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 2,153
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 601–700 of 863
Mitochondria and Alzheimer’s Disease: An Electron Microscopy Study
Balogiannis, S. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.84881 · Cited by 9
Yang, I., Kuan, C., Zhang, S., Chen, Z., Li, C.-H., Liang, Y., Kuo, W., Chang, C., Lin, J., Hsieh, H., et al. (2024) · European Polymer Journal · doi:10.1016/j.eurpolymj.2024.113151 · Cited by 7
Moreira, P., Macedo, J., Matos, P., Bicker, J., Fortuna, A. C., Figueirinha, A., Salgueiro, L., Batista, M. T., da Silva, A. P., Silva, S., et al. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.117652 · Cited by 7
Chen, X., Zhou, X., Lan, C., Fu, H.-J., Li, Z.-C., Chen, M.-Y., Wen, Y.-P., Yu, L., Qin, D., Wu, J., et al. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05242-4 · Cited by 7
Yang, A., Yi, X., Zhang, H., Shen, R., & Kou, X. (2024) · Chemical Biology & Drug Design · doi:10.1111/cbdd.14529 · Cited by 7
Mengr, A., Šmotková, Z., Pačesová, A., Železná, B., Kuneš, J., & Maletı́nská, L. (2025) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-025-10174-w · Cited by 7
Role of Oxidized Gly25, Gly29, and Gly33 Residues on the Interactions of Aβ1–42 with Lipid Membranes
Fatafta, H., Poojari, C., Sayyed–Ahmad, A., Strodel, B., & Owen, M. C. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00558 · Cited by 8
Borah, S., Sarkar, P., & Sharma, H. K. (2021) · 3 Biotech · doi:10.1007/s13205-021-02793-w · Cited by 7
Effects of Oxygen Tension for Membrane Lipidome Remodeling of Cockayne Syndrome Cell Models
Ferreri, C., Sansone, A., Krokidis, M. G., Masi, A., Pascucci, B., D’Errico, M., & Chatgilialoglu, C. (2022) · Cells · doi:10.3390/cells11081286 · Cited by 8
Demirel, G., Sanajou, S., Yirün, A., Çakır, D. A., Balcı, A., Berkkan, A., Baydar, T., & Erkekoğlu, P. (2024) · Toxicology Research · doi:10.1093/toxres/tfae097 · Cited by 7
Redox-sensitive GFP to monitor oxidative stress in neurodegenerative diseases
Esposito, S., Masala, A., Sanna, S., Rassu, M., Pimxayvong, V., Iaccarino, C., & Crosio, C. (2016) · Reviews in the Neurosciences · doi:10.1515/revneuro-2016-0041 · Cited by 7
Hong, Z., Feng, Y., Ding, H., Hu, X., Lu, J., Ge, X., Ge, Y., & Yao, B. (2017) · The Journal of Sexual Medicine · doi:10.1016/j.jsxm.2016.11.002 · Cited by 7
Pak, M. E., Oh, Y.-C., Park, Y. J., Kim, J. K., Shin, M., Yoon, J. H., & Go, Y. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/6970578 · Cited by 7
Amyloid Beta (Aβ) and Oxidative Stress: Progression of Alzheimer’s Disease
Haque, R. (2018) · Advances in Biotechnology & Microbiology · doi:10.19080/aibm.2018.11.555802 · Cited by 7
Remifentanil induces autophagy and prevents hydrogen peroxide-induced apoptosis in Cos-7 cells
Yoon, J.-Y., Baek, C.-W., Woo, M.-N., Kim, E.-J., Yoon, J.-U., & Park, C.-H. (2016) · Journal of Dental Anesthesia and Pain Medicine · doi:10.17245/jdapm.2016.16.3.175 · Cited by 7
Zhang, G., Pare, R. B., Chin, K. L., & Qian, Y. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.120178 · Cited by 7
RetractedSaporito-Magriñá, C., Lairion, F., Musacco-Sebio, R., Fuda, J., Torti, H., & Repetto, M. G. (2022) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-022-01960-5 · Cited by 6
Sun, Y., Xia, Q., Du, L., Gan, Y., Ren, X., Liu, G., Wang, Y., Yan, S., Li, S., Zhang, X., et al. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116754 · Cited by 6
Crosstalk between copper, Alzheimer’s disease, and melatonin
Deepika, Thakur, A., Panghal, A., Pundir, R., Singh, C., Goyal, M., Namdeo, A. G., & Kumar, J. (2025) · BioMetals · doi:10.1007/s10534-025-00712-7 · Cited by 6
Thakur, A., Singh, R., Mehta, V., & Paliwal, D. (2025) · ChemistrySelect · doi:10.1002/slct.202500130 · Cited by 6
Aerobic Fitness and Cognition Changes After Exercise Training in Alzheimer's Disease
Salisbury, D. L., & Yu, F. (2017) · Journal of Clinical Exercise Physiology · doi:10.31189/2165-6193-6.2.22 · Cited by 6
Choi, H.-I., Kim, K., Lee, J., Chang, Y., Rhee, H. Y., Park, S., Lee, W.-I., Choe, W., Ryu, C., & Jahng, G. (2021) · Diagnostics · doi:10.3390/diagnostics11050740 · Cited by 6
Mitochondrial response to environmental toxicants
Salimi, A., & Jamali, Z. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822416-8.00003-8 · Cited by 6
Althobaiti, N. A., Menaa, F., Albalawi, A. E., Dalzell, J. J., Warnock, N. D., Mccammick, E. M., Alsolais, A., Alkhaibari, A. M., & Green, B. D. (2021) · Cells · doi:10.3390/cells10092481 · Cited by 7
Ion Channels and Neurodegenerative Disease Aging Related
Cordaro, M., Cuzzocrea, S., & Paola, R. D. (2022) · Biochemistry · doi:10.5772/intechopen.103074 · Cited by 6
Microglia as a Possible Alternative Therapeutic for Dementia
Alavez-Rubio, J. S., & Juárez‐Cedillo, T. (2024) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-230112 · Cited by 6
Sharma, S., Sharma, S., & Vig, A. P. (2016) · Physiology and Molecular Biology of Plants · doi:10.1007/s12298-016-0346-2 · Cited by 6
Pathways Driving Neuroprogression in Depression: The Role of Immune Activation
Oriolo, G., Grande, I., Martín‐Santos, R., Vieta, E., & Carvalho, A. F. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-811073-7.00010-6 · Cited by 6
ALTERED SERUM MARKER OF THYROID PROFILE AND ANTIOXIDANT ENZYMES IN INDIVIDUALS ALZHEIMER'S DISEASE
Sarhat, E. R. (2019) · International Research Journal of Pharmacy · doi:10.7897/2230-8407.100110 · Cited by 6
Nutraceuticals for Cognitive Dysfunction
Gupta, R. C., Doss, R. B., Srivastava, A., Lall, R., & Sinha, A. (2019) · Springer eBooks · doi:10.1007/978-3-030-04624-8_26 · Cited by 6
Xu, M. Q., Zhang, L., Li, P., Wang, C., & Shi, Y. (2020) · Journal of Traditional Chinese Medical Sciences · doi:10.1016/j.jtcms.2020.04.002 · Cited by 7
A Systematic Review of Updated Mechanistic Insights Towards Alzheimer’s Disease
Mittal, A., Sharma, R., Sardana, S., Goyal, P. K., Piplani, M., & Pandey, A. (2022) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527321666220510144127 · Cited by 6
Savale, S. A., Pol, C. S., Khare, R., Verma, N., Gaikwad, S. B., Mandal, B., & Behera, B. C. (2015) · Pharmaceutical Biology · doi:10.3109/13880209.2015.1072567 · Cited by 6
CONVOLVULUS PLURICAULIS AS A COGNITION BOOSTER: RELEVANCE TO ALZHEIMER’S DISEASE
Bihaqi, S. W., Alkhamaiseh, S. I., & Tiwari, M. (2016) · International Journal of Pharmaceutical Sciences and Drug Research · doi:10.25004/ijpsdr.2016.080201 · Cited by 6
A proteomics study of hyperhomocysteinemia injury of the hippocampal neurons using iTRAQ
Fang, M., Wang, J., Han, Y., ZHAO, Y.-X., & LIU, X.-Y. (2014) · Molecular Medicine Reports · doi:10.3892/mmr.2014.2557 · Cited by 6
Self-citationBagheri, S., Rashno, M., Salehi, I., Karimi, S. A., Raoufi, S., & Komaki, A. (2024) · Journal of Alzheimer s Disease · doi:10.1177/13872877241290695 · Cited by 5
The silent invaders: Biofilms in neurological, cardiovascular, and metabolic diseases
Kumar, V., & Tyagi, A. (2025) · Life Sciences · doi:10.1016/j.lfs.2025.123886 · Cited by 5
Bailo, P. S., Martín, E. L., Calmarza, P., Breva, S. M., Gómez, A. B., Giráldez, A. P., Callau, J. J. S.-P., Santamaría, J. M. V., Dayaldasani, A., Micó, C. C., et al. (2022) · Advances in Laboratory Medicine / Avances en Medicina de Laboratorio · doi:10.1515/almed-2022-0022 · Cited by 5
Meng, X., Liu, H., Zhao, N., Yang, Y., Zhao, K., & Dai, Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241310926 · Cited by 5
Singh, M., Guru, A., Murugan, R., Gopi, M., & Arockiaraj, J. (2023) · Molecular Biology Reports · doi:10.1007/s11033-023-08729-2 · Cited by 5
Nassrallah, W. B., Li, H. R., Irani, L., Wijesinghe, P., Hogg, P. W., Hui, L., Oh, J., Mackenzie, I. R., Hirsch‐Reinshagen, V., Hsiung, G. R., et al. (2024) · Acta Neuropathologica Communications · doi:10.1186/s40478-024-01898-6 · Cited by 9
Bourdakou, M. M., Loizidou, E. M., & Spyrou, G. M. (2025) · Antioxidants · doi:10.3390/antiox14080952 · Cited by 5
Ahmed, S. A., Nasry, M., & Mohammed, W. (2022) · Records of Pharmaceutical and Biomedical Sciences/Records of Pharmaceutical & Biomedical Sciences · doi:10.21608/rpbs.2022.129511.1132 · Cited by 5
Zhang, G.-H., Chin, K.-L., Yan, S.-Y., & Pare, R. (2023) · PLoS ONE · doi:10.1371/journal.pone.0287817 · Cited by 8
Haider, R., Agnello, L., Shah, S. M., Sufyan, M., Khan, N., Nazir, A., Ciaccio, M., & Rehman, S. (2025) · Journal of Food Science · doi:10.1111/1750-3841.17619 · Cited by 5
Zadehvakili, B., McNeill, S. M., Fawcett, J. P., & Giles, G. I. (2016) · Biochemical Pharmacology · doi:10.1016/j.bcp.2016.01.012 · Cited by 5
Oxidative Stress, Inflammation, and Formation of Beta‐ Amyloid 1‐42 in Brain
Rivas-Arancibia, S., Rodrı́guez-Martı́nez, E., Méndez-García, A., Moctezuma-Salgado, M., Jiménez-Espíndola, P., & López-González, U. (2016) · InTech eBooks · doi:10.5772/64709 · Cited by 5
The Effects of Amyloid-β on Metabolomic Profiles of Cardiomyocytes and Coronary Endothelial Cells
Jang, S., Chorna, N., Rodríguez‐Graciani, K. M., Inyushin, M. Y., Fossati, S., & Javadov, S. A. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-221199 · Cited by 5
Fusigen Reduces Intracellular Reactive Oxygen Species and Nitric Oxide Levels
Kitiyanant, V., Lotrakul, P., Kanchanabanca, C., Padungros, P., Punnapayak, H., Prasongsuk, S., & Pithi Chanvorachote, B. (2019) · In Vivo · doi:10.21873/invivo.11490 · Cited by 5
NEUROPROTECTIVE ACTIVITY OF NOVEL CUR-CA-THIONE AND ITS OXIDATIVE STRESS STUDY
Shelat, D. Y., & Acharya, S. R. (2016) · International Journal of Pharmacy and Pharmaceutical Sciences · doi:10.22159/ijpps.2016v8i12.15141 · Cited by 5
Murumulla, L., Bandaru, L. J. M., Ajumeera, R., Dhayal, V. S., & Challa, S. (2025) · Journal of Applied Toxicology · doi:10.1002/jat.4839 · Cited by 5
A Review on the Pathophysiology of Alzheimer’s Disease
Agarwal, U., Kapoor, G. T., & Tonk, R. K. (2025) · Current Protein and Peptide Science · doi:10.2174/0113892037416859250915091846 · Cited by 5
Mishra, J., Singh, C., & Bhatti, J. S. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05297-3 · Cited by 4
Pareja-Navarro, K. A., King, C. D., Kauwe, G., Ngwala, Y. Y., Lokitiyakul, D., Wong, I., Vira, A., Liu, Y., Chen, J. H., Sharma, M., et al. (2026) · Molecular Neurodegeneration · doi:10.1186/s13024-026-00928-2 · Cited by 6
Huang, S., Nunez, J., Toresco, D. L., Wen, C., Slotabec, L. A., Wang, H., Zhang, H., Rouhi, N., Adenawoola, M. I., & Li, J. (2025) · The FASEB Journal · doi:10.1096/fj.202402725rr · Cited by 4
Lee, S., Sohal, I. S., Therrien, M., Pal, A. K., Bello, D., & Shea, T. B. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-150099 · Cited by 4
Živković, L., Bajić, V., Pirković, A., Dekanski, D., Forbes-Hernández, T. Y., Zlatković‐Švenda, M., Perry, G. L., & Spremo‐Potparević, B. (2021) · Journal of Food Biochemistry · doi:10.1111/jfbc.13637 · Cited by 4
He, S., Lv, X., He, X., Guo, J., Pan, R., Jin, Y., Tian, Z., Pan, L., & Zhang, S. (2023) · Human Gene Therapy · doi:10.1089/hum.2021.222 · Cited by 4
A Copper-Selective Sensor and Its Inhibition of Copper-Amyloid Beta Aggregation
Nguyen, N. K., Poduska, B., Franks, M., Bera, M., MacCormack, I., Lin, G., Petroff, A. P., Das, S., & Nag, A. (2024) · Biosensors · doi:10.3390/bios14050247 · Cited by 4
Liu, Y., Chen, Y., & Fukui, K. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25158428 · Cited by 5
Yutani, R., Venketaraman, V., & Sheren, N. (2024) · Antioxidants · doi:10.3390/antiox13091106 · Cited by 5
Chu, Z., Chen, Y., Xie, D., Song, C., Lin, Y., Qin, T., Zhai, Z., Cao, Z., Xu, Y., & Sun, T. (2025) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2025.119879 · Cited by 5
Kim, M. H., Kim, D. Y., Lee, H. J., Park, Y., Huh, J., & Lee, D. (2021) · Redox Report · doi:10.1080/13510002.2021.1901028 · Cited by 4
Gupta, L., Sood, P. K., Nehru, B., & Sharma, S. (2022) · Biological Trace Element Research · doi:10.1007/s12011-022-03366-5 · Cited by 4
The role of oxidative stress in the development of Alzheimer's disease
Nikolenko, V. N., Rizaeva, N. A., Bulygin, K. V., Anokhina, V. M., & Bolotskaya, A. A. (2022) · Neurology neuropsychiatry Psychosomatics · doi:10.14412/2074-2711-2022-4-68-74 · Cited by 6
Rahman, M. M., Islam, M. R., Tumpa, M. A. A., Shohag, S., shuvo, S. K., Ferdous, J., Kajol, S. A., Aljohani, A. S. M., Abdulmonem, W. A., Rauf, A., et al. (2023) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2023.110375 · Cited by 4
Kang, M. H., Han, Y. M., Lee, Y. J., Ji, Y., Seong, H., & Kim, H. D. (2023) · Horticultural Science and Technology · doi:10.7235/hort.20230037 · Cited by 4
Combinatorial therapy in Alzheimer's disease
Giri, M. A., Kendre, P. N., Bhalke, R. D., Pande, V. V., Autade, K. A., & Sumbe, R. B. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-13205-6.00026-1 · Cited by 4
San-Millán, I., Martinez, J. L., Sparagna, G. C., D’Alessandro, A., Stefanoni, D., Nemkov, T. G., & Hill, J. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.08.19.608601 · Cited by 4
How vanadium and manganese compounds impact cardiac mitochondrial function
Dolan, C. C., Whitcomb, L. A., Carpio, E. D., Rose, L., Chicco, A. J., & Crans, D. C. (2025) · Frontiers in Chemical Biology · doi:10.3389/fchbi.2025.1602602 · Cited by 3
NLRP3 Inflammasome Activation in Oxidative Stress: A Key Mechanism Driving Neuroinflammation
Ramirez-Celis, C., Martínez-Torres, A. M., & Morán, J. (2026) · NeuroImmunoModulation · doi:10.1159/000551943 · Cited by 3
Nowe strategie terapeutyczne choroby Alzheimera
Nowak, D., Słupski, W., & Rutkowska, M. (2021) · Postępy Higieny i Medycyny Doświadczalnej · doi:10.5604/01.3001.0014.9532 · Cited by 5
Immune Mechanisms in Alzheimer’s Disease: The Role of Toll-Like Receptors Signalling
Sharma, D., Manjunatha, P. M., Babu, T. H., Dhungel, A., Swaraj, S., Janadari, S., Sharma, U., Surendra, V., Taj, N., & Gayathri, S. V. (2024) · Current Pharmacology Reports · doi:10.1007/s40495-024-00376-w · Cited by 3
Soni, A., Kumar, A., & Kumar, V. (2024) · Russian Journal of Bioorganic Chemistry · doi:10.1134/s1068162024050212 · Cited by 3
Mishra, A. K., Srivastava, A., Raj, V., Saini, V., Khan, G., Singh, H., Mishra, A., & Paliwal, S. (2024) · Current Alzheimer Research · doi:10.2174/0115672050361294241211071813 · Cited by 3
Reevaluating Alzheimer’s disease treatment: Can phytochemicals bridge the therapeutic Gap?
Roy, K. K., Mehta, D. K., & Das, R. (2025) · Neuroscience · doi:10.1016/j.neuroscience.2025.04.014 · Cited by 3
Karakaya, A., Çevik, U. A., Kaya, B., Çi̇ftci̇, B., Necip, A., Işık, M., Beydemir, Ş., Özkay, Y., & Kaplancıklı, Z. A. (2025) · ChemistryOpen · doi:10.1002/open.202500305 · Cited by 3
Neurodegenerative Diseases and the Aging Brain
Godin, S. K., Seo, J., & Tsai, L. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-811304-2.00017-1 · Cited by 3
The Involvement of Melatonin and Tasimelteon against Alzheimer’s Disease
Ravikumar, M., Mohan, S., & Velpandian, C. (2022) · Current Drug Safety · doi:10.2174/1574886317666220517125644 · Cited by 4
Redhwan, M. A. M., Samaddar, S., Hariprasad, M. G., Hard, S. A. A. A., Deka, G., & Godfrey, A. (2023) · Pharmacognosy Research · doi:10.5530/pres.15.3.057 · Cited by 3
Bustos-Rangel, A., Muñoz-Cabrera, J., Suárez, L. E. C., Arboleda, G., Murillo, M. C. Á., & Sandoval-Hernández, A. G. (2023) · Frontiers in Natural Products · doi:10.3389/fntpr.2023.1169182 · Cited by 3
Effect of donepezil hydrochloride on the transgenic Drosophila expressing human Aβ-42
Siddique, Y. H., Naz, F., Rahul, Varshney, H., Idrisi, M., & Shahid, M. (2023) · International Journal of Neuroscience · doi:10.1080/00207454.2023.2262109 · Cited by 4
Zhou, X., Almoallim, H. S. M., Ravindran, B., & Qin, R. (2023) · Indian Journal of Pharmaceutical Education and Research · doi:10.5530/ijper.57.4.127 · Cited by 3
Pannangrong, W., Nillert, N., Boonyarat, C., Welbat, J. U., Yannasithinon, S., & Choowong-In, P. (2024) · BMC Complementary Medicine and Therapies · doi:10.1186/s12906-024-04662-4 · Cited by 3
Two Lycopodium alkaloids from the aerial parts of Huperzia phlegmaria
Tung, B., Thu, D. K., & Vui, D. T. (2019) · Pharmacognosy Research · doi:10.4103/pr.pr_82_19 · Cited by 3
Involvement of neuroinflammatory mediators in the pathogenesis of neurodegeneration
Singh, R. K., & Srivastava, A. (2020) · Asian Journal of Pharmacy and Pharmacology · doi:10.31024/ajpp.2020.6.1.2 · Cited by 3
Kozin, S. V., Кравцов, А. А., Zlischeva, E. I., Шурыгина, Л. В., Malyshko, V. V., Моисеев, А. В., Елкина, А. А., & Барышев, М. Г. (2020) · BIOPHYSICS · doi:10.1134/s0006350920060093 · Cited by 3
Alzheimer’s disease, Epidemiology, causes, diagnosis and novel treatments: A review.
Ullah, N., khan, N. M., & Ullah, W. (2015) · Cited by 3
Estrategias de investigación para el tratamiento de Alzheimer con antioxidantes polifenólicos
Sierra, L. (2016) · Revista de la Academia Colombiana de Ciencias Exactas Físicas y Naturales · doi:10.18257/raccefyn.408 · Cited by 2
Kouémou, N. E., Fotio, A. L., Nguepi, M. S. D., Ouafo, A. C., Palé, S., Kandeda, A. K., Taïwé, G. S., & Bum, E. N. (2017) · International Journal of Pharmacology Phytochemistry and Ethnomedicine · doi:10.18052/www.scipress.com/ijppe.8.41 · Cited by 3
Effects of Bioactive Components of Green Tea on Alzheimer's Disease
Ide, K., Kawasaki, Y., Kawakami, K., & Yamada, H. (2018) · Studies in natural products chemistry · doi:10.1016/b978-0-444-64058-1.00005-4 · Cited by 3
Kanika, & Singh, L. (2024) · Molecular Biology Reports · doi:10.1007/s11033-024-09502-9 · Cited by 3
Adnan, M., Siddiqui, A. J., Bardakçi, F., Surti, M., Badraoui, R., & Patel, M. B. (2025) · Pharmaceuticals · doi:10.3390/ph18040489 · Cited by 2
Cheng, A. P., Dhavarasa, P., van Heeswyk, J., Richards, S. M., Li, X., Shapiro, A. M., & Wells, P. G. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103856 · Cited by 2
Valle, M. L., Getaneh, B., William, C. M., Ghiso, J. A., & Rostagno, A. A. (2025) · Antioxidants · doi:10.3390/antiox14111375 · Cited by 2
Wang, Y., Wang, Y., Zhang, W., Xu, Y., Narayan, N. S., Cheng, H., Yang, H., Huang, Y., Zhang, C. M., & Wang, C. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c02549 · Cited by 2
Aghababaee, L., Farrokhi, K., Karimi‐Jafari, M. H., Shahpasand, K., & Riazi, G. H. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05454-8 · Cited by 2
From Lipid Regulation to Neuroprotection: Multitarget (Benzo)thiazine Derivatives as Promising Leads
Tzara, A., Andreou, A. G., & Kourounakis, A. P. (2025) · Molecules · doi:10.3390/molecules30234542 · Cited by 2
Cheng, Y., Santucci, K., Gao, Y., Takenaka, K., Lindner, G., Xu, S.-M., & Janitz, M. (2026) · Journal of Molecular Neuroscience · doi:10.1007/s12031-025-02469-7 · Cited by 3
Privitera, A., Cardaci, V., Zupan, M. C., Pietro, L. D., Carota, G., Sibbitts, J., Mangione, R., Graziani, A., Buccarello, L., Bellia, F., et al. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1768094 · Cited by 2
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