The DOI matches its Crossref record; 234 of the 237 references it cites were found in a registry or an index.
Oxidative Stress, Synaptic Dysfunction, and Alzheimer’s Disease
Open accessAbstract
Alzheimer's disease (AD) is a devastating neurodegenerative disorder without a cure. Most AD cases are sporadic where age represents the greatest risk factor. Lack of understanding of the disease mechanism hinders the development of efficacious therapeutic approaches. The loss of synapses in the affected brain regions correlates best with cognitive impairment in AD patients and has been considered as the early mechanism that precedes neuronal loss. Oxidative stress has been recognized as a contributing factor in aging and in the progression of multiple neurodegenerative diseases including AD. Increased production of reactive oxygen species (ROS) associated with age- and disease-dependent loss of mitochondrial function, altered metal homeostasis, and reduced antioxidant defense directly affect synaptic activity and neurotransmission in neurons leading to cognitive dysfunction. In addition, molecular targets affected by ROS include nuclear and mitochondrial DNA, lipids, proteins, calcium homeostasis, mitochondrial dynamics and function, cellular architecture, receptor trafficking and endocytosis, and energy homeostasis. Abnormal cellular metabolism in turn could affect the production and accumulation of amyloid-β (Aβ) and hyperphosphorylated Tau protein, which independently could exacerbate mitochondrial dysfunction and ROS production, thereby contributing to a vicious cycle. While mounting evidence implicates ROS in the AD etiology, clinical trials with antioxidant therapies have not produced consistent results. In this review, we will discuss the role of oxidative stress in synaptic dysfunction in AD, innovative therapeutic strategies evolved based on a better understanding of the complexity of molecular mechanisms of AD, and the dual role ROS play in health and disease.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Oxidative stress is associated with a number of inflammatory and degenerative pathologies and is a significant biomarker common to the pathophysiology of both AD and PD. 55 , 58”
From Therapeutic Properties and Pharmacological Activities of Asiaticoside and Madecassoside: A Review (2023) · cites this paper as [58]
Experimental — accuracy not yet measuredIn the citing paper
“since there is a strong correlation between immune activation and oxidative damage in neurodegenerative disease [42,43,44]”
From ROS Generation in Microglia: Understanding Oxidative Stress and Inflammation in Neurodegenerative Disease (2020) · cites this paper as [43]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Free Radicals in the Physiological Control of Cell Function
Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855
Oxyl radicals, redox-sensitive signalling cascades and antioxidants
Genestra, M. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.04.009 · Cited by 4,930
Hypothetical model of dynamic biomarkers of the Alzheimer's pathological cascade
Jack, C. R., Knopman, D. S., Jagust, W. J., Shaw, L. M., Aisen, P. S., Weiner, M. W., Petersen, R. C., & Trojanowski, J. Q. (2010) · The Lancet Neurology · doi:10.1016/s1474-4422(09)70299-6 · Cited by 4,806
Terry, R. D., Masliah, E., Salmon, D. P., Butters, N., DeTeresa, R., Hill, R., Hansen, L. A., & Katzman, R. (1991) · Annals of Neurology · doi:10.1002/ana.410300410 · Cited by 4,397
Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling
Ray, P. D., Huang, B.-W., & Tsuji, Y. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.01.008 · Cited by 4,373
Oxidative mechanisms in the toxicity of metal ions
Stohs, S. J., & Bagchi, D. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(94)00159-h · Cited by 4,219
Triple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles
Oddo, S., Caccamo, A., Shepherd, J. D., Murphy, M. P., Golde, T. E., Kayed, R., Metherate, R., Mattson, M. P., Akbari, Y., & LaFerla, F. M. (2003) · Neuron · doi:10.1016/s0896-6273(03)00434-3 · Cited by 4,126
Malenka, R. C., & Bear, M. F. (2004) · Neuron · doi:10.1016/j.neuron.2004.09.012 · Cited by 3,968
Clinical and biomarker changes in dominantly inherited Alzheimer's disease
Bateman, R. J., Xiong, C., Benzinger, T. L. S., Fagan, A. M., Goate, A., Fox, N. C., Marcus, D. S., Cairns, N. J., Xie, X., Blazey, T. M., et al. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1202753 · Cited by 3,814
Cell Survival Responses to Environmental Stresses Via the Keap1-Nrf2-ARE Pathway
Kensler, T. W., Wakabayashi, N., & Biswal, S. (2007) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.46.120604.141046 · Cited by 3,630
Uttara, B., Singh, A., Zamboni, P., & Mahajan, R. (2009) · Current Neuropharmacology · doi:10.2174/157015909787602823 · Cited by 3,378
Neuropathological alterations in Alzheimer disease
Serrano-Pozo, A., Frosch, M. P., Masliah, E., & Hyman, B. T. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006189 · Cited by 3,345
Meta-Analysis: High-Dosage Vitamin E Supplementation May Increase All-Cause Mortality
Miller, E. R., Pastor-Barriuso, R., Dalal, D., Riemersma, R. A., Appel, L. J., & Guallar, E. (2005) · Annals of Internal Medicine · doi:10.7326/0003-4819-142-1-200501040-00110 · Cited by 2,577
Oxidative stress hypothesis in Alzheimer’s disease
Markesbery, W. R. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00629-6 · Cited by 2,383
A Controlled Trial of Selegiline, Alpha-Tocopherol, or Both as Treatment for Alzheimer's Disease
Sano, M., Ernesto, C., Thomas, R. G., Klauber, M. R., Schafer, K., Grundman, M., Woodbury, P., Growdon, J., Cotman, C. W., Pfeiffer, E., et al. (1997) · New England Journal of Medicine · doi:10.1056/nejm199704243361704 · Cited by 2,380
Synapse loss in frontal cortex biopsies in Alzheimer's disease: Correlation with cognitive severity
DeKosky, S. T., & Scheff, S. W. (1990) · Annals of Neurology · doi:10.1002/ana.410270502 · Cited by 2,376
The organization of recent and remote memories
Frankland, P. W., & Bontempi, B. (2005) · Nature Reviews Neuroscience · doi:10.1038/nrn1607 · Cited by 2,138
Copper, iron and zinc in Alzheimer's disease senile plaques
Lovell, M. A., Robertson, J. D., Teesdale, W. J., Campbell, J. L., & Markesbery, W. R. (1998) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(98)00092-6 · Cited by 2,120
Cellular mechanisms and physiological consequences of redox-dependent signalling
Holmström, K. M., & Finkel, T. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3801 · Cited by 2,093
Intracellular amyloid-β in Alzheimer's disease
LaFerla, F. M., Green, K. N., & Oddo, S. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2168 · Cited by 1,942
Vitamin E and Donepezil for the Treatment of Mild Cognitive Impairment
Petersen, R. C., Thomas, R. G., Grundman, M., Bennett, D., Doody, R., Ferris, S., Galasko, D., Jin, S., Kaye, J., Levey, A., et al. (2005) · New England Journal of Medicine · doi:10.1056/nejmoa050151 · Cited by 1,844
Jones, D. P. (2006) · Antioxidants & Redox Signaling · doi:10.1089/ars.2006.8.1865 · Cited by 1,726
Natural oligomers of the amyloid-β protein specifically disrupt cognitive function
Cleary, J. P., Walsh, D. M., Hofmeister, J. J., Shankar, G. M., Kuskowski, M. A., Selkoe, D. J., & Ashe, K. H. (2004) · Nature Neuroscience · doi:10.1038/nn1372 · Cited by 1,722
Role of ROS and RNS Sources in Physiological and Pathological Conditions
Meo, S. D., Reed, T. T., Venditti, P., & Víctor, V. M. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/1245049 · Cited by 1,712
Baumgart, M., Snyder, H. M., Carrillo, M. C., Fazio, S., Kim, H., & Johns, H. (2015) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2015.05.016 · Cited by 1,660
Regulation of NMDA receptor trafficking by amyloid-β
Snyder, E. M., Nong, Y., Almeida, C. G., Paul, S., Moran, T., Choi, E. Y., Nairn, A. C., Salter, M. W., Lombroso, P. J., Gouras, G. K., et al. (2005) · Nature Neuroscience · doi:10.1038/nn1503 · Cited by 1,561 · cited 1×
“However, in AD, in addition to age-related changes, the expression of neurotoxic A has been shown to reduce the amount of surface NMDA receptors in neurons and in brain tissue of AD mice [162], trigger NMDA-mediated Ca2+ influx inducing excitotoxicity and stress-related signaling pathways, exacerbating aging-related i…”
Rapid induction of Alzheimer A beta amyloid formation by zinc
Bush, A., Pettingell, W., Multhaup, G., d Paradis, M., Vonsattel, J., Gusella, J., Beyreuther, K., Masters, C., & Tanzi, R. (1994) · Science · doi:10.1126/science.8073293 · Cited by 1,522
Cherny, R. A., Atwood, C. S., Xilinas, M. E., Gray, D. N., Jones, W. D., McLean, C. A., Barnham, K. J., Volitakis, I., Fraser, F. W., Kim, Y.-S., et al. (2001) · Neuron · doi:10.1016/s0896-6273(01)00317-8 · Cited by 1,447
Alzheimer’s Disease: The Challenge of the Second Century
Holtzman, D. M., Morris, J. C., & Goate, A. M. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3002369 · Cited by 1,424
Synaptic plasticity, memory and the hippocampus: a neural network approach to causality
Neves, G., Cooke, S. F., & Bliss, T. (2007) · Nature reviews. Neuroscience · doi:10.1038/nrn2303 · Cited by 1,287
Mattson, M. P. (2008) · Ageing Research Reviews · doi:10.1016/j.arr.2007.08.007 · Cited by 1,253
The Intersection of Amyloid Beta and Tau at Synapses in Alzheimer’s Disease
Spires-Jones, T. L., & Hyman, B. T. (2014) · Neuron · doi:10.1016/j.neuron.2014.05.004 · Cited by 1,201
Tau PET patterns mirror clinical and neuroanatomical variability in Alzheimer’s disease
Ossenkoppele, R., Schonhaut, D. R., Schöll, M., Lockhart, S. N., Ayakta, N., Baker, S. L., O’Neil, J. P., Janabi, M., Lazaris, A., Cantwell, A., et al. (2016) · Brain · doi:10.1093/brain/aww027 · Cited by 1,185
Huang, X., Atwood, C., Hartshorn, M. A., Multhaup, G., Goldstein, L. E., Scarpa, R. C., Cuajungco, M. P., Gray, D. N., Lim, J. T., Moir, R. D., et al. (1999) · Biochemistry · doi:10.1021/bi990438f · Cited by 1,117
Manczak, M., Anekonda, T. S., Henson, E., Park, B. S., Quinn, J., & Reddy, P. H. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl066 · Cited by 1,104
The cholinergic system in aging and neuronal degeneration
Schliebs, R., & Arendt, T. (2011) · Behavioural Brain Research · doi:10.1016/j.bbr.2010.11.058 · Cited by 1,047
AMPAR Removal Underlies Aβ-Induced Synaptic Depression and Dendritic Spine Loss
Hsieh, H., Boehm, J., Sato, C., Iwatsubo, T., Tomita, T., Sisodia, S., & Malinow, R. (2006) · Neuron · doi:10.1016/j.neuron.2006.10.035 · Cited by 1,042
Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo
Meng, T.-C., Fukada, T., & Tonks, N. K. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00445-8 · Cited by 1,040
Soluble oligomers of the amyloid β-protein impair synaptic plasticity and behavior
Selkoe, D. J. (2008) · Behavioural Brain Research · doi:10.1016/j.bbr.2008.02.016 · Cited by 1,038
Cutler, R. G., Kelly, J., Storie, K., Pedersen, W. A., Tammara, A., Hatanpaa, K., Troncoso, J. C., & Mattson, M. P. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0305799101 · Cited by 1,008
Biomarker Modeling of Alzheimer’s Disease
Jack, C. R., & Holtzman, D. M. (2013) · Neuron · doi:10.1016/j.neuron.2013.12.003 · Cited by 1,002
Functional brain abnormalities in young adults at genetic risk for late-onset Alzheimer's dementia
Reiman, E. M., Chen, K., Alexander, G. E., Caselli, R. J., Bandy, D., Osborne, D., Saunders, A. M., & Hardy, J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2635903100 · Cited by 977
Reddy, P. H., & Beal, M. F. (2008) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2007.12.002 · Cited by 975
Lammich, S., Kojro, E., Postina, R., Gilbert, S., Pfeiffer, R., Jasionowski, M., Haass, C., & Fahrenholz, F. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3922 · Cited by 975
A systematic RNAi screen identifies a critical role for mitochondria in C. elegans longevity
Lee, S. S., Lee, R. Y. N., Fraser, A. G., Kamath, R. S., Ahringer, J., & Ruvkun, G. (2003) · Nature Genetics · doi:10.1038/ng1056 · Cited by 969
Oxidative stress, mitochondrial dysfunction and neurodegenerative diseases; a mechanistic insight
Bhat, A. H., Dar, K. B., Anees, S., Zargar, M. A., Masood, A., Sofi, M. A., & Ganie, S. A. (2015) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2015.07.025 · Cited by 962
Ageing and neuronal vulnerability
Mattson, M. P., & Magnus, T. (2006) · Nature Reviews Neuroscience · doi:10.1038/nrn1886 · Cited by 957
Mitochondria take center stage in aging and neurodegeneration
Beal, M. F. (2005) · Annals of Neurology · doi:10.1002/ana.20624 · Cited by 957
Yao, J., Irwin, R. W., Zhao, L., Nilsen, J., Hamilton, R. T., & Brinton, R. D. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903563106 · Cited by 940
Neuronal calcium mishandling and the pathogenesis of Alzheimer's disease
Bezprozvanny, I., & Mattson, M. P. (2008) · Trends in Neurosciences · doi:10.1016/j.tins.2008.06.005 · Cited by 938
Peroxiredoxins are conserved markers of circadian rhythms
Edgar, R. S., Green, E. W., Zhao, Y., Gerben Van Ooijen, A., Olmedo, M., Qin, X., Xu, Y. Q., Pan, M., Valekunja, U. K., Feeney, K. A., et al. (2012) · Nature · doi:10.1038/nature11088 · Cited by 915
Paradigm shift in neuroprotection by NMDA receptor blockade: memantine and beyond
Lipton, S. A. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd1958 · Cited by 909
De Felice, F. G., Velasco, P. T., Lambert, M. P., Viola, K., Fernandez, S. J., Ferreira, S. T., & Klein, W. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607483200 · Cited by 882
Clark, C. M., Pontecorvo, M. J., Beach, T. G., Bedell, B. J., Coleman, R. E., Doraiswamy, P. M., Fleisher, A. S., Reiman, E. M., Sabbagh, M. N., Sadowsky, C. H., et al. (2012) · The Lancet Neurology · doi:10.1016/s1474-4422(12)70142-4 · Cited by 855
A Direct Role for Dual Oxidase in Drosophila Gut Immunity
Ha, E.-M., Oh, C.-T., Bae, Y. S., & Lee, W. (2005) · Science · doi:10.1126/science.1117311 · Cited by 849
Mańczak, M., Calkins, M. J., & Reddy, P. H. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr139 · Cited by 847
Mitochondrial Dysfunction in Neurodegenerative Diseases
Johri, A., & Beal, M. F. (2012) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.112.192138 · Cited by 806
The Alzheimer’s disease mitochondrial cascade hypothesis: progress and perspectives
Swerdlow, R. H., Burns, J. M., & Khan, S. M. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.09.010 · Cited by 786 · cited 1×
“The mitochondrial cascade hypothesis states that in sporadic, late-onset AD, loss of mitochondrial function associated with age affects the expression and processing of A PP initiating A accumulation [33].”
BackgroundThe case for rejecting the amyloid cascade hypothesis
Herrup, K. (2015) · Nature Neuroscience · doi:10.1038/nn.4017 · Cited by 768
Expression of Nrf2 in Neurodegenerative Diseases
Ramsey, C. P., Glass, C. A., Montgomery, M. B., Lindl, K. A., Ritson, G. P., Chia, L. A., Hamilton, R. L., Chu, C. T., & Jordan-Sciutto, K. L. (2007) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/nen.0b013e31802d6da9 · Cited by 760
Mitochondrial Aβ: a potential focal point for neuronal metabolic dysfunction in Alzheimer's disease
Caspersen, C., Wang, N., Yao, J., Sosunov, A., Chen, X., Lustbader, J. W., Xu, H. W., Stern, D., McKhann, G., & Du Yan, S. (2005) · The FASEB Journal · doi:10.1096/fj.05-3735fje · Cited by 738
Early deficits in synaptic mitochondria in an Alzheimer's disease mouse model
Du, H., Guo, L., Yan, S., Sosunov, A. A., McKhann, G. M., & ShiDu Yan, S. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1006586107 · Cited by 704
Adlard, P. A., Cherny, R. A., Finkelstein, D. I., Gautier, E., Robb, E., Cortes, M., Volitakis, I., Liu, X., Smith, J. P., Perez, K., et al. (2008) · Neuron · doi:10.1016/j.neuron.2008.06.018 · Cited by 672
Structure and novel exons of the human .tau. gene
Andreadis, A., Brown, W. M., & Kosik, K. S. (1992) · Biochemistry · doi:10.1021/bi00158a027 · Cited by 659
Calkins, M. J., Manczak, M., Mao, P., Shirendeb, U., & Reddy, P. H. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr381 · Cited by 646
Kwon, J., Lee, S.-R., Yang, K.-S., Ahn, Y., Kim, Y. J., Stadtman, E. R., & Rhee, S. G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407396101 · Cited by 631
Dysken, M. W., Sano, M., Asthana, S., Vertrees, J. E., Pallaki, M., Llorente, M., Love, S., Schellenberg, G. D., McCarten, J. R., Malphurs, J., et al. (2014) · JAMA · doi:10.1001/jama.2013.282834 · Cited by 628
Mitochondrial abnormalities in Alzheimer brain: Mechanistic implications
Bubber, P., Haroutunian, V., Fisch, G., Blass, J. P., & Gibson, G. E. (2005) · Annals of Neurology · doi:10.1002/ana.20474 · Cited by 622
Is Alzheimer’s disease a type 3 diabetes? A critical appraisal
Kandimalla, R., Thirumala, V., & Reddy, P. H. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.08.018 · Cited by 621
Brain Glucose Hypometabolism and Oxidative Stress in Preclinical Alzheimer's Disease
Mosconi, L., Pupi, A., & de Leon, M. J. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1427.007 · Cited by 616
Mitochondrial dysfunction in neurodegenerative diseases
Beal, M. F. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00114-5 · Cited by 611
Sites of reactive oxygen species generation by mitochondria oxidizing different substrates
Quinlan, C. L., Perevoshchikova, I. V., Hey‐Mogensen, M., Orr, A. L., & Brand, M. D. (2013) · Redox Biology · doi:10.1016/j.redox.2013.04.005 · Cited by 608
Oxidative stress hypothesis in Alzheimer’s disease: a reappraisal
Praticò, D. (2008) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2008.09.001 · Cited by 606
Miller, L. M., Wang, Q., Telivala, T. P., Smith, R., Lanzirotti, A., & Judith Miklossy, A. (2005) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.09.004 · Cited by 588
Crystal, H., Dickson, D., Fuld, P., Masur, D., Scott, R., Mehler, M., Masdeu, J., Kawas, C., Aronson, M., & Wolfson, L. (1988) · Neurology · doi:10.1212/wnl.38.11.1682 · Cited by 586
Extrasynaptic NMDA Receptor Involvement in Central Nervous System Disorders
Parsons, M. P., & Raymond, L. A. (2014) · Neuron · doi:10.1016/j.neuron.2014.03.030 · Cited by 567
Ringman, J. M., Frautschy, S. A., Teng, E., Begum, A. N., Bardens, J., Beigi, M., Gylys, K. H., Badmaev, V., Heath, D. D., Apostolova, L. G., et al. (2012) · Alzheimer s Research & Therapy · doi:10.1186/alzrt146 · Cited by 559
In Situ Oxidative Catalysis by Neurofibrillary Tangles and Senile Plaques in Alzheimer’s Disease
Sayre, L. M., Perry, G. L., Harris, P. L. R., Liu, Y. A., Schubert, K. A., & Smith, M. A. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0740270.x · Cited by 543
Oxidative DNA damage in mild cognitive impairment and late-stage Alzheimer's disease
Lovell, M. A., & Markesbery, W. R. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm821 · Cited by 515
Kamat, P. K., Kalani, A., Rai, S., Swarnkar, S., Tota, S., Nath, C., & Tyagi, N. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-9053-6 · Cited by 511
Biological metals and metal-targeting compounds in major neurodegenerative diseases
Barnham, K. J., & Bush, A. I. (2014) · Chem. Soc. Rev. · doi:10.1039/c4cs00138a · Cited by 497
Alzheimer's disease results from the cerebral accumulation and cytotoxicity of amyloid ß-protein
Selkoe, D. J. (2001) · Journal of Alzheimer's Disease · doi:10.3233/jad-2001-3111 · Cited by 466
Mantyh, P. W., Ghilardi, J. R., Rogers, S. D., DeMaster, E., Allen, C. J., Stimson, E. R., & Maggio, J. E. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb03639.x · Cited by 466
Drug development in Alzheimer’s disease: the path to 2025
Cummings, J., Aisen, P. S., DuBois, B., Frölich, L., Jack, C. R., Jones, R. W., Morris, J. C., Raskin, J., Dowsett, S. A., & Scheltens, P. (2016) · Alzheimer's Research & Therapy · doi:10.1186/s13195-016-0207-9 · Cited by 459
Regulation of cholesterol and sphingomyelin metabolism by amyloid-β and presenilin
Grimm, M. O. W., Grimm, H. S., Pätzold, A. J., Zinser, E. G., Halonen, R., Duering, M., Tschäpe, J., Strooper, B. D., Müller, U., Shen, J., et al. (2005) · Nature Cell Biology · doi:10.1038/ncb1313 · Cited by 454
Oxidative stress and mitochondrial dysfunction in neurodegenerative diseases
Trushina, E. V., & McMurray, C. T. (2007) · Neuroscience · doi:10.1016/j.neuroscience.2006.10.056 · Cited by 451
Self-citationMetal dyshomeostasis and oxidative stress in Alzheimer’s disease
Greenough, M. A., Camakaris, J., & Bush, A. I. (2012) · Neurochemistry International · doi:10.1016/j.neuint.2012.08.014 · Cited by 447
Trushina, E., Dutta, T., Persson, X.-M. T., Mielke, M. M., & Petersen, R. C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0063644 · Cited by 438
Self-citationLee, J., Cole, T. B., Palmiter, R. D., Suh, S. W., & Koh, J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092034699 · Cited by 432
Synaptic loss in Alzheimer's disease and other dementias
Hamos, J. E., DeGennaro, L. J., & Drachman, D. A. (1989) · Neurology · doi:10.1212/wnl.39.3.355 · Cited by 432
Han, X., Rozen, S., Boyle, S. H., Hellegers, C., Cheng, H., Burke, J. R., Welsh-Bohmer, K. A., Doraiswamy, P. M., & Kaddurah-Daouk, R. (2011) · PLoS ONE · doi:10.1371/journal.pone.0021643 · Cited by 429
Heme oxygenase-1 is associated with the neurofibrillary pathology of Alzheimer's disease.
Smith, M. A., Kutty, R. K., Richey, P. L., Yan, S. D., Stern, D., Chader, G. J., Wiggert, B. O., Petersen, R. B., & Perry, G. L. (1994) · PubMed Central · Cited by 425
Unraveling the Truth About Antioxidants: Mitohormesis explains ROS-induced health benefits
Ristow, M. (2014) · Nature Medicine · doi:10.1038/nm.3624 · Cited by 417
Extension of Drosophila Life Span by RNAi of the Mitochondrial Respiratory Chain
Copeland, J. M., Cho, J., Lo, T., Hur, J. H., Bahadorani, S., Arabyan, T., Rabie, J., Soh, J., & Walker, D. W. (2009) · Current Biology · doi:10.1016/j.cub.2009.08.016 · Cited by 409
Spatial correlation between brain aerobic glycolysis and amyloid-β (Aβ) deposition
Vlassenko, A. G., Vaishnavi, S. N., Couture, L., Sacco, D., Shannon, B. J., Mach, R. H., Morris, J. C., Raichle, M. E., & Mintun, M. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1010461107 · Cited by 404
Pospisilik, J. A., Knauf, C., Joza, N., Benit, P., Orthofer, M., Cani, P. D., Ebersberger, I., Nakashima, T., Sarao, R., Neely, G., et al. (2007) · Cell · doi:10.1016/j.cell.2007.08.047 · Cited by 404
Butterfield, D. A., Di Domenico, F., & Barone, E. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.06.010 · Cited by 402
The BCM theory of synapse modification at 30: interaction of theory with experiment
Cooper, L. N., & Bear, M. F. (2012) · Nature Reviews Neuroscience · doi:10.1038/nrn3353 · Cited by 395
Reddy, P. H., Tripathi, R., Troung, Q., Tirumala, K., Reddy, T. P., Anekonda, V., Shirendeb, U. P., Calkins, M. J., Reddy, A. P., Mao, P., et al. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.10.011 · Cited by 394
Galasko, D. R., Peskind, E., Clark, C. M., Quinn, J. F., Ringman, J. M., Jicha, G. A., Cotman, C., Cottrell, B., Montine, T. J., Thomas, R. G., et al. (2012) · Archives of Neurology · doi:10.1001/archneurol.2012.85 · Cited by 377
Gabuzda, D., Busciglio, J., Chen, L. B., Matsudaira, P., & Yankner, B. A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36875-8 · Cited by 373
Microglia: activation and their significance in the central nervous system
Nakajima, K., & Kohsaka, S. (2001) · Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a002969 · Cited by 371
Mitochondrion-derived reactive oxygen species lead to enhanced amyloid beta formation
Leuner, K., Schütt, T., Kurz, C., Eckert, S. H., Schiller, C., Occhipinti, A., Mai, S., Jendrach, M., Eckert, G. P., Kruse, S. E., et al. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4173 · Cited by 354
Suh, S. W., Jensen, K. B., Jensen, M. S., Silva, D. S., Kesslak, P. J., Danscher, G., & Frederickson, C. J. (2000) · Brain Research · doi:10.1016/s0006-8993(99)02096-x · Cited by 353
Liu, X., Jiang, N., Hughes, B., Bigras, E., Shoubridge, E., & Hekimi, S. (2005) · Genes & Development · doi:10.1101/gad.1352905 · Cited by 345
The Role of Oxidative Stress in Alzheimer Disease
Markesbery, W. R. (1999) · Archives of Neurology · doi:10.1001/archneur.56.12.1449 · Cited by 312
Targeting Oxidative Stress in Central Nervous System Disorders
Patel, M. (2016) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2016.06.007 · Cited by 312
Reddy, P. H. (2011) · Brain Research · doi:10.1016/j.brainres.2011.07.052 · Cited by 311
Baker, L. D., Frank, L. L., Foster‐Schubert, K. E., Green, P. S., Wilkinson, C. W., McTiernan, A., Cholerton, B., Plymate, S. R., Fishel, M. A., Watson, G. S., et al. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100768 · Cited by 309
Oxidative stress, protein modification and Alzheimer disease
Tramutola, A., Lanzillotta, C., Perluigi, M., & Butterfield, D. A. (2017) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.06.005 · Cited by 303
Wang, L. Y., Benzinger, T. L. S., Su, Y., Christensen, J. J., Friedrichsen, K. A., Aldea, P., McConathy, J., Cairns, N. J., Fagan, A. M., Morris, J. C., et al. (2016) · JAMA Neurology · doi:10.1001/jamaneurol.2016.2078 · Cited by 301
Long Chain Ceramides Activate Protein Phosphatase-1 and Protein Phosphatase-2A
Chalfant, C. E., Kishikawa, K., Mumby, M. C., Kamibayashi, C., Bielawska, A. E., & Hannun, Y. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.29.20313 · Cited by 300
Decreased plasma antioxidants in patients with Alzheimer's disease
Kim, T., Pae, C., Yoon, S.-J., Jang, W., Lee, N. J., Kim, J.-J., Lee, S., Lee, C., Paik, I.-H., & Lee, C. (2006) · International Journal of Geriatric Psychiatry · doi:10.1002/gps.1469 · Cited by 293
Heizmann, C. W., & Cox, J. A. (1998) · BioMetals · doi:10.1023/a:1009212521172 · Cited by 285
Kinoshita, A., Fukumoto, H., Shah, T., Whelan, C. M., Irizarry, M. C., & Hyman, B. T. (2003) · Journal of Cell Science · doi:10.1242/jcs.00643 · Cited by 284
Implications of GABAergic Neurotransmission in Alzheimer’s Disease
Li, Y., Sun, H., Chen, Z., Xu, H., Bu, G., & Zheng, H. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00031 · Cited by 282
Lee, J.-T., Xu, J., Lee, J.-M., Ku, G., Han, X., Yang, D.-I., Chen, S., & Hsu, C. Y. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200307017 · Cited by 280
Mechanisms of mitochondrial dysfunction and energy deficiency in Alzheimer’s disease
Atamna, H., & Frey, W. H. (2007) · Mitochondrion · doi:10.1016/j.mito.2007.06.001 · Cited by 278
Antioxidant clinical trials in mild cognitive impairment and Alzheimer's disease
Mecocci, P., & Polidori, M. C. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.10.006 · Cited by 277
Roles for dysfunctional sphingolipid metabolism in Alzheimer's disease neuropathogenesis
Haughey, N. J., Bandaru, V. V. R., Bae, M. H., & Mattson, M. P. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2010.05.003 · Cited by 277
Trushina, E. V., Nemutlu, E., Zhang, S., Christensen, T. A., Camp, J. J., Mesa, J., Siddiqui, A., Tamura, Y., Sesaki, H., Wengenack, T. M., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0032737 · Cited by 268
Self-citationOxidative DNA damage in peripheral leukocytes of mild cognitive impairment and AD patients
Migliore, L., Fontana, I., Trippi, F., Colognato, R., Coppedè, F., Tognoni, G., Nucciarone, B., & Siciliano, G. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.07.016 · Cited by 266
Mitochondria dysfunction of Alzheimer's disease cybrids enhances Aβ toxicity
Cardoso, S. M., Santana, I. J., Swerdlow, R. H., & Oliveira, C. R. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02438.x · Cited by 262
Therapies for Prevention and Treatment of Alzheimer’s Disease
Mendiola-Precoma, J., Berumen, L. C., Padilla, K., & García‐Alcocer, G. (2016) · BioMed Research International · doi:10.1155/2016/2589276 · Cited by 262
Intracellular Aβ and cognitive deficits precede β-amyloid deposition in transgenic arcAβ mice
Knobloch, M., Konietzko, U., Krebs, D. C., & Nitsch, R. M. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.06.019 · Cited by 259
Nuclear factor erythroid 2-related factor 2 protects against beta amyloid
Kanninen, K. M., Malm, T., Jyrkkänen, H.-K., Goldsteins, G., Keksa-Goldsteine, V., Tanila, H., Yamamoto, M. P., Ylä‐Herttuala, S., Levonen, A., & Koıstınaho, J. (2008) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2008.07.010 · Cited by 259
Intraneuronal Aβ-Amyloid Precedes Development of Amyloid Plaques in Down Syndrome
Gyure, K. A., Durham, R., Stewart, W. F., Smialek, J. E., & Troncoso, J. C. (2001) · Archives of Pathology & Laboratory Medicine · doi:10.5858/2001-125-0489-iaapdo · Cited by 248
The Nrf2-ARE Pathway: A Valuable Therapeutic Target for the Treatment of Neurodegenerative Diseases
Gururaj Joshi, A., & Johnson, J. A. (2012) · Recent Patents on CNS Drug Discovery · doi:10.2174/157488912803252023 · Cited by 246
Vernochet, C., Mourier, A., Bezy, O., Macotela, Y., Boucher, J., Rardin, M. J., An, D., Lee, K. Y., Ilkayeva, O. R., Zingaretti, C. M., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.10.016 · Cited by 245
Abnormal Mitochondrial Dynamics in the Pathogenesis of Alzheimer's Disease
Zhu, X., Perry, G., Smith, M. A., & Wang, X. (2012) · Journal of Alzheimer's Disease · doi:10.3233/jad-2012-129005 · Cited by 242
Smith, M. A., Rudnicka-Nawrot, M., Richey, P., Praprotnik, D., Mulvihill, P., Miller, C., Sayre, L., & Perry, G. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.64062660.x · Cited by 240
NMDA receptor function, memory, and brain aging
Newcomer, J. W., Farber, N. B., & Olney, J. W. (2000) · Dialogues in Clinical Neuroscience · doi:10.31887/dcns.2000.2.3/jnewcomer · Cited by 232
A Randomized Trial of Vitamin E Supplementation and Cognitive Function in Women
Kang, J. H. (2006) · Archives of Internal Medicine · doi:10.1001/archinte.166.22.2462 · Cited by 227
The Metabolism of Tyramine by Monoamine Oxidase A/B Causes Oxidative Damage to Mitochondrial DNA
Hauptmann, N., Grimsby, J. S., Shih, J. C., & Cadenas, E. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0510 · Cited by 221
Binding of zinc(II) and copper(II) to the full‐length Alzheimer’s amyloid‐β peptide
Tõugu, V., Tiiman, A., & Palumaa, P. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.05061.x · Cited by 219
Mitochondrial membrane fluidity and oxidative damage to mitochondrial DNA in aged and AD human brain
Mecocci, P., Beal, M. F., Cecchetti, R., Polidori, M. C., Cherubini, A., Chionne, F., Avellini, L., Romano, G., & Senin, U. (1997) · Molecular and Chemical Neuropathology · doi:10.1007/bf02815160 · Cited by 215
Mitochondrial alterations Alzheimer's disease
Baloyannis, S. J., Costa, V., & Michmizos, D. (2004) · American Journal of Alzheimer's Disease & Other Dementias® · doi:10.1177/153331750401900205 · Cited by 206
Increased lipoprotein oxidation in alzheimer’s disease
Schippling, S., Kontush, A., Arlt, S., Buhmann, C., Stürenburg, H.-J., Mann, U. M., Müller‐Thomsen, T., & Beisiegel†, U. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00247-6 · Cited by 202
Altered brain energetics induces mitochondrial fission arrest in Alzheimer’s Disease
Zhang, L., Trushin, S., Christensen, T. A., Bachmeier, B. V., Gateno, B., Schroeder, A., Yao, J., Itoh, K., Sesaki, H., Poon, W. W., et al. (2016) · Scientific Reports · doi:10.1038/srep18725 · Cited by 201
Self-citationRecent advances in the application of metabolomics to Alzheimer's Disease
Trushina, E. V., & Mielke, M. M. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.06.014 · Cited by 200
Self-citationThe influence of common free radicals and antioxidants on development of Alzheimer’s Disease
Wojtunik‐Kulesza, K. A., Oniszczuk, A., Oniszczuk, T., & Waksmundzka‐Hajnos, M. (2016) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2015.12.024 · Cited by 200
Glial heme oxygenase-1 expression in Alzheimer disease and mild cognitive impairment
Schipper, H. M., BENNETT, D., Liberman, A., Bienias, J. L., Schneider, J. A., Kelly, J. W., & Arvanitakis, Z. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.01.016 · Cited by 199
Carbonyl Toxicology and Alzheimer's Disease
Picklo, M. J. (2002) · Toxicology and Applied Pharmacology · doi:10.1006/taap.2002.9506 · Cited by 194
In Vivo Tau, Amyloid, and Gray Matter Profiles in the Aging Brain
Sepulcre, J., Schultz, A. P., Sabuncu, M. R., Gómez‐Isla, T., Chhatwal, J. P., Becker, A., Sperling, R. A., & Johnson, K. A. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.0639-16.2016 · Cited by 182
Dias, K. S. T., & Viegas, C. (2014) · Current Neuropharmacology · doi:10.2174/1570159x1203140511153200 · Cited by 178
Alzheimer's disease cybrids replicate beta-amyloid abnormalities through cell death pathways.
Khan, S. M., Cassarino, D. S., Abramova, N. N., Keeney, P. M., Borland, M. K., Pa, T., Krebs, C. T., Bennett, J. C., Parks, J. K., Swerdlow, R. H., et al. (2000) · PubMed · Cited by 176
Mitohormesis in exercise training
Merry, T. L., & Ristow, M. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.11.032 · Cited by 176
Increased amount of zinc in the hippocampus and amygdala of Alzheimer's diseased brains
Danscher, G., Jensen, K. B., Frederickson, C. J., Kemp, K., Andreasen, A., Juhl, S., Stoltenberg, M., & Ravid, R. (1997) · Journal of Neuroscience Methods · doi:10.1016/s0165-0270(97)00079-4 · Cited by 174
Regulated Formation of Golgi Secretory Vesicles Containing Alzheimer β-Amyloid Precursor Protein
Xu, H., Greengard, P., & Gandy, S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.40.23243 · Cited by 168
Mondragón‐Rodríguez, S., Perry, G. L., Zhu, X., Moreira, P. I., Acevedo, M., & Williams, S. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/940603 · Cited by 163
Apolipoprotein E, not fibrillar β-amyloid, reduces cerebral glucose metabolism in normal aging
Jagust, W. J., Landau, S. M., & Initiative, F. T. A. D. N. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.3266-12.2012 · Cited by 162
Chronic dietary α-lipoic acid reduces deficits in hippocampal memory of aged Tg2576 mice
Quinn, J. F., Bussiere, J. R., Hammond, R., Montine, T. J., Henson, E., Jones, R. E., & Stackman, R. W. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.12.014 · Cited by 161
Kumar, A., & Singh, A. (2015) · Frontiers in Pharmacology · doi:10.3389/fphar.2015.00206 · Cited by 157
Robinson, J. L., Molina-Porcel, L., Corrada, M. M., Raible, K., Lee, E. B., Lee, V. M.-Y., Kawas, C. H., & Trojanowski, J. Q. (2014) · Brain · doi:10.1093/brain/awu190 · Cited by 157
Eckert, A., Hauptmann, S., Scherping, I., Rhein, V. F., Müller-Spahn, F., Götz, J., & Müller, W. E. (2008) · Neurodegenerative Diseases · doi:10.1159/000113689 · Cited by 155
Han, X. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2010.01.010 · Cited by 154
The oxidative stress hypothesis in Alzheimer's disease.
Pădurariu, M., Ciobica, A. S., Lefter, R. M., Șerban, I. L., Ștefănescu, C., & Chiriță, R. (2013) · PubMed · Cited by 151
Valla, J., Yaari, R., Wolf, A. B., Kusne, Y., Beach, T. G., Roher, A. E., Corneveaux, J. J., Huentelman, M. J., Caselli, R. J., & Reiman, E. M. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100129 · Cited by 150
The Mitochondrial Spiral: An Adequate Cause of Dementia in the Alzheimer's Syndrome
Blass, J. P. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb05576.x · Cited by 150
Baumgart, M., Priebe, S., Groth, M., Hartmann, N., Menzel, U., Pandolfini, L., Koch, P., Felder, M., Ristow, M., Englert, C., et al. (2016) · Cell Systems · doi:10.1016/j.cels.2016.01.014 · Cited by 150
Multiple faces of dynamin-related protein 1 and its role in Alzheimer's disease pathogenesis
Kandimalla, R. J. L., & Reddy, P. H. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.12.018 · Cited by 148
Schmeisser, S., Priebe, S., Groth, M., Monajembashi, S., Hemmerich, P. H., Guthke, R., Platzer, M., & Ristow, M. (2013) · Molecular Metabolism · doi:10.1016/j.molmet.2013.02.002 · Cited by 147
Metals and Neuronal Metal Binding Proteins Implicated in Alzheimer’s Disease
Cristóvão, J. S., Santos, R., & Gomes, C. M. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/9812178 · Cited by 146
Ichimura, H., Parthasarathi, K., Quadri, S. K., Issekutz, A. C., & Bhattacharya, J. (2003) · Journal of Clinical Investigation · doi:10.1172/jci17271 · Cited by 141
Respiratory chain dysfunction in skeletal muscle does not cause insulin resistance
Wredenberg, A., Freyer, C., Sandström, M. E., Katz, A., Wibom, R., Westerblad, H., & Larsson, N.-G. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.09.029 · Cited by 141
Friedlich, A. L., Lee, J., van Groen, T., Cherny, R. A., Volitakis, I., Cole, T. B., Palmiter, R. D., Koh, J., & Bush, A. I. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.0297-04.2004 · Cited by 138
Biochemistry and Molecular Biology of Amyloid β‐Protein and the Mechanism of Alzheimer's Disease
(2008) · Handbook of Clinical Neurology · doi:10.1016/s0072-9752(07)01223-7 · Cited by 137
Induction of Alzheimer Antigens by an Uncoupler of Oxidative Phosphorylation
Blass, J. P., Baker, A. C., Ko, L., & Black, R. S. (1990) · Archives of Neurology · doi:10.1001/archneur.1990.00530080046009 · Cited by 137
Current Alzheimer's disease clinical trials: Methods and placebo outcomes
Schneider, L. S. S., & Sano, M. C. (2009) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2009.07.038 · Cited by 137
Kang, J. H., Cook, N. R., Manson, J. E., Buring, J. E., Albert, C. M., & Grodstein, F. (2009) · Circulation · doi:10.1161/circulationaha.108.816900 · Cited by 136
Lee, J., Mook‐Jung, I., & Koh, J. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-11-j0002.1999 · Cited by 136
Metal exposure and Alzheimer’s pathogenesis
Liu, G., Huang, W., Moir, R. D., Vanderburg, C. R., Lai, B. C. H., Peng, Z., Tanzi, R. E., Rogers, J. T., & Huang, X. (2006) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.12.011 · Cited by 135
Antioxidant and cytoprotective responses to redox stress
Mathers, J. E., Fraser, J. A., McMahon, M. J., Saunders, R. D. C., Hayes, J. D., & McLellan, L. I. (2004) · Biochemical Society Symposia · doi:10.1042/bss0710157 · Cited by 134
Lai, A. Y., & McLaurin, J. (2010) · International Journal of Alzheimer s Disease · doi:10.4061/2011/548380 · Cited by 132
Insights into Mitochondrial Dysfunction: Aging, Amyloid-β, and Tau–A Deleterious Trio
Schmitt, K., Grimm, A., Wilkaniec, A., Strosznajder, J. B., Götz, J., & Eckert, A. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4400 · Cited by 132
Miller, E. C., Teravskis, P. J., Dummer, B. W., Zhao, X., Huganir, R. L., & Liao, D. (2014) · European Journal of Neuroscience · doi:10.1111/ejn.12507 · Cited by 131
Compounding artefacts with uncertainty, and an amyloid cascade hypothesis that is ‘too big to fail’
Castellani, R. J., & Smith, M. A. (2011) · The Journal of Pathology · doi:10.1002/path.2885 · Cited by 129
A study on neuroinflammation and NMDA receptor function in STZ (ICV) induced memory impaired rats
Rai, S., Kamat, P. K., Nath, C., & Shukla, R. (2012) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2012.08.008 · Cited by 129
Metal ions influx is a double edged sword for the pathogenesis of Alzheimer’s disease
Wang, P., & Wang, Z. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.10.003 · Cited by 123
Caloric restriction: Beneficial effects on brain aging and Alzheimer’s disease
Van Cauwenberghe, C., Vandendriessche, C., Libert, C., & Vandenbroucke, R. E. (2016) · Mammalian Genome · doi:10.1007/s00335-016-9647-6 · Cited by 121
Stoltenberg, M., Bush, A. I., Bach, G., Smidt, K., Larsen, A., Rungby, J., Lund, S. A., Doering, P., & Danscher, G. (2007) · Neuroscience · doi:10.1016/j.neuroscience.2007.09.025 · Cited by 114
Nucleic acid oxidation: an early feature of Alzheimer's disease
Bradley‐Whitman, M. A., Timmons, M. D., Beckett, T. L., Murphy, M. P., Lynn, B. C., & Lovell, M. A. (2014) · Journal of Neurochemistry · doi:10.1111/jnc.12444 · Cited by 112
Zhang, L., Zhang, S., Maezawa, I., Trushin, S., Minhas, P. S., Pinto, M., Jin, L., Prasain, K., Nguyen, T. D. T., Yamazaki, Y., et al. (2015) · EBioMedicine · doi:10.1016/j.ebiom.2015.03.009 · Cited by 111
Self-citationSultana, R., Mecocci, P., Mangialasche, F., Cecchetti, R., Baglioni, M., & Butterfield, D. A. (2011) · Journal of Alzheimer's Disease · doi:10.3233/jad-2011-101425 · Cited by 111
Arlt, S., Müller‐Thomsen, T., Beisiegel†, U., & Kontush, A. (2012) · Neurochemical Research · doi:10.1007/s11064-012-0860-8 · Cited by 100
Raule, N., Sevini, F., Li, S., Barbieri, A., Tallaro, F., Lomartire, L., Vianello, D., Montesanto, A., Moilanen, J. S., Bezrukov, V. V., et al. (2013) · Aging Cell · doi:10.1111/acel.12186 · Cited by 97
Impact of apoE deficiency on oxidative insults and antioxidant levels in the brain
Ramassamy, C., Krzywkowski, P., Averill‐Bates, D. A., Lussier‐Cacan, S., Théroux, L., Christen, Y., Davignon, J., & Poirier, J. (2001) · Molecular Brain Research · doi:10.1016/s0169-328x(00)00268-0 · Cited by 96
Oxidative damage as an early marker of Alzheimer's disease and mild cognitive impairment
Beal, M. F. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.09.022 · Cited by 94
Oxidatively modified RNA in mild cognitive impairment
Lovell, M. A., & Markesbery, W. R. (2007) · Neurobiology of Disease · doi:10.1016/j.nbd.2007.07.030 · Cited by 93
Emerging Link between Alzheimer’s Disease and Homeostatic Synaptic Plasticity
Jang, S.-S., & Chung, H. J. (2016) · Neural Plasticity · doi:10.1155/2016/7969272 · Cited by 93
Denzer, I., Münch, G. W., & Friedland, K. (2015) · Pharmacological Research · doi:10.1016/j.phrs.2015.11.019 · Cited by 91
Effect of energy shortage and oxidative stress on amyloid precursor protein metabolism in COS cells
Gasparini, L., Racchi, M., Benussi, L., Curti, D., Binetti, G., Bianchetti, A., Trabucchi, M., & Govoni, S. (1997) · Neuroscience Letters · doi:10.1016/s0304-3940(97)00536-3 · Cited by 89
Okadaic acid-induced Tau phosphorylation in rat brain: Role of NMDA receptor
Kamat, P., Rai, S., Swarnkar, S., Shukla, R., Ali, S., Najmi, A. K., & Nath, C. (2013) · Neuroscience · doi:10.1016/j.neuroscience.2013.01.075 · Cited by 89
Bertram, S., Brixius, K., & Brinkmann, C. K. (2016) · Endocrine · doi:10.1007/s12020-016-0976-8 · Cited by 89
Targeting the Prodromal Stage of Alzheimer's Disease: Bioenergetic and Mitochondrial Opportunities
Caldwell, C. C., Yao, J., & Brinton, R. D. (2014) · Neurotherapeutics · doi:10.1007/s13311-014-0324-8 · Cited by 86
Neuroprotective effect of curcumin on okadaic acid induced memory impairment in mice
Rajasekar, N., Dwivedi, S., Tota, S., Kamat, P. K., Hanif, K., Nath, C., & Shukla, R. (2013) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2013.04.033 · Cited by 85
Szabados, T., Dul, C., Majtényi, K., Hargitai, J., Pénzes, Z., & Urbanics, R. (2004) · Behavioural Brain Research · doi:10.1016/j.bbr.2004.01.016 · Cited by 84
Copper reduction by copper binding proteins and its relation to neurodegenerative diseases
Opazo, C., Barría, M. I., Ruiz, F. H., & Inestrosa, N. C. (2003) · BioMetals · doi:10.1023/a:1020795422185 · Cited by 83
Boom, A., Pochet, R., Authelet, M., Pradier, L., Borghgraef, P., LEUVEN, F. V., Heizmann, C. W., & Brion, J. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.09.011 · Cited by 83
The role of iron as a mediator of oxidative stress in Alzheimer disease
Castellani, R. J., Moreira, P. I., Perry, G. L., & Zhu, X. (2012) · BioFactors · doi:10.1002/biof.1010 · Cited by 82
Flagged first, then by citations
3 of the 237 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- 10.1007/s12603-013-0004-0 · DOI
Cited by
Sorted by citations
Oxidative stress, aging, and diseases
Liguori, I., Russo, G., Curcio, F., Bulli, G., Aran, L., Della-Morte, D., Gargiulo, G., Testa, G., Cacciatore, F., Bonaduce, D., et al. (2018) · Clinical Interventions in Aging · doi:10.2147/cia.s158513 · Cited by 3,979
Simpson, D. S. A., & Oliver, P. L. (2020) · Antioxidants · doi:10.3390/antiox9080743 · Cited by 1,044
Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease
Guo, T., Zhang, D., Zeng, Y., Huang, T. Y., Xu, H., & Zhao, Y. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00391-7 · Cited by 994
Role of oxidative stress in depression
Bhatt, S., Nagappa, A. N., & Patil, C. R. (2020) · Drug Discovery Today · doi:10.1016/j.drudis.2020.05.001 · Cited by 854
The plastic brain: neurotoxicity of micro- and nanoplastics
Prüst, M., Meijer, J., & Westerink, R. H. S. (2020) · Particle and Fibre Toxicology · doi:10.1186/s12989-020-00358-y · Cited by 811
Metadata
- Authors
- Tönnies, E., & Trushina, E.
- Affiliations
- Mayo Clinic (US)
- Corresponding author
- Trushina, Eugenia
- ORCID
- Trushina, Eugenia
- Venue
- Journal of Alzheimer s Disease
- Publisher
- SAGE Publications
- Published
- 2017-04-19
- Volume
- 57
- Issue
- 4
- Pages
- 1105-1121
- ISSN
- 1387-2877 (ISSN-L)
- 1875-8908
- PMC
- PMC5409043
- OpenAlex
- W2568450381
- Cited by
- 1,750
- References
- 237
- Citations by year
- 2026: 135 · 2025: 220 · 2024: 259 · 2023: 258 · 2022: 253 · 2021: 246 · 2020: 193 · 2019: 101 · 2018: 54 · 2017: 30
- FWCI
- 12.72
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Alzheimer s Disease (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute on Aging (RF1AG055549)
- National Institute of Environmental Health Sciences (R01ES020715)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- Alzheimer's disease, oxidative stress
- MeSH terms
- Alzheimer Disease, Animals, Humans, Synapses, Oxidative Stress
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