The DOI matches its Crossref record; 103 of the 103 references it cites were found in a registry or an index.
Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
Abstract
Many lines of evidence suggest that mitochondria have a central role in ageing-related neurodegenerative diseases. Mitochondria are critical regulators of cell death, a key feature of neurodegeneration. Mutations in mitochondrial DNA and oxidative stress both contribute to ageing, which is the greatest risk factor for neurodegenerative diseases. In all major examples of these diseases there is strong evidence that mitochondrial dysfunction occurs early and acts causally in disease pathogenesis. Moreover, an impressive number of disease-specific proteins interact with mitochondria. Thus, therapies targeting basic mitochondrial processes, such as energy metabolism or free-radical generation, or specific interactions of disease-related proteins with mitochondria, hold great promise.
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In the citing paper
“Evidence also suggests that not only does Aβ increase cellular RS but that these RS may in turn increase production of Aβ in a destructive autocatalytic cycle (Misonou et al., 2000; Tamagno et al., 2002, 2005; Lin and Beal, 2006; Quiroz-Baez et al., 2009).”
From The mitochondria-targeted antioxidant MitoQ prevents loss of spatial memory retention and early neuropathology in a transgenic mouse model of Alzheimer’s disease (2011) · cites this paper as Lin and Beal, 2006
In the citing paper
“Aβ appears to enhance production of cellular RS, and these RS in turn may to contribute to Aβ toxicity.”
From The mitochondria-targeted antioxidant MitoQ prevents loss of spatial memory retention and early neuropathology in a transgenic mouse model of Alzheimer’s disease (2011) · cites this paper as Lin and Beal, 2006
In the citing paper
“On the basis of evidence from post-mortem brain tissues from AD patients as well as different AD mouse models, damaged mitochondria and increased oxidative stress are common features of AD (Lin and Beal, 2006; Mattson et al., 2008).”
From NAD+ in Brain Aging and Neurodegenerative Disorders (2019) · cites this paper as Lin and Beal, 2006
In the citing paper
“Due to the content of multiple electron carriers and an extensive antioxidant defence, they represent a key centre for ROS/antioxidant balance regulation [56].”
From The Role of Antioxidants in the Interplay between Oxidative Stress and Senescence (2022) · cites this paper as [56]
In the citing paper
“and the AD brain displays insulin resistance and impaired mitochondrial function (45,46)”
From Altered mitochondrial function in insulin-deficient and insulin-resistant states (2018) · cites this paper as [46]
In the citing paper
“a range of distinct aetologies, which manifest as a variety of different syndromes or diseases, converge at some point on an autocatalytic series of reactions, involving imperfectly liganded iron, in the production of the very damaging hydroxyl radical, that by causing the destruction of appropriate cellular structures and proteins liberates further ‘free’ iron and other reactive oxygen species,”
In the citing paper
“Aging-associated expression changes in genes associated with mitochondrial function, protein metabolism, and immune response have been identified in several tissues (173) and are consistent with some proposed mechanisms for late-onset neurodegenerative diseases (98, 113, 124, 166).”
From Unraveling a Multifactorial Late-Onset Disease: From Genetic Susceptibility to Disease Mechanisms for Age-Related Macular Degeneration (2009) · cites this paper as [98]
In the citing paper
“Mitochondrial dysfunction and oxidative stress, including mitochondrial DNA damage, have been implicated in all three diseases—AD, PD, and AMD (12, 17, 98, 165).”
From Unraveling a Multifactorial Late-Onset Disease: From Genetic Susceptibility to Disease Mechanisms for Age-Related Macular Degeneration (2009) · cites this paper as [98]
In the citing paper
“Numerous studies have demonstrated a central role of mitochondria and energy homeostasis in the pathogenesis of aging-associated neurodegenerative diseases (98, 157, 166).”
From Unraveling a Multifactorial Late-Onset Disease: From Genetic Susceptibility to Disease Mechanisms for Age-Related Macular Degeneration (2009) · cites this paper as [98]
In the citing paper
“Much evidence suggests a role for mitochondrial dysfunction in the pathophysiology of PD, a common age-associated neurodegenerative disease characterized by progressive degeneration of the nigrostriatal dopamine (DA) pathway and presence of the intraneuronal protein inclusions (Lewy bodies)1-3.”
From Mitochondrial Approaches for Neuroprotection (2008) · cites this paper as [2]
In the citing paper
“Several different pathogenic mechanisms have been identified in the CNS and peripheral tissues during the disease course in ALS, but mitochondrial and bioenergetic defects are implicated widely in ALS pathogenesis2.”
From Mitochondrial Approaches for Neuroprotection (2008) · cites this paper as [2]
In the citing paper
“These studies provide compelling evidence for a role of PGC-1α in the pathogenesis of neurodegenerative diseases, and thus it is a promising therapeutic target for neurodegenerative disorders2, 72.”
From Mitochondrial Approaches for Neuroprotection (2008) · cites this paper as [2]
In the citing paper
“Second, high cellular ROS levels are associated with cancer, diabetes, inflammatory diseases, ischemia-related diseases, and neurodegeneration, and are thus commonly thought to contribute to human pathologies and aging 80–83.”
From Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes (2010) · cites this paper as [81]
Citations
Cites
Danial, N. N., & Korsmeyer, S. J. (2004) · Cell · doi:10.1016/s0092-8674(04)00046-7 · Cited by 4,651
Chronic systemic pesticide exposure reproduces features of Parkinson's disease
Betarbet, R. S., Sherer, T., MacKenzie, G. M., Garcia‐Osuna, M., Panov, A. V., & Greenamyre, J. T. (2000) · Nature Neuroscience · doi:10.1038/81834 · Cited by 3,770
Hereditary Early-Onset Parkinson's Disease Caused by Mutations in PINK1
Valente, E. M., Abou-Sleiman, P. M., Caputo, V., Muqit, M. M. K., Harvey, K., Gispert, S., Ali, Z., Del Turco, D., Bentivoglio, A. R., Healy, D. G., et al. (2004) · Science · doi:10.1126/science.1096284 · Cited by 3,481
Wallace, D. C. (2005) · Annual Review of Genetics · doi:10.1146/annurev.genet.39.110304.095751 · Cited by 3,185
Mutations in the DJ-1 Gene Associated with Autosomal Recessive Early-Onset Parkinsonism
Bonifati, V., Rizzu, P., van Baren, M. J., Schaap, O., Breedveld, G. J., Krieger, E., Dekker, M. C. J., Squitieri, F., Ibáñez, P., Joosse, M., et al. (2003) · Science · doi:10.1126/science.1077209 · Cited by 2,854
Direct Activation of Bax by p53 Mediates Mitochondrial Membrane Permeabilization and Apoptosis
Chipuk, J. E., Kuwana, T., Bouchier-Hayes, L., Droin, N. M., Newmeyer, D. D., Schuler, M., & Green, D. R. (2004) · Science · doi:10.1126/science.1092734 · Cited by 2,108
Oxidative Damage Is the Earliest Event in Alzheimer Disease
Nunomura, A., Perry, G., Aliev, G., Hirai, K., Takeda, A., Balraj, E. K., Jones, P. K., Ghanbari, H., Wataya, T., Shimohama, S., et al. (2001) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/60.8.759 · Cited by 1,885
Gene regulation and DNA damage in the ageing human brain
Lu, T., Pan, Y., Kao, S.-Y., Li, C., Kohane, I., Chan, J., & Yankner, B. A. (2004) · Nature · doi:10.1038/nature02661 · Cited by 1,874
MITOCHONDRIAL COMPLEX I DEFICIENCY IN PARKINSON'S DISEASE
Schapira, A. H. V., Cooper, J. A. D., Dexter, D. T., Jenner, P. G., Clark, J. B., & MARSDEN, C. D. (1989) · The Lancet · doi:10.1016/s0140-6736(89)92366-0 · Cited by 1,757
Extension of murine life span by overexpression of catalase targeted to mitochondria
Schriner, S. E., Linford, N. J., Martin, G. M., Treuting, P., Ogburn, C. E., Emond, M., Coskun, P. E., Ladiges, W., Wolf, N., Van Remmen, H., et al. (2005) · Science · doi:10.1126/science.1106653 · Cited by 1,724
Cited by
Sorted by citations
Items 701–800 of 1,096
Bess, A. S., Crocker, T. L., Ryde, I. T., & Meyer, J. N. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks532 · Cited by 138
Oxidation of potassium channels by ROS: a general mechanism of aging and neurodegeneration?
Sesti, F., Liu, S., & Cai, S. (2009) · Trends in Cell Biology · doi:10.1016/j.tcb.2009.09.008 · Cited by 138
Ischemic A/D transition of mitochondrial complex I and its role in ROS generation
Dröse, S., Степанова, А., & Galkin, A. S. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2015.12.013 · Cited by 140
Roles of sigma-1 receptors on mitochondrial functions relevant to neurodegenerative diseases
Weng, T.-Y., Tsai, S., & Su, T. (2017) · Journal of Biomedical Science · doi:10.1186/s12929-017-0380-6 · Cited by 142
Emerging roles of mitochondria in synaptic transmission and neurodegeneration
Lee, A., Hirabayashi, Y., Kwon, S., Lewis, T. L., & Polleux, F. (2018) · Current Opinion in Physiology · doi:10.1016/j.cophys.2018.03.009 · Cited by 131
Min, Y., Suminda, G. G. D., Heo, Y., Kim, M., Ghosh, M., & Son, Y. (2023) · Antioxidants · doi:10.3390/antiox12030703 · Cited by 138
Esterházy, D., King, M. S., Yakovlev, G., & Hirst, J. (2008) · Biochemistry · doi:10.1021/bi702243b · Cited by 144
Nmnat delays axonal degeneration caused by mitochondrial and oxidative stress
Press, C., & Milbrandt, J. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.0525-08.2008 · Cited by 137
“Mitochondrial dysfunction caused by mutations or toxic agents has been implicated in many neurodegenerative diseases, including those associated with axonal degeneration (Lin and Beal, 2006).”
BackgroundInfluentialWang, C., Li, J., Liu, Q., Yang, R., Zhang, J. H., Cao, Y., & Sun, X. (2011) · Neuroscience Letters · doi:10.1016/j.neulet.2011.01.022 · Cited by 137
RetractedZheng, X., Boyer, L. F., Jin, M., Kim, Y., Fan, W., Bardy, C., Berggren, W. T., Evans, R. M., Gage, F. H., & Hunter, T. R. (2016) · eLife · doi:10.7554/elife.13378 · Cited by 139
Bai, X., Wang, S., Yan, X., Zhou, H., Zhan, J., Liu, S., Sharma, V. K., Jiang, G., Zhu, H., & Yan, B. (2019) · ACS Nano · doi:10.1021/acsnano.9b04407 · Cited by 139
Hassan, S. S. U., Samanta, S., Dash, R., Karpiński, T. M. M., Habibi, E., Sadiq, A., Ahmadi, A., & BUNGAU, S. G. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.1015835 · Cited by 139
Thiamine Deficiency: An Update of Pathophysiologic Mechanisms and Future Therapeutic Considerations
Abdou, E., & Hazell, A. S. (2014) · Neurochemical Research · doi:10.1007/s11064-014-1430-z · Cited by 139
Yin, N., Liu, Q. S., Liu, J., He, B., Cui, L., Li, Z., Yun, Z., Qu, G., Liu, S., Zhou, Q., et al. (2013) · Small · doi:10.1002/smll.201202732 · Cited by 136
Successful Aging: Focus on Cognitive and Emotional Health
Depp, C. A., Vahia, I. V., & Jeste, D. V. (2010) · Annual Review of Clinical Psychology · doi:10.1146/annurev.clinpsy.121208.131449 · Cited by 148
Oxidative stress by inorganic nanoparticles
Tee, J. K., Ong, C. N., Bay, B., Ho, H. K., & Leong, D. T. (2015) · Wiley Interdisciplinary Reviews Nanomedicine and Nanobiotechnology · doi:10.1002/wnan.1374 · Cited by 139
Localization of sequence variations in PGC-1α influence their modifying effect in Huntington disease
Hong Van, B., Metzger, S., Portal, E., Deyle, C., Rieß, O., & Nguyen, H. P. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-1 · Cited by 136
Peng, S., Zhang, B., Meng, X., Yao, J., & Fang, J. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00410 · Cited by 136
Tewari, D., Stankiewicz, A. M., Mocan, A., Sah, A. N., Tzvetkov, N. T., Huminiecki, Ł., Horbańczuk, J. O., & Atanasov, A. G. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00003 · Cited by 142
Elevating acetyl-CoA levels reduces aspects of brain aging
Currais, A. J. M., Huang, L., Goldberg, J., Petrascheck, M., Ates, G., Pinto‐Duarte, A., Shokhirev, M. N., Schubert, D. A., & Maher, P. A. (2019) · eLife · doi:10.7554/elife.47866 · Cited by 138
Fields, M., Marcuzzi, A., Gonelli, A., Celeghini, C., Maximova, N., & Rimondi, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24043739 · Cited by 147
Mosconi, L., Rinne, J. O., Tsui, W. H., Berti, V., Li, Y., Wang, H., Murray, J., Scheinin, N., Någren, K., Williams, S., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914141107 · Cited by 135
Piers, T. M., Cosker, K., Mallach, A., Johnson, G. T., Guerreiro, R., Hardy, J., & Pocock, J. M. (2020) · The FASEB Journal · doi:10.1096/fj.201902447r · Cited by 135
Chen-Plotkin, A. S., Geser, F., Plotkin, J. B., Clark, C. M., Kwong, L. K., Yuan, W., Grossman, M., Van Deerlin, V. M., Trojanowski, J. Q., & Lee, V. M.-Y. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn023 · Cited by 135
Wavelet images and Chou’s pseudo amino acid composition for protein classification
Nanni, L., Brahnam, S., & Lumini, A. (2011) · Amino Acids · doi:10.1007/s00726-011-1114-9 · Cited by 136
Antioxidants halt axonal degeneration in a mouse model of X‐adrenoleukodystrophy
López‐Erauskin, J., Fourcade, S., Galino, J., Ruíz, M., Schlüter, A., Naudí, A., Jové, M., Portero‐Otín, M., Pamplona, R., Ferrer, I., et al. (2011) · Annals of Neurology · doi:10.1002/ana.22363 · Cited by 135
Owen, L., & Sünram‐Lea, S. I. (2011) · Nutrients · doi:10.3390/nu3080735 · Cited by 137
Areti, A., Komirishetty, P., Akuthota, M., Malik, R. A., & Kumar, A. (2017) · Journal of Pineal Research · doi:10.1111/jpi.12393 · Cited by 135
Sanjeewa, K. K. A., Kang, N., Ahn, G., Jee, Y., Kim, Y.-T., & Jeon, Y. (2018) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2018.02.040 · Cited by 139
Exercise and metformin counteract altered mitochondrial function in the insulin-resistant brain
Ruegsegger, G. N., Vanderboom, P. M., Dasari, S., Klaus, K. A., Kabiraj, P., McCarthy, C. B., Lucchinetti, C. F., & Nair, K. S. (2019) · JCI Insight · doi:10.1172/jci.insight.130681 · Cited by 141
Sepsis induces brain mitochondrial dysfunction.
d’Avila, J. D. C. P., Santiago, A. P. S. A., Amâncio, R. T., Galina, A., Oliveira, M. F., & Bozza, F. A. (2008) · Critical Care Medicine · doi:10.1097/ccm.0b013e3181760c4b · Cited by 134
Kuang, X., Chen, Y.-S., Wang, L.-F., Li, Y., Liu, K., Zhang, M., Li, L.-J., Chen, C., He, Q., Wang, Y., et al. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.07.019 · Cited by 134
Fisetin Reduces the Impact of Aging on Behavior and Physiology in the Rapidly Aging SAMP8 Mouse
Currais, A. J. M., Farrokhi, C. B., Dargusch, R., Armando, A. M., Quehenberger, O., Schubert, D. A., & Maher, P. A. (2017) · The Journals of Gerontology Series A · doi:10.1093/gerona/glx104 · Cited by 135
Chou, S. H.-Y., Lan, J., Esposito, E., Ning, M., Balaj, L., Ji, X., Lo, E. H., & Hayakawa, K. (2017) · Stroke · doi:10.1161/strokeaha.117.017758 · Cited by 134
Behl, T., Makkar, R., Sehgal, A., Singh, S., Sharma, N., Zengin, G., BUNGAU, S. G., Andronie-Cioară, F. L., Munteanu, M. A., Brisc, M. C., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147432 · Cited by 134
Oxidative insults induce DJ-1 upregulation and redistribution: Implications for neuroprotection
Lev, N., Ickowicz, D., Melamed, E., & Offen, D. (2008) · NeuroToxicology · doi:10.1016/j.neuro.2008.01.007 · Cited by 134
Lee, S., Sheck, L. H. N., Crowston, J. G., Bergen, N. J. V., O’Neill, E. C., O’Hare, F., Kong, Y. X. G., Chrysostomou, V., Vincent, A. L., & Trounce, I. A. (2012) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.12-9596 · Cited by 133
Regulation of Hippocampal Firing by Network Oscillations during Sleep
Miyawaki, H., & Diba, K. (2016) · Current Biology · doi:10.1016/j.cub.2016.02.024 · Cited by 140
Underwood, J., Robertson, K. R., & Winston, A. (2014) · AIDS · doi:10.1097/qad.0000000000000538 · Cited by 136
Mastroeni, D., Khdour, O. M., Delvaux, E., Nolz, J., Olsen, G., Berchtold, N. C., Cotman, C. W., Hecht, S. M., & Coleman, P. D. (2016) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2016.09.003 · Cited by 134
Boronate-Based Fluorescent Probes
Lin, V., Dickinson, B. C., & Chang, C. J. (2013) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-405883-5.00002-8 · Cited by 135
Oh, C.-K., Sultan, A., Platzer, J., Dolatabadi, N., Soldner, F., McClatchy, D. B., Diedrich, J. K., Yates, J. R., Ambasudhan, R., Nakamura, T., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.10.068 · Cited by 136
Li, S.-P., Wang, Y., Qi, S., Zhang, Y., Deng, G., Ding, W.-Z., Ma, C., Lin, Q., Guan, H., Liu, W., et al. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.00346 · Cited by 134
Amyloid β: linking synaptic plasticity failure to memory disruption in Alzheimer’s disease
Ma, T., & Klann, E. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07506.x · Cited by 140
Mitochondria Are the Source of Hydrogen Peroxide for Dynamic Brain-Cell Signaling
Bao, L., Avshalumov, M. V., Patel, J. C., Lee, C. R., Miller, E. W., Chang, C. J., & Rice, M. E. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.1706-09.2009 · Cited by 136
Marques‐Aleixo, I., Oliveira, P. J., Moreira, P. I., Magalhães, J., & Ascensão, A. A. M. R. (2012) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2012.08.002 · Cited by 134
Cruickshank, T. M., Reyes, A. P., & Ziman, M. R. (2015) · Medicine · doi:10.1097/md.0000000000000411 · Cited by 145
Alzheimer's disease: new approaches to drug discovery
Bolognesi, M. L., Matera, R., Minarini, A., Rosini, M., & Melchiorre, C. (2009) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2009.04.619 · Cited by 132
Muller, A. P., Ferreira, G. K., Pires, A. J., Silveira, G. D. B., de Souza, D. L., Brandolfi, J. D. A., de Souza, C. T., Paula, M. M. D. S., & Silveira, P. C. L. (2017) · Materials Science and Engineering C · doi:10.1016/j.msec.2017.03.283 · Cited by 132
Mei, H., Zhao, L., Li, W., Zheng, Z., Tang, D., Lu, X., & He, Y. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.15839 · Cited by 133
Nakamura, T., Cieplak, P., Cho, D., Godzik, A., & Lipton, S. A. (2010) · Mitochondrion · doi:10.1016/j.mito.2010.04.007 · Cited by 138
PGC-1α, a New Therapeutic Target in Huntington's Disease?
McGill, J. K., & Beal, M. F. (2006) · Cell · doi:10.1016/j.cell.2006.10.023 · Cited by 131
Self-citationMeasurement of Mitochondrial NADH and FAD Autofluorescence in Live Cells
Bartolomé, F. B., & Abramov, A. Y. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2257-4_23 · Cited by 133
Expression of β-Amyloid Induced Age-Dependent Presynaptic and Axonal Changes in Drosophila
Zhao, X.-L., Wang, W.-A., Tan, J.-X., Huang, J.-K., Zhang, X., Zhang, B.-Z., Wang, Y.-H., YangCheng, H.-Y., Zhu, H.-L., Sun, X.-J., et al. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.3699-09.2010 · Cited by 130
Laar, V. S. V., & Berman, S. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.05.015 · Cited by 137
Eckert, A., Hauptmann, S., Scherping, I., Meinhardt, J., Rhein, V. F., Dröse, S., Brandt, U., Fändrich, M., Müller, W. E., & Götz, J. (2008) · Journal of Molecular Medicine · doi:10.1007/s00109-008-0391-6 · Cited by 132
TNFα drives mitochondrial stress in POMC neurons in obesity
Yi, C., Walter, M., Gao, Y., Pitra, S., Legutko, B., Kälin, S., Layritz, C., García‐Cáceres, C., Bielohuby, M., Bidlingmaier, M., et al. (2017) · Nature Communications · doi:10.1038/ncomms15143 · Cited by 131
Feng, Y., Jia, Y., Su, L., Wang, D., Lv, L., Xu, L., & Yao, Y. (2013) · Autophagy · doi:10.4161/auto.25468 · Cited by 130
Liu, L., Peritore, C., Rogers, J. G., Shih, J., Arun, S., & Dönmez, G. (2014) · Behavioural Brain Research · doi:10.1016/j.bbr.2014.12.035 · Cited by 128
Tavares, L., Figueira, I., Macedo, D., McDougall, G. J., Leitão, M. C., Vieira, H. L. A., Stewart, D., Alves, P. M., Ferreira, R. B., & dos Santos, C. N. (2011) · Food Chemistry · doi:10.1016/j.foodchem.2011.10.025 · Cited by 132
Idebenone and neuroprotection: antioxidant, pro-oxidant, or electron carrier?
Jaber, S. M., & Polster, B. M. (2014) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-014-9571-y · Cited by 130
Use of Carnosine for Oxidative Stress Reduction in Different Pathologies
Prokopieva, V. D., Yarygina, E. G., Bokhan, N. A., & Ivanova, S. А. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/2939087 · Cited by 132
The Role of Sigma-1 Receptor, an Intracellular Chaperone in Neurodegenerative Diseases
Penke, B., Fülöp, L., Szűcs, M., & Frecska, E. (2017) · Current Neuropharmacology · doi:10.2174/1570159x15666170529104323 · Cited by 132
Molecular mechanisms of nickel induced neurotoxicity and chemoprevention
Song, X., Kenston, S. S. F., Kong, L., & Zhao, J. (2017) · Toxicology · doi:10.1016/j.tox.2017.10.006 · Cited by 137
Jiang, X., Wang, H., Yuan, R., & Chai, Y. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b01168 · Cited by 130
Rehman, M. U., Sehar, N., Dar, N. J., Khan, A., Arafah, A., Rashid, S., Rashid, S. M., & Ganaie, M. A. (2023) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2022.104961 · Cited by 130
Electron tunneling in respiratory complex I
Hayashi, T., & Stuchebrukhov, A. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009181107 · Cited by 129
Research Advances on Pathways of Nickel-Induced Apoptosis
Guo, H., Chen, L., Cui, H., Peng, X., Fang, J. S., Zuo, Z., Deng, J., Wang, X., & Wu, B. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms17010010 · Cited by 129
Gowd, V., Bao, T., Wang, L., Huang, Y., Chen, S., Zheng, X., Cui, S., & Chen, W. (2018) · Food Chemistry · doi:10.1016/j.foodchem.2018.07.020 · Cited by 129
Zhuang, X., Wang, S.-F., Tan, Y., Song, J., Zhu, Z., Wang, Z., Wu, M.-Y., Cai, C.-Z., Huang, Z., Tan, J., et al. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2322-6 · Cited by 136
Wood, E., Hall, K., & Tate, W. P. (2020) · Chronic Diseases and Translational Medicine · doi:10.1016/j.cdtm.2020.11.002 · Cited by 132
Cytochrome c oxidase deficiency: Patients and animal models
Diaz, F. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.07.013 · Cited by 127
Cellular Respiration: The Nexus of Stress, Condition, and Ornamentation
Hill, G. E. (2014) · Integrative and Comparative Biology · doi:10.1093/icb/icu029 · Cited by 130
Cheng, J., Wang, F., Yu, D., Wu, P., & Chen, J. (2010) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2010.09.033 · Cited by 128
A Strategy for Highly Selective Detection and Imaging of Hypochlorite Using Selenoxide Elimination
Li, G., Zhu, D., Liu, Q. L., Xue, L., & Jiang, H. (2013) · Organic Letters · doi:10.1021/ol4006823 · Cited by 128
Curcumin alleviates oxidative stress and mitochondrial dysfunction in astrocytes
Daverey, A., & Agrawal, S. K. (2016) · Neuroscience · doi:10.1016/j.neuroscience.2016.07.012 · Cited by 134
Kahroba, H., Ramezani, B., Maadi, H., Sadeghi, M. R., Jaberie, H., & Ramezani, F. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101211 · Cited by 130
Physical bioenergetics: Energy fluxes, budgets, and constraints in cells
Yang, X., Heinemann, M., Howard, J., Huber, G., Iyer‐Biswas, S., Treut, G. L., Lynch, M., Montooth, K. L., Needleman, D. J., Simone Pigolotti, A., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2026786118 · Cited by 130
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Calí, T., Ottolini, D., & Brini, M. (2012) · Cell Calcium · doi:10.1016/j.ceca.2012.04.015 · Cited by 132
Kang, Y., Tiziani, S., Park, G., Kaul, M., & Paternostro, G. (2014) · Nature Communications · doi:10.1038/ncomms4672 · Cited by 129
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Baloh, R. H. (2007) · The Neuroscientist · doi:10.1177/1073858407307354 · Cited by 127
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Yi, C., Mei, X., Ezan, P., Mato, S., Matias, I., Giaume, C., & Koulakoff, A. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2016.63 · Cited by 133
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Gupta, R. V., Sahu, M., Srivastava, D., Tiwari, S., Ambasta, R. K., & Kumar, P. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101336 · Cited by 126
Lippert, A. R., Gschneidtner, T. A., & Chang, C. J. (2010) · Chemical Communications · doi:10.1039/c0cc01560a · Cited by 129
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Halliday, M., & Mallucci, G. R. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.08.034 · Cited by 125
Kooragayala, K., Gotoh, N., Cogliati, T., Nellissery, J. K., Kaden, T. R., French, S. A., Balaban, R. S., Li, W. S., Covián, R., & Swaroop, A. (2015) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.15-17901 · Cited by 129
Wang, J., Luo, B., Li, X., Lu, W., Yang, J., Hu, Y., Huang, P., & Wen, S. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.272 · Cited by 127
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Eschbach, J., von Einem, B., Müller, K., Bayer, H., Scheffold, A., Morrison, B. E., Rudolph, K. L., Thal, D. R., Witting, A., Weydt, P., et al. (2014) · Annals of Neurology · doi:10.1002/ana.24294 · Cited by 126
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Hayashi, T., Asano, Y., Shintani, Y., Aoyama, H., Kioka, H., Tsukamoto, O., Hikita, M., Shinzawa‐Itoh, K., Takafuji, K., Higo, S., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1419767112 · Cited by 125
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Correia, S. C., & Moreira, P. I. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06443.x · Cited by 125
López-Erauskin, J., Galino, J., Ruiz, M., Cuezva, J. M., Fabregat, I., Cacabelos, D., Boada, J., Martínez, J., Ferrer, I., Pamplona, R., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt186 · Cited by 125
Impact of gene mutation in the development of Parkinson's disease
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Tewari, D., Sah, A. N., Bawari, S., Nabavi, S. F., Dehpour, A. R., Shirooie, S., Braidy, N., Fiebich, B. L., Vacca, R. A., & Nabavi, S. M. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200429001549 · Cited by 132
Han, R., Liang, J., & Zhou, B. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115887 · Cited by 125
Slowed progression in models of huntington disease by adipose stem cell transplantation
Lee, S., Chu, K., Jung, K., Im, W., Park, J., Lim, H.-C., Won, C. H., Shin, S., Lee, S. K., Kim, M., et al. (2009) · Annals of Neurology · doi:10.1002/ana.21788 · Cited by 128
Yan, J., Liu, X.-H., Han, M., Wang, Y., Sun, X., Yu, N., Li, T., Su, B., & Chen, Z.-Y. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.08.005 · Cited by 126
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Senger, D. R., Li, D., Jaminet, S.-C., & Cao, S. (2016) · PLOS ONE · doi:10.1371/journal.pone.0148042 · Cited by 124
Metadata
- Authors
- Lin, M. T., & Beal, M. F.
- Affiliations
- Cornell University (US)
- Corresponding author
- Beal, M. Flint
- ORCID
- Beal, M. Flint
- Venue
- Nature
- Published
- 2006-10
- Volume
- 443
- Issue
- 7113
- Pages
- 787-795
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2152165298
- Cited by
- 6,455
- References
- 103
- Citations by year
- 2026: 266 · 2025: 386 · 2024: 393 · 2023: 362 · 2022: 408 · 2021: 454 · 2020: 412 · 2019: 366 · 2018: 450 · 2017: 373 · 2016: 356 · 2015: 326 · 2014: 290 · 2013: 296 · 2012: 293
- FWCI
- 13.10
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- American Federation for Aging Research
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- mitochondrial dysfunction, oxidative stress, neurodegenerative diseases, aging, mitochondrial DNA mutations, cell death, energy metabolism, free radicals, pathogenesis, mitochondrial-targeted therapy
- MeSH terms
- Aging, Animals, Humans, Mitochondria, Apoptosis, Oxidative Stress, Neurodegenerative Diseases
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