Role of oxidative stress in Alzheimer’s disease
Open accessAbstract
Alzheimer's disease (AD) is the most common cause of disability in individuals aged >65 years worldwide. AD is characterized by the abnormal deposition of amyloid β (Aβ) peptide, and intracellular accumulation of neurofibrillary tangles of hyperphosphorylated τ protein and dementia. The neurotoxic oligomer Aβ peptide, which is the neuropathological diagnostic criterion of the disease, together with τ protein, are mediators of the neurodegeneration that is among the main causative factors. However, these phenomena are mainly initiated and enhanced by oxidative stress, a process referring to an imbalance between antioxidants and oxidants in favour of oxidants. This imbalance can occur as a result of increased free radicals or a decrease in antioxidant defense, free radicals being a species that contains one or more unpaired electrons in its outer shell. The major source of potent free radicals is the reduction of molecular oxygen in water, that initially yields the superoxide radical, which produces hydrogen peroxide by the addition of an electron. The reduction of hydrogen peroxide produces highly reactive hydroxyl radicals, termed reactive oxygen species (ROS) that can react with lipids, proteins, nucleic acids, and other molecules and may also alter their structures and functions. Thus, tissues and organs, particularly the brain, a vulnerable organ, are affected by ROS due to its composition. The brain is largely composed of easily oxidizable lipids while featuring a high oxygen consumption rate. The current review examined the role of oxidative stress in AD.
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Oxidative stress has a crucial role in Alzheimer's disease pathogenesis.
“Furthermore, oxidative stress has also been determined to have a crucial role in AD pathogenesis [27].”
From The Multifaceted Role of Neuroprotective Plants in Alzheimer’s Disease Treatment (2022) · cites this paper as [27]
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Cites
Free Radicals in the Physiological Control of Cell Function
Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855 · see citing works
Oxidants, oxidative stress and the biology of ageing
Finkel, T., & Holbrook, N. J. (2000) · Nature · doi:10.1038/35041687 · Cited by 9,413 · see citing works
Free radicals, metals and antioxidants in oxidative stress-induced cancer
Valko, M., Rhodes, C. J., Moncol, J., Izakovic, M., & Mazur, M. (2006) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2005.12.009 · Cited by 6,680 · see citing works
Mitochondrial formation of reactive oxygen species
Turrens, J. F. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.049478 · Cited by 5,084 · see citing works
Metals, Toxicity and Oxidative Stress
Valko, M., Morris, H., & Cronin, M. (2005) · Current Medicinal Chemistry · doi:10.2174/0929867053764635 · Cited by 5,018 · see citing works
Oxyl radicals, redox-sensitive signalling cascades and antioxidants
Genestra, M. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.04.009 · Cited by 4,930 · see citing works
Superoxide radical and superoxide dismutases
Fridovich, I. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.000525 · Cited by 3,455 · see citing works
Oxidative DNA damage: mechanisms, mutation, and disease
Cooke, M. S., Evans, M. D., Dizdaroglu, M., & Lunec, J. (2003) · The FASEB Journal · doi:10.1096/fj.02-0752rev · Cited by 3,245 · see citing works
Reactive Oxygen Species and the Central Nervous System
Halliwell, B. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb10990.x · Cited by 2,947 · see citing works
Oxidative stress hypothesis in Alzheimer’s disease
Markesbery, W. R. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00629-6 · Cited by 2,383 · see citing works
Protein carbonyl groups as biomarkers of oxidative stress
Dalle‐Donne, I., Rossi, R., Giustarini, D., Milzani, A., & Colombo, R. (2003) · Clinica Chimica Acta · doi:10.1016/s0009-8981(03)00003-2 · Cited by 2,353 · see citing works
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 · see citing works
A review on Alzheimer's disease pathophysiology and its management: an update
Kumar, A., Singh, A., & Ekavali (2015) · Pharmacological Reports · doi:10.1016/j.pharep.2014.09.004 · Cited by 1,578 · see citing works
Free Radicals as Mediators of Tissue Injury and Disease
Kehrer, J. P. (1993) · Critical Reviews in Toxicology · doi:10.3109/10408449309104073 · Cited by 1,460 · see citing works
Rubbo, H., Radí, R., Trujillo, M., Telleri, R., Kalyanaraman, B., Barnes, S., KIRK, M. C., & Freeman, B. Α. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47160-8 · Cited by 1,350 · see citing works
Mitochondrial metabolism of reactive oxygen species
Andreyev, A. Y., Kushnareva, Y. E., & Starkov, A. A. (2005) · Biochemistry (Moscow) · doi:10.1007/s10541-005-0102-7 · Cited by 1,336 · see citing works
Oxidative stress and Alzheimer disease
Christen, Y. (2000) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/71.2.621s · Cited by 1,158 · see citing works
An introduction to free radical biochemistry
Cheeseman, K. H., & Slater, T. F. (1993) · British Medical Bulletin · doi:10.1093/oxfordjournals.bmb.a072625 · Cited by 1,126 · see citing works
Phagocytes and oxidative stress
Babior, B. M. (2000) · The American Journal of Medicine · doi:10.1016/s0002-9343(00)00481-2 · Cited by 1,061 · see citing works
Stadtman, E. R., & Levine, R. L. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06187.x · Cited by 1,037 · see citing works
Subcellular Distribution of Superoxide Dismutases (SOD) in Rat Liver
Okado‐Matsumoto, A., & Fridovich, I. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105395200 · Cited by 1,013 · see citing works
Reactive oxygen species, aging and antioxidative nutraceuticals
Lee, J., Koo, N., & Min, D. B. (2004) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/j.1541-4337.2004.tb00058.x · Cited by 864 · see citing works
Mitochondrial Dysfunction in Neurodegenerative Diseases
Johri, A., & Beal, M. F. (2012) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.112.192138 · Cited by 806 · see citing works
Allan Butterfield, D. (2002) · Free Radical Research · doi:10.1080/1071576021000049890 · Cited by 786 · see citing works
The superoxide-generating NADPH oxidase: structural aspects and activation mechanism
Vignais, P. V. (2002) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-002-8520-9 · Cited by 773 · see citing works
Review: Alzheimer's Amyloid β-Peptide-Associated Free Radical Oxidative Stress and Neurotoxicity
Varadarajan, S., Yatin, S., Aksenova, M., & Butterfield, D. A. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4274 · Cited by 735 · see citing works
Kaur, H., & Halliwell, B. B. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00722-5 · Cited by 706 · see citing works
Amyloid diseases: Abnormal protein aggregation in neurodegeneration
Koo, E. H., Lansbury, P. T., & Kelly, J. W. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.18.9989 · Cited by 686 · see citing works
Sheldon, R. A., & Kochi, J. K. (1981) · Cited by 657 · see citing works
Mitochondrial dysfunction in neurodegenerative diseases
Beal, M. F. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00114-5 · Cited by 608 · see citing works
Demyelination: The Role of Reactive Oxygen and Nitrogen Species
Smith, K. J., Kapoor, R., & Felts, P. A. (1999) · Brain Pathology · doi:10.1111/j.1750-3639.1999.tb00212.x · Cited by 601 · see citing works
Kozłowski, H., Janicka-Kłos, A., Brasuń, J., Gaggelli, E., Valensin, D., & Valensin, G. (2009) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2009.05.011 · Cited by 467 · see citing works
Metal Binding Modes of Alzheimer's Amyloid β-Peptide in Insoluble Aggregates and Soluble Complexes
Miura, T., Suzuki, K., Kohata, N., & Takeuchi, H. (2000) · Biochemistry · doi:10.1021/bi0002479 · Cited by 452 · see citing works
Oxidative Stress and Antioxidants in Exercise
Leeuwenburgh, C., & Heinecke, J. W. (2001) · Current Medicinal Chemistry · doi:10.2174/0929867013372896 · Cited by 430 · see citing works
Redox‐Active Metals, Oxidative Stress, and Alzheimer's Disease Pathology
HUANG, X., MOIR, R. D., TANZI, R. E., BUSH, A. I., & ROGERS, J. T. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1306.012 · Cited by 425 · see citing works
The Role of Oxidative Stress in Alzheimer Disease
Markesbery, W. R. (1999) · Archives of Neurology · doi:10.1001/archneur.56.12.1449 · Cited by 307 · see citing works
Structure of the Alzheimer's Disease Amyloid Precursor Protein Copper Binding Domain
Barnham, K. J., McKinstry, W. J., Multhaup, G., Galatis, D., Morton, C. J., Curtain, C. C., Williamson, N. A., White, A. R., Hinds, M. G., Norton, R. S., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300629200 · Cited by 274 · see citing works
Kinetics and mechanism of the reduction of ferricytochrome c by the superoxide anion.
Butler, J., Koppenol, W. H., & Margoliash, E. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33886-9 · Cited by 261 · see citing works
Hoeberichts, F. A., & Woltering, E. J. (2002) · BioEssays · doi:10.1002/bies.10175 · Cited by 257 · see citing works
Zinc takes the center stage: its paradoxical role in Alzheimer’s disease
Cuajungco, M. P., & Faget, K. Y. (2003) · Brain Research Reviews · doi:10.1016/s0165-0173(02)00219-9 · Cited by 242 · see citing works
Superoxide and iron: Partners in crime
Liochev, S. I., & Fridovich, I. (1999) · International Union of Biochemistry and Molecular Biology: Life · doi:10.1080/152165499307161 · Cited by 219 · see citing works
Clarke, J. R., Lyra e Silva, N. M., Figueiredo, C. P., Frozza, R. L., Ledo, J. H., Beckman, D., Katashima, C. K., Razolli, D., Carvalho, B. M., Frazão, R., et al. (2015) · EMBO Molecular Medicine · doi:10.15252/emmm.201404183 · Cited by 214 · see citing works
Cytochrome P450: progress and predictions
Coon, M. J., Ding, X., Pernecky, S. J., & Vaz, A. D. N. (1992) · The FASEB Journal · doi:10.1096/fasebj.6.2.1537454 · Cited by 209 · see citing works
The NADPH Oxidase of Endothelial Cells
BABIOR, B. M. (2000) · IUBMB Life · doi:10.1080/713803730 · Cited by 196 · see citing works
Butterfield, D. A., Hensley, K., Cole, P. S., Ramachandran, S., Aksenov, M. Y., Aksenova, M. V., Bummer, P. M., Haley, B. E., & Carney, J. M. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.68062451.x · Cited by 191 · see citing works
Circulating xanthine oxidase: potential mediator of ischemic injury
Yokoyama, Y., Beckman, J. S., Beckman, T. K., Wheat, J. K., Cash, T., Freeman, B. Α., & Parks, D. A. (1990) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.1990.258.4.g564 · Cited by 188 · see citing works
Fatty acids and oxidative stress in psychiatric disorders
Tsaluchidu, S., Cocchi, M., Tonello, L., & Puri, B. K. (2008) · BMC Psychiatry · doi:10.1186/1471-244x-8-s1-s5 · Cited by 178 · see citing works
ROS signaling and redox biology in endothelial cells
Panieri, E., & Santoro, M. M. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1928-9 · Cited by 168 · see citing works
Zinc and copper modulate Alzheimer Aβ levels in human cerebrospinal fluid
Altschul, D., Launer, L. J., Adlard, P. A., Cherny, R. A., Tsatsanis, A., Volitakis, I., Blennow, K., Petrovitch, H., White, L. R., & Bush, A. I. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.10.012 · Cited by 154 · see citing works
Reactive Oxygen Species and the Central Nervous System
Halliwell, B. B. (1992) · Springer eBooks · doi:10.1007/978-3-642-77609-0_2 · Cited by 111 · see citing works
Astrocyte Mitochondrial Mechanisms of Ischemic Brain Injury and Neuroprotection
Bambrick, L. L., Kristián, T., & Fiskum, G. M. (2004) · Neurochemical Research · doi:10.1023/b:nere.0000014830.06376.e6 · Cited by 110 · see citing works
Aboul-Fotouh, S. (2013) · Pharmacology Biochemistry and Behavior · doi:10.1016/j.pbb.2012.12.027 · Cited by 97 · see citing works
Glycation and Advanced Glycation End-Product Formation with Icodextrin and Dextrose
Anne, B., Dawnayand, S. J., & Millar, D. J. (1997) · Peritoneal Dialysis International · doi:10.1177/089686089701700112 · Cited by 91 · see citing works
Pal, A., Badyal, R. K., Vasishta, R. K., Attri, S. V., Thapa, B. R., & Prasad, R. (2013) · Biological Trace Element Research · doi:10.1007/s12011-013-9665-0 · Cited by 82 · see citing works
Mustafa, S. A., Karieb, S. S., Davies, S. J., & Jha, A. N. (2014) · Mutagenesis · doi:10.1093/mutage/geu048 · Cited by 78 · see citing works
Therade-Matharan, S., Laemmel, E., Duranteau, J., & Vicaut, É. (2004) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00048.2004 · Cited by 75 · see citing works
Hwang, H. J., Lynn, S. G., Vengellur, A., Saini, Y., Grier, E. A., Ferguson-Miller, S. M., & LaPres, J. J. (2015) · Biochemistry · doi:10.1021/bi5012892 · Cited by 47 · see citing works
Harkany, T., Penke, B., & Luiten, P. G. M. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06389.x · Cited by 42 · see citing works
Zhang, X., & Gao, F. (2015) · Free Radical Research · doi:10.3109/10715762.2015.1014813 · Cited by 40 · see citing works
Self-citationHebelstrup, K. H., & Møller, I. M. (2014) · Signaling and communication in plants · doi:10.1007/978-3-319-10079-1_4 · Cited by 38 · see citing works
Corvo, M. L., Marinho, H. S., Marcelino, P. A., Lopes, R. M., Vale, C., Marques, C. R., Martins, L. C. D., Laverman, P., Storm, G., & Martins, M. B. F. (2014) · Pharmaceutical Research · doi:10.1007/s11095-014-1447-7 · Cited by 38 · see citing works
Hlavica, P. (2015) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-16009-2_10 · Cited by 31 · see citing works
Antioxidant Therapies for Neurodegenerative Diseases: Mechanisms, Current Trends, and Perspectives
Gelain, D. P., Behr, G. A., de Oliveira, R. B., & Trujillo, M. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/895153 · Cited by 27 · see citing works
Protective role of glutathione against oxidative stress in Streptococcus thermophilus
Wang, T., Lu, W., Lu, S., et al. (2015) · International Dairy Journal · doi:10.1016/j.idairyj.2015.01.015 · Cited by 24 · see citing works
Alzheimers Disease and Oxidative Stress: The Old Problem Remains Unsolved
Moreira, P. I., Honda, K., Liu, Q., Aliev, G. M., Oliveira, C. R., Santos, M. S., Zhu, X., Smith, M. A., & Perry, G. L. (2005) · Central Nervous System Agents in Medicinal Chemistry · doi:10.2174/1568015053202714 · Cited by 22 · see citing works
Oxidative Stress in Nonalcoholic Fatty Liver Disease
Marı́, M., Morales, A., Colell, A., García‐Ruiz, C., & Fernández-Checa, J. C. (2015) · Oxidative stress in applied basic research and clinical practice · doi:10.1007/978-3-319-15539-5_12 · Cited by 14 · see citing works
Protein Oxidation in Toxicology
Reeg, S., & Grune, T. (2015) · Oxidative stress in applied basic research and clinical practice · doi:10.1007/978-3-319-19096-9_5 · Cited by 3 · see citing works
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An Overview of Oxidative Stress, Neuroinflammation, and Neurodegenerative Diseases
Teleanu, D. M., Niculescu, A.-G., Lungu, I. I., Radu, C. I., Vladâcenco, O., Roza, E., Costăchescu, B., Grumezescu, A. M., & Teleanu, R. I. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23115938 · Cited by 1,085 · 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
Park, M. W., Cha, H. W., Kim, J., Kim, J. H., Yang, H., Yoon, S., Boonpraman, N., Yi, S. S., Yoo, I. D., & Moon, J.-S. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101947 · Cited by 683 · see citing works
Is Alzheimer’s disease a type 3 diabetes? A critical appraisal
Kandimalla, R., Thirumala, V., & Reddy, P. H. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.08.018 · Cited by 621 · see citing works
Neuroprotective effect of SGLT2 inhibitors.
Pawlos, A., Broncel, M., Woźniak, E., & Gorzelak-Pabiś, P. (2021) · Molecules · doi:10.3390/molecules26237213 · Cited by 304 · see citing works
Andrade, S., Ramalho, M. J., Loureiro, J. A., & Pereira, M. D. C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092313 · Cited by 240 · see citing works
Griñán-Ferré, C., Bellver-Sanchis, A., Izquierdo, V., Corpas, R., Roig-Soriano, J., Chillón, M., Andres-Lacueva, C., Somogyvári, M., Sőti, C., Sanfeliu, C., et al. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101271 · Cited by 208 · see citing works
Inflammasomes, hormesis, and antioxidants in neuroinflammation: Role of NRLP3 in Alzheimer disease
Pennisi, M., Crupi, R., Di Paola, R., Ontario, M. L., Bella, R., Calabrese, E. J., Crea, R., Cuzzocrea, S., & Calabrese, V. (2017) · Journal of Neuroscience Research · doi:10.1002/jnr.23986 · Cited by 157 · see citing works
Role of natural products for the treatment of Alzheimer’s disease
Noori, T., Dehpour, A. R., Sureda, A., Sobarzo-Sanchez, E., & Shirooie, S. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.173974 · Cited by 141 · see citing works
Sun, M., Ma, K., Wen, J., Wang, G., Zhang, C., Li, Q., Bao, X., & Wang, H. (2020) · Journal of Alzheimer’s Disease · doi:10.3233/jad-190872 · Cited by 113 · see citing works
In silico repurposing of antipsychotic drugs for Alzheimer’s disease
Kumar, S., Chowdhury, S., & Kumar, S. (2017) · BMC Neuroscience · doi:10.1186/s12868-017-0394-8 · Cited by 103 · see citing works
Venkataraman, A. V., Mansur, A., Rizzo, G., Bishop, C., Lewis, Y., Kocagoncu, E., Lingford-Hughes, A., Huiban, M., Passchier, J., Rowe, J. B., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abk1051 · Cited by 101 · see citing works
Fracassi, A., Marcatti, M., Zolochevska, O., Tabor, N., Woltjer, R., Moreno, S., & Taglialatela, G. (2021) · The Journal of Neuroscience · doi:10.1523/jneurosci.0295-20.2020 · Cited by 81 · see citing works
Liu, B., Hinshaw, R. G., Le, K. X., Park, M.-A., Wang, S., Belanger, A. P., Dubey, S., Frost, J. L., Shi, Q., Holton, P., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-48615-1 · Cited by 73 · see citing works
Hybrid Multifunctional Modulators Inhibit Multifaceted Aβ Toxicity and Prevent Mitochondrial Damage
Rajasekhar, K., Mehta, K., & Govindaraju, T. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00033 · Cited by 69 · see citing works
Stigger, F. S., Zago Marcolino, M. A., Portela, K. M., & Plentz, R. D. M. (2019) · The Journals of Gerontology: Series A · doi:10.1093/gerona/gly173 · Cited by 68 · see citing works
Cecerska-Heryć, E., Polikowska, A., Serwin, N., Roszak, M., Grygorcewicz, B., Heryć, R., Michalczyk, A., & Dołęgowska, B. (2022) · Neurochemistry International · doi:10.1016/j.neuint.2021.105269 · Cited by 68 · see citing works
Etiology of type 2 diabetes and Alzheimer’s disease: Exploring the mitochondria
Silzer, T. K., & Phillips, N. R. (2018) · Mitochondrion · doi:10.1016/j.mito.2018.04.004 · Cited by 53 · see citing works
Kochman, U., Sitka, H., Kuźniar, J., Czaja, M., Kozubek, P., Beszłej, J. A., & Leszek, J. (2026) · Molecular Neurobiology · doi:10.1007/s12035-025-05417-z · Cited by 60 · see citing works
Makhaeva, G. F., Kovaleva, N. V., Boltneva, N. P., Lushchekina, S. V., Astakhova, T. Y., Rudakova, E. V., Proshin, A. N., Serkov, I. V., Radchenko, E. V., Palyulin, V. A., et al. (2020) · Molecules · doi:10.3390/molecules25173915 · Cited by 53 · see citing works
Koh, E.-J., Kim, K.-J., Song, J.-H., Choi, J., Lee, H., Kang, D.-H., Heo, H., & Lee, B.-Y. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18112401 · Cited by 48 · see citing works
Stanciu, G. D., Rusu, R. N., Bild, V., Filipiuc, L. E., Tamba, B.-I., & Ababei, D. C. (2021) · Biomedicines · doi:10.3390/biomedicines9050576 · Cited by 47 · see citing works
Polis, B., & Samson, A. O. (2024) · Journal of Alzheimer's Disease · doi:10.3233/jad-240058 · Cited by 43 · see citing works
Molaei, A., Hatami, H., Dehghan, G., Sadeghian, R., & Khajehnasiri, N. (2020) · IfADo - Leibniz Research Centre for Working Environment and Human Factors, Dortmund · doi:10.17179/excli2019-2082 · Cited by 41 · see citing works
Challenges of Repurposing Tetracyclines for the Treatment of Alzheimer’s and Parkinson’s Disease
Markulin, I., Matasin, M., Turk, V. E., & Salković-Petrisic, M. (2022) · Journal of Neural Transmission · doi:10.1007/s00702-021-02457-2 · Cited by 36 · see citing works
Influential role of 7-Ketocholesterol in the progression of Alzheimer’s disease
Mahalakshmi, K., Parimalanandhini, D., Sangeetha, R., Livya Catherene, M., Beulaja, M., Thiagarajan, R., Arumugam, M., Janarthanan, S., & Manikandan, R. (2021) · Prostaglandins & Other Lipid Mediators · doi:10.1016/j.prostaglandins.2021.106582 · Cited by 32 · see citing works
Ding, H., Reiss, A. B., Pinkhasov, A., & Kasselman, L. J. (2022) · Medicina · doi:10.3390/medicina58081025 · Cited by 32 · see citing works
Association between thyroid function and Alzheimer's disease: A systematic review
Figueroa, P. B. S., Ferreira, A. F. F., Britto, L. R., Doussoulin, A. P., & Torrão, A. D. S. (2021) · Metabolic Brain Disease · doi:10.1007/s11011-021-00760-1 · Cited by 28 · see citing works
Mechanism of anti-dementia effects of mangiferin in a senescence accelerated mouse (SAMP8) model
Du, Z., Fanshi, F., Lai, Y.-H., Chen, J.-R., Hao, E., Deng, J., & Hsiao, C.-D. (2019) · Bioscience Reports · doi:10.1042/bsr20190488 · Cited by 30 · see citing works
The Multifaceted Role of Neuroprotective Plants in Alzheimer’s Disease Treatment
Zieneldien, T., Kim, J., & Cao, C. (2022) · Geriatrics · doi:10.3390/geriatrics7020024 · Cited by 29 · see citing works
“Furthermore, oxidative stress has also been determined to have a crucial role in AD pathogenesis [27].”
BackgroundRecent trends of natural based therapeutics for mitochondria targeting in Alzheimer’s disease
Dhiman, A., Handa, M., Ruwali, M., Singh, D. P., Kesharwani, P., & Shukla, R. (2022) · Mitochondrion · doi:10.1016/j.mito.2022.03.006 · Cited by 21 · see citing works
Souchet, B., Michaïl, A., Heuillet, M., Dupuy-Gayral, A., Haudebourg, E., Pech, C., Berthemy, A., Autelitano, F., Billoir, B., Domoto-Reilly, K., et al. (2024) · The Journal of Prevention of Alzheimer's Disease · doi:10.14283/jpad.2024.34 · Cited by 15 · see citing works
- Authors
- HUANG, W.-J., ZHANG, X., & CHEN, W.-W.
- Affiliations
- Xuzhou Central Hospital (CN)
- ORCID
- ZHANG, XIA
- Venue
- Biomedical Reports
- Publisher
- Spandidos Publications
- Published
- 2016-03-15
- Volume
- 4
- Issue
- 5
- Pages
- 519-522
- ISSN
- 2049-9434 (ISSN-L)
- 2049-9442
- PMC
- PMC4840676
- OpenAlex
- W2300480290
- Cited by
- 1,023
- References
- 67
- Citations by year
- 2026: 71 · 2025: 120 · 2024: 130 · 2023: 106 · 2022: 132 · 2021: 135 · 2020: 112 · 2019: 105 · 2018: 63 · 2017: 37 · 2016: 11
- FWCI
- 58.25
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-nd
- Locations
- Biomedical Reports (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Keywords
- Alzheimer's disease, oxidative stress, reactive oxygen species, amyloid-beta, tau protein, neurofibrillary tangles, neurodegeneration, free radicals, antioxidant defense, superoxide, hydrogen peroxide, hydroxyl radicals, lipid oxidation, brain vulnerability
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