Neuroprotective strategies involving ROS in Alzheimer disease

Dumont, Magali; Beal, M. Flint

doi:10.1016/j.freeradbiomed.2010.11.026

Cited by 407Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeurological Disorders and Treatments

Neuroprotective strategies involving ROS in Alzheimer disease

Open access

Dumont, Magali, Beal, M. Flint·2011·Free Radical Biology and Medicine

DOI 10.1016/j.freeradbiomed.2010.11.026PMC PMC3070183

Open this paper in CoChat — free account

Abstract

Alzheimer disease (AD) is a neurodegenerative disorder in which oxidative stress is a key hallmark. It occurs early in disease pathogenesis and can exacerbate its progression. Several causes of oxidative stress have been determined over the years. First, mitochondria play an important role in the generation and accumulation of free radicals. In addition to mitochondria, inflammation can also induce oxidative damage, especially via microglia, and microglia are also important for Aβ clearance. In AD, both mitochondrial function and inflammatory response are affected, leading to increased ROS formation and oxidative damage to lipid, proteins, and nucleic acids. Some other sources have also been identified. From these findings, various neuroprotective strategies against ROS-mediated damages have been elaborated in AD research. This review recapitulates some of the major strategies used to prevent oxidative stress and disease progression. Outcomes from in vitro and in vivo studies using models of AD are encouraging. However, only a few clinical trials have provided positive results in terms of slowing down cognitive decline. Nonetheless, there is still hope for improved compounds that would better target pathways implicated in ROS production. In fact, facilitating the endogenous antioxidant system by modulating transcription has great promise for AD therapy.

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

Crossref · 10.1016/j.freeradbiomed.2010.11.026

Cites

185 of 185 references verified0 citation errors · 0 not checkable

Statistics

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?

Oxidative stress markers increase even in the preclinical phase and during mild cognitive impairment, while antioxidant therapies in animal models delay the disease course and improve cognitive functions.
“Oxidative stress markers increase even in the preclinical phase and during MCI, while antioxidant therapies in animal models have been shown to delay the disease course and improve cognitive functions [122, 123].”
From Targeted Nanoparticles for Drug Delivery Across the Blood–Brain Barrier in Early and Late Stages of Alzheimer's Disease: A Review (2026) · cites this paper as [123]
The Introduction (page unavailable) reports elevated oxidation markers in people with MCI and describes oxidative stress as an early event, before hallmark pathology. The neuroprotective-strategies sections (page unavailable) report improved memory and reduced amyloid pathology in treated AD mice, but do not establish that antioxidant therapies delayed the disease course in those models; the explicit report of slowed disease progression concerns patients. (LLM, conf=0.82)
Experimental — accuracy not yet measured
In advanced Alzheimer's disease, the effectiveness of antioxidant therapy is significantly reduced, with numerous unsuccessful clinical trials reporting minimal cognitive improvements.
“In contrast, in advanced AD—characterized by widespread neuronal damage and complex pathological remodeling—the effectiveness of antioxidant therapy is significantly reduced. Numerous unsuccessful clinical trials have reported minimal cognitive improvements in patients at advanced disease stages [123–125].”
From Targeted Nanoparticles for Drug Delivery Across the Blood–Brain Barrier in Early and Late Stages of Alzheimer's Disease: A Review (2026) · cites this paper as [123]
The Concluding remarks (page unavailable) say treatment timing is critical and success in human trials is less frequent, noting that disease may be well advanced by diagnosis. They also report mixed trial results, including studies finding no difference from placebo. The paper does not establish significantly reduced effectiveness specifically in patients with advanced AD or show that numerous trials in that group found minimal cognitive improvement. (LLM, conf=0.84)
Experimental — accuracy not yet measured
Targeting reactive oxygen species and oxidative stress is more effective during the early stages of Alzheimer's disease than in advanced stages.
“Scientific evidence clearly indicates that targeting ROS and oxidative stress is more effective during the early stages of AD than in advanced stages.”
From Targeted Nanoparticles for Drug Delivery Across the Blood–Brain Barrier in Early and Late Stages of Alzheimer's Disease: A Review (2026) · cites this paper as [123]
The Concluding remarks say treatment timing is critical and suggest that earlier treatment in animal models may help explain why results are better than in human trials, where disease may be advanced at diagnosis. The paper presents this as a possible explanation, not clear evidence that targeting ROS is more effective in early-stage than advanced-stage AD patients. (LLM, conf=0.86)
Experimental — accuracy not yet measured
Reactive oxygen species-targeting strategies exhibit the greatest efficacy in early Alzheimer's disease, before irreversible neuronal damage occurs.
“In summary, ROS-targeting strategies exhibit the greatest efficacy in early AD, before irreversible neuronal damage occurs [122, 123].”
From Targeted Nanoparticles for Drug Delivery Across the Blood–Brain Barrier in Early and Late Stages of Alzheimer's Disease: A Review (2026) · cites this paper as [123]
The Concluding remarks (page not provided) say treatment timing is extremely critical and suggest that early treatment in animal models may help explain their better outcomes than human trials begun after diagnosis. The paper does not establish that ROS-targeting strategies have their greatest efficacy in early AD or identify irreversible neuronal damage as the cutoff. (LLM, conf=0.86)
Experimental — accuracy not yet measured

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

1 retracted

RETRACTED: Activation of the PPAR/PGC-1α Pathway Prevents a Bioenergetic Deficit and Effectively Improves a Mitochondrial Myopathy Phenotype
Wenz, T., Diaz, F., Spiegelman, B. M., & Moraes, C. T. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.07.006 · Cited by 297 · see citing works
Retracted
Mitochondrial Dysfunction and Oxidative Stress in Neurodegenerative Diseases
Lin, M. T., & Beal, M. F. (2006) · Nature · doi:10.1038/nature05292 · Cited by 6,455 · see citing works
Self-citation
The Nrf2-antioxidant response element signaling pathway and its activation by oxidative stress
Nguyen, T., Nioi, P., & Pickett, C. B. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.r900010200 · Cited by 2,655 · see citing works
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 · see citing works
Curcumin Inhibits Formation of Amyloid β Oligomers and Fibrils, Binds Plaques, and Reduces Amyloid in Vivo
Yang, F., Lim, G. P., Begum, A. N., Ubeda, O. J., Simmons, M. R., Ambegaokar, S. S., Chen, P. P., Kayed, R., Glabe, C. G., Frautschy, S. A., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m404751200 · Cited by 2,336 · see citing works
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 · see citing works
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 · see citing works
Isolation of NF-E2-related factor 2 (Nrf2), a NF-E2-like basic leucine zipper transcriptional activator that binds to the tandem NF-E2/AP1 repeat of the beta-globin locus control region
Moi, P., Chan, K., Asunis, I., Cao, A., & Kan, Y. W. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.21.9926 · Cited by 1,607 · see citing works
Microglia in neurodegenerative disease
Perry, V. H., Nicoll, J. A. R., & Holmes, C. (2010) · Nature Reviews Neurology · doi:10.1038/nrneurol.2010.17 · Cited by 1,543 · see citing works
The Curry Spice Curcumin Reduces Oxidative Damage and Amyloid Pathology in an Alzheimer Transgenic Mouse
Lim, G. P., Chu, T., Yang, F., Beech, W., Frautschy, S. A., & Cole, G. M. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-21-08370.2001 · Cited by 1,530 · see citing works
Vitamin E, antioxidant and nothing more
Traber, M. G., & Atkinson, J. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.03.024 · Cited by 1,501 · see citing works
Microglial Dysfunction and Defective β-Amyloid Clearance Pathways in Aging Alzheimer's Disease Mice
Hickman, S. E., Allison, E. K., & El Khoury, J. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.0616-08.2008 · Cited by 1,329 · cited 2× · see citing works
“In the same animals, microglial levels of proinflammatory cytokines interleukin-1β and tumor necrosis factor alpha were markedly increased [122].”
Background
Mitochondrial Oxidative Stress: Implications for Cell Death
Orrenius, S., Gogvadze, V. G., & Zhivotovsky, B. (2006) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.47.120505.105122 · Cited by 1,266 · see citing works
Impaired Balance of Mitochondrial Fission and Fusion in Alzheimer's Disease
Wang, X., Su, B., Lee, H.-G., Li, X., Perry, G., Smith, M. A., & Zhu, X. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.1357-09.2009 · Cited by 1,224 · see citing works
Systemic inflammation and disease progression in Alzheimer disease
Holmes, C., Cunningham, C., Zotova, E., Woolford, J., Dean, C., Kerr, S., Culliford, D., & Perry, V. H. (2009) · Neurology · doi:10.1212/wnl.0b013e3181b6bb95 · Cited by 1,139 · see citing works
The Aβ Peptide of Alzheimer's Disease Directly Produces Hydrogen Peroxide through Metal Ion Reduction
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 1,107 · see citing works
Oxidative damage to mitochondrial DNA is increased in Alzheimer’s disease
Mecocci, P., MacGarvey, U., & Beal, M. F. (1994) · Annals of Neurology · doi:10.1002/ana.410360510 · Cited by 1,037 · see citing works
Self-citation
Metal-Protein Attenuation With Iodochlorhydroxyquin (Clioquinol) Targeting Aβ Amyloid Deposition and Toxicity in Alzheimer Disease: A Pilot Phase 2 Clinical Trial
Ritchie, C. W., Bush, A. I., Mackinnon, A., Macfarlane, S., Mastwyk, M., MacGregor, L., Kiers, L., Cherny, R., Li, Q.-X., Tammer, A., et al. (2003) · Archives of Neurology · doi:10.1001/archneur.60.12.1685 · Cited by 988 · see citing works
Cyclophilin D deficiency attenuates mitochondrial and neuronal perturbation and ameliorates learning and memory in Alzheimer's disease
Du, H., Guo, L., Fang, F., Chen, D., Sosunov, A. A., McKhann, G. M., Yan, Y., Wang, C., Zhang, H., Molkentin, J. D., et al. (2008) · Nature Medicine · doi:10.1038/nm.1868 · Cited by 935 · see citing works
Assessment of antioxidant capacity in vitro and in vivo
Niki, E. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.04.016 · Cited by 873 · see citing works
Molecular mechanisms of Nrf2‐mediated antioxidant response
Li, W., & Kong, A. T. (2008) · Molecular Carcinogenesis · doi:10.1002/mc.20465 · Cited by 786 · see citing works
Increased Lipid Peroxidation Precedes Amyloid Plaque Formation in an Animal Model of Alzheimer Amyloidosis
Praticò, D., Uryu, K., Leight, S., Trojanoswki, J. Q., & Lee, V. M.-Y. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-12-04183.2001 · Cited by 777 · see citing works
Safety, efficacy, and biomarker findings of PBT2 in targeting Aβ as a modifying therapy for Alzheimer's disease: a phase IIa, double-blind, randomised, placebo-controlled trial
Lannfelt, L., Blennow, K., Zetterberg, H., Batsman, S., Ames, D., Harrison, J., Masters, C. L., Targum, S., Bush, A. I., Murdoch, R., et al. (2008) · The Lancet Neurology · doi:10.1016/s1474-4422(08)70167-4 · Cited by 725 · see citing works
The role of microglia in amyloid clearance from the AD brain
Lee, C. Y. D., & Landreth, G. E. (2010) · Journal of Neural Transmission · doi:10.1007/s00702-010-0433-4 · Cited by 701 · see citing works
Efficacy of rosiglitazone in a genetically defined population with mild-to-moderate Alzheimer’s disease
Risner, M. E., Saunders, A. M., Altman, J. F. B., Ormandy, G. C., Craft, S., Foley, I. M., Zvartau-Hind, M. E., Hosford, D. A., Roses, A. D., & for the Rosiglitazone in Alzheimer's Disease Study Group (2006) · The Pharmacogenomics Journal · doi:10.1038/sj.tpj.6500369 · Cited by 686 · see citing works
Rapid Restoration of Cognition in Alzheimer's Transgenic Mice with 8-Hydroxy Quinoline Analogs Is Associated with Decreased Interstitial Aβ
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 · see citing works
Curcumin labels amyloid pathology in vivo , disrupts existing plaques, and partially restores distorted neurites in an Alzheimer mouse model
Garcı́a-Alloza, M., Borrelli, L. A., Rozkalne, A., Hyman, B. T., & Bacskai, B. J. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04613.x · Cited by 663 · see citing works
Amyloid-β and tau synergistically impair the oxidative phosphorylation system in triple transgenic Alzheimer's disease mice
Rhein, V., Song, X., Wiesner, A., Ittner, L. M., Baysang, G., Meier, F., Ozmen, L., Bluethmann, H., Dröse, S., Brandt, U., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0905529106 · Cited by 655 · see citing works
Effect of Tarenflurbil on Cognitive Decline and Activities of Daily Living in Patients With Mild Alzheimer Disease<subtitle>A Randomized Controlled Trial</subtitle>
Green, R. C. (2009) · JAMA · doi:10.1001/jama.2009.1866 · Cited by 643 · see citing works
Triterpenoids and rexinoids as multifunctional agents for the prevention and treatment of cancer
Liby, K. T., Yore, M. M., & Sporn, M. B. (2007) · Nature Reviews Cancer · doi:10.1038/nrc2129 · Cited by 637 · see citing works
Involvement of oxidative stress in Alzheimer disease
Nunomura, A., Castellani, R. J., Zhu, X., Moreira, P. I., Perry, G., & Smith, M. A. (2006) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/01.jnen.0000228136.58062.bf · Cited by 611 · see citing works
Preserved Cognition in Patients With Early Alzheimer Disease and Amnestic Mild Cognitive Impairment During Treatment With Rosiglitazone
Watson, G. S., Cholerton, B. A., Reger, M. A., Baker, L. D., Plymate, S. R., Asthana, S., Fishel, M. A., Kulstad, J. J., Green, P. S., Cook, D. G., et al. (2005) · American Journal of Geriatric Psychiatry · doi:10.1176/appi.ajgp.13.11.950 · Cited by 607 · see citing works
A double‐blind, placebo‐controlled study to assess the mitochondria‐targeted antioxidant MitoQ as a disease‐modifying therapy in Parkinson's disease
Snow, B. J., Rolfe, F. L., Lockhart, M. M., Frampton, C. M., O'Sullivan, J. D., Fung, V., Smith, R. A. J., Murphy, M. P., Taylor, K. M., & On behalf of the Protect Study Group (2010) · Movement Disorders · doi:10.1002/mds.23148 · Cited by 606 · see citing works
Curcumin Structure-Function, Bioavailability, and Efficacy in Models of Neuroinflammation and Alzheimer’s Disease
Begum, A. N., Jones, M. R., Lim, G. P., Morihara, T., Kim, P., Heath, D. D., Rock, C. L., Pruitt, M. A., Yang, F., Hudspeth, B., et al. (2008) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.108.137455 · Cited by 604 · see citing works
Six-Month Randomized, Placebo-Controlled, Double-Blind, Pilot Clinical Trial of Curcumin in Patients With Alzheimer Disease
Baum, L., Lam, C. W. K., Cheung, S. K. K., Kwok, T. C. Y., Lui, V. W.-C., Tsoh, J., LAM, L. C. W., Leung, V., Hui, E., Ng, C., et al. (2008) · Journal of Clinical Psychopharmacology · doi:10.1097/jcp.0b013e318160862c · Cited by 594 · see citing works
Microglial Cx3cr1 knockout prevents neuron loss in a mouse model of Alzheimer's disease
Fuhrmann, M., Bittner, T., Jung, C. K. E., Burgold, S., Page, R. M., Mitteregger, G., Haass, C., LaFerla, F. M., Kretzschmar, H., & Herms, J. (2010) · Nature Neuroscience · doi:10.1038/nn.2511 · Cited by 562 · see citing works
Alzheimer's brains harbor somatic mtDNA control-region mutations that suppress mitochondrial transcription and replication
Coskun, P. E., Beal, M. F., & Wallace, D. C. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403649101 · Cited by 556 · see citing works
Self-citation
Animal and human studies with the mitochondria‐targeted antioxidant MitoQ
Smith, R. A. J., & Murphy, M. P. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05627.x · Cited by 553 · see citing works
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 · see citing works
Copper in the brain and Alzheimer’s disease
Hung, Y. H., Bush, A. I., & Cherny, R. A. (2009) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-009-0600-y · Cited by 496 · see citing works
Oxidative stress in Alzheimer disease: A possibility for prevention
Bonda, D., Wang, X., Perry, G. L., Nunomura, A., Tabaton, M., Zhu, X., & Smith, M. A. (2010) · Neuropharmacology · doi:10.1016/j.neuropharm.2010.04.005 · Cited by 481 · see citing works
NOX Enzymes in the Central Nervous System: From Signaling to Disease
Sorce, S., & Krause, K. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2578 · Cited by 472 · see citing works
Mitochondria-targeted antioxidants protect against amyloid-β toxicity in Alzheimer's disease neurons
Manczak, M., Mao, P., Calkins, M. J., Cornea, A., Reddy, A. P., Murphy, M. P., Szeto, H. H., Park, B., & Reddy, P. H. (2010) · Journal of Alzheimer's Disease · doi:10.3233/jad-2010-100564 · Cited by 469 · see citing works
Effect of dimebon on cognition, activities of daily living, behaviour, and global function in patients with mild-to-moderate Alzheimer's disease: a randomised, double-blind, placebo-controlled study
Doody, R. S., Si, G., Sano, M. C., Thomas, R. G., Aisen, P. S. S., Бачурин, С. О., Seely, L., & Hung, D. S.-Y. (2008) · The Lancet · doi:10.1016/s0140-6736(08)61074-0 · Cited by 460 · see citing works
L-N6-(1-Iminoethyl)lysine: A Selective Inhibitor of Inducible Nitric Oxide Synthase
Moore, W. M., Webber, R. K., Jerome, G. M., Tjoeng, F. S., Misko, T. P., & Currie, M. G. (1994) · Journal of Medicinal Chemistry · doi:10.1021/jm00049a007 · Cited by 458 · see citing works
Cyclooxygenase-2 expression is increased in frontal cortex of Alzheimer's disease brain.
Pasinetti, G., & Aisen, P. (1998) · Neuroscience · doi:10.1016/s0306-4522(98)00218-8 · Cited by 457 · see citing works
Microglia Mediate the Clearance of Soluble Aβ through Fluid Phase Macropinocytosis
Mandrekar, S., Jiang, Q., Lee, C. Y. D., Koenigsknecht-Talboo, J., Holtzman, D. M., & Landreth, G. E. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.5572-08.2009 · Cited by 415 · see citing works
Increased Iron and Free Radical Generation in Preclinical Alzheimer Disease and Mild Cognitive Impairment
Smith, M. A., Zhu, X., Tabaton, M., Liu, G., McKeel, D. W., Cohen, M. L., Wang, X., Siedlak, S. L., Dwyer, B. E., Hayashi, T., et al. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1239 · Cited by 400 · see citing works
Decreased pyruvate dehydrogenase complex activity in Huntington and Alzheimer brain
Sorbi, S., Bird, E. D., & Blass, J. P. (1983) · Annals of Neurology · doi:10.1002/ana.410130116 · Cited by 395 · see citing works
Cognitive Function Over Time in the Alzheimer's Disease Anti-inflammatory Prevention Trial (ADAPT): Results of a Randomized, Controlled Trial of Naproxen and Celecoxib
(2008) · Archives of Neurology · doi:10.1001/archneur.2008.65.7.nct70006 · Cited by 387 · see citing works
PGC-1α Expression Decreases in the Alzheimer Disease Brain as a Function of Dementia
Qin, W., Haroutunian, V. H., Katsel, P., Cardozo, C. P., Ho, L., Buxbaum, J. D., & Pasinetti, G. M. (2009) · Archives of Neurology · doi:10.1001/archneurol.2008.588 · Cited by 381 · see citing works
Mitochondrial Oxidative Stress Causes Hyperphosphorylation of Tau
Melov, S., Adlard, P. A., Morten, K., Johnson, F., Golden, T. R., Hinerfeld, D., Schilling, B., Mavros, C., Masters, C. L., Volitakis, I., et al. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000536 · Cited by 363 · see citing works
Grape-Derived Polyphenolics Prevent A Oligomerization and Attenuate Cognitive Deterioration in a Mouse Model of Alzheimer's Disease
Wang, J., Ho, L., Zhao, W., Ono, K., Rosensweig, C., Chen, L., Humala, N., Teplow, D. B., & Pasinetti, G. M. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.0364-08.2008 · Cited by 358 · see citing works
SOD1 mutations disrupt redox-sensitive Rac regulation of NADPH oxidase in a familial ALS model
Harraz, M. M., Marden, J. J., Zhou, W., Zhang, Y., Williams, A. J., Sharov, V. S., Nelson, K., Luo, M., Paulson, H. L., Schöneich, C., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci34060 · Cited by 357 · see citing works
Naturally occurring phytochemicals for the prevention of Alzheimer’s disease
Kim, J., Lee, H. J., & Lee, K. W. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06562.x · Cited by 354 · see citing works
Lipoic acid as an anti-inflammatory and neuroprotective treatment for Alzheimer's disease
Maczurek, A. E., Häger, K., Kenklies, M., Sharman, M. J., Martins, R. N., Engel, J., Carlson, D. A., & Münch, G. W. (2008) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2008.04.015 · Cited by 350 · see citing works
Neuroinflammation in Alzheimer's Disease and Mild Cognitive Impairment: A Field in Its Infancy
Mcgeer, E., & McGeer, P. (2010) · Journal of Alzheimer's Disease · doi:10.3233/jad-2010-1219 · Cited by 349 · see citing works
Apocynin: Molecular Aptitudes
Stefanska, J., & Pawliczak, R. (2008) · Mediators of Inflammation · doi:10.1155/2008/106507 · Cited by 349 · see citing works
Brain oxidative stress in a triple-transgenic mouse model of Alzheimer disease
Resende, R., Moreira, P. I., Proença, T., Deshpande, A., Busciglio, J., Pereira, C., & Oliveira, C. R. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.012 · Cited by 343 · see citing works
Identification of a novel mitochondrial protein (“mitoNEET”) cross-linked specifically by a thiazolidinedione photoprobe
Colca, J. R., McDonald, W. G., Waldon, D. J., Leone, J. W., Lull, J. M., Bannow, C. A., Lund, E. T., & Mathews, W. R. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00424.2003 · Cited by 339 · see citing works
Causes of oxidative stress in Alzheimer disease
Zhu, X., Su, B., Wang, X., Smith, M. A., & Perry, G. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7218-4 · Cited by 336 · see citing works
Nox2-derived radicals contribute to neurovascular and behavioral dysfunction in mice overexpressing the amyloid precursor protein
Park, L., Zhou, P., Pitstick, R., Capone, C., Anrather, J., Norris, E. H., Younkin, L., Younkin, S., Carlson, G., McEwen, B. S., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711568105 · Cited by 332 · see citing works
β‐Site APP cleaving enzyme up‐regulation induced by 4‐hydroxynonenal is mediated by stress‐activated protein kinases pathways
Tamagno, E., Parola, M., Bardini, P., Piccini, A., Borghi, R., Guglielmotto, M., Santoro, G., Davit, A., Danni, O., Smith, M. A., et al. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02895.x · Cited by 324 · see citing works
MitoNEET is a uniquely folded 2Fe-2S outer mitochondrial membrane protein stabilized by pioglitazone
Paddock, M. L., Wiley, S. E., Axelrod, H. L., Cohen, A. E., Roy, M., Abresch, E. C., Capraro, D. T., Murphy, A. N., Nechushtai, R., Dixon, J. E., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707189104 · Cited by 302 · see citing works
Early Vitamin E supplementation in young but not aged mice reduces Aβ levels and amyloid deposition in a transgenic model of Alzheimer's disease
Sung, S., Yao, Y., Uryu, K., Yang, H., Lee, V. M. ‐., Trojanowski, J. Q., & Praticò, D. (2003) · The FASEB Journal · doi:10.1096/fj.03-0961fje · Cited by 298 · see citing works
Intrahippocampal injection of a lentiviral vector expressing Nrf2 improves spatial learning in a mouse model of Alzheimer's disease
Kanninen, K. M., Heikkinen, R., Malm, T., Rõlova, T., Kemppainen, S., Leinonen, H. M., Ylä‐Herttuala, S., Tanila, H., Levonen, A., Koistinaho, M., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908397106 · Cited by 293 · see citing works
Inducible nitric oxide synthase in tangle-bearing neurons of patients with Alzheimer's disease.
Yoram Vodovotz, B., Lucia, M. S., Flanders, K. C., Chesler, L., Xie, Q. W., Smith, T. W., Weidner, J. R., Mumford, R. A., Webber, R., Nathan, C., et al. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.184.4.1425 · Cited by 289 · see citing works
The synthetic triterpenoids, CDDO and CDDO-imidazolide, are potent inducers of heme oxygenase-1 and Nrf2/ARE signaling
Liby, K., Hock, T., Yore, M. M., Suh, N., Place, A. E., Risingsong, R., Williams, C. R., Royce, D. B., Honda, T., Honda, Y., et al. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-4539 · Cited by 283 · see citing works
Cytochrome c oxidase is decreased in Alzheimer’s disease platelets
Cardoso, S. M., Proença, M. T., Santos, S., Santana, I., & Oliveira, C. R. (2004) · Neurobiology of Aging · doi:10.1016/s0197-4580(03)00033-2 · Cited by 281 · see citing works
Increased plaque burden in brains of APP mutant MnSOD heterozygous knockout mice
Li, F., Calingasan, N. Y., Yu, F., Mauck, W. M., Toidze, M., Almeida, C. G., Takahashi, R. H., Carlson, G. A., Beal, M. F., Lin, M. T. S., et al. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02455.x · Cited by 276 · see citing works
Self-citation
Lipid peroxidation is an early event in the brain in amnestic mild cognitive impairment
Markesbery, W. R., Kryscio, R. J., Lovell, M. A., & Morrow, J. D. (2005) · Annals of Neurology · doi:10.1002/ana.20629 · Cited by 272 · see citing works
Complete Rescue of Cerebrovascular Function in Aged Alzheimer's Disease Transgenic Mice by Antioxidants and Pioglitazone, a Peroxisome Proliferator-Activated Receptor γ Agonist
Nicolakakis, N., Aboulkassim, T., Ongali, B., Lecrux, C., Fernandes, P., Rosa-Neto, P., Tong, X.-K., & Hamel, E. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.3348-08.2008 · Cited by 262 · see citing works
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 256 · see citing works
Reduction in mitochondrial superoxide dismutase modulates Alzheimer’s disease-like pathology and accelerates the onset of behavioral changes in human amyloid precursor protein transgenic mice
Esposito, L., Raber, J., Kekonius, L., Yan, F., Yu, G.-Q., Bien-Ly, N., Puoliväli, J., Scearce-Levie, K., Masliah, E., & Mucke, L. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.0482-06.2006 · Cited by 254 · see citing works
Mitochondria-targeted peptide prevents mitochondrial depolarization and apoptosis induced by tert-butyl hydroperoxide in neuronal cell lines
Zhao, K., Luo, G., Giannelli, S., & Szeto, H. H. (2005) · Biochemical Pharmacology · doi:10.1016/j.bcp.2005.08.022 · Cited by 251 · see citing works
Small-Molecule NOX Inhibitors: ROS-Generating NADPH Oxidases as Therapeutic Targets
Jaquet, V., Scapozza, L., Clark, R. A., Krause, K. H., & Lambeth, J. D. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2585 · Cited by 243 · see citing works
Hydrogen Peroxide Is Generated during the Very Early Stages of Aggregation of the Amyloid Peptides Implicated in Alzheimer Disease and Familial British Dementia
Tabner, B. J., El‐Agnaf, O. M. A., Turnbull, S., German, M. J., Paleologou, K. E., Hayashi, Y., Cooper, L. J., Fullwood, N. J., & Allsop, D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500238200 · Cited by 241 · see citing works
Systemic inflammatory cells fight off neurodegenerative disease
Schwartz, M., & Shechter, R. (2010) · Nature Reviews Neurology · doi:10.1038/nrneurol.2010.71 · Cited by 240 · see citing works
The microglial NADPH oxidase complex as a source of oxidative stress in Alzheimer's disease.
Wilkinson, B. L., & Landreth, G. E. (2006) · Journal of Neuroinflammation · doi:10.1186/1742-2094-3-30 · Cited by 235 · see citing works
Mitochondrial permeability transition pore in Alzheimer's disease: Cyclophilin D and amyloid beta
Du, H., & Yan, S. S. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.07.005 · Cited by 235 · see citing works
Aberrant expression of NOS isoforms in Alzheimer's disease is structurally related to nitrotyrosine formation.
Lüth, H., Münch, G., & Arendt, T. (2002) · Brain Research · doi:10.1016/s0006-8993(02)03280-8 · Cited by 233 · see citing works
Cyclophilin D deficiency improves mitochondrial function and learning/memory in aging Alzheimer disease mouse model
Du, H., Guo, L., Zhang, W., Rydzewska, M., & Yan, S.-D. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.03.003 · Cited by 230 · see citing works
Overexpression of SOD-2 reduces hippocampal superoxide and prevents memory deficits in a mouse model of Alzheimer's disease
Massaad, C. A., Washington, T. M., Pautler, R. G., & Klann, E. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902714106 · Cited by 223 · see citing works
Reduction of oxidative stress, amyloid deposition, and memory deficit by manganese superoxide dismutase overexpression in a transgenic mouse model of Alzheimer's disease
Dumont, M., Wille, E., Stack, C., Calingasan, N. Y., Beal, M. F., & Lin, M. T. (2009) · The FASEB Journal · doi:10.1096/fj.09-132928 · Cited by 221 · see citing works
Self-citation
Biomarkers of Oxidative Damage and Inflammation in Alzheimer's Disease
Galasko, D. R., & Montine, T. J. (2010) · Biomarkers in Medicine · doi:10.2217/bmm.09.89 · Cited by 221 · see citing works
Nitric oxide and nitroxidative stress in Alzheimer's disease
Malinski, T. (2007) · Journal of Alzheimer s Disease · doi:10.3233/jad-2007-11208 · Cited by 220 · see citing works
Consequences of long-term oral administration of the mitochondria-targeted antioxidant MitoQ to wild-type mice
Rodriguez-Cuenca, S., Cochemé, H. M., Logan, A., Abakumova, I., Prime, T. A., Rose, C., Vidal-Puig, A., Smith, A. C., Rubinsztein, D. C., Fearnley, I. M., et al. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.10.039 · Cited by 218 · see citing works
Oral fumaric acid esters for the treatment of active multiple sclerosis: an open‐label, baseline‐controlled pilot study
Schimrigk, S., Brune, N., Hellwig, K., Lukas, C., Bellenberg, B., Rieks, M., Hoffmann, V., Pöhlau, D., & Przuntek, H. (2006) · European Journal of Neurology · doi:10.1111/j.1468-1331.2006.01292.x · Cited by 217 · see citing works
Oxidatively modified proteins in Alzheimer’s disease (AD), mild cognitive impairment and animal models of AD: role of Abeta in pathogenesis
Sultana, R., Perluigi, M., & Butterfield, D. A. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0517-0 · Cited by 215 · see citing works
Protection from Alzheimer's-like disease in the mouse by genetic ablation of inducible nitric oxide synthase
Nathan, C., Calingasan, N., Nezezon, J., Ding, A., Lucia, M. S., La Perle, K., Fuortes, M., Lin, M., Ehrt, S., Kwon, N. S., et al. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20051529 · Cited by 214 · see citing works
Self-citation
Meta-analysis of double blind randomized controlled clinical trials of acetyl-L-carnitine versus placebo in the treatment of mild cognitive impairment and mild Alzheimer??s disease
Montgomery, S. A., Thal, L. J., & Amrein, R. (2003) · International Clinical Psychopharmacology · doi:10.1097/00004850-200303000-00001 · Cited by 209 · see citing works
The Nrf2-ARE Signalling Pathway: Promising Drug Target to Combat Oxidative Stress in Neurodegenerative Disorders
Muiswinkel, F. L. V., & Kuiperij, H. B. (2005) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1568007054038238 · Cited by 207 · see citing works
Induction of hyperphosphorylated tau in primary rat cortical neuron cultures mediated by oxidative stress and glycogen synthase kinase-3
Lovell, M., Xiong, S., Xie, C.-S., Davies, P., & Markesbery, W. (2005) · Journal of Alzheimer's Disease · doi:10.3233/jad-2004-6610 · Cited by 207 · see citing works
NADPH oxidase as a therapeutic target in Alzheimer's disease
Block, M. L. (2008) · BMC Neuroscience · doi:10.1186/1471-2202-9-s2-s8 · Cited by 202 · see citing works
Transcriptional and translational regulation of BACE1 expression—Implications for Alzheimer's disease
Roßner, S., Sastre, M., Bourne, K. Z., & Lichtenthaler, S. F. (2006) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2006.06.001 · Cited by 196 · see citing works
Effects of Grape Seed-derived Polyphenols on Amyloid β-Protein Self-assembly and Cytotoxicity*
Ono, K., Condron, M. M., Ho, L., Wang, J., Zhao, W., Pasinetti, G. M., & Teplow, D. B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806154200 · Cited by 190 · see citing works
In vivo oxidative stress in brain of Alzheimer disease transgenic mice: Requirement for methionine 35 in amyloid β-peptide of APP
Butterfield, D. A., Galván, V., Lange, M. L. B., Tang, H., Robinson, R. A. S., Spilman, P. R., Fombonne, J., Gorostiza, O. F., Zhang, J., Rukhsana Sultana, A., et al. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.10.035 · Cited by 188 · see citing works
Coenzyme Q10 effects in neurodegenerative disease
Henchcliffe, C. (2009) · Neuropsychiatric Disease and Treatment · doi:10.2147/ndt.s5212 · Cited by 188 · see citing works
Transcriptional control of mitochondrial energy metabolism through the PGC1 coactivators
Spiegelman, B. M. (2007) · Novartis Foundation Symposia · doi:10.1002/9780470725207.ch5 · Cited by 187 · cited 1× · see citing works
“The peroxisome proliferatoractivated receptor-γ coactivator 1 alpha (PGC-1α) is an important transcription cofactor involved in energy metabolism [157,158].”
Background
Curcuminoids enhance amyloid-β uptake by macrophages of Alzheimer's disease patients
Zhang, L., Fiala, M., Cashman, J. R., Sayre, J. W., Monteros, A. E. D. L., Mahanian, M., Zaghi, J., Badmaev, V., Graves, M. C., Bernard, G. W., et al. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-10101 · Cited by 183 · see citing works
Expression of endothelial and inducible NOS-isoforms is increased in Alzheimer’s disease, in APP23 transgenic mice and after experimental brain lesion in rat: Evidence for an induction by amyloid pathology
Lüth, H.-J., Holzer, M., Gärtner, U., Staufenbiel, M., & Arendt, T. (2001) · Brain Research · doi:10.1016/s0006-8993(01)02758-5 · Cited by 183 · see citing works
The α-Ketoglutarate–Dehydrogenase Complex: A Mediator Between Mitochondria and Oxidative Stress in Neurodegeneration
Gibson, G. E., Blass, J. P., Beal, M. F., & Bunik, V. I. (2005) · Molecular Neurobiology · doi:10.1385/mn:31:1-3:043 · Cited by 180 · see citing works
Self-citation
A randomized controlled study on effects of ibuprofen on cognitive progression of Alzheimer’s disease
Pasqualetti, P., Bonomini, C., Dal Forno, G., Paulon, L., Sinforiani, E., Marra, C., Zanetti, O., & Maria Rossini, P. (2009) · Aging Clinical and Experimental Research · doi:10.1007/bf03325217 · Cited by 172 · see citing works
Neuroprotective Effects of the Triterpenoid, CDDO Methyl Amide, a Potent Inducer of Nrf2-Mediated Transcription
Yang, L., Calingasan, N. Y., Thomas, B., Chaturvedi, R. K., Kiaei, M., Wille, E. J., Liby, K. T., Williams, C. R., Royce, D. B., Risingsong, R., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005757 · Cited by 172 · see citing works
Self-citation
Triterpenoids CDDO-ethyl amide and CDDO-trifluoroethyl amide improve the behavioral phenotype and brain pathology in a transgenic mouse model of Huntington's disease
Stack, C., Ho, D. J., Wille, E. J., Calingasan, N. Y., Williams, C. R., Liby, K. T., Sporn, M. B., Dumont, M., & Beal, M. F. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.03.017 · Cited by 171 · see citing works
Self-citation
Is α‐lipoic acid a scavenger of reactive oxygen species in vivo? Evidence for its initiation of stress signaling pathways that promote endogenous antioxidant capacity
Shay, K. P., Moreau, R. F., Smith, E. J., & Hagen, T. M. (2008) · IUBMB Life · doi:10.1002/iub.40 · Cited by 170 · see citing works
A Novel Cell-permeable Antioxidant Peptide, SS31, Attenuates Ischemic Brain Injury by Down-regulating CD36
Cho, S., Szeto, H. H., Kim, E., Kim, H., Tolhurst, A. T., & Pinto, J. T. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m609388200 · Cited by 170 · see citing works
Mitochondria Targeted Peptides Protect Against 1-Methyl-4-Phenyl-1,2,3,6-Tetrahydropyridine Neurotoxicity
Yang, L., Zhao, K., Calingasan, N. Y., Luo, G., Szeto, H. H., & Beal, M. F. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2445 · Cited by 169 · see citing works
Self-citation
Methionine residue 35 is important in amyloid β-peptide-associated free radical oxidative stress
Varadarajan, S., Yatin, S. M., Kański, J., Jahanshahi, F., & Butterfield, D. A. (1999) · Brain Research Bulletin · doi:10.1016/s0361-9230(99)00093-3 · Cited by 169 · see citing works
Cell‐permeable peptide antioxidants as a novel therapeutic approach in a mouse model of amyotrophic lateral sclerosis
Petri, S., Kiaei, M., Damiano, M., Hiller, A., Wille, E., Manfredi, G., Calingasan, N. Y., Szeto, H. H., & Beal, M. F. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04018.x · Cited by 166 · see citing works
Self-citation
Convergence of Amyloid-β and Tau Pathologies on Mitochondria In Vivo
Eckert, A., Schulz, K. L., Rhein, V. F., & Götz, J. (2010) · Molecular Neurobiology · doi:10.1007/s12035-010-8109-5 · Cited by 158 · see citing works
Idebenone treatment fails to slow cognitive decline in Alzheimer’s disease
Thal, L. J., Grundman, M., Berg, J., Ernstrom, K., Margolin, R., Pfeiffer, E., Weiner, M. F., Zamrini, E., & Thomas, R. G. (2003) · Neurology · doi:10.1212/01.wnl.0000096376.03678.c1 · Cited by 156 · see citing works
Protective effect of curcumin against lead neurotoxicity in rat
Shukla, P. K., Khanna, V. K., Khan, M. Y., & Srimal, R. C. (2003) · Human & Experimental Toxicology · doi:10.1191/0960327103ht411oa · Cited by 155 · see citing works
A 1-year multicenter placebo-controlled study of acetyl-L-carnitine in patients with Alzheimer's disease
Thal, L. J., Carta, A., Clarke, W. R., Ferris, S. H., Friedland, R. P., Petersen, R. C., Pettegrew, J. W., Pfeiffer, E., Raskind, M. A., Sano, M., et al. (1996) · Neurology · doi:10.1212/wnl.47.3.705 · Cited by 150 · see citing works
DNA Damage and Repair in Alzheimers Disease
Coppede, F., & Migliore, L. (2009) · Current Alzheimer Research · doi:10.2174/156720509787313970 · Cited by 148 · see citing works
Clinical and neurochemical effects of acetyl-L-carnitine in Alzheimer's disease
Pettegrew, J. W., Klunk, W. E., Panchalingam, K., Kanfer, J. N., & McClure, R. J. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)80001-8 · Cited by 148 · see citing works
Mitochondrial DNA Mutations in Disease, Aging, and Neurodegeneration
Reeve, A. K., Krishnan, K. J., & Turnbull, D. M. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1427.016 · Cited by 146 · see citing works
Neuronal Death and Survival Under Oxidative Stress in Alzheimer and Parkinson Diseases
Nunomura, A., Moreira, P. I., Lee, H., Zhu, X., Castellani, R. J., Smith, M. A., & Perry, G. L. (2007) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152707783399201 · Cited by 139 · see citing works
Rosiglitazone reverses memory decline and hippocampal glucocorticoid receptor down-regulation in an Alzheimer’s disease mouse model
Escribano, L., Simón, A., Pérez‐Mediavilla, A., Colocho, P. E. S., Río, J. D., & Frechilla, D. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.12.071 · Cited by 135 · see citing works
Cyclooxygenase-2 Promotes Amyloid Plaque Deposition in a Mouse Model of Alzheimer's Disease Neuropathology
Xiang, Z., Ho, L., Yemul, S., Zhao, Z., Pompl, P. N., Kelley, K. A., Dang, A., Qing, W., Teplow, D. B., & Pasinetti, G. M. (2002) · Gene Expression · doi:10.3727/000000002783992352 · Cited by 135 · see citing works
MitoQ--a mitochondria-targeted antioxidant.
Tauskela, J. S. (2007) · PubMed · Cited by 133 · see citing works
Fibrillar β-Amyloid-stimulated Intracellular Signaling Cascades Require Vav for Induction of Respiratory Burst and Phagocytosis in Monocytes and Microglia
Wilkinson, B. L., Koenigsknecht-Talboo, J., Grommes, C., Lee, C. Y. D., & Landreth, G. E. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600627200 · Cited by 131 · see citing works
NO synthase 2 ( <i>NOS2</i> ) deletion promotes multiple pathologies in a mouse model of Alzheimer's disease
Colton, C. A., Vitek, M. P., Wink, D. A., Xu, Q., Cantillana, V., Previti, M. L., Van Nostrand, W. E., Weinberg, J. B., & Dawson, H. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601075103 · Cited by 128 · see citing works
Heterogeneity in Red Wine Polyphenolic Contents Differentially Influences Alzheimer's Disease-type Neuropathology and Cognitive Deterioration
Ho, L., Chen, L. H., Wang, J., Zhao, W., Talcott, S. T., Ono, K., Teplow, D. B., Humala, N., Cheng, A., Percival, S. S., et al. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-0916 · Cited by 126 · see citing works
Neuronal mitochondrial amelioration by feeding acetyl‐L‐carnitine and lipoic acid to aged rats
Aliev, G. M., Liu, J., Shenk, J. C., Fischbach, K., Pacheco, G. J., Chen, S. G., Obrenovich, M. E., Ward, W. F., Richardson, A. G., Smith, M. A., et al. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00324.x · Cited by 123 · see citing works
A Controlled Study of 2 Doses of Idebenone in the Treatment of Alzheimer’s Disease
Weyer, G., Babej-Dölle, R. M., Hadler, D., Hofmann, S., & Herrmann, W. M. (2008) · Neuropsychobiology · doi:10.1159/000119366 · Cited by 120 · cited 1× · see citing works
“Although several smaller studies reported beneficial effects on memory and attention after several months of treatment [53–55], a larger study reported no effect in slowing disease progression [56].”
Background
Evaluation of Dimebon in cellular model of Huntington's disease
Wu, J., Li, Q., & Борисович, Б. И. (2008) · Molecular Neurodegeneration · doi:10.1186/1750-1326-3-15 · Cited by 117 · see citing works
Ibuprofen attenuates oxidative damage through NOX2 inhibition in Alzheimer's disease
Wilkinson, B. L., Cramer, P. E., Varvel, N. H., Reed-Geaghan, E. G., Jiang, Q., Szabo, A., Herrup, K., Lamb, B. T., & Landreth, G. E. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.06.014 · Cited by 116 · see citing works
Expression of nitric oxide system in clinically evaluated cases of Alzheimer's disease
Fernández‐Vizarra, P., Fernández, A. P., Castro‐Blanco, S., Encinas, J. M., Serrano, J., Bentura, M. L., Muñoz, P., Martínez‐Murillo, R., & Rodrigo, J. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2003.10.010 · Cited by 115 · see citing works
Non-Steroidal Anti-Inflammatory Drugs and Alzheimers Disease: The Epidemiological Evidence
Szekely, C. A., & Zandi, P. P. (2010) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152710791012026 · Cited by 114 · see citing works
Inducible Nitric Oxide Synthase Immunoreactivity in the Alzheimer Disease Hippocampus: Association with Hirano Bodies, Neurofibrillary Tangles, and Senile Plaques
Lee, S. C., Zhao, M., Hirano, A., & Dickson, D. W. (1999) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199911000-00006 · Cited by 113 · see citing works
Triterpenoid CDDO‐methylamide improves memory and decreases amyloid plaques in a transgenic mouse model of Alzheimer’s disease
Dumont, M., Wille, E. J., Calingasan, N. Y., Tampellini, D., Williams, C. R., Gouras, G. K., Liby, K. T., Sporn, M. B., Beal, M. F., & Lin, M. T. S. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.05970.x · Cited by 112 · see citing works
Self-citation
Coenzyme Q10 Attenuates β-Amyloid Pathology in the Aged Transgenic Mice with Alzheimer Presenilin 1 Mutation
Yang, X., Yang, Y., Li, G., Wang, J., & Yang, E. S. (2008) · Journal of Molecular Neuroscience · doi:10.1007/s12031-007-9033-7 · Cited by 111 · see citing works
Cyclooxygenase (COX)-2 and COX-1 Potentiate β-Amyloid Peptide Generation through Mechanisms That Involve γ-Secretase Activity
Qin, W., Ho, L., Pompl, P. N., Peng, Y., Zhao, Z., Xiang, Z., Robakis, N. K. R. K., Shioi, J., Suh, J., & Pasinetti, G. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307699200 · Cited by 110 · see citing works
Scavenging of hypochlorous acid by lipoic acid
Haenen, G. R. M. M., & Bast, A. (1991) · Biochemical Pharmacology · doi:10.1016/0006-2952(91)90363-a · Cited by 110 · see citing works
α‐ketoglutarate dehydrogenase in alzheimer brains bearing the APP670/671 mutation
Gibson, G. E., Zhang, H., Sheu, K. ‐. R., Bogdanovich, N. K., LINDSAY, J. G., Lannfelt, L., Vestling, M., & Cowburn, R. F. (1998) · Annals of Neurology · doi:10.1002/ana.410440414 · Cited by 108 · see citing works
Mitochondrial Dynamics in Alzheimerʼs Disease
Bonda, D., Wang, X., Perry, G. L., Smith, M. A., & Zhu, X. (2010) · Drugs & Aging · doi:10.2165/11532140-000000000-00000 · Cited by 106 · see citing works
Delaying the Mitochondrial Decay of Aging with Acetylcarnitine
Ames, B. N., & Liu, J. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1320.010 · Cited by 103 · see citing works
A 1-year controlled trial of acetyl- l -carnitine in early-onset AD
Thal, L. J., Calvani, M., Amato, A., & Carta, A. (2000) · Neurology · doi:10.1212/wnl.55.6.805 · Cited by 102 · see citing works
NOX Activity Is Increased in Mild Cognitive Impairment
Bruce‐Keller, A. J., Gupta, S., Parrino, T. E., Knight, A. G., Ebenezer, P. J., Weidner, A. M., LeVine, H., Keller, J. N., & Markesbery, W. R. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2823 · Cited by 100 · see citing works
Evaluation of Coenzyme Q as an Antioxidant Strategy for Alzheimer's Disease
Wadsworth, T. L., Bishop, J. A., Pappu, A. S., Woltjer, R. L., & Quinn, J. F. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-14210 · Cited by 97 · see citing works
Comparative Study of Action Mechanisms of Dimebon and Memantine on AMPA- and NMDA-Subtypes Glutamate Receptors in Rat Cerebral Neurons
Григорьев, В. В., Dranyi, O. A., & Бачурин, С. О. (2003) · Bulletin of Experimental Biology and Medicine · doi:10.1023/b:bebm.0000017097.75818.14 · Cited by 95 · see citing works
The effect of acetyl-L-carnitine and R-α-lipoic acid treatment in ApoE4 mouse as a model of human Alzheimer's disease
Shenk, J. C., Liu, J., Fischbach, K., Xu, K., Puchowicz, M., Obrenovich, M. E., Gasimov, E. K., Morales, L., Ames, B. N., LaManna, J. C., et al. (2009) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2009.03.002 · Cited by 94 · see citing works
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 · see citing works
The Effects of NOS2 Gene Deletion on Mice Expressing Mutated Human AβPP
Colton, C. A., Wilcock, D. M., Wink, D. A., Davis, J., Nostrand, W. E. V., & Vitek, M. P. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-15405 · Cited by 92 · see citing works
Oxidative RNA Damage and Neurodegeneration
Nunomura, A., Moreira, P. I., Takeda, A., Smith, M., & Perry, G. L. (2007) · Current Medicinal Chemistry · doi:10.2174/092986707782794078 · Cited by 91 · see citing works
Dimebon and Tacrine Inhibit Neurotoxic Action of β-Amyloid in Culture and Block L-type Ca2+ Channels
Lermontova, N. N., Redkozubov, A., Shevtsova, E. F., Serkova, T. P., Kireeva, E. G., & Бачурин, С. О. (2001) · Bulletin of Experimental Biology and Medicine · doi:10.1023/a:1017972709652 · Cited by 89 · see citing works
Oxidative Damage and Progression to Alzheimer's Disease in Patients with Mild Cognitive Impairment
Baldeiras, I., Santana, I. J., Proença, M. T., Garrucho, M. H., Pascoal, R., Rodrigues, A. P., Duro, D., & Oliveira, C. R. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-091723 · Cited by 88 · see citing works
Mitochondrial Decay in the Brains of Old Rats: Ameliorating Effect of Alpha-Lipoic Acid and Acetyl-l-carnitine
Long, J., Gao, F., Tong, L., Cotman, C. W., Ames, B. N., & Liu, J. (2008) · Neurochemical Research · doi:10.1007/s11064-008-9850-2 · Cited by 86 · see citing works
Safety and Efficacy of Idebenone versus Tacrine in Patients with Alzheimer's Disease: Results of a Randomized, Double-Blind, Parallel-Group Multicenter Study
Gutzmann, H., Kühl, K.-P., Hadler, D., & Rapp, M. A. (2002) · Pharmacopsychiatry · doi:10.1055/s-2002-19833 · Cited by 85 · see citing works
Dimebon (Latrepirdine) Enhances Mitochondrial Function and Protects Neuronal Cells from Death
Zhang, S., Hedskog, L., Petersen, C. H., Winblad, B. G., & Ankarcrona, M. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100174 · Cited by 85 · see citing works
Mechanisms of Action of Non-Steroidal Anti-Inflammatory Drugs for the Prevention of Alzheimers Disease
Cole, G. M., & Frautschy, S. A. (2010) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152710791011991 · Cited by 84 · see citing works
Coenzyme Q10 Reduces β-Amyloid Plaque in an APP/PS1 Transgenic Mouse Model of Alzheimer’s Disease
Yang, X., Dai, G., Li, G., & Yang, E. S. (2009) · Journal of Molecular Neuroscience · doi:10.1007/s12031-009-9297-1 · Cited by 83 · see citing works
Grape Seed Polyphenolic Extract as a Potential Novel Therapeutic Agent in Tauopathies
Ho, L., Yemul, S., Wang, J., & Pasinetti, G. M. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-0969 · Cited by 82 · see citing works
Mitochondrial accumulation of APP and Aβ: significance for Alzheimer disease pathogenesis
Pavlov, P. F., Petersen, C. H., Glaser, E. G., & Ankarcrona, M. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00892.x · Cited by 82 · see citing works
Oxidative damage in brain from human mutant APP/PS-1 double knock-in mice as a function of age
Abdul, H. M., Rukhsana Sultana, A., Clair, D. K. S., Markesbery, W. R., & Butterfield, D. A. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.08.012 · Cited by 81 · see citing works
KNS‐760704 [(6R)‐4,5,6,7‐tetrahydro‐N6‐propyl‐2, 6‐benzothiazole‐diamine dihydrochloride monohydrate] for the Treatment of Amyotrophic Lateral Sclerosis
Gribkoff, V. K., & Bozik, M. E. (2008) · CNS Neuroscience & Therapeutics · doi:10.1111/j.1755-5949.2008.00048.x · Cited by 77 · see citing works
Mechanism of Inducible Nitric Oxide Synthase Inactivation by Aminoguanidine and l -N6-(1-Iminoethyl)lysine
Bryk, R., & Wolff, D. J. (1998) · Biochemistry · doi:10.1021/bi972065t · Cited by 77 · see citing works
Inhibition by R(+) or S(–) pramipexole of caspase activation and cell death induced by methylpyridinium ion or beta amyloid peptide in SH‐SY5Y neuroblastoma
Abramova, N. N., Cassarino, D. S., Khan, S. M., Painter, T. W., & Bennett, J. P. (2002) · Journal of Neuroscience Research · doi:10.1002/jnr.10127 · Cited by 74 · see citing works
Mitochondrial dihydrolipoyl succinyltransferase deficiency accelerates amyloid pathology and memory deficit in a transgenic mouse model of amyloid deposition
Dumont, M., Ho, D. J., Calingasan, N. Y., Xu, H., Gibson, G. E., & Beal, M. F. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.07.008 · Cited by 74 · see citing works
Self-citation
Idebenone in senile dementia of Alzheimer type: A multicentre study
Senin, U., Parnetti, L., Barbagallo-Sangiorgi, G., Bartorelli, L., Bocola, V., Capurso, A., Cuzzupoli, M., Denaro, M., Marigliano, V., Tammaro, A. E., et al. (1992) · Archives of Gerontology and Geriatrics · doi:10.1016/0167-4943(92)90060-h · Cited by 72 · see citing works
Acetyl-l-carnitine (ALCAR) prevents hypobaric hypoxia–induced spatial memory impairment through extracellular related kinase–mediated nuclear factor erythroid 2-related factor 2 phosphorylation
Barhwal, K. K., Hota, S. K., Jain, V., Prasad, D. N., Singh, S. B., & Ilavazhagan, G. (2009) · Neuroscience · doi:10.1016/j.neuroscience.2009.02.086 · Cited by 72 · see citing works
Mitochondrial Superoxide Contributes to Blood Flow and Axonal Transport Deficits in the Tg2576 Mouse Model of Alzheimer's Disease
Massaad, C. A., Amin, S. K., Hu, L., Yuan, M., Klann, E., & Pautler, R. G. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010561 · Cited by 71 · see citing works
Nitric oxide in the cerebral cortex of amyloid-precursor protein (SW) Tg2576 transgenic mice
Rodrigo, J., Fernández‐Vizarra, P., Castro‐Blanco, S., Bentura, M. L., Nieto, M., Gómez‐Isla, T., Martínez‐Murillo, R., Martı́nez, A., Serrano, J., & Fernández, A. P. (2004) · Neuroscience · doi:10.1016/j.neuroscience.2004.06.030 · Cited by 70 · see citing works
The neurobiology of isoprostanes and Alzheimer's disease
Praticò, D. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2010.01.009 · Cited by 65 · see citing works
Mitochondria-targeted antioxidant effects of S(-) and R(+) pramipexole
Ferrari‐Toninelli, G., Maccarinelli, G., Uberti, D. L., Buerger, E., & Memo, M. (2010) · BMC Pharmacology · doi:10.1186/1471-2210-10-2 · Cited by 65 · see citing works
From Anti-allergic to Anti-Alzheimer ’ s: Molecular Pharmacology of Dimebon™
Okun, I. M., Tkachenko, S. N., Khvat, A. V., Mitkin, O. D., Kazey, V. I., & Ivachtchenko, A. V. (2010) · Current Alzheimer Research · doi:10.2174/156720510790691100 · Cited by 65 · see citing works
Severe Motor Neuron Degeneration in the Spinal Cord of the Tg2576 Mouse Model of Alzheimer Disease
Seo, J., Leem, Y., Lee, K.-W., Kim, S., Lee, J.-K., & Han, P. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-091528 · Cited by 62 · see citing works
Dietary supplementation with a combination of α-lipoic acid, acetyl-l-carnitine, glycerophosphocoline, docosahexaenoic acid, and phosphatidylserine reduces oxidative damage to murine brain and improves cognitive performance
Suchy, J. J., Chan, A., & Shea, T. B. (2009) · Nutrition Research · doi:10.1016/j.nutres.2008.11.004 · Cited by 60 · see citing works
Novel drug targets based on metallobiology of Alzheimer's disease
Bandyopadhyay, S., Huang, X., Lahiri, D. K., & Rogers, J. T. (2010) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2010.525352 · Cited by 58 · see citing works
Transcriptional Control of Energy Homeostasis through the PGC1 Coactivators
Spiegelman, B. M. (2007) · Novartis Foundation symposium · doi:10.1002/9780470985571.ch2 · Cited by 56 · see citing works
Pharmacological modulation of nitric oxide synthesis by mechanism-based inactivators and related inhibitors
Bryk, R., & Wolff, D. J. (1999) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(99)00030-3 · Cited by 51 · see citing works
Neuroprotection of Pramipexole in UPS Impairment Induced Animal Model of Parkinson’s Disease
Li, C., Guo, Y. L., Xie, W., Li, X., Janokovic, J., & Le, W. (2010) · Neurochemical Research · doi:10.1007/s11064-010-0214-3 · Cited by 49 · see citing works
The role of cytochrome c oxidase deficiency in ROS and amyloid plaque formation
Pickrell, A. M., Fukui, H., & Moraes, C. T. (2009) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-009-9245-3 · Cited by 46 · see citing works
Acute dosing of latrepirdine (Dimebon™), a possible Alzheimer therapeutic, elevates extracellular amyloid-β levels in vitro and in vivo
Steele, J., Kim, S. H., Cirrito, J. R., Verges, D. K., Restivo, J. L., Westaway, D. A., Fraser, P., George‐Hyslop, P. S., Sano, M. C., Борисович, Б. И., et al. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-51 · Cited by 44 · see citing works
Neuroprotection through Stimulation of Mitochondrial Antioxidant Protein Expression
Greco, T., & Fiskum, G. M. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100519 · Cited by 34 · see citing works
Modulatory effect of acetyl-l-carnitine on amyloid precursor protein metabolism in hippocampal neurons
Epis, R., Marcello, E. E., Gardoni, F., Longhi, A., Calvani, M., Iannuccelli, M., Cattabeni, F., Canonico, P. L., & Luca, M. D. (2008) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2008.09.001 · Cited by 33 · see citing works
Inactivation of nitric oxide synthases and cellular nitric oxide formation by N6-iminoethyl-l-lysine and N5-iminoethyl-l-ornithine
Wolff, D. J., Lubeskie, A., Gauld, D. S., & Neulander, M. J. (1998) · European Journal of Pharmacology · doi:10.1016/s0014-2999(98)00267-2 · Cited by 33 · see citing works
Inhibition of cyclooxygenase as potential novel therapeutic strategy in N141I presenilin-2 familial Alzheimer's disease
Qin, W., Peng, Y., Ksiȩżak-Reding, H., Ho, L., Stetka, B., Lovati, E., & Pasinetti, G. M. (2005) · Molecular Psychiatry · doi:10.1038/sj.mp.4001773 · Cited by 29 · see citing works
Differing short-term neuroprotective effects of the fibrates fenofibrate and bezafibrate in MPTP and 6-OHDA experimental models of Parkinson's disease
Kreisler, A., Duhamel, A., Vanbesien-Mailliot, C., Destée, A., & Bordet, R. (2010) · Behavioural Pharmacology · doi:10.1097/fbp.0b013e32833a5c81 · Cited by 24 · see citing works
N-iminoethyl-l-lysine improves memory and reduces amyloid pathology in a transgenic mouse model of amyloid deposition
Dumont, M., Wille, E. J., Calingasan, N. Y., Nathan, C., Beal, M. F., & Lin, M. T. S. (2009) · Neurochemistry International · doi:10.1016/j.neuint.2009.11.006 · Cited by 13 · see citing works
Self-citation
Dimebon as a Potential Therapy for Alzheimer's Disease
Doody, R. S. (2009) · CNS Spectrums · doi:10.1017/s1092852900024913 · Cited by 10 · see citing works
Acetyl-L-carnitine. Monograph.
(2010) · PubMed · Cited by 10 · see citing works
Effect of idebenone and various nootropic drugs on lipid peroxidation in rat brain homogenate in the presence of succinate.
Suno, M., & Nagaoka, A. (1988) · Folia Pharmacologica Japonica · doi:10.1254/fpj.91.295 · Cited by 8 · see citing works
P3‐181: Oxidative damage and mitochondrial dysfunction in patients with mild cognitive impairment and Alzheimer's disease
Baldeiras, I., Santana, I. J., Proença, M. T., Garrucho, M. H., Pascoal, R., Rodrigues, A. S., Duro, D., Silva, D. F., Cardoso, S. M., & Oliveira, C. R. (2010) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2010.05.1679 · Cited by 4 · see citing works

Flagged first, then by citations

3 of the 188 references couldn’t be matched to a known paper.

Sorted by citations

The Role of Oxidative Stress in Parkinson's Disease
Dias, V., Junn, E., & Mouradian, M. M. (2013) · Journal of Parkinson’s Disease · doi:10.3233/jpd-130230 · Cited by 1,845 · see citing works
Progressive multiple sclerosis: pathology and pathogenesis
Lassmann, H., van Horssen, J., & Mahad, D. (2012) · Nature Reviews Neurology · doi:10.1038/nrneurol.2012.168 · Cited by 1,033 · see citing works
Oxidative Stress in Neurodegenerative Diseases: From Molecular Mechanisms to Clinical Applications
Liu, Z., Zhou, T., Ziegler, A. C., Dimitrion, P., & Zuo, L. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/2525967 · Cited by 810 · see citing works
Bioinorganic Chemistry of Alzheimer’s Disease
Kepp, K. P. (2012) · Chemical Reviews · doi:10.1021/cr300009x · Cited by 672 · see citing works
Why does Brain Metabolism not Favor Burning of Fatty Acids to Provide Energy? - Reflections on Disadvantages of the Use of Free Fatty Acids as Fuel for Brain
Schönfeld, P., & Reiser, G. (2013) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2013.128 · Cited by 457 · see citing works
Influence of gut microbiota on neuropsychiatric disorders
Cénit, M. C., Sanz, Y., & Codoñer‐Franch, P. (2017) · World Journal of Gastroenterology · doi:10.3748/wjg.v23.i30.5486 · Cited by 418 · see citing works
Neuroprotective action of resveratrol
Bastianetto, S., Ménard, C., & Quirion, R. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.09.011 · Cited by 411 · see citing works
Neuroprotective Mechanisms of Resveratrol in Alzheimer’s Disease: Role of SIRT1
Gomes, B. A. Q., Silva, J. P. B., Romeiro, C. F. R., dos Santos, S. M., Rodrigues, C. A., Gonçalves, P. R., Sakai, J. T., Mendes, P. F. S., Varela, E. L. P., & Monteiro, M. C. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/8152373 · Cited by 403 · see citing works
Neuroprotective and Antioxidant Effect of Ginkgo biloba Extract Against AD and Other Neurological Disorders
Singh, S. K., Srivastav, S., Castellani, R. J., Plascencia‐Villa, G., & Perry, G. L. (2019) · Neurotherapeutics · doi:10.1007/s13311-019-00767-8 · Cited by 402 · see citing works
Comprehensive Review in Current Developments of Benzimidazole‐Based Medicinal Chemistry
Keri, R. S., Hiremathad, A., Budagumpi, S., & Nagaraja, B. M. (2014) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12462 · Cited by 397 · see citing works
Flavonoids as Prospective Neuroprotectants and Their Therapeutic Propensity in Aging Associated Neurological Disorders
Ayaz, M., Sadiq, A., Junaid, M., Ullah, F., Ovais, M., Ullah, I., Ahmed, J., & Shahid, M. M. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00155 · Cited by 348 · see citing works
Phytocannabinoids as novel therapeutic agents in {CNS} disorders.
Hill, A. J., Williams, C. M., Whalley, B. J., & Stephens, G. J. (2012) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2011.09.002 · Cited by 312 · see citing works
Antioxidant properties of natural polyphenols and their therapeutic potentials for Alzheimer's disease
Choi, D., Lee, Y., Hong, J. T., & Lee, H. (2011) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2011.11.014 · Cited by 305 · see citing works
Microglia in Alzheimer Disease: Well-Known Targets and New Opportunities
Hemonnot, A.-L., Hua, J., Ulmann, L., & Hirbec, H. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00233 · Cited by 298 · see citing works
Mechanistic insights and perspectives involved in neuroprotective action of quercetin
Grewal, A. K., Singh, T. G., Sharma, D., Sharma, V., Singh, M., Rahman, M. H., Najda, A., Walasek-Janusz, M., Kamel, M. S., Albadrani, G. M., et al. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111729 · Cited by 287 · see citing works
Oxidative stress and β-amyloid protein in Alzheimer’s disease
Cai, Z., Zhao, B., & Ratka, A. (2011) · NeuroMolecular Medicine · doi:10.1007/s12017-011-8155-9 · Cited by 279 · see citing works
Mitochondrial Aspects of Synaptic Dysfunction in Alzheimer’s Disease
Cai, Q., & Tammineni, P. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160726 · Cited by 274 · see citing works
Nicotinamide forestalls pathology and cognitive decline in Alzheimer mice: evidence for improved neuronal bioenergetics and autophagy procession
Liu, D., Pitta, M., Jiang, H., Lee, J.-H., Zhang, G., Chen, X., Kawamoto, E. M., & Mattson, M. P. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.11.020 · Cited by 238 · see citing works
Pivotal role of glycogen synthase kinase-3: A therapeutic target for Alzheimer's disease
Maqbool, M., Mobashir, M., & Hoda, N. (2015) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2015.10.018 · Cited by 228 · see citing works
LRP1 in Brain Vascular Smooth Muscle Cells Mediates Local Clearance of Alzheimer's Amyloid-β
Kanekiyo, T., Liu, C., Shinohara, M., Li, J., & Bu, G. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.3987-12.2012 · Cited by 221 · see citing works
Chronic Stress and Oxidative Stress as Common Factors of the Pathogenesis of Depression and Alzheimer’s Disease: The Role of Antioxidants in Prevention and Treatment
Juszczyk, G., Mikulska, J., Kasperek, K., Pietrzak, D., Mrozek, W., & Herbet, M. (2021) · Antioxidants · doi:10.3390/antiox10091439 · Cited by 235 · see citing works
Nicotinamide mononucleotide protects against β-amyloid oligomer-induced cognitive impairment and neuronal death
Wang, X., Hu, X., Yang, Y., Takata, T., & Sakurai, T. (2016) · Brain Research · doi:10.1016/j.brainres.2016.04.060 · Cited by 217 · see citing works
Plant Food Residues as a Source of Nutraceuticals and Functional Foods
Varzakas, T. H., Zakynthinos, G., & Verpoort, F. (2016) · Foods · doi:10.3390/foods5040088 · Cited by 202 · see citing works
Oxidative Stress in Alzheimer’s Disease: Are We Connecting the Dots?
Rosini, M., Simoni, E., Milelli, A., Minarini, A., & Melchiorre, C. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400970m · Cited by 202 · see citing works
Mitochondrial dysfunction in Alzheimer’s disease
D’Alessandro, M. C. B., Kanaan, S., Geller, M., Praticò, D., & Daher, J. P. L. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102713 · Cited by 201 · see citing works
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 198 · see citing works
Shared Mechanisms of Neurodegeneration in Alzheimer’s Disease and Parkinson’s Disease
Xie, A., Gao, J., Xu, L., & Meng, D.-M. (2014) · BioMed Research International · doi:10.1155/2014/648740 · Cited by 196 · see citing works
Overview of Alzheimer’s Disease and Some Therapeutic Approaches Targeting Aβ by Using Several Synthetic and Herbal Compounds
Singh, S. K., Srivastav, S., Yadav, A. K., Srikrishna, S., & Perry, G. L. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/7361613 · Cited by 188 · see citing works
Mitochondrial DNA Oxidative Damage and Repair in Aging and Alzheimer's Disease
Santos, R. X., Correia, S. C., Zhu, X., Smith, M. A., Moreira, P. I., Castellani, R. J., Nunomura, A., & Perry, G. L. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.5039 · Cited by 176 · see citing works
Alzheimer’s disease: How metal ions define β-amyloid function
Kepp, K. P. (2017) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2017.05.007 · Cited by 151 · see citing works
Transcription factor NRF2 as a promising therapeutic target for Alzheimer’s disease
Qu, Z., Sun, J., Zhang, W., Yu, J., & Zhuang, C. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.06.028 · Cited by 140 · see citing works
Indigenous microorganisms as potential bioremediators for environments contaminated with heavy metals
Colin, V. L., Villegas, L. B., & Abate, C. M. (2012) · International Biodeterioration & Biodegradation · doi:10.1016/j.ibiod.2011.12.001 · Cited by 132 · see citing works
Current Screening Methodologies in Drug Discovery for Selected Human Diseases
Lage, O. M., Ramos, M. C., Calisto, R., Almeida, E., Vasconcelos, V. M., & Vicente, F. (2018) · Marine Drugs · doi:10.3390/md16080279 · Cited by 133 · see citing works
3-Hydroxybutyrate methyl ester as a potential drug against Alzheimer's disease via mitochondria protection mechanism
Zhang, J., Cao, Q., Li, S., Lu, X., Zhao, Y., Guan, J., Chen, J., Wu, Q., & Chen, G. (2013) · Biomaterials · doi:10.1016/j.biomaterials.2013.06.043 · Cited by 130 · see citing works
Neuroprotective effect of blackberry (Rubus sp.) polyphenols is potentiated after simulated gastrointestinal digestion
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 130 · see citing works
NSAIDs as potential treatment option for preventing amyloid β toxicity in Alzheimer’s disease: an investigation by docking, molecular dynamics, and DFT studies
Azam, F., Alabdullah, N. H., Ehmedat, H. M., Abulifa, A. R., Taban, I. M., & Upadhyayula, S. (2017) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2017.1338164 · Cited by 123 · see citing works
Curcumin- and Fish Oil-Loaded Spongosome and Cubosome Nanoparticles with Neuroprotective Potential against H2O2-Induced Oxidative Stress in Differentiated Human SH-SY5Y Cells
Rakotoarisoa, M., Angelov, B., Garamus, V. M., & Angelova, A. (2019) · ACS Omega · doi:10.1021/acsomega.8b03101 · Cited by 122 · see citing works
Near infrared-activatable biomimetic nanogels enabling deep tumor drug penetration inhibit orthotopic glioblastoma
Zhang, D., Tian, S., Liu, Y., Zheng, M., Yang, X., Zou, Y., Shi, B., & Luo, L. (2022) · Nature Communications · doi:10.1038/s41467-022-34462-8 · Cited by 121 · see citing works
Andrographolide reduces cognitive impairment in young and mature AβPPswe/PS-1 mice
Serrano, F. G., Tapia‐Rojas, C., Carvajal, F. J., Hancke, J. L., Cerpa, W. F., & Inestrosa, N. C. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-61 · Cited by 117 · see citing works
Modulation of Mitochondrial Complex I Activity Averts Cognitive Decline in Multiple Animal Models of Familial Alzheimer's Disease
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 110 · see citing works
Oxidative Stress, Mitochondrial Dysfunction and the Mitochondria Theory of Aging
Kong, Y., Trabucco, S. E., & Zhang, H. (2014) · Interdisciplinary topics in gerontology and geriatrics · doi:10.1159/000358901 · Cited by 112 · see citing works
SIRT3 Regulation of Mitochondrial Quality Control in Neurodegenerative Diseases
Meng, H., Yan, W.-Y., Lei, Y.-H., Wan, Z., Hou, Y.-Y., Sun, L., & Zhou, J.-P. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00313 · Cited by 112 · see citing works
TRPM2 dependence of ROS-induced NLRP3 activation in Alzheimer's disease
Aminzadeh, M., Roghani, M., Sarfallah, A., & Riazi, G. H. (2017) · International Immunopharmacology · doi:10.1016/j.intimp.2017.10.024 · Cited by 109 · see citing works
Resveratrol activation of AMPK-dependent pathways is neuroprotective in human neural stem cells against amyloid-beta-induced inflammation and oxidative stress
Chiang, M., Nicol, C. J. B., & Cheng, Y. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.10.002 · Cited by 109 · see citing works
Amelioration of Scopolamine‐Induced Learning and Memory Impairment by α‐Pinene in C57BL/6 Mice
Gil-Yong, L., Lee, C., Park, G. H., & Jang, J. (2017) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2017/4926815 · Cited by 109 · see citing works
Oxidative stress underlying axonal degeneration in adrenoleukodystrophy: A paradigm for multifactorial neurodegenerative diseases?
Galea, E., Launay, N., Portero-Otin, M., Ruiz, M., Pamplona, R., Aubourg, P., Ferrer, I., & Pujol, A. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.02.005 · Cited by 108 · see citing works
Central and Peripheral Metabolic Defects Contribute to the Pathogenesis of Alzheimer's Disease: Targeting Mitochondria for Diagnosis and Prevention
Peng, Y., Gao, P., Shi, L., Chen, L., Liu, J., & Long, J. (2020) · Antioxidants & Redox Signaling · doi:10.1089/ars.2019.7763 · Cited by 110 · see citing works
Recent Advances in the Treatment of Neurodegenerative Diseases Based on GSH Delivery Systems
Cacciatore, I., Baldassarre, L., Fornasari, E., Mollica, A., & Pinnen, F. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/240146 · Cited by 106 · see citing works
Evidence of neuroprotective effects of saffron and crocin in a Drosophila model of parkinsonism
Rao, S. V., ., M., Yenisetti, S. C., & Rajini, P. S. (2015) · NeuroToxicology · doi:10.1016/j.neuro.2015.12.010 · Cited by 104 · see citing works
Is Alzheimer's disease related to metabolic syndrome? A Wnt signaling conundrum
Ríos, J. A., Cisternas, P., Arrese, M. A., Salesa Barja, Y., & Inestrosa, N. C. (2014) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2014.07.004 · Cited by 104 · see citing works
Age-Related Decrease in the Mitochondrial Sirtuin Deacetylase Sirt3 Expression Associated with ROS Accumulation in the Auditory Cortex of the Mimetic Aging Rat Model
Zeng, L., Yang, Y., Hu, Y., Sun, Y., Du, Z., Xie, Z., Zhou, T., & Kong, W. (2014) · PLoS ONE · doi:10.1371/journal.pone.0088019 · Cited by 103 · see citing works
HPLC-PDA-MS/MS profiling of secondary metabolites from Opuntia ficus-indica cladode, peel and fruit pulp extracts and their antioxidant, neuroprotective effect in rats with aluminum chloride induced neurotoxicity
El-Hawary, S. S., Sobeh, M., Badr, W. K., Abdelfattah, M. A. O., Ali, Z. Y., El-Tantawy, M. E., Rabeh, M. A., & Wink, M. (2020) · Saudi Journal of Biological Sciences · doi:10.1016/j.sjbs.2020.07.003 · Cited by 102 · see citing works
Alzheimer’s disease treated patients showed different patterns for oxidative stress and inflammation markers
Gubandru, M., Margina, D. M., Tsitsimpikou, C., Goutzourelas, N., Tsarouhas, K., Ilie, M., Tsatsakis, A. M., & Kouretas, D. (2013) · Food and Chemical Toxicology · doi:10.1016/j.fct.2013.07.013 · Cited by 102 · see citing works
Slow Excitotoxicity in Alzheimer's Disease
Ong, W.-Y., Tanaka, K., Dawe, G. S., Ittner, L. M., & Farooqui, A. A. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-121990 · Cited by 101 · see citing works
Maternal Docosahexaenoic Acid Feeding Protects Against Impairment of Learning and Memory and Oxidative Stress in Prenatally Stressed Rats: Possible Role of Neuronal Mitochondria Metabolism
Feng, Z., Zou, X., Jia, H., Li, X., Zhu, Z., Liu, X., Bucheli, P., Ballèvre, O. P., Hou, Y., Zhang, W., et al. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3750 · Cited by 97 · see citing works
NOX4 as a critical effector mediating neuroinflammatory cytokines, myeloperoxidase and osteopontin, specifically in astrocytes in the hippocampus in Parkinson's disease
Boonpraman, N., Yoon, S., Kim, C. Y., Moon, J., & Yi, S. S. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102698 · Cited by 95 · see citing works
Development of a PET radiotracer for non-invasive imaging of the reactive oxygen species, superoxide, in vivo
Chu, W., Chepetan, A. M., Zhou, D., Shoghi, K. I., Xu, J., Dugan, L. L., Gropler, R. J., Mintun, M. A., & Mach, R. H. (2014) · Organic & Biomolecular Chemistry · doi:10.1039/c3ob42379d · Cited by 93 · see citing works
Mechanisms and Neuroprotective Activities of Stigmasterol Against Oxidative Stress-Induced Neuronal Cell Death via Sirtuin Family
Pratiwi, R., Nantasenamat, C., Ruankham, W., Suwanjang, W., Prachayasittikul, V., Prachayasittikul, S., & Phopin, K. (2021) · Frontiers in Nutrition · doi:10.3389/fnut.2021.648995 · Cited by 96 · see citing works
Schizandrin, an Antioxidant Lignan fromSchisandra chinensis,Ameliorates Aβ1–42-Induced Memory Impairment in Mice
Hu, D., Cao, Y., He, R., Han, N., Liu, Z., Miao, L., & Yin, J. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/721721 · Cited by 92 · see citing works
Reactive oxygen species in development and infection processes
Marschall, R., & Tudzynski, P. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.03.020 · Cited by 87 · see citing works
Towards the prevention of potential aluminum toxic effects and an effective treatment for Alzheimer's disease
Percy, M. E., Kruck, T. P. A., Pogue, A. I., & Lukiw, W. J. (2011) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2011.08.001 · Cited by 88 · see citing works
A Pivotal Role of Nrf2 in Neurodegenerative Disorders: A New Way for Therapeutic Strategies
Süzen, S., Tucci, P., Profumo, E., Buttari, B., & Saso, L. (2022) · Pharmaceuticals · doi:10.3390/ph15060692 · Cited by 87 · see citing works
Peroxiredoxin I is a ROS/p38 MAPK-dependent inducible antioxidant that regulates NF-κB-mediated iNOS induction and microglial activation
Kim, S., Park, Y., Min, J., Sun, H.-N., Han, Y., Hua, J.-M., Lee, T., Lee, S., Chang, K.-T., Kang, S. W., et al. (2013) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2013.03.006 · Cited by 88 · see citing works
Abnormal thiamine-dependent processes in Alzheimer's Disease. Lessons from diabetes
Gibson, G. E., Hirsch, J. A., Cirio, R. T., Jordan, B. D., Fonzetti, P., & Elder, J. (2012) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2012.09.001 · Cited by 88 · see citing works
The early events of Alzheimer's disease pathology: from mitochondrial dysfunction to BDNF axonal transport deficits
Ye, X., Tai, W., & Zhang, D. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.11.004 · Cited by 88 · see citing works
Flavonoids and Other Polyphenols: Bioactive Molecules from Traditional Medicine Recipes/Medicinal Plants and Their Potential for Phytopharmaceutical and Medical Application
Intharuksa, A., Kuljarusnont, S., Sasaki, Y., & Tungmunnithum, D. (2024) · Molecules · doi:10.3390/molecules29235760 · Cited by 101 · see citing works
Impaired Short-Term Plasticity in Mossy Fiber Synapses Caused by Mitochondrial Dysfunction of Dentate Granule Cells Is the Earliest Synaptic Deficit in a Mouse Model of Alzheimer's Disease
Lee, S. H., Kim, K.-R., Ryu, S.-Y., Son, S., Hong, H. S., Mook-Jung, I., Lee, S.-H., & Ho, W.-K. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.0465-12.2012 · Cited by 86 · see citing works
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 83 · see citing works
Oxidative Stress in Genetic Mouse Models of Parkinson’s Disease
Varçin, M., Bentea, E., Michotte, Y. M., & Sarre, S. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/624925 · Cited by 84 · see citing works
Coenzyme Q and Its Role in the Dietary Therapy against Aging
Varela-López, A., Giampieri, F., Battino, M., & Quiles, J. (2016) · Molecules · doi:10.3390/molecules21030373 · Cited by 86 · see citing works
Neuroprotective effects of digested polyphenols from wild blackberry species
Tavares, L., Figueira, I., McDougall, G. J., Vieira, H. L. A., Stewart, D., Alves, P. M., Ferreira, R. B., & dos Santos, C. N. (2012) · European Journal of Nutrition · doi:10.1007/s00394-012-0307-7 · Cited by 85 · see citing works
Oxidative Stress in Alzheimer's and Parkinson's Diseases: Insights from the YeastSaccharomyces cerevisiae
Pimentel, C., Batista-Nascimento, L. S., Rodrigues‐Pousada, C., & Menezes, R. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/132146 · Cited by 83 · see citing works
Amphiphilic Nanocarrier Systems for Curcumin Delivery in Neurodegenerative Disorders
Rakotoarisoa, M., & Angelova, A. (2018) · Medicines · doi:10.3390/medicines5040126 · Cited by 84 · see citing works
The antioxidant activity and neuroprotective mechanism of isoliquiritigenin
Shi, D., Yang, J., Jiang, Y., Wen, L., Wang, Z., & Yang, B. J. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.03.016 · Cited by 83 · see citing works
Potential Role of Natural Polyphenols against Protein Aggregation Toxicity: In Vitro, In Vivo, and Clinical Studies
Henríquez, G., Gomez, A., Guerrero, E., & Narayan, M. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00381 · Cited by 83 · see citing works
The protective role of plant biophenols in mechanisms of Alzheimer's disease
Omar, S. H., Scott, C., Hamlin, A. S., & Obied, H. K. (2017) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2017.02.016 · Cited by 82 · see citing works
Inhibition of the Mitochondrial Enzyme ABAD Restores the Amyloid-β-Mediated Deregulation of Estradiol
Lim, Y., Grimm, A., Giese, M. H., Mensah‐Nyagan, A. G., Villafranca, J. E., Ittner, L. M., Eckert, A., & Götz, J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0028887 · Cited by 82 · see citing works
Inhibition of neuroinflammation in BV2 microglia by the biflavonoid kolaviron is dependent on the Nrf2/ARE antioxidant protective mechanism
Onasanwo, S. A., Velagapudi, R., El‐Bakoush, A., & Olajide, O. A. (2016) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-016-2655-8 · Cited by 80 · see citing works
Induction of Mitochondrial Changes Associated with Oxidative Stress on Very Long Chain Fatty Acids (C22:0, C24:0, or C26:0)-Treated Human Neuronal Cells (SK-NB-E)
Zarrouk, A., Véjux, A., Nury, T., Hajj, H. I. E., Haddad, M., Cherkaoui‐Malki, M., Riedinger, J., Hammami, M., & Lizard, G. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/623257 · Cited by 90 · see citing works
Dual-Channel Imaging of Amyloid-β Plaques and Peroxynitrite To Illuminate Their Correlations in Alzheimer’s Disease Using a Unimolecular Two-Photon Fluorescent Probe
Xie, X., Liu, G., Niu, Y., Xu, C., Li, Y., Zhang, J., Jiao, X., Wang, X., & Tang, B. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.1c03334 · Cited by 77 · see citing works
Enhanced memory in Wistar rats by virgin coconut oil is associated with increased antioxidative, cholinergic activities and reduced oxidative stress
Rahim, N. S., Lim, S. M., Mani, V., Majeed, A. B. A., & Ramasamy, K. (2017) · Pharmaceutical Biology · doi:10.1080/13880209.2017.1280688 · Cited by 77 · see citing works
Aqueous Extracts of the Edible Gracilaria tenuistipitata are Protective Against H2O2-Induced DNA Damage, Growth Inhibition, and Cell Cycle Arrest
Yang, J.-I., Yeh, C.-C., Lee, J., Yi, S., Huang, H., Tseng, C., & Chang, H. (2012) · Molecules · doi:10.3390/molecules17067241 · Cited by 76 · see citing works
Baicalin protects PC-12 cells from oxidative stress induced by hydrogen peroxide via anti-apoptotic effects
Zheng, W., Wang, F., Cao, X., Pan, H.-Y., Liu, X., Hu, X., & Sun, Y.-Y. (2014) · Brain Injury · doi:10.3109/02699052.2013.860469 · Cited by 75 · see citing works
Targeting Mitochondria in Alzheimer Disease: Rationale and Perspectives
Lanzillotta, C., Domenico, F. D., Marzia Perluigi, A., & Butterfield, D. A. (2019) · CNS Drugs · doi:10.1007/s40263-019-00658-8 · Cited by 72 · see citing works
Identification of two novel prenylated flavonoids in mulberry leaf and their bioactivities
Wen, L., Shi, D., Zhou, T., Tu, J., He, M., Jiang, Y., & Yang, B. J. (2020) · Food Chemistry · doi:10.1016/j.foodchem.2020.126236 · Cited by 71 · see citing works
Identification of phenolic secondary metabolites from Schotia brachypetala Sond. (Fabaceae) and demonstration of their antioxidant activities in Caenorhabditis elegans
Sobeh, M., Elhawary, E. A., Peixoto, H. S., Labib, R. M., Handoussa, H., Swilam, N., El‐Khatib, A. H., Sharapov, F., Mohamed, T., Krstin, S., et al. (2016) · PeerJ · doi:10.7717/peerj.2404 · Cited by 71 · see citing works
SIRT3 Acts as a Neuroprotective Agent in Rotenone-Induced Parkinson Cell Model
Zhang, J., Deng, Y., Zhang, M., Su, H., & Qu, Q. (2016) · Neurochemical Research · doi:10.1007/s11064-016-1892-2 · Cited by 70 · see citing works
Nanomicellar formulation of coenzyme Q10 (Ubisol-Q10) effectively blocks ongoing neurodegeneration in the mouse 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine model: potential use as an adjuvant treatment in Parkinson's disease
Sikorska, M., Lanthier, P., Miller, H., Beyers, M., Sodja, C., Zurakowski, B., Gangaraju, S., Pandey, S., & Sandhu, J. K. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.03.032 · Cited by 70 · see citing works
Role of Gasotransmitters in Oxidative Stresses, Neuroinflammation, and Neuronal Repair
Shefa, U., Yeo, S. G., Kim, M., Song, I. O., Jung, J., Jeong, N. Y., & Huh, Y. (2017) · BioMed Research International · doi:10.1155/2017/1689341 · Cited by 70 · see citing works
New developments on the functions of coenzyme Q in mitochondria
Genova, M. L., & Lenaz, G. (2011) · BioFactors · doi:10.1002/biof.168 · Cited by 67 · see citing works
Neuroprotective and Anti-Oxidative Effects of the Hemodialysate Actovegin on Primary Rat Neurons in Vitro
Elmlinger, M. W., Kriebel, M., & Ziegler, D. (2011) · NeuroMolecular Medicine · doi:10.1007/s12017-011-8157-7 · Cited by 67 · see citing works
Chlorogenic acid protects against aluminium-induced cytotoxicity through chelation and antioxidant actions in primary hippocampal neuronal cells
Wang, X., Fan, X., Yuan, S., Jiao, W., Liu, B., Cao, J., & Jiang, W. (2017) · Food & Function · doi:10.1039/c7fo00659d · Cited by 66 · see citing works
The Multifaceted Roles of DJ-1 as an Antioxidant
Raninga, P. V., Trapani, G. D., & Tonissen, K. F. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-6583-5_6 · Cited by 64 · see citing works
Comorbidity Analysis between Alzheimer’s Disease and Type 2 Diabetes Mellitus (T2DM) Based on Shared Pathways and the Role of T2DM Drugs
Karki, R., Kodamullil, A. T., & Hofmann‐Apitius, M. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170440 · Cited by 64 · see citing works
Neuroprotective effects of Kukoamine B against hydrogen peroxide-induced apoptosis and potential mechanisms in SH-SY5Y cells
Hu, X., Niu, Y., Zhang, Q., Tian, X., Gao, L., Guo, L.-P., Meng, W., & Zhao, Q.-C. (2015) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2015.06.017 · Cited by 63 · see citing works
Involvement and interplay of Parkin, PINK1, and DJ1 in neurodegenerative and neuroinflammatory disorders
Wilhelmus, M. M. M., Nijland, P. G., Drukarch, B., de Vries, H. E., & van Horssen, J. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.05.040 · Cited by 62 · see citing works
The potential of chrysophanol in protecting against high fat-induced cardiac injury through Nrf2-regulated anti-inflammation, anti-oxidant and anti-fibrosis in Nrf2 knockout mice
Lian, Y., Xia, X.-J., Zhao, H., & Zhu, Y. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2017.05.148 · Cited by 62 · see citing works
Peroxisome Proliferators Reduce Spatial Memory Impairment, Synaptic Failure, and Neurodegeneration in Brains of a Double Transgenic Mice Model of Alzheimer's Disease
Inestrosa, N. C., Carvajal, F. J., Zolezzi, J. M., Tapia‐Rojas, C., Serrano, F. G., Karmelic, D., Toledo, E. M., Toro, A., Toro, J., & Santos, M. J. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-120397 · Cited by 62 · see citing works
Molecular and biological functions of resveratrol in psychiatric disorders: a review of recent evidence
Shayganfard, M. (2020) · Cell & Bioscience · doi:10.1186/s13578-020-00491-3 · Cited by 61 · see citing works
Synthesis, antioxidant, and antimicrobial evaluation of some 2-arylbenzimidazole derivatives
Zhou, B., Li, B., Yi, W., Bu, X., & Ma, L. (2013) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2013.05.004 · Cited by 60 · see citing works

Delineation of Neuroprotective Effects and Possible Benefits of AntioxidantsTherapy for the Treatment of Alzheimer's Diseases by Targeting Mitochondrial-Derived Reactive Oxygen Species: Bench to Bedside
Walia, V., Kaushik, D., Mittal, V., Kumar, K., Verma, R., Parashar, J., Akter, R., Rahman, M. H., Bhatia, S., Al-Harrasi, A., et al. (2022) · Molecular Neurobiology · doi:10.1007/s12035-021-02617-1 · Cited by 47 · see citing works
The immunopathogenic role of reactive oxygen species in Alzheimer disease.
Mohsenzadegan, M., & Mirshafiey, A. (2012) · PubMed · Cited by 71 · see citing works
Causes of oxidative stress in Alzheimer disease
Zhu, X., Su, B., Wang, X., Smith, M. A., & Perry, G. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7218-4 · Cited by 336 · see citing works
Interplay of antioxidants in Alzheimer’s disease
Sajjad, N., Wani, A., Hassan, S., Ali, R., Hamid, R., Akbar, S., Ganai, B., & Bhat, E. A. (2019) · Journal of Translational Science · doi:10.15761/jts.1000313 · Cited by 10 · see citing works
Neuroprotective Therapies for Alzheimers Disease
Huber, A., Stuchbury, G., Bürkle, A., Burnell, J. N., & Münch, G. W. (2006) · Current Pharmaceutical Design · doi:10.2174/138161206775474251 · Cited by 39 · see citing works

Authors: Dumont, M., & Beal, M. F.
Affiliations: Weill Cornell Medicine (US)
Corresponding author: Dumont, Magali
ORCID: Dumont, Magali
Beal, M. Flint
Venue: Free Radical Biology and Medicine
Publisher: Elsevier BV
Published: 2011-09
Volume: 51
Issue: 5
Pages: 1014-1026
ISSN: 0891-5849 (ISSN-L)
DOI: 10.1016/j.freeradbiomed.2010.11.026
PMC: PMC3070183
OpenAlex: W2080084871
Cited by: 402
References: 188
Citations by year: 2026: 12 · 2025: 19 · 2024: 21 · 2023: 20 · 2022: 21 · 2021: 22 · 2020: 26 · 2019: 28 · 2018: 19 · 2017: 36 · 2016: 28 · 2015: 29 · 2014: 36 · 2013: 34 · 2012: 34
FWCI: 2.76
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Free Radical Biology and Medicine (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health
National Institute on Aging (R01AG20729, R01AG020729, P01AG014930, P01-AG14930)
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Life Sciences › Neuroscience › Neurology › Neurological Disorders and Treatments
Keywords: Alzheimer's disease, reactive oxygen species, oxidative stress, neuroprotection, mitochondria, microglia, neuroinflammation, amyloid-beta clearance, antioxidant defense, transcriptional regulation, neurodegeneration, cognitive decline
MeSH terms: Alzheimer Disease, Animals, Antioxidants, Clinical Trials as Topic, Disease Models, Animal, Humans, Inflammation, Mitochondria, Oxidation-Reduction, Reactive Oxygen Species, Microglia, Oxidative Stress, Disease Progression, Neuroprotective Agents, Molecular Targeted Therapy

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

Neuroprotective strategies involving ROS in Alzheimer disease

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks