The DOI matches its Crossref record; 138 of the 140 references it cites were found in a registry or an index.
Oxidative Stress and the Pathogenesis of Alzheimer's Disease
Open accessAbstract
Alzheimer's disease (AD) is the most common neurodegenerative disease that causes dementia in the elderly. Patients with AD suffer a gradual deterioration of memory and other cognitive functions, which eventually leads to a complete incapacity and death. A complicated array of molecular events has been implicated in the pathogenesis of AD. The major pathological characteristics of AD brains are the presence of senile plaques, neurofibrillary tangles, and neuronal loss. Growing evidence has demonstrated that oxidative stress is an important factor contributing to the initiation and progression of AD. However, the mechanisms that lead to the disruption of redox balance and the sources of free radicals remain elusive. The excessive reactive oxygen species may be generated from mechanisms such as mitochondria dysfunction and/or aberrant accumulation of transition metals, while the abnormal accumulation of Abeta and tau proteins appears to promote the redox imbalance. The resulted oxidative stress has been implicated in Abeta- or tau-induced neurotoxicity. In addition, evidence has suggested that oxidative stress may augment the production and aggregation of Abeta and facilitate the phosphorylation and polymerization of tau, thus forming a vicious cycle that promotes the initiation and progression of AD.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“In the context of Aβ production, multiple investigations have revealed that oxidative stress leads to the formation of SPs by lowering α-secretase activity while increasing both βand γ-secretase activities [52].”
From Unlocking the Therapeutic Potential of Medicinal Plants for Alzheimer’s Disease: Preclinical to Clinical Trial Insights (2023) · cites this paper as [52]
In the citing paper
“However, when the hyperphosphorylated Tau protein is overexpressed (which is a pathophysiological indicator of AD) a depletion of these organelles has been evidenced, suggesting it is the cause of H2O2 and ROS increase [72,108,126].”
From Multi-Target Mechanisms of Phytochemicals in Alzheimer’s Disease: Effects on Oxidative Stress, Neuroinflammation and Protein Aggregation (2022) · cites this paper as [126]
In the citing paper
“Hydrogen peroxide seems to be the relevant actor in promoting excessive oxidation in neuronal cells.”
From Multi-Target Mechanisms of Phytochemicals in Alzheimer’s Disease: Effects on Oxidative Stress, Neuroinflammation and Protein Aggregation (2022) · cites this paper as [126]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Global prevalence of dementia: a Delphi consensus study
Ferri, C. P., Prince, M. J., Brayne, C., Brodaty, H., Fratiglioni, L., Ganguli, M., Hall, K. S., Hasegawa, K., Hendrie, H. C., Huang, Y., et al. (2005) · The Lancet · doi:10.1016/s0140-6736(05)67889-0 · Cited by 5,336
Querfurth, H. W., & LaFerla, F. M. (2010) · New England Journal of Medicine · doi:10.1056/nejmra0909142 · Cited by 4,569
Correlative Memory Deficits, Aβ Elevation, and Amyloid Plaques in Transgenic Mice
Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F., & Cole, G. (1996) · Science · doi:10.1126/science.274.5284.99 · Cited by 4,210
Synapse Loss and Microglial Activation Precede Tangles in a P301S Tauopathy Mouse Model
Yoshiyama, Y., Higuchi, M., Zhang, B., Huang, S.-M., Iwata, N., Saido, T. C., Maeda, J., Suhara, T., Trojanowski, J. Q., & Lee, V. M.-Y. (2007) · Neuron · doi:10.1016/j.neuron.2007.01.010 · Cited by 2,208
A Century of Alzheimer's Disease
Goedert, M., & Spillantini, M. G. (2006) · Science · doi:10.1126/science.1132814 · Cited by 2,150
Copper, iron and zinc in Alzheimer's disease senile plaques
Lovell, M. A., Robertson, J. D., Teesdale, W. J., Campbell, J. L., & Markesbery, W. R. (1998) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(98)00092-6 · Cited by 2,120
Hydrogen peroxide mediates amyloid β protein toxicity
Behl, C. (1994) · Cell · doi:10.1016/0092-8674(94)90131-7 · Cited by 2,074
Aβ Oligomers – a decade of discovery
Walsh, D. M., & Selkoe, D. J. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04426.x · Cited by 1,938
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
Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP
Lewis, J., Dickson, D. W., Lin, W.-L., Chisholm, L., Corral, A., Jones, G., Yen, S.-H., Sahara, N., Skipper, L., Yager, D., et al. (2001) · Science · doi:10.1126/science.1058189 · Cited by 1,611
Flagged first, then by citations
2 of the 140 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 801–863 of 863
Lee, J. M., Choi, Y. J., Sung, D.-E., Sim, T. H., Kim, S., Yeo, S. G., & Kim, Y. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1632640
Metabolic disorder and its underlying redox biomarkers
Duttaroy, A. K., & Jena, A. B. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-43884-4.00001-5
Gluščević, S. V. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-27333-9.00009-9
Epidemiological studies on heavy metal exposure and neurodegeneration
Choudhury, D. R., & Kumar, P. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-36575-1.00001-7
Yang, X., Hu, D., Zhao, S., Wan, J., Chen, L., Bao, Q., Zhang, Y., Wang, Q., & Huang, Z. (2025) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2025.110107
Franco, F. N., Cardoso, L. D. C., Silva, B. N. M., de Araújo, G. R., & Chaves, M. M. (2025) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2025.102291
Antioxidants as immunomodulators for Tau and Amyloid-β in Alzheimer’s disease
Chinnathambi, S., Rangappa, N., & Chandrashekar, M. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.10.007
Özbay, A., & Oruç‐Emre, E. E. (2025) · International Journal of Chemistry and Technology · doi:10.32571/ijct.1772368
The Role of Nuts in Alzheimer’s Prevention and Management
Göğer, G., & Saltan, N. (2025) · Nutritional neurosciences · doi:10.1007/978-981-95-2736-6_9
Kuppusamy, K., & Elango, H. (2025) · Journal of Natural Remedies · doi:10.18311/jnr/2025/50960
Development and Characterization of Low Caloric Papaya (Carica papaya L.) drink
Javed, M. S., Amjad, A., Riaz, M., Shah, F.-U.-H., Aurangzaib, M., Khan, A. A., Amir, M., Jawad, M., & Saad, A. (2020) · International Journal of Biosciences (IJB) · doi:10.12692/ijb/17.6.408-420
Lin, G.-B., Liu, H.-H., Kuo, Y.-Y., Chen, Y.-M., Hsu, F.-T., Wang, Y.-W., Kung, Y., Ching, C., & Chao, C. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.10.693347
Zhang, X., Ma, C., Sun, L., He, Z., Feng, Y., Li, X., Gan, J., & Chen, X. (2021) · Figshare · doi:10.6084/m9.figshare.14344481
Aldayel, T. S., Gad El Hak, H. N., Nafie, M. S., Saad, R., Abdelrazek, H. M. A., & Kilany, O. E. (2023) · Figshare · doi:10.6084/m9.figshare.24819458
Biosimilars: Antibody and nanobody-based therapeutic approaches towards protein misfolding diseases
Chinnathambi, S., & Rangappa, N. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.10.014
Exploring the Role of Antioxidant Compounds in Brain Health
Sonkar, A., & Sonkar, P. (2026) · Springer eBooks · doi:10.1007/978-981-95-4169-0_6
Isoform-specific roles and overlooked complexity of AMPKα in Alzheimer's disease
Zimmermann, H. R., Jester, H. M., Vassar, R. J., & Ma, T. (2026) · Brain medicine : · doi:10.61373/bm026y.0003
Twiss, E., McPherson, C., & Weaver, D. F. (2026) · Current Alzheimer Research · doi:10.2174/0115672050414496251124094000
Matanaq, H. R., Mohammadzadeh, A., Sheykhsaran, E., Abbasi, A., Jafari-Sales, A., Rasizadeh, R., & Baghi, H. B. (2026) · Future Virology · doi:10.1080/17460794.2026.2635310 · Cited by 1
Clitoria ternatea as a potential candidate in treating Alzheimer’s disease
Chin, J. Y., Sucedaram, Y., Hassan, Z., & Kumaran, K. R. (2026) · Pharmacological Research - Natural Products · doi:10.1016/j.prenap.2026.100602
Singh, L. K., Singh, S. P., & Sharma, P. (2026) · Journal of Biomaterials Science Polymer Edition · doi:10.1080/09205063.2026.2644503
Lefèvre‐Arbogast, S. (2019) · theses.fr (ABES) · doi:10.70675/6915e632z663fz4caaz9c7az455ad25755da
Re-Purposing a Rho-Associated Coiled-Coil Kinase (ROCK) Inhibitor for Alzheimer’s Disease
Cambi, X., Liu, Z., Guo, K., & Xia, W. (2026) · Journal of Clinical Medicine · doi:10.3390/jcm15093379
Ansari, S., Khali, A., Joshi, B. C., & Uniyal, S. (2026) · Physiological Mini Reviews · doi:10.2174/0116695410415209251114033740
Ozberk, U., Lay, İ., Yılmaz, A., Şendur, S. N., & Gürlek, Ö. A. (2026) · Cureus · doi:10.7759/cureus.109915
Wan, X., Lu, W., Liu, S., Zhao, Y., Hu, J., Ding, X., Gu, P., Zou, Y., Jiang, B., & Yang, Y. (2026) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2026.05.341
Self-citationKatti, V. B., Kolusu, A. S., Madhana, R. M., Pindiprolu, S. K. S. S., Thummala, U., & Samudrala, P. K. (2026) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.5c01768
Recent advances (2021–2023) in indole heterocycles, docking studies based anti-Alzheimer's agents
Lamie, P. F., Abdelgawad, M. A., & Philoppes, J. N. (2026) · Chemical Papers · doi:10.1007/s11696-026-05112-w
Napolitano, L. (2026) · Firenze University Press eBooks · doi:10.36253/979-12-215-0993-9.05
Napolitano, L. (2026) · Firenze University Press eBooks · doi:10.36253/979-12-215-0993-9.references
Napolitano, L. (2026) · Firenze University Press eBooks · doi:10.36253/979-12-215-0993-9.07
Third Section: Design of a dimeric-nanobody specific for Aβ42 oligomers: the Dimeric-DesAb-O
Napolitano, L. (2026) · Firenze University Press eBooks · doi:10.36253/979-12-215-0993-9.06
Napolitano, L. (2026) · Firenze University Press eBooks · doi:10.36253/979-12-215-0993-9
Napolitano, L. (2026) · Firenze University Press eBooks · doi:10.36253/979-12-215-0993-9.03
Napolitano, L. (2026) · Firenze University Press eBooks · doi:10.36253/979-12-215-0993-9.04
Napolitano, L. (2026) · Firenze University Press eBooks · doi:10.36253/979-12-215-0993-9.02
Conclusion and Future Perspectives
Napolitano, L. (2026) · Firenze University Press eBooks · doi:10.36253/979-12-215-0993-9.08
Günal, Ş. E., Tunçel, Ş. T., Demir, İ., Baysal, İ., Telli, G., Erdem, S. S., Uçar, G., Hanzlova, M., Musílek, K., Doğan, İ., et al. (2026) · Drug Development Research · doi:10.1002/ddr.70341
Pathophysiological Insights and Therapeutic Approaches of Oxidative Stress in Alzheimer’s Disease
Karati, D., Garai, T., Sen, S., Mukherjee, S., Jha, S. K., & Debnath, B. (2026) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9798898815646126010008
Multitargeted drug strategies for Alzheimer’s and Parkinson’s diseases
Khan, A. U., Abdullah, A., Naqvi, S. F., Tahir, H., Khalid, H., Sarfraz, H., & Khan, Y. (2026) · Zeitschrift für Naturforschung C · doi:10.1515/znc-2026-0116
Andrographolide: Mechanisms and Therapeutic Potential in Alzheimer’s and Parkinson’s Disease
Ríos-Gallardo, A. P., Herrera-Ramírez, D., Candia, S. B., & Inestrosa, N. C. (2026) · Molecules · doi:10.3390/molecules31183139
Han, S., Liu, F., Wang, D., & Song, G. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1933588
Dashti, N., Ashrafzadeh, Z., Sadeghi, G., Solhirad, M., & Karimi‐Zandi, L. (2026) · Behavioural Brain Research · doi:10.1016/j.bbr.2026.116476
Shukla, S., Tiwari, C., Sharma, S., Vasudeva, N., Khatri, R., Dar, M. O., Hooda, T., & Lather, A. (2026) · Inflammopharmacology · doi:10.1007/s10787-026-02403-2
Perina, M. L., Calcagno, D., Sbardella, D., Deodato, D., Distefano, A., Tuccitto, N., Oliveri, V., Schlotter, F., Faller, P., & Grasso, G. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.154678
Cavalluzzi, M. M., Terlizzi, F., Catalano, A. A., Pannunzio, A., Rotondo, N. P., Habtemariam, S., & Lentini, G. (2026) · Molecules · doi:10.3390/molecules31203728
Zainuddin, M.-S., Wei, A. C., Bhuvanendran, S., & Azman, A. S. (2026) · Beni-Suef University Journal of Basic and Applied Sciences · doi:10.1186/s43088-026-00842-y
Krause, C. A., Woods, S. P., Litson, K., Ledoux, T. A., & Medina, L. D. (2026) · Journal of Nutrition · doi:10.1016/j.tjnut.2026.101904
Metadata
- Authors
- Zhao, Y., & Zhao, B.
- Affiliations
- Harbin Institute of Technology (CN)
- Chinese Academy of Sciences (CN)
- Corresponding author
- Zhao, Yan
- Zhao, Baolu
- ORCID
- Zhao, Yan
- Venue
- Oxidative Medicine and Cellular Longevity
- Publisher
- Wiley
- Published
- 2013
- Volume
- 2013
- Pages
- 1-10
- ISSN
- 1942-0994 (ISSN-L)
- 1942-0900
- PMC
- PMC3745981
- OpenAlex
- W2141262291
- Cited by
- 855
- References
- 140
- Citations by year
- 2026: 47 · 2025: 61 · 2024: 82 · 2023: 78 · 2022: 80 · 2021: 83 · 2020: 76 · 2019: 71 · 2018: 64 · 2017: 64 · 2016: 53 · 2015: 54 · 2014: 36 · 2013: 5
- FWCI
- 5.44
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Oxidative Medicine and Cellular Longevity (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Natural Science Foundation of China (30930036, 31201338, 30870587, 2009-3-93, 2011DXGJ14, Y200902, 2009147, 2006CB500706)
- Weihai Science and Technology Development Program (30930036, 31201338, 30870587, 2009-3-93, 2011DXGJ14, Y200902, 2009147, 2006CB500706)
- Harbin Institute of Technology (30930036, 31201338, 30870587, 2009-3-93, 2011DXGJ14, Y200902, 2009147, 2006CB500706)
- National Basic Research Program of China (30930036, 31201338, 30870587, 2009-3-93, 2011DXGJ14, Y200902, 2009147, 2006CB500706)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- Alzheimer's disease, oxidative stress, redox imbalance, reactive oxygen species, free radicals, mitochondrial dysfunction, amyloid-beta, tau protein, neurofibrillary tangles, amyloid plaques, neurotoxicity, neurodegeneration, dementia
- MeSH terms
- Alzheimer Disease, Humans, Reactive Oxygen Species, Oxidative Stress
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
