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.
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Oxidative stress leads to the formation of senile plaques by lowering alpha-secretase activity while increasing both beta- and gamma-secretase activities.
“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]
When hyperphosphorylated Tau protein is overexpressed, peroxisome depletion occurs, suggesting that this depletion causes H2O2 and ROS increase.
“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]
Hydrogen peroxide is the relevant actor in promoting excessive oxidation in neuronal cells.
“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]
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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 · see citing works
Querfurth, H. W., & LaFerla, F. M. (2010) · New England Journal of Medicine · doi:10.1056/nejmra0909142 · Cited by 4,569 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
A Century of Alzheimer's Disease
Goedert, M., & Spillantini, M. G. (2006) · Science · doi:10.1126/science.1132814 · Cited by 2,106 · see citing works
Hydrogen peroxide mediates amyloid β protein toxicity
Behl, C. (1994) · Cell · doi:10.1016/0092-8674(94)90131-7 · Cited by 2,074 · 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
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
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 · see citing works
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
Formation of Neurofibrillary Tangles in P301L Tau Transgenic Mice Induced by Aβ42 Fibrils
Götz, J., Chen, F., van Dorpe, J., & Nitsch, R. M. (2001) · Science · doi:10.1126/science.1062097 · Cited by 1,526 · see citing works
Rapid induction of Alzheimer A beta amyloid formation by zinc
Bush, A., Pettingell, W., Multhaup, G., d Paradis, M., Vonsattel, J., Gusella, J., Beyreuther, K., Masters, C., & Tanzi, R. (1994) · Science · doi:10.1126/science.8073293 · Cited by 1,522 · see citing works
Cherny, R. A., Atwood, C. S., Xilinas, M. E., Gray, D. N., Jones, W. D., McLean, C. A., Barnham, K. J., Volitakis, I., Fraser, F. W., Kim, Y.-S., et al. (2001) · Neuron · doi:10.1016/s0896-6273(01)00317-8 · Cited by 1,447 · see citing works
Mitochondrial abnormalities in Alzheimer's disease
Hirai, K., Aliev, G., Nunomura, A., Fujioka, H., Russell, R. L., Atwood, C. S., Johnson, A. B., Kress, Y., Vinters, H. V., Tabaton, M., et al. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-09-03017.2001 · Cited by 1,367 · see citing works
Kalaria, R. N., Maestre, G. E., Arizaga, R., Friedland, R. P., Galasko, D., Hall, K., Luchsinger, J. A., Ogunniyi, A., Perry, E. K., Potocnik, F., et al. (2008) · The Lancet Neurology · doi:10.1016/s1474-4422(08)70169-8 · Cited by 1,233 · see citing works
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
Manczak, M., Anekonda, T. S., Henson, E., Park, B. S., Quinn, J., & Reddy, P. H. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl066 · Cited by 1,104 · 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
Atwood, C. S., Moir, R. D., Huang, X., Scarpa, R. C., Bacarra, N. M. E., Romano, D. M., Hartshorn, M. A., Tanzi, R. E., & Bush, A. I. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.21.12817 · Cited by 1,009 · see citing works
Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives
Mattson, M. P. (1997) · Physiological Reviews · doi:10.1152/physrev.1997.77.4.1081 · Cited by 1,006 · cited 1× · see citing works
“It has been demonstrated that the levels of protein carbonyls and 3-nitrotyrosine, which are resulted from protein oxidation, and markers of oxidative damage to DNA and RNA, such as 8-hydroxydeoxyguanosine (8-OHdG) and 8- hydroxyguanosine, are elevated in AD brains [8–12].”
BackgroundRitchie, 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
Mandelkow, E., & Mandelkow, E. (1998) · Trends in Cell Biology · doi:10.1016/s0962-8924(98)01368-3 · Cited by 951 · see citing works
Stamer, K., Vogel, R., Thies, E., Mandelkow, E., & Mandelkow, E.-M. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200108057 · Cited by 885 · see citing works
De Felice, F. G., Velasco, P. T., Lambert, M. P., Viola, K., Fernandez, S. J., Ferreira, S. T., & Klein, W. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607483200 · Cited by 882 · see citing works
RNA Oxidation Is a Prominent Feature of Vulnerable Neurons in Alzheimer’s Disease
Nunomura, A., Perry, G., Pappolla, M., Wade, R., Hirai, K., Chiba, S., & Smith, M. A. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-06-01959.1999 · Cited by 768 · see citing works
Beal, M. F. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00780-3 · Cited by 763 · see citing works
Cu(II) Potentiation of Alzheimer Aβ Neurotoxicity
Huang, X., Cuajungco, M. P., Atwood, C. S., Hartshorn, M. A., Tyndall, J. D. A., Hanson, G. R., Stokes, K. C., Leopold, M., Multhaup, G., Goldstein, L. E., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.52.37111 · Cited by 762 · see citing works
Picomolar Amyloid-β Positively Modulates Synaptic Plasticity and Memory in Hippocampus
Puzzo, D., Privitera, L., Leznik, E., Fà, M., Staniszewski, A., Palmeri, A., & Arancio, O. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.2692-08.2008 · Cited by 740 · see citing works
Mitochondrial Aβ: a potential focal point for neuronal metabolic dysfunction in Alzheimer's disease
Caspersen, C., Wang, N., Yao, J., Sosunov, A., Chen, X., Lustbader, J. W., Xu, H. W., Stern, D., McKhann, G., & Du Yan, S. (2005) · The FASEB Journal · doi:10.1096/fj.05-3735fje · Cited by 738 · see citing works
The Regulation of Reactive Oxygen Species Production during Programmed Cell Death
Tan, S., Sagara, Y., Liu, Y., Maher, P. A., & Schubert, D. A. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.6.1423 · Cited by 730 · see citing works
Elevated β-secretase expression and enzymatic activity detected in sporadic Alzheimer disease
Yang, L.-B., Lindholm, K., Yan, R., Citron, M., Xia, W., Yang, X.-L., Beach, T., Sue, L., Wong, P., Price, D., et al. (2003) · Nature Medicine · doi:10.1038/nm0103-3 · Cited by 729 · see citing works
β-Secretase Protein and Activity Are Increased in the Neocortex in Alzheimer Disease
Fukumoto, H. (2002) · Archives of Neurology · doi:10.1001/archneur.59.9.1381 · Cited by 694 · see citing works
2010 Alzheimer's disease facts and figures
Alzheimer's Association (2010) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2010.01.009 · Cited by 692 · see citing works
Markesbery, W. R., & Lovell, M. A. (1998) · Neurobiology of Aging · doi:10.1016/s0197-4580(98)00009-8 · Cited by 680 · see citing works
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
Curtain, C. C., Ali, F. E. A., Volitakis, I., Cherny, R. A., Norton, R. S., Beyreuther, K. T., Barrow, C. J., Masters, C. L., Bush, A. I., & Barnham, K. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100175200 · Cited by 653 · see citing works
Lovell, M. A., Ehmann, W. D., Butler, S. M., & Markesbery, W. R. (1995) · Neurology · doi:10.1212/wnl.45.8.1594 · Cited by 644 · see citing works
Mechanisms of tau-induced neurodegeneration
Iqbal, K., Liu, F., Gong, C.-X., Alonso, A. D. C., & Grundke-Iqbal, I. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0486-3 · Cited by 628 · 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
Oxidative stress hypothesis in Alzheimer’s disease: a reappraisal
Praticò, D. (2008) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2008.09.001 · Cited by 606 · see citing works
Oxidative stress in the progression of Alzheimer disease in the frontal cortex
Ansari, M. A., & Scheff, S. W. (2010) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181cb5af4 · Cited by 605 · see citing works
Metalloenzyme-like Activity of Alzheimer's Disease β-Amyloid
Opazo, C., Huang, X., Cherny, R. A., Moir, R. D., Roher, A. E., White, A. R., Cappai, R., Masters, C. L., Tanzi, R. E., Inestrosa, N. C., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206428200 · Cited by 580 · see citing works
The Biology of Mitochondrial Uncoupling Proteins
Rousset, S., Alves‐Guerra, M., Mozo, J., Miroux, B., Cassard, A., Bouillaud, F., & Ricquier, D. (2004) · Diabetes · doi:10.2337/diabetes.53.2007.s130 · Cited by 556 · see citing works
Rogers, J. T., Randall, J. D., Cahill, C. M., Eder, P. S., Huang, X., Gunshin, H., Leiter, L., McPhee, J., Sarang, S. S., Utsuki, T., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207435200 · Cited by 551 · see citing works
100 Years and Counting: Prospects for Defeating Alzheimer's Disease
Roberson, E. D., & Mucke, L. (2006) · Science · doi:10.1126/science.1132813 · Cited by 550 · see citing works
Amyloid‐β Deposition in Alzheimer Transgenic Mice Is Associated with Oxidative Stress
Smith, M. A., Hirai, K., Hsiao, K., Pappolla, M. A., Harris, P. L. R., Siedlak, S. L., Tabaton, M., & Perry, G. L. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.70052212.x · Cited by 547 · see citing works
Deibel, M. A., Ehmann, W. D., & Markesbery, W. R. (1996) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(96)00203-1 · Cited by 540 · see citing works
Cortical Cytochrome Oxidase Activity Is Reduced in Alzheimer's Disease
Mutisya, E. M., Bowling, A. C., & Beal, M. F. (1994) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1994.63062179.x · Cited by 531 · see citing works
Neuroprotective effects of curcumin
Cole, G. M., Teter, B., & Frautschy, S. A. (2007) · ADVANCES IN EXPERIMENTAL MEDICINE AND BIOLOGY · doi:10.1007/978-0-387-46401-5_8 · Cited by 516 · see citing works
Increased peroxidation and reduced antioxidant enzyme activity in Alzheimer's disease
Marcus, D. L., Thomas, C., Rodriguez, C., Simberkoff, K., Tsai, J. S., Strafaci, J. A., & Freedman, M. L. (1998) · Experimental Neurology · doi:10.1006/exnr.1997.6750 · Cited by 513 · see citing works
Copper in disorders with neurological symptoms: Alzheimer’s, Menkes, and Wilson diseases
Strausak, D., Mercer, J. F. B., Dieter, H. H., Stremmel, W., & Multhaup, G. (2001) · Brain Research Bulletin · doi:10.1016/s0361-9230(01)00454-3 · Cited by 508 · see citing works
A Portrait of Alzheimer Secretases--New Features and Familiar Faces
Esler, W. P., & Wolfe, M. S. (2001) · Science · doi:10.1126/science.1064638 · Cited by 493 · see citing works
β‐Amyloid inhibits integrated mitochondrial respiration and key enzyme activities
Casley, C. S., Canevari, L., Land, J. M., Clark, J. B., & Sharpe, M. A. (2001) · Journal of Neurochemistry · doi:10.1046/j.0022-3042.2001.00681.x · Cited by 485 · see citing works
Increased Nuclear DNA Oxidation in the Brain in Alzheimer's Disease
Gabbita, S. P., Lovell, M. A., & Markesbery, W. R. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.71052034.x · Cited by 479 · see citing works
The molecular bases of Alzheimer’s disease and other neurodegenerative disorders
Maccioni, R. B., Muñoz, J. P., & Barbeito, L. (2001) · Archives of Medical Research · doi:10.1016/s0188-4409(01)00316-2 · Cited by 474 · see citing works
Billingsley, M., & Kincaid, R. (1997) · Biochemical Journal · doi:10.1042/bj3230577 · Cited by 469 · see citing works
Proteomic and functional analyses reveal a mitochondrial dysfunction in P301L tau transgenic mice
David, D. C., Hauptmann, S., Scherping, I., Schuessel, K., Keil, U., Rizzu, P., Ravid, R., Dröse, S., Brandt, U., Müller, W. E., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500356200 · Cited by 447 · see citing works
Zhu, X.-W., Raina, A., Rottkamp, C., Aliev, G., Perry, G., Boux, H., & Smith, M. A. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00046.x · Cited by 440 · see citing works
Butterfield, D. A., & Kański, J. (2001) · Mechanisms of Ageing and Development · doi:10.1016/s0047-6374(01)00249-4 · Cited by 418 · see citing works
Williams, T. I., Lynn, B. C., Markesbery, W. R., & Lovell, M. A. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.06.004 · Cited by 390 · see citing works
Oxidative stress increases expression and activity of BACE in NT2 neurons
Tamagno, E., Bardini, P., Obbili, A., Vitali, A., Borghi, R., Zaccheo, D., Pronzato, M. A., Danni, O., Smith, M. A., Perry, G., et al. (2002) · Neurobiology of Disease · doi:10.1006/nbdi.2002.0515 · Cited by 385 · see citing works
Generation of superoxide by the mitochondrial Complex I
Grivennikova, V. G., & Vinogradov, A. D. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.03.013 · Cited by 379 · see citing works
Padurariu, M., Ciobica, A., Hritcu, L., Stoica, B., Bild, W., & Stefanescu, C. (2010) · Neuroscience Letters · doi:10.1016/j.neulet.2009.11.033 · Cited by 378 · see citing works
Zhu, X., Rottkamp, C. A., Boux, H., Takeda, A., Perry, G., & Smith, M. A. (2000) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/59.10.880 · Cited by 378 · see citing works
Redox-active iron mediates amyloid-β toxicity
Rottkamp, C. A., Raina, A. K., Zhu, X., Gaier, E., Bush, A. I., Atwood, C., Chevion, M., Perry, G. L., & Smith, M. A. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00494-9 · Cited by 376 · 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
Maynard, C. J., Cappai, R., Volitakis, I., Cherny, R. A., White, A. R., Beyreuther, K. T., Masters, C. L., Bush, A. I., & Li, Q. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204379200 · Cited by 352 · see citing works
Studies on molecular mechanisms of Ginkgo biloba extract
Luo, Y., & Smith, J. V. (2004) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-003-1527-9 · Cited by 344 · see citing works
Tamagno, E., Guglielmotto, M., Aragno, M., Borghi, R., Autelli, R., Giliberto, L., Muraca, G., Danni, O., Zhu, X., Smith, M. A., et al. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.05072.x · Cited by 338 · see citing works
Mitochondrial uncoupling proteins—What is their physiological role?
Echtay, K. S. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.08.011 · Cited by 338 · see citing works
Zheng, W.-H., Bastianetto, S., Mennicken, F., Ma, W., & Kar, S. (2002) · Neuroscience · doi:10.1016/s0306-4522(02)00404-9 · Cited by 321 · see citing works
de la Monte, S. M., & Wands, J. R. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9209 · Cited by 318 · see citing works
Oxidative stress mediates tau-induced neurodegeneration in Drosophila
Dias-Santagata, D., Fulga, T. A., Duttaroy, A., & Feany, M. B. (2007) · Journal of Clinical Investigation · doi:10.1172/jci28769 · Cited by 318 · see citing works
Metal complexing agents as therapies for Alzheimer’s disease
Bush, A. I. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00120-3 · Cited by 310 · see citing works
Phosphorylation of microtubule‐associated protein tau by stress‐activated protein kinases
Goedert, M., Hasegawa, M., Jakes, R., Lawler, S., Cuenda, A., & Cohen, P. R. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00483-3 · Cited by 308 · see citing works
Zou, K., Gong, J.-S., Yanagisawa, K., & Michikawa, M. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-12-04833.2002 · Cited by 305 · see citing works
Copper levels are increased in the cerebral cortex and liver of APP and APLP2 knockout mice
White, A. R., Reyes, R., Mercer, J. F. B., Camakaris, J., Zheng, H., Bush, A. I., Multhaup, G., Beyreuther, K. T., Masters, C. L., & Cappai, R. (1999) · Brain Research · doi:10.1016/s0006-8993(99)01861-2 · Cited by 283 · 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
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
The Production of Amyloid β Peptide Is a Critical Requirement for the Viability of Central Neurons
Plant, L. D., Boyle, J. P., Smith, I. F., Peers, C., & Pearson, H. A. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-13-05531.2003 · Cited by 248 · see citing works
The βA4 amyloid precursor protein binding to copper
Hesse, L., Beher, D., Masters, C. L., & Multhaup, G. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00658-x · Cited by 247 · see citing works
Zn2+ Ions: Modulators of Excitatory and Inhibitory Synaptic Activity
Smart, T. G., Hosie, A. M., & Miller, P. S. (2004) · The Neuroscientist · doi:10.1177/1073858404263463 · Cited by 247 · see citing works
Murakami, K., Murata, N., Noda, Y., Tahara, S., Kaneko, T., Kinoshita, N., Hatsuta, H., Murayama, S., Barnham, K. J., Irie, K., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.279208 · Cited by 241 · see citing works
Yao, M., Nguyen, T. V., & Pike, C. J. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.4736-04.2005 · Cited by 233 · see citing works
Lipid peroxidation and oxidative imbalance: early functional events in Alzheimer's disease
Praticò, D., & Sung, S. (2004) · Journal of Alzheimer s Disease · doi:10.3233/jad-2004-6209 · Cited by 229 · cited 1× · see citing works
“[13] D.”
Amyloid β-Protein Toxicity and the Pathogenesis of Alzheimer Disease
Yankner, B. A., & Lu, T. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800018200 · Cited by 225 · see citing works
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
Mitochondrial abnormalities and oxidative imbalance in Alzheimer disease
Zhu, X., Perry, G. L., Moreira, P. I., Aliev, G. M., Cash, A., Hirai, K., & Smith, M. A. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9207 · Cited by 196 · see citing works
Expression of APP pathway mRNAs and proteins in Alzheimer’s disease
Matsui, T., Ingelsson, M., Fukumoto, H., Ramasamy, K., Kowa, H., Frosch, M. P., Irizarry, M. C., & Hyman, B. T. (2007) · Brain Research · doi:10.1016/j.brainres.2007.05.050 · Cited by 187 · see citing works
Amyloid-β is an antioxidant for lipoproteins in cerebrospinal fluid and plasma
Kontush, A., Berndt, C., Weber, W., Akopyan, V., Arlt, S., Schippling, S., & Beisiegel, U. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00458-5 · Cited by 180 · see citing works
Gene structure and organization of the human β‐secretase ( BACE ) promoter
Sambamurti, K., Kinsey, R., Maloney, B., Ge, Y., & Lahiri, D. K. (2004) · The FASEB Journal · doi:10.1096/fj.03-1378fje · Cited by 179 · see citing works
Apelt, J., Bigl, M., Wunderlich, P., & Schliebs, R. (2004) · International Journal of Developmental Neuroscience · doi:10.1016/j.ijdevneu.2004.07.006 · Cited by 175 · see citing works
Borchardt, T., Camakaris, J., Cappai, R., Masters, C. L., Beyreuther, K. T., & Multhaup, G. (1999) · Biochemical Journal · doi:10.1042/bj3440461 · Cited by 174 · see citing works
Hydrogen Peroxide Promotes Aβ Production through JNK-dependent Activation of γ-Secretase
Shen, C., Chen, Y., Liu, H., Zhang, K., Zhang, T., Lin, A., & Jing, N. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800013200 · Cited by 168 · see citing works
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
Metal Ion Physiopathology in Neurodegenerative Disorders
Bolognin, S., Luigi Messori, A., & Zatta, P. F. (2009) · NeuroMolecular Medicine · doi:10.1007/s12017-009-8102-1 · Cited by 157 · see citing works
Oxidative Regulation of Fatty Acid-Induced Tau Polymerization
Gamblin, T. C., King, M. E., Kuret, J., Berry, R. W., & Binder, L. I. (2000) · Biochemistry · doi:10.1021/bi001876l · Cited by 151 · see citing works
Furuta, A., Price, D. L., Pardo, C. A., Troncoso, J. C., Xu, Z., Taniguchi, N., & Martin, L. J. (1995) · Europe PMC (PubMed Central) · Cited by 151 · see citing works
Increased Expression but Reduced Activity of Antioxidant Enzymes in Alzheimer's Disease
Omar, R., Chyan, Y., Andorn, A. C., Poeggeler, B., Robakis, N. K. R. K., & Pappolla, M. A. (1999) · Journal of Alzheimer s Disease · doi:10.3233/jad-1999-1301 · Cited by 149 · see citing works
Yoo, M., Gu, X., Xu, X.-M., Kim, J. Y., Carlson, B. A., Patterson, A. D., Cai, H., Gladyshev, V. N., & Hatfield, D. L. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2891 · Cited by 148 · see citing works
Oxidative processes in Alzheimer's disease: the role of Aβ-metal interactions
Lynch, T. (2000) · Experimental Gerontology · doi:10.1016/s0531-5565(00)00112-1 · Cited by 148 · see citing works
Targeting Multiple Neurodegenerative Diseases Etiologies with Multimodal-Acting Green Tea Catechins
Mandel, S. A., Amit, T., Kalfon, L., Reznichenko, L., & Youdim, M. B. H. (2008) · Journal of Nutrition · doi:10.1093/jn/138.8.1578s · Cited by 148 · see citing works
Fibrillar β-amyloid evokes oxidative damage in a transgenic mouse model of Alzheimer’s disease
Matsuoka, Y., Picciano, M., LaFrancois, J. J., & Duff, K. (2001) · Neuroscience · doi:10.1016/s0306-4522(01)00115-4 · Cited by 147 · see citing works
Alzheimer's disease & metals: therapeutic opportunities
Kenche, V. B., & Barnham, K. J. (2011) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2011.01221.x · Cited by 144 · see citing works
β-Amyloid Mediated Nitration of Manganese Superoxide Dismutase
Muthuswamy, A., Tangpong, J., Keller, J. N., Murphy, M. P., Markesbery, W. R., Kiningham, K. K., & Clair, D. K. S. (2006) · American Journal Of Pathology · doi:10.2353/ajpath.2006.051223 · Cited by 143 · see citing works
Schlief, M. L., & Gitlin, J. D. (2006) · Molecular Neurobiology · doi:10.1385/mn:33:2:81 · Cited by 140 · see citing works
Dumont, M., Stack, C., Elipenahli, C., Jainuddin, S., Gerges, M., Starkova, N. N., Yang, L., Starkov, A. A., & Beal, F. M. (2011) · The FASEB Journal · doi:10.1096/fj.11-186650 · Cited by 139 · see citing works
Neuronal RNA oxidation is a prominent feature of familial Alzheimer's disease
Nunomura, A., Chiba, S., Lippa, C. F., Cras, P. P., Kalaria, R. N., Takeda, A., Honda, K., Smith, M. A., & Perry, G. L. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2004.06.003 · Cited by 137 · see citing works
Lee, J., Mook‐Jung, I., & Koh, J. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-11-j0002.1999 · Cited by 136 · see citing works
Dong, M., Peng, B., Lin, X., Zhao, J., Zhou, Y.-R., & Wang, R. (2007) · Age and Ageing · doi:10.1093/ageing/afm128 · Cited by 132 · see citing works
Wan, L., Nie, G., Zhang, J., Luo, Y., Zhang, P., Zhang, Z., & Zhao, B. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.10.707 · Cited by 121 · see citing works
Self-citationChen, L., Na, R., Gu, M., Richardson, A. G., & Ran, Q. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05603.x · Cited by 119 · see citing works
Abdul, H. M., Rukhsana Sultana, A., Keller, J. N., Clair, D. K. S., Markesbery, W. R., & Butterfield, D. A. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03647.x · Cited by 114 · see citing works
Copper Promotes the Trafficking of the Amyloid Precursor Protein
Acevedo, K. M., Hung, Y. H., Dalziel, A. H., Li, Q., Laughton, K. M., Wikhe, K., Rembach, A., Roberts, B. R., Masters, C. L., Bush, A. I., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.128512 · Cited by 104 · see citing works
Bellingham, S. A., Ciccotosto, G. D., Needham, B. E., Fodero, L. R., White, A. R., Masters, C. L., Cappai, R., & Camakaris, J. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02731.x · Cited by 100 · see citing works
Abundant expression of zinc transporters in the amyloid plaques of Alzheimer's disease brain
Zhang, L., Wang, X., Stoltenberg, M., Danscher, G., Huang, L., & Wang, Z. (2008) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2008.03.014 · Cited by 97 · see citing works
Divalent metal transporter 1 is involved in amyloid precursor protein processing and Aβ generation
Zheng, W. H., Xin, N., Chi, Z., Zhao, B.-L., Zhang, J., Li, J., & Wang, Z. (2009) · The FASEB Journal · doi:10.1096/fj.09-135749 · Cited by 95 · see citing works
Self-citationIron deficiency on neuronal function
Muñoz, P., & Humeres, A. (2012) · BioMetals · doi:10.1007/s10534-012-9550-x · Cited by 92 · see citing works
Quiroz‐Baez, R., Rojas, E., & Arias, C. (2009) · Neurochemistry International · doi:10.1016/j.neuint.2009.06.012 · Cited by 92 · see citing works
Rodrigues, C. M. P., Solá, S., Brito, M. A., Brondino, C. D., Brites, D. M. T. O., & Moura, J. J. G. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.4370 · Cited by 89 · see citing works
Deletion of vitamin E enhances phenotype of Alzheimer disease model mouse
Nishida, Y., Yokota, T., Takahashi, T., Uchihara, T., Jishage, K.-I., & Mizusawa, H. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.09.083 · Cited by 86 · see citing works
Expression of a truncated tau protein induces oxidative stress in a rodent model of tauopathy
Cente, M., Filipcik, P., Pevalova, M., & Novak, M. (2006) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2006.04986.x · Cited by 82 · see citing works
Intraneuronal amyloid β accumulation and oxidative damage to nucleic acids in Alzheimer disease
Nunomura, A., Tamaoki, T., Tanaka, K., Motohashi, N., Nakamura, M., Hayashi, T., Yamaguchi, H., Shimohama, S., Lee, H., Zhu, X., et al. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.12.012 · Cited by 80 · see citing works
Oxidative stress up-regulates presenilin 1 in lipid rafts in neuronal cells
Oda, A., Tamaoka, A., & Araki, W. (2010) · Journal of Neuroscience Research · doi:10.1002/jnr.22271 · Cited by 76 · see citing works
Altered expression and distribution of zinc transporters in APP/PS1 transgenic mouse brain
Zhang, L., Wang, X., Zheng, Z., Ren, H., Stoltenberg, M., Danscher, G., Huang, L., Rong, M., & Wang, Z. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.02.018 · Cited by 69 · see citing works
Nicotine attenuates the β‐amyloid neurotoxicity through regulating metal homeostasis
Zhang, J., Liu, Q., Chen, Q., Liu, N.-Q., Li, F., Lu, Z., Qin, C., Zhu, H., Huang, Y., He, W., et al. (2006) · The FASEB Journal · doi:10.1096/fj.05-5214fje · Cited by 69 · see citing works
Self-citationFormation of Phospho-SAPK/JNK Granules in the Hippocampus Is an Early Event in Alzheimer Disease
Lagalwar, S., Guillozet-Bongaarts, A. L., Berry, R. W., & Binder, L. I. (2006) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000229236.98124.d8 · Cited by 64 · see citing works
JKK1, an upstream activator of JNK/SAPK, is activated in Alzheimer's disease
Zhu, X.-W., Ogawa, O., Wang, Y., Perry, G., & Smith, M. A. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01645.x · Cited by 61 · see citing works
Physiological levels of β-amyloid peptide promote PC12 cell proliferation
Luo, Y., Sunderland, T., Roth, G. S., & Wolozin, B. L. (1996) · Neuroscience Letters · doi:10.1016/0304-3940(96)13087-1 · Cited by 49 · see citing works
Behavioral Improvement after Chronic Administration of Coenzyme Q10 in P301S Transgenic Mice
Elipenahli, C., Stack, C., Jainuddin, S., Gerges, M., Yang, L., Starkov, A. A., Beal, M. F., & Dumont, M. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-111190 · Cited by 48 · see citing works
Superoxide Anion Regulates the Mitochondrial Free Ca 2+ Through Uncoupling Proteins
Wu, Z., Zhang, J., & Zhao, B. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2427 · Cited by 47 · see citing works
Self-citationSteiner, H. (2004) · Current Alzheimer Research · doi:10.2174/1567205043332081 · Cited by 45 · see citing works
Nicotine attenuates beta-amyloid-induced neurotoxicity by regulating metal homeostasis.
Zhang, Liu, Chen, Nq, Li, ., F., Lu, Zb, Qin, L., Zhu, Z., et al. (2006) · 中国生物学文摘 · Cited by 39 · see citing works
Natural antioxidants in prevention and management of Alzheimer's disease
Zhao, Y. (2011) · Frontiers in Bioscience-Elite · doi:10.2741/419 · Cited by 35 · see citing works
Self-citationCente, M., Filipčík, P., Mandakova, S., Žilka, N., Krajciova, G., & Novák, M. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1107 · Cited by 31 · see citing works
Membrane-inserted conformation of transmembrane domain 4 of divalent-metal transporter
Hongyan, L. I., Li, F., Sun, H., & Qian, Z. (2003) · Biochemical Journal · doi:10.1042/bj20030075 · Cited by 31 · see citing works
Metal Metabolic Homeostasis Disruption and Early Initiation of Mechanism for Alzheimer′s Disease*
Zhao, B., & Wan, L. (2012) · PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS · doi:10.3724/sp.j.1206.2012.00297 · Cited by 4 · see citing works
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Oxidative Stress: A Key Modulator in Neurodegenerative Diseases
Singh, A., Kukreti, R., Saso, L., & Kukreti, S. (2019) · Molecules · doi:10.3390/molecules24081583 · Cited by 2,305 · see citing works
Oxidative stress and the amyloid beta peptide in Alzheimer’s disease
Cheignon, C., Tomas, M., Bonnefont-Rousselot, D., Faller, P., Hureau, C., & Collin, F. (2018) · Redox Biology · doi:10.1016/j.redox.2017.10.014 · Cited by 2,185 · see citing works
Bhatti, J. S., Bhatti, G. K., & Reddy, P. H. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.11.010 · Cited by 1,655 · see citing works
The role of oxidative stress in neurodegenerative diseases
Kim, G. H., Kim, J. E., Rhie, S. J., & Yoon, S. (2015) · Experimental Neurobiology · doi:10.5607/en.2015.24.4.325 · Cited by 1,355 · see citing works
Role of pro-inflammatory cytokines released from microglia in Alzheimer's disease.
(2015) · Europe PMC (PubMed Central) · doi:10.3978/j.issn.2305-5839.2015.03.49 · Cited by 1,288 · see citing works
Oxidative stress and mitochondrial dysfunction-linked neurodegenerative disorders
Islam, M. T. (2016) · Neurological Research · doi:10.1080/01616412.2016.1251711 · Cited by 989 · see citing works
Oxidative stress, mitochondrial dysfunction and neurodegenerative diseases; a mechanistic insight
Bhat, A. H., Dar, K. B., Anees, S., Zargar, M. A., Masood, A., Sofi, M. A., & Ganie, S. A. (2015) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2015.07.025 · Cited by 938 · see citing works
Oxidative Stress in Human Pathology and Aging: Molecular Mechanisms and Perspectives
Hajam, Y. A., Rani, R., Ganie, S. Y., Sheikh, T. A., Javaid, D., Qadri, S. S., Pramodh, S., Alsulimani, A., Alkhanani, M. F., Harakeh, S., et al. (2022) · Cells · doi:10.3390/cells11030552 · Cited by 915 · see citing works
Pisoschi, A. M., Pop, A., Iordache, F., Stanca, L., Predoi, G., & Șerban, A. I. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112891 · Cited by 849 · see citing works
Chemical Basis of Reactive Oxygen Species Reactivity and Involvement in Neurodegenerative Diseases
Collin, F. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20102407 · Cited by 822 · see citing works
Oxidative stress in Alzheimer’s disease
Chen, Z., & Zhong, C. (2014) · Neuroscience Bulletin · doi:10.1007/s12264-013-1423-y · Cited by 797 · see citing works
Apoptosis and Oxidative Stress in Neurodegenerative Diseases
Radi, E., Formichi, P., Battisti, C., & Federico, A. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-132738 · Cited by 632 · see citing works
Savelieff, M. G., Nam, G., Kang, J., Lee, H. J., Lee, M., & Lim, M. H. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00138 · Cited by 603 · see citing works
Microglia, neuroinflammation, and beta-amyloid protein in Alzheimer’s disease
Cai, Z., Hussain, M. D., & Yan, L.-J. (2014) · International Journal of Neuroscience · doi:10.3109/00207454.2013.833510 · Cited by 583 · see citing works
Ageing, age-related diseases and oxidative stress: What to do next?
Luo, J., Mills, K., le Cessie, S., Noordam, R., & van Heemst, D. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2019.100982 · Cited by 581 · see citing works
Brain Photobiomodulation Therapy: a Narrative Review
Salehpour, F., Mahmoudi, J., Kamari, F., Sadigh‐Eteghad, S., Rasta, S. H., & Hamblin, M. R. (2018) · Molecular Neurobiology · doi:10.1007/s12035-017-0852-4 · Cited by 534 · see citing works
Effect of High-Fat Diets on Oxidative Stress, Cellular Inflammatory Response and Cognitive Function
Tan, B. L., & Norhaizan, M. E. (2019) · Nutrients · doi:10.3390/nu11112579 · Cited by 525 · see citing works
Blázquez, E., Velázquez, E., Hurtado-Carneiro, V., & Ruiz-Albusac, J. M. (2014) · Frontiers in Endocrinology · doi:10.3389/fendo.2014.00161 · Cited by 502 · see citing works
Activation of microglia and astrocytes: a roadway to neuroinflammation and Alzheimer’s disease
Kaur, D., Sharma, V., & Deshmukh, R. R. (2019) · Inflammopharmacology · doi:10.1007/s10787-019-00580-x · Cited by 492 · see citing works
Rutin as a Potent Antioxidant: Implications for Neurodegenerative Disorders
Enogieru, A. B., Haylett, W. L., Hiss, D. C., Bardien, S., & Ekpo, O. E. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/6241017 · Cited by 483 · see citing works
Leyane, T. S., Jere, S. W., & Houreld, N. N. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23137273 · Cited by 510 · see citing works
Molecular Pathogenesis of Alzheimer's Disease: An Update
Sanabria‐Castro, A., Echeverría, I. A., & Bonilla, C. M. (2017) · Annals of Neurosciences · doi:10.1159/000464422 · Cited by 419 · see citing works
Bisht, K., Sharma, K. P., & Tremblay, M. (2018) · Neurobiology of Stress · doi:10.1016/j.ynstr.2018.05.003 · Cited by 351 · see citing works
Neurodegenerative and neurological disorders by small inhaled particles
Heusinkveld, H. J., Wahle, T., Campbell, A., Westerink, R. H. S., Tran, L., Johnston, H. J., Stone, V., Cassee, F. R., & Schins, R. P. F. (2016) · NeuroToxicology · doi:10.1016/j.neuro.2016.07.007 · Cited by 358 · see citing works
Melatonin and its metabolites vs oxidative stress: From individual actions to collective protection
Galano, A., & Reiter, R. J. (2018) · Journal of Pineal Research · doi:10.1111/jpi.12514 · Cited by 361 · see citing works
Heavy Metals Exposure and Alzheimer’s Disease and Related Dementias
Bakulski, K. M., Seo, Y. A., Hickman, R. C., Brandt, D. J., Vadari, H. S., Hu, H., & Park, S. K. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200282 · Cited by 355 · see citing works
Copper Dyshomeostasis in Neurodegenerative Diseases—Therapeutic Implications
Gromadzka, G., Tarnacka, B., Flaga, A., & Adamczyk, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21239259 · Cited by 339 · see citing works
Sharma, P., Srivastava, P., Seth, A., Tripathi, P. N., Banerjee, A. G., & Shrivastava, S. K. (2019) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.12.006 · Cited by 331 · see citing works
Guzior, N., Wi.eckowska, A., Panek, D., & Malawska, B. (2014) · Current Medicinal Chemistry · doi:10.2174/0929867321666141106122628 · Cited by 323 · see citing works
Oxidative Stress in Autism Spectrum Disorder
Bjørklund, G., Meguid, N. A., El-Bana, M. A., Tinkov, A. A., Saad, K., Dadar, M., Hemimi, M., Skalny, A. V., Hosnedlová, B., Kizek, R., et al. (2020) · Molecular Neurobiology · doi:10.1007/s12035-019-01742-2 · Cited by 323 · see citing works
The Mechanisms of Action of Curcumin in Alzheimer’s Disease
Tang, M., & Taghibiglou, C. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170188 · Cited by 305 · see citing works
Oxidative stress, protein modification and Alzheimer disease
Tramutola, A., Lanzillotta, C., Perluigi, M., & Butterfield, D. A. (2017) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.06.005 · Cited by 303 · 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
Galano, A., & Alvarez-Idaboy, J. R. (2018) · International Journal of Quantum Chemistry · doi:10.1002/qua.25665 · Cited by 282 · see citing works
Harris, S. A., & Harris, E. A. (2015) · Journal of Alzheimer's Disease · doi:10.3233/jad-142853 · Cited by 279 · see citing works
Oxidative stress in alzheimer’s disease: A review on emergent natural polyphenolic therapeutics
Cassidy, L., Fernandez, F., Johnson, J. B., Naiker, M., Owoola, A. G., & Broszczak, D. A. (2019) · Complementary Therapies in Medicine · doi:10.1016/j.ctim.2019.102294 · Cited by 283 · see citing works
Manganese Superoxide Dismutase and Oxidative Stress Modulation
Bresciani, G., da Cruz, I. B. M., & González‐Gallego, J. (2015) · Advances in clinical chemistry · doi:10.1016/bs.acc.2014.11.001 · Cited by 285 · see citing works
Bonfili, L., Cecarini, V., Cuccioloni, M., Angeletti, M., Berardi, S., Scarpona, S., Rossi, G., & Eleuteri, A. M. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-0973-4 · Cited by 277 · see citing works
Combating oxidative stress disorders with citrus flavonoid: Naringenin
Zaidun, N. H., Thent, Z. C., & Latiff, A. A. (2018) · Life Sciences · doi:10.1016/j.lfs.2018.07.017 · Cited by 266 · see citing works
Circulating microRNAs as potential biomarkers for psychiatric and neurodegenerative disorders
van den Berg, M. M. J., Krauskopf, J., Ramaekers, J. G., Kleinjans, J. C. S., Prickaerts, J., & Briedé, J. J. (2019) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2019.101732 · Cited by 253 · see citing works
Jazvinšćak Jembrek, M., Hof, P. R., & Šimić, G. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/346783 · Cited by 244 · see citing works
On the role of 4-hydroxynonenal in health and disease
Csala, M., Kardon, T., Legeza, B., Lizák, B., Mandl, J., Margittai, É., Puskás, F., Száraz, P., Szelényi, P., & Bánhegyi, G. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.01.015 · Cited by 244 · see citing works
A molecular approach in drug development for Alzheimer’s disease
Agatonović-Kuštrin, S., Kettle, C., & Morton, D. W. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.06.147 · Cited by 236 · see citing works
Mancuso, C., & Santangelo, R. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2017.12.009 · Cited by 232 · see citing works
Protein Posttranslational Modifications: Roles in Aging and Age‐Related Disease
Santos, A. L., & Lindner, A. B. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/5716409 · Cited by 225 · see citing works
The Key Role of Mitochondrial Function in Health and Disease
San-Millán, I. (2023) · Antioxidants · doi:10.3390/antiox12040782 · Cited by 229 · see citing works
New insights into the role of mitochondrial dynamics in oxidative stress-induced diseases
Chen, S., Li, Q., Shi, H., Li, F., Duan, Y., & Guo, Q. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.117084 · Cited by 234 · see citing works
Bhatia, V., & Sharma, S. (2020) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2020.117253 · Cited by 226 · see citing works
Pinton, S., Sampaio, T. B., Savall, A. S. P., & Gutierrez, M. Z. (2017) · Neural Regeneration Research · doi:10.4103/1673-5374.205084 · Cited by 219 · see citing works
Mitochondrial Dysfunction: a Potential Therapeutic Target to Treat Alzheimer’s Disease
Nand, S., Singh, C., Singh, A., Singh, M. P., & Singh, S. P. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-01945-y · Cited by 213 · see citing works
Liu, Z., Li, T., Li, P., Wei, N., Zhao, Z., Liang, H., Ji, X., Chen, W., Xue, M., & Wei, J. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/352723 · Cited by 208 · see citing works
OxInflammation: From Subclinical Condition to Pathological Biomarker
Valacchi, G., Virgili, F., Cervellati, C., & Pecorelli, A. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00858 · Cited by 206 · see citing works
Getting to the Heart of Alzheimer Disease
Tublin, J. M., Adelstein, J. M., del Monte, F., Combs, C. K., & Wold, L. E. (2019) · Circulation Research · doi:10.1161/circresaha.118.313563 · Cited by 188 · see citing works
Oxidative Stress-Mediated Blood-Brain Barrier (BBB) Disruption in Neurological Diseases
Song, K., Li, Y., Zhang, H., An, N., Wei, Y., Wang, L., Tian, C., Yuan, M., Sun, Y., Xing, Y., et al. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/4356386 · Cited by 199 · see citing works
The neuroinflammatory response of postoperative cognitive decline
Vacas, S., Degos, V., Feng, X., & Maze, M. (2013) · British Medical Bulletin · doi:10.1093/bmb/ldt006 · Cited by 190 · see citing works
Biomarkers of lipid peroxidation in Alzheimer disease (AD): an update
Bradley‐Whitman, M. A., & Lovell, M. A. (2015) · Archives of Toxicology · doi:10.1007/s00204-015-1517-6 · Cited by 192 · see citing works
Hypoxia, Oxidative Stress, and Inflammation: Three Faces of Neurodegenerative Diseases
Merelli, A., Repetto, M. G., Lazarowski, A., & Auzmendi, J. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-201074 · Cited by 182 · see citing works
Protein Oxidation in Aging: Does It Play a Role in Aging Progression?
Reeg, S., & Grune, T. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6062 · Cited by 179 · see citing works
Consequences of Disturbing Manganese Homeostasis
Baj, J., Flieger, W., Barbachowska, A., Kowalska, B., Flieger, M., Forma, A., Teresiński, G., Portincasa, P., Buszewicz, G., Radzikowska-Büchner, E., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241914959 · Cited by 184 · see citing works
Hussien, H. M., Abd-Elmegied, A., Ghareeb, D. A., Hafez, H. S., Ahmed, H. E. A., & Moneam, N. M. A. E. (2017) · Food and Chemical Toxicology · doi:10.1016/j.fct.2017.11.025 · Cited by 176 · see citing works
Suganthy, N., Ramkumar, V. S., Pugazhendhi, A., Benelli, G., & Archunan, G. (2017) · Environmental Science and Pollution Research · doi:10.1007/s11356-017-9789-4 · Cited by 178 · see citing works
Effects of Vitamin E on Cognitive Performance during Ageing and in Alzheimer’s Disease
Fata, G. L., Weber, P., & Mohajeri, M. H. (2014) · Nutrients · doi:10.3390/nu6125453 · Cited by 174 · see citing works
Role of Vitamin E in the Treatment of Alzheimer’s Disease: Evidence from Animal Models
Gugliandolo, A., Bramanti, P., & Mazzon, E. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18122504 · Cited by 167 · see citing works
Lü, Y., Guo, Z., Zhang, Y., Li, C., Zhang, Y., Guo, Q., Chen, Q., Chen, X., He, X., Liu, L., et al. (2018) · Advanced Science · doi:10.1002/advs.201801586 · Cited by 162 · see citing works
Ghag, G., Bhatt, N. N., Cantu, D. V., Guerrero‐Munoz, M. J., Ellsworth, A., Sengupta, U., & Kayed, R. (2018) · Protein Science · doi:10.1002/pro.3499 · Cited by 156 · see citing works
Isoprostanes and Neuroprostanes as Biomarkers of Oxidative Stress in Neurodegenerative Diseases
Miller, E. D., Morel, A., Saso, L., & Saluk, J. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/572491 · Cited by 154 · see citing works
Aureliano, M., Sousa‐Coelho, A. L. D., Dolan, C. C., Roess, D. A., & Crans, D. C. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24065382 · Cited by 156 · see citing works
Molecular Mechanisms for Herpes Simplex Virus Type 1 Pathogenesis in Alzheimer’s Disease
Harris, S. A., & Harris, E. A. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00048 · Cited by 147 · see citing works
Kong, Y. R., Jong, Y. X., Balakrishnan, M., Bok, Z. K., Weng, J. K. K., Tay, K. C., Goh, B. H., Ong, Y. S., Chan, K., Lee, L., et al. (2021) · Biology · doi:10.3390/biology10040287 · Cited by 168 · see citing works
Tan, S. H., Karri, V., Tay, N. W. R., Chang, K. H., Ah, H. Y., Ng, P. Q., Ho, H. S., Keh, H. W., & Candasamy, M. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.12.101 · Cited by 148 · see citing works
Glial cells in Alzheimer’s disease: From neuropathological changes to therapeutic implications
Uddin, M. S., & Lim, L. W. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101622 · Cited by 149 · see citing works
Quirici, V., Guerrero, C. J., Krause, J. S., Wingfield, J. C., & Vásquez, R. A. (2016) · Frontiers in Zoology · doi:10.1186/s12983-016-0133-5 · Cited by 145 · see citing works
Ionizing radiation, antioxidant response and oxidative damage: A meta-analysis
Einor, D., Bonisoli‐Alquati, A., Costantini, D., Mousseau, T. A., & Møller, A. P. (2016) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2016.01.027 · Cited by 139 · see citing works
Birnbaum, J. H., Wanner, D., Gietl, A. F., Saake, A., Kündig, T. M., Hock, C., Nitsch, R. M., & Tackenberg, C. (2018) · Stem Cell Research · doi:10.1016/j.scr.2018.01.019 · Cited by 135 · see citing works
Oxidant/antioxidant imbalance and the risk of Alzheimer's disease
Moneim, A. (2015) · Current Alzheimer Research · doi:10.2174/1567205012666150325182702 · Cited by 136 · see citing works
Natural Tripeptide-Based Inhibitor of Multifaceted Amyloid β Toxicity
Rajasekhar, K., Madhu, C., & Govindaraju, T. (2016) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6b00175 · Cited by 136 · see citing works
Qin, X.-Y., Cao, C., Cawley, N. X., Liu, T.-T., Yuan, J., Loh, Y. P., & Cheng, Y. (2016) · Molecular Psychiatry · doi:10.1038/mp.2016.62 · Cited by 135 · see citing works
Metallothionein in Brain Disorders
Juárez-Rebollar, D., Rı́os, C., Nava-Ruíz, C., & Méndez‐Armenta, M. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/5828056 · Cited by 134 · see citing works
Chakrabarti, S., Kumar Khemka, V., Banerjee, A., Chatterjee, G., Ganguly, A., & Biswas, A. (2015) · Aging and disease · doi:10.14336/ad.2014.002 · Cited by 134 · see citing works
Cheignon, C., Jones, M., Atrián-Blasco, E., Kieffer, I., Faller, P., Collin, F., & Hureau, C. (2017) · Chemical Science · doi:10.1039/c7sc00809k · Cited by 132 · see citing works
Rehman, M. U., Sehar, N., Dar, N. J., Khan, A., Arafah, A., Rashid, S., Rashid, S. M., & Ganaie, M. A. (2023) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2022.104961 · Cited by 130 · see citing works
Reactive Oxygen Species: Physiological Roles in the Regulation of Vascular Cells
Vara, D. S., & Pula, G. (2014) · Current Molecular Medicine · doi:10.2174/1566524014666140603114010 · Cited by 130 · see citing works
Jacobs, K. R., Lim, C. K., Blennow, K., Zetterberg, H., Chatterjee, P., Martins, R. N., Brew, B. J., Guillemin, G. J., & Lovejoy, D. B. (2019) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2019.03.015 · Cited by 127 · see citing works
Walker, J., & Harrison, F. E. (2015) · Nutrients · doi:10.3390/nu7095341 · Cited by 127 · see citing works
Caruso, G., Fresta, C. G., Musso, N., Giambirtone, M., Grasso, M., Spampinato, S. F., Merlo, S., Drago, F., Lazzarino, G., Sortino, M. A., et al. (2019) · Cells · doi:10.3390/cells8010064 · Cited by 129 · see citing works
Mitochondrial Dysfunction in Neural Injury
Zhao, X., Lu, M., Yuan, D., Xu, D.-E., Yao, P.-P., Ji, W., Chen, H., Liu, W., Yan, C.-X., Xia, Y., et al. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00030 · Cited by 126 · see citing works
Zhang, Z., & Schluesener, H. J. (2013) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e318283114a · Cited by 125 · see citing works
Dietary phytochemicals and neuro-inflammaging: from mechanistic insights to translational challenges
Davinelli, S., Maes, M., Corbi, G., Zarrelli, A., Willcox, D. C., & Scapagnini, G. (2016) · Immunity & Ageing · doi:10.1186/s12979-016-0070-3 · Cited by 122 · see citing works
Viral infections and their relationship to neurological disorders
Wouk, J., Rechenchoski, D. Z., Rodrigues, B. C. D., Ribelato, E. V., & Galhardi, L. C. F. (2021) · Archives of Virology · doi:10.1007/s00705-021-04959-6 · Cited by 122 · see citing works
Marzia Perluigi, A., Domenico, F. D., Barone, E., & Butterfield, D. A. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.04.025 · Cited by 121 · see citing works
Sharifi-Rad, J., Rapposelli, S., Sestito, S., Herrera-Bravo, J., Arancibia-Diaz, A., Salazar, L. A., Yeskaliyeva, B., Beyatli, A., Leyva-Gómez, G., González-Contreras, C., et al. (2022) · Journal of Personalized Medicine · doi:10.3390/jpm12091515 · Cited by 125 · see citing works
Mitochondrial Biology and Neurological Diseases
Arun, S., Liu, L., & Donmez, G. (2016) · Current Neuropharmacology · doi:10.2174/1570159x13666150703154541 · Cited by 113 · see citing works
Scassellati, C., Galoforo, A. C., Bonvicini, C., Esposito, C., & Ricevuti, G. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101138 · Cited by 121 · see citing works
Advances in Mid-Infrared Spectroscopy-Based Sensing Techniques for Exhaled Breath Diagnostics
Selvaraj, R., Vasa, N. J., Nagendra, S. M. S., & Mizaikoff, B. (2020) · Molecules · doi:10.3390/molecules25092227 · Cited by 112 · see citing works
Uddin, M. S., Mamun, A. A., Kabir, M. T., Jakaria, M., Mathew, B., Barreto, G. E., & Ashraf, G. M. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1420-2 · Cited by 110 · 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 110 · see citing works
Zhao, Y., Dang, M., Zhang, W., Lei, Y., Ramesh, T., Veeraraghavan, V. P., & Hou, X. (2020) · Journal of Functional Foods · doi:10.1016/j.jff.2020.104009 · Cited by 110 · see citing works
Self-citationNew Insights into Oxidative Stress and Inflammatory Response in Neurodegenerative Diseases
Scarian, E., Viola, C., Dragoni, F., Gerlando, R. D., Rizzo, B., Diamanti, L., Gagliardi, S., Bordoni, M., & Pansarasa, O. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25052698 · Cited by 115 · see citing works
Asghar, N., Naqvi, S. A. R., Hussain, Z., Rasool, N., Khan, Z. A., Shahzad, S. A., Sherazi, T. A., Janjua, M. R. S. A., Nagra, S. A., Zia‐Ul‐Haq, M., et al. (2016) · Chemistry Central Journal · doi:10.1186/s13065-016-0149-0 · Cited by 109 · see citing works
Uddin, M. S., Mamun, A. A., Hossain, M. S., Akter, F., Iqbal, M. A., & Asaduzzaman, M. (2016) · Annals of Neurosciences · doi:10.1159/000449482 · Cited by 109 · see citing works
- 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 · 2012: 1
- 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
- Health Sciences › Medicine › Physiology › 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
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