016.01.013 · Cited by 123
A ratiometric two-photon probe for quantitative imaging of mitochondrial pH values
Sarkar, A. R., Heo, C. H., Xu, L., Lee, H. W., Si, H. Y., Byun, J. W., & Kim, H. M. (2015) · Chemical Science · doi:10.1039/c5sc03708e · Cited by 123
The Role of Mitochondrial DNA in Mediating Alveolar Epithelial Cell Apoptosis and Pulmonary Fibrosis
Kim, S.-J., Cheresh, P., Jablonski, R. P., Williams, D. B., & Kamp, D. W. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms160921486 · Cited by 125
Sirtuins in neurodegenerative diseases: an update on potential mechanisms
Min, S., Sohn, P., Cho, S.-H., Swanson, R. A., & Gan, L. (2013) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2013.00053 · Cited by 124
Yao, J., Rettberg, J. R., Klosinski, L. P., Cadenas, E., & Brinton, R. D. (2011) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2011.10.005 · Cited by 125
Chakrabarti, S., Munshi, S., Banerjee, K., Thakurta, I. G., Sinha, M. S., & Bagh, M. B. (2011) · Europe PMC (PubMed Central) · Cited by 122
Jiang, G., Hu, Y., Liu, L., Cai, J., Peng, C., & Li, Q. (2014) · Neurochemistry International · doi:10.1016/j.neuint.2014.06.003 · Cited by 122
Nitric Oxide Donors as Neuroprotective Agents after an Ischemic Stroke-Related Inflammatory Reaction
Godínez-Rubí, M., Rojas-Mayorquín, A. E., & Ortuño‐Sahagún, D. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/297357 · Cited by 122
3-Hydroxykynurenine: An intriguing molecule exerting dual actions in the Central Nervous System
Colín-González, A. L., Maldonado, P. D., & Santamarı́a, A. (2012) · NeuroToxicology · doi:10.1016/j.neuro.2012.11.007 · Cited by 121
Awh, C. C., Lane, A. M., Hawken, S., Zanke, B. W., & Kim, I. K. (2013) · Ophthalmology · doi:10.1016/j.ophtha.2013.07.039 · Cited by 123
Neuroprotective Properties of Berberine: Molecular Mechanisms and Clinical Implications
Tian, E., Sharma, G., & Dai, C. (2023) · Antioxidants · doi:10.3390/antiox12101883 · Cited by 137
Boukhzar, L., Hamieh, A., Cartier, D., Tanguy, Y., Alsharif, I., Castex, M., Arabo, A., Hajji, S. E., Bonnet, J., Errami, M., et al. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6478 · Cited by 119
He, P., Yan, S., Zheng, J., Gao, Y., Zhang, S., Liu, Z., Liu, X., & Xiao, C. (2018) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.8b03731 · Cited by 122
Magnesium and the Brain: A Focus on Neuroinflammation and Neurodegeneration
Maier, J. A. M., Locatelli, L., Fedele, G., Cazzaniga, A., & Mazur, A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms24010223 · Cited by 139
Hypoxia Activation of Mitophagy and Its Role in Disease Pathogenesis
Wu, H., & Chen, Q. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6204 · Cited by 119
Nanoencapsulation of gallic acid and evaluation of its cytotoxicity and antioxidant activity
Alves, A. D. C. S., Mainardes, R. M., & Khalil, N. M. (2015) · Materials Science and Engineering C · doi:10.1016/j.msec.2015.11.014 · Cited by 120
Mitochondrial Biology and Neurological Diseases
Arun, S., Liu, L., & Dönmez, G. (2015) · Current Neuropharmacology · doi:10.2174/1570159x13666150703154541 · Cited by 123
Neurotoxicity in Preclinical Models of Occupational Exposure to Organophosphorus Compounds
Voorhees, J. R., Rohlman, D. S., Lein, P. J., & Pieper, A. A. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2016.00590 · Cited by 120
Macroalgae-Derived Ingredients for Cosmetic Industry—An Update
Pimentel, F. B., Alves, R. C., Rodrigues, F., & Oliveira, M. B. P. P. (2017) · Cosmetics · doi:10.3390/cosmetics5010002 · Cited by 122
Mitochondrial Ca2+ Signaling in Health, Disease and Therapy
Modesti, L., Danese, A., Vitto, V. A. M., Ramaccini, D., Aguiari, G., Gafà, R., Lanza, G., Giorgi, C., & Pinton, P. (2021) · Cells · doi:10.3390/cells10061317 · Cited by 123
Nanoparticles, a Double-Edged Sword with Oxidant as Well as Antioxidant Properties—A Review
Samrot, A. V., Singh, S. P. R., Rajalakshmi, D., Rajesh, V. V., Padmanaban, S., & Radhakrishnan, K. (2022) · Oxygen · doi:10.3390/oxygen2040039 · Cited by 124
NMR Investigation of the Interaction between the Neuronal Protein Tau and the Microtubules
Sillen, A., Barbier, P., Landrieu, I., Lefebvre, S., Wieruszeski, J., Leroy, A., Peyrot, V., & Lippens, G. M. (2007) · Biochemistry · doi:10.1021/bi061920i · Cited by 121
Effects of mitochondrial dysfunction on the immunological properties of microglia
Ferger, A. I., Campanelli, L., Reimer, V., Muth, K. N., Merdian, I., Ludolph, A. C., & Witting, A. (2010) · Journal of Neuroinflammation · doi:10.1186/1742-2094-7-45 · Cited by 122
Motor neuron mitochondrial dysfunction in spinal muscular atrophy
Miller, N., Shi, H., Zelikovich, A. S., & Ma, Y.-C. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw262 · Cited by 119
Reactive oxygen species and the brain in sleep apnea
Wang, Y., Zhang, S. X. L., & Gozal, D. (2010) · Respiratory Physiology & Neurobiology · doi:10.1016/j.resp.2010.09.001 · Cited by 124
Methylene blue alleviates nuclear and mitochondrial abnormalities in progeria
Xiong, Z., Choi, J. Y., Wang, K., Zhang, H., Tariq, Z., Wu, D., Ko, E., LaDana, C., Sesaki, H., & Cao, K. (2015) · Aging Cell · doi:10.1111/acel.12434 · Cited by 123
van der Merwe, C., Dyk, H. C. V., Engelbrecht, L., van der Westhuizen, F. H., Kinnear, C. J., Loos, B., & Bardien, S. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9843-0 · Cited by 121
Molecular Hydrogen as a Neuroprotective Agent
Iketani, M., & Ohsawa, I. (2016) · Current Neuropharmacology · doi:10.2174/1570159x14666160607205417 · Cited by 118
Wang, X. H., Souders, C. L., Zhao, Y. H., & Martyniuk, C. J. (2017) · Chemosphere · doi:10.1016/j.chemosphere.2017.10.032 · Cited by 118
A Mitochondria-Associated Oxidative Stress Perspective on Huntington’s Disease
Zheng, J., Winderickx, J., Franssens, V., & Liu, B. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00329 · Cited by 122
Recent advances of electrochemical sensors for detecting and monitoring ROS/RNS
Zhao, S., Zang, G., Zhang, Y., Liu, H., Wang, N., Cai, S., Durkan, C., Xie, G., & Wang, G. (2021) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2021.113052 · Cited by 123
Begum, R., Saurav, H., Mamun-Or-Rashid, A. N. M., Rafiquzzaman, S. M., Ashraf, G. M., Albadrani, G. M., Sayed, A. A., Peluso, I., Abdel‐Daim, M. M., & Uddin, M. S. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/9974890 · Cited by 127
Bolaños, J. P., Moro, M. Á., Lizasoaín, I., & Almeida, Á. (2009) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2009.05.009 · Cited by 120
Silva‐Adaya, D., Cruz, V. P. L., Herrera‐Mundo, M. N., Mendoza‐Macedo, K., Villeda‐Hernández, J., BINIENDA, Z. K., Ali, S. F., & Santamarı́a, A. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.05174.x · Cited by 119
Therapeutic role of sirtuins in neurodegenerative disease
Outeiro, T. F., Marques, O., & Kazantsev, A. G. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.02.010 · Cited by 122
Mutation analysis ofCHCHD10in different neurodegenerative diseases
Zhang, M., Xi, Z., Zinman, L. H., Bruni, A. C., Maletta, R., Curcio, S. A. M., Rainero, I., Rubino, E., Pinessi, L., Nacmias, B., et al. (2015) · Brain · doi:10.1093/brain/awv082 · Cited by 119
Intrinsic and integrative properties of substantia nigra pars reticulata neurons
Zhou, F., & Lee, C. R. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.07.061 · Cited by 116
Ma, Q., Fang, H., Shang, W. H., Liu, L., Xu, Z., Tao, Y., Wang, X., Zheng, M., Chen, Q., & Cheng, H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.241794 · Cited by 119
New Insights in the Amyloid-Beta Interaction with Mitochondria
Spuch, C., Ortolano, S., & Fernández-Balbuena, C. N. (2012) · Journal of Aging Research · doi:10.1155/2012/324968 · Cited by 121
A TIGAR-Regulated Metabolic Pathway Is Critical for Protection of Brain Ischemia
Li, M., Sun, M., Cao, L., Gu, J., Ge, J., Chen, J., Han, R., Qin, Y., Zhou, Z., Ding, Y., et al. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.4655-13.2014 · Cited by 117
Zuo, L., Hemmelgarn, B. T., Chuang, C., & Best, T. M. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/604658 · Cited by 122
Mitochondrial Abnormalities in a Streptozotocin-Induced Rat Model of Sporadic Alzheimer's Disease
Correia, S. C., Santos, R. X., Santos, M. S., Casadesús, G., LaManna, J. C., Perry, G. L., Smith, M. A., & Moreira, P. I. (2013) · Current Alzheimer Research · doi:10.2174/1567205011310040006 · Cited by 117
Brain imaging with near-infrared fluorophores
Wang, H., Mu, X., Jiang, Y., Liang, Y., Zhang, X., & Ming, D. (2018) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2018.11.003 · Cited by 119
Identification of altered exosomal microRNAs and mRNAs in Alzheimer's disease
Su, L., Li, R., Zhang, Z.-Q., Liu, J., Du, J., & Wei, H. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101497 · Cited by 118
Sharma, N., & Nehru, B. (2015) · Neurochemistry International · doi:10.1016/j.neuint.2015.06.004 · Cited by 118
The role of the blood–CNS barrier in CNS disorders and their treatment
Palmer, A. M. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.07.029 · Cited by 124
Tau Phosphorylation by GSK3 in Different Conditions
Ávila, J., León‐Espinosa, G., García, E., García‐Escudero, V., Hernández, F., & DeFelipe, J. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/578373 · Cited by 119
Iijima‐Ando, K., Hearn, S., Shenton, C., Gatt, A., Zhao, L., & Iijima, K. (2009) · PLoS ONE · doi:10.1371/journal.pone.0008310 · Cited by 126
A neuro-immune model of myalgic encephalomyelitis/chronic fatigue syndrome
Morris, G., & Maes, M. (2013) · Metabolic Brain Disease · doi:10.1007/s11011-012-9324-8 · Cited by 117
Potula, R., Hawkins, B. J., Cenna, J. M., Fan, S., Dykstra, H., Ramirez, S. H., Morsey, B., Brodie, M. R., & Persidsky, Y. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0903691 · Cited by 116
From Intrinsic Firing Properties to Selective Neuronal Vulnerability in Neurodegenerative Diseases
Roselli, F., & Caroni, P. (2015) · Neuron · doi:10.1016/j.neuron.2014.12.063 · Cited by 117
Mechanisms of Altered Redox Regulation in Neurodegenerative Diseases—Focus on S-Glutathionylation
Liedhegner, E. S., Gao, X., & Mieyal, J. J. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4119 · Cited by 118
Analysis of the mitochondrial proteome in multiple sclerosis cortex
Broadwater, L., Pandit, A., Clements, R. J., Azzam, S., Vadnal, J., Sulak, M. A., Yong, V. W., Freeman, E. J., Gregory, R. B., & McDonough, J. A. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.01.012 · Cited by 119
Moya‐Alvarado, G., Gershoni‐Emek, N., Perlson, E., & Bronfman, F. C. (2016) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r115.053330 · Cited by 124
Dynamics of Human Mitochondrial Complex I Assembly: Implications for Neurodegenerative Diseases
Giachin, G., Bouverot, R., Acajjaoui, S., Pantalone, S., & Soler‐López, M. (2016) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2016.00043 · Cited by 118
Ye, X., Feng, D., Tao, K. X., Wang, R., Shi, Y., Qin, H., Murphy, M. P., Yang, Q., & Zhao, G. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.05.018 · Cited by 119
Lieke, T., Zhang, X., Steinberg, C. E. W., & Pan, B. (2018) · Environmental Science & Technology · doi:10.1021/acs.est.8b01338 · Cited by 119
TDP-43 proteinopathy and mitochondrial abnormalities in neurodegeneration
Gao, J., Wang, L., Yan, T., Perry, G. L., & Wang, X. (2019) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2019.103396 · Cited by 124
Mirzadeh, M., Lelekami, A. K., & Khedmat, L. (2021) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2021.118134 · Cited by 117
Lü, Y., Bu, F., Wang, F., Liu, L., Zhang, S., Wang, G., & Hu, X. (2023) · Translational Neurodegeneration · doi:10.1186/s40035-023-00341-5 · Cited by 128
Metal–organic frameworks (MOFs) as apt luminescent probes for the detection of biochemical analytes
Luo, D., Huang, J., Jian, Y., Singh, A., Kumar, A., Liu, J., Pan, Y. H., & Ouyang, Q. (2023) · Journal of Materials Chemistry B · doi:10.1039/d3tb00505d · Cited by 117
Huang, T., Lin, R., Su, Y., Sun, H., Zheng, X., Zhang, J., Lu, X., Zhao, B.-Q., Jiang, X., Huang, L., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-41529-7 · Cited by 123
Neuropathogenesis-on-chips for neurodegenerative diseases
Amartumur, S., Nguyen, H. M., Huynh, T., Kim, T. S., Woo, R., Oh, E., Kim, K. K., Lee, L. P., & Heo, C. (2024) · Nature Communications · doi:10.1038/s41467-024-46554-8 · Cited by 131
He, Y., Ge, J., & Tombran‐Tink, J. (2008) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.08-2192 · Cited by 117
Tsunemi, T., & Spada, A. R. L. (2011) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2011.10.004 · Cited by 119
Reduced brain somatostatin in mood disorders: a common pathophysiological substrate and drug target?
Lin, L., & Sibille, E. L. (2013) · Frontiers in Pharmacology · doi:10.3389/fphar.2013.00110 · Cited by 122
Mäkelä, J., Tselykh, T. V., Maiorana, F., Eriksson, O., Thi, H., Mudò, G., Korhonen, L., Belluardo, N., & Lindholm, D. (2014) · SpringerPlus · doi:10.1186/2193-1801-3-2 · Cited by 119
Adverse outcome pathways: Application to enhance mechanistic understanding of neurotoxicity
Bal‐Price, A., & Meek, M. E. (2017) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2017.05.006 · Cited by 124
Therapeutic Approaches to Alzheimer’s Disease Through Modulation of NRF2
Bahn, G., & Jo, D. (2019) · NeuroMolecular Medicine · doi:10.1007/s12017-018-08523-5 · Cited by 118
Biomolecular condensates in neurodegeneration and cancer
Spannl, S., Tereshchenko, M., Mastromarco, G. J., Ihn, S. J., & Lee, H. O. (2019) · Traffic · doi:10.1111/tra.12704 · Cited by 116
Effect of ApoE isoforms on mitochondria in Alzheimer disease
Yin, J., Reiman, E. M., Beach, T. G., Serrano, G. E., Sabbagh, M. N., Nielsen, M., Caselli, R. J., & Shi, J. (2020) · Neurology · doi:10.1212/wnl.0000000000009582 · Cited by 116
Clinical Application of Antioxidants to Improve Human Oocyte Mitochondrial Function: A Review
Rodríguez-Varela, C., & Labarta, E. (2020) · Antioxidants · doi:10.3390/antiox9121197 · Cited by 116
Shabbir, U., Rubab, M., Tyagi, A., & Oh, D. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms22010196 · Cited by 120
Mitochondrial iron metabolism and neurodegenerative diseases
Cheng, R., Dhorajia, V. V., Kim, J., & Kim, Y. (2021) · NeuroToxicology · doi:10.1016/j.neuro.2021.11.003 · Cited by 121
Dai, Y., Guo, Y., Tang, W., Chen, D., Xue, L., Chen, Y., Guo, Y., Wei, S., Wu, M., Dai, J., et al. (2024) · Journal of Nanobiotechnology · doi:10.1186/s12951-024-02501-9 · Cited by 128
High-resolution in situ structures of mammalian respiratory supercomplexes
Zheng, W., Chai, P., Zhu, J., & Zhang, K. (2024) · Nature · doi:10.1038/s41586-024-07488-9 · Cited by 128
Osborne, N. N., Li, G., Ji, D., Mortiboys, H., & Jackson, S. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05320.x · Cited by 119
A Hydrogen Peroxide-Responsive Hyperpolarized 13C MRI Contrast Agent
Lippert, A. R., Keshari, K. R., Kurhanewicz, J. V., & Chang, C. J. (2011) · Journal of the American Chemical Society · doi:10.1021/ja111589a · Cited by 115
Mechanisms and mathematical modeling of ROS production by the mitochondrial electron transport chain
Chenna, S., Koopman, W. J. H., Prehn, J. H. M., & Connolly, N. M. C. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00455.2021 · Cited by 122
Xiao, S., Zhang, Y., Liu, Z., Li, A., Tong, W., Xiong, X., Nie, J., Zhong, N., Zhu, G., Liu, J., et al. (2023) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.14085 · Cited by 118
Szutowicz, A., Bielarczyk, H., Jankowska-Kulawy, A., Pawełczyk, T., & Ronowska, A. (2013) · Neurochemical Research · doi:10.1007/s11064-013-1060-x · Cited by 117
Steroid and thyroid hormone receptors in mitochondria
Psarra, A. G., & Sekeris, C. E. (2008) · IUBMB Life · doi:10.1002/iub.37 · Cited by 116
Amyotrophic lateral sclerosis: Current perspectives from basic research to the clinic
Mancuso, R., & Navarro, X. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.07.004 · Cited by 125
Neuronal failure in Alzheimer’s disease: a view through the oxidative stress looking-glass
Bonda, D., Wang, X., Lee, H., Smith, M. A., Perry, G. L., & Zhu, X. (2014) · Neuroscience Bulletin · doi:10.1007/s12264-013-1424-x · Cited by 114
The Striatum Is Highly Susceptible to Mitochondrial Oxidative Phosphorylation Dysfunctions
Pickrell, A. M., Fukui, H., Wang, X., Pinto, M., & Moraes, C. T. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.6223-10.2011 · Cited by 114
Cholesterol metabolism in pathogenesis of osteoarthritis disease
Farnaghi, S., Crawford, R., Xiao, Y., & Prasadam, I. (2017) · International Journal of Rheumatic Diseases · doi:10.1111/1756-185x.13061 · Cited by 115
Genetic reduction of eEF2 kinase alleviates pathophysiology in Alzheimer’s disease model mice
Beckelman, B. C., Yang, W., Kasica, N. P., Zimmermann, H. R., Zhou, X., Keene, C. D., Ryazanov, A. G., & Ma, T. (2019) · Journal of Clinical Investigation · doi:10.1172/jci122954 · Cited by 116
Phytosterols: Physiological Functions and Potential Application
Shen, M., Yuan, L., Zhang, J., Wang, X., Zhang, M., Li, H., Jing, Y., Zeng, F., & Xie, J. (2024) · Foods · doi:10.3390/foods13111754 · Cited by 122
Su, Y. A., Wu, J., Zhang, L., Zhang, Q., Su, D. M., He, P., Wang, B.-D., Li, H., Webster, M. J., Group, T. S. B. S., et al. (2008) · International Journal of Biological Sciences · doi:10.7150/ijbs.4.223 · Cited by 113
Salminen, L. E., & Paul, R. H. (2014) · Reviews in the Neurosciences · doi:10.1515/revneuro-2014-0046 · Cited by 113
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
