Cited by 794Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

The DOI matches its Crossref record; 58 of the 58 references it cites were found in a registry or an index.

Amyloid β-peptide (1-42)-induced Oxidative Stress and Neurotoxicity: Implications for Neurodegeneration in Alzheimer's Disease Brain. A Review

Allan Butterfield, D.·2002·Free Radical Research

DOI 10.1080/1071576021000049890

Open this paper in CoChat — free account

Abstract

Oxidative stress, manifested by protein oxidation, lipid peroxidation, DNA oxidation and 3-nitrotyrosine formation, among other indices, is observed in Alzheimer's disease (AD) brain. Amyloid beta-peptide (1-42) [Abeta(1-42)] may be central to the pathogenesis of AD. Our laboratory and others have implicated Abeta(1-42)-induced free radical oxidative stress in the neurodegeneration observed in AD brain. This paper reviews some of these studies from our laboratory. Recently, we showed both in-vitro and in-vivo that methionine residue 35 (Met-35) of Abeta(1-42) was critical to its oxidative stress and neurotoxic properties. Because the C-terminal region of Abeta(1-42) is helical, and invoking the i + 4 rule of helices, we hypothesized that the carboxyl oxygen of lle-31, known to be within a van der Waals distance of the S atom of Met-35, would interact with the latter. This interaction could alter the susceptibility for oxidation of Met-35, i.e. free radical formation. Consistent with this hypothesis, substitution of lle-31 by the helix-breaking amino acid, proline, completely abrogated the oxidative stress and neurotoxic properties of Abeta(1-42). Removal of the Met-35 residue from the lipid bilayer by substitution of the negatively charged Asp for Gly-37 abrogated oxidative stress and neurotoxic properties of Abeta(1-42). The free radical scavenger vitamin E prevented A(beta (1-42)-induced ROS formation, protein oxidation, lipid peroxidation, and neurotoxicity in hippocampal neurons, consistent with our model for Abeta-associated free radical oxidative stress induced neurodegeneration in AD. ApoE, allele 4, is a risk factor for AD. Synaptosomes from apoE knock-out mice are more vulnerable to Abeta-induced oxidative stress (protein oxidation, lipid peroxidation, and ROS generation) than are those from wild-type mice. We also studied synaptosomes from allele-specific human apoE knock-in mice. Brain membranes from human apoE4 mice have greater vulnerability to Abeta(1-42)-induced oxidative stress than brain membranes from apoE2 or E3, assessed by the same indices, consistent with the notion of a coupling of the oxidative environment in AD brain and increased risk of developing this disorder. Using immunoprecipitation of proteins from AD and control brain obtained no longer than 4h PMI, selective oxidized proteins were identified in the AD brain. Creatine kinase (CK) and beta-actin have increased carbonyl groups, an index of protein oxidation, and Glt-1, the principal glutamate transporter, has increased binding of the lipid peroxidation product, 4-hydroxy-2-nonenal (HNE). Abeta inhibits CK and causes lipid peroxidation, leading to HNE formation. Implications of these findings relate to decreased energy utilization, altered assembly of cytoskeletal proteins, and increased excitotoxicity to neurons by glutamate, all reported for AD. Other oxidatively modified proteins have been identified in AD brain by proteomics analysis, and these oxidatively-modified proteins may be related to increased excitotoxicity (glutamine synthetase), aberrant proteasomal degradation of damaged or aggregated proteins (ubiquitin C-terminal hydrolase L-1), altered energy production (alpha-enolase), and diminished growth cone elongation and directionality (dihydropyrimindase-related protein 2). Taken together, these studies outlined above suggest that Met-35 is key to the oxidative stress and neurotoxic properties of Abeta(1-42) and may help explain the apoE allele dependence on risk for AD, some of the functional and structural alterations in AD brain, and strongly support a causative role of Abeta(1-42)-induced oxidative stress and neurodegeneration in AD.

Integrity signals

Registry

Crossref · 10.1080/1071576021000049890

Cites

58 of 58 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Free radicals in biology and medicine
Gutteridge, J. M. C. (1991) · General Pharmacology The Vascular System · doi:10.1016/0306-3623(91)90478-o · Cited by 17,178
Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
Esterbauer, H., Schaur, R. J., & Zollner, H. (1991) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(91)90192-6 · Cited by 6,672
Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291
Apolipoprotein E: Cholesterol Transport Protein with Expanding Role in Cell Biology
Mahley, R. W. (1988) · Science · doi:10.1126/science.3283935 · Cited by 4,028
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
Excess brain protein oxidation and enzyme dysfunction in normal aging and in Alzheimer disease.
Smith, C. D., Carney, J. M., Starke-Reed, P. E., Oliver, C. N., Stadtman, E. R., Floyd, R. A., & Markesbery, W. R. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.23.10540 · Cited by 1,296
Amyloid β-Protein Fibrillogenesis
Walsh, D. M., Hartley, D. M., Kusumoto, Y., Fezoui, Y., Condron, M. M., Lomakin, A., Benedek, G. B., Selkoe, D. J., & Teplow, D. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25945 · Cited by 1,046
Lipid peroxidation and protein oxidation in Alzheimer’s disease brain: potential causes and consequences involving amyloid β-peptide-associated free radical oxidative stress
Butterfield, D. A., & Lauderback, C. M. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00794-3 · Cited by 1,013
Impaired Proteasome Function in Alzheimer's Disease
Keller, J. N., Hanni, K. B., & Markesbery, W. R. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0750436.x · Cited by 848
A Role for 4‐Hydroxynonenal, an Aldehydic Product of Lipid Peroxidation, in Disruption of Ion Homeostasis and Neuronal Death Induced by Amyloid β‐Peptide
Mark, R. J., Lovell, M. A., Markesbery, W. R., Uchida, K., & Mattson, M. P. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.68010255.x · Cited by 781

Show all 58 references

Sorted by citations

Items 301–400 of 794

Swedish amyloid precursor protein mutation increases phosphorylation of eIF2α in vitro and in vivo
Kim, H., Choi, Y., Shin, K. Y., Joo, Y., Lee, Y., Jung, S. Y., Suh, Y., & Kim, J. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21267 · Cited by 49
Rosiglitazone activation of PPARγ-dependent pathways is neuroprotective in human neural stem cells against amyloid-beta–induced mitochondrial dysfunction and oxidative stress
Chiang, M., Nicol, C. J. B., Cheng, Y., Lin, K., Yen, C., & Lin, C. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.01.132 · Cited by 52
Amyloid-beta and tau proteins as biochemical markers of Alzheimer's disease
Sobów, T., Flirski, M., & Liberski, P. P. (2004) · Acta Neurobiologiae Experimentalis · doi:10.55782/ane-2004-1491 · Cited by 53
Proteomics‐driven progress in neurodegeneration research
Fountoulakis, M., & Κοσσίδα, Σ. (2006) · Electrophoresis · doi:10.1002/elps.200500738 · Cited by 52
Neuroprotective Effects of Resveratrol on Damages of Mouse Cortical Neurons Induced by β-amyloid through Activation of SIRT1/Akt1 Pathway
Zhang, J., Feng, X., Wu, J., Xu, H., Li, G., Zhu, D., Yue, Q., Liu, H., Zhang, Y., Sun, D., et al. (2014) · BioFactors · doi:10.1002/biof.1149 · Cited by 50
Behavioral stress causes mitochondrial dysfunction via ABAD up-regulation and aggravates plaque pathology in the brain of a mouse model of Alzheimer disease
Seo, J., Lee, K.-W., Kim, T., Baek, I., Im, J., & Han, P. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.02.035 · Cited by 51
Common biochemical defects linkage between post-traumatic stress disorders, mild traumatic brain injury (TBI) and penetrating TBI
Prasad, K. N., & Bondy, S. C. (2014) · Brain Research · doi:10.1016/j.brainres.2014.12.038 · Cited by 54
Amyloid β-induced erythrocytic damage and its attenuation by carotenoids
Nakagawa, K., Kiko, T., Miyazawa, T., Sookwong, P., Tsuduki, T., Satoh, A., & Miyazawa, T. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.03.060 · Cited by 51
Anti-convulsant Effect and Mechanism of Astragalus mongholicus Extract In Vitro and In Vivo: Protection Against Oxidative Damage and Mitochondrial Dysfunction
Jalsrai, A., Liu, Z., Long, J., Mo, X., Ma, J., & Liu, J. (2009) · Neurochemical Research · doi:10.1007/s11064-009-0027-4 · Cited by 50
miR-302 Attenuates Amyloid-β-Induced Neurotoxicity through Activation of Akt Signaling
Li, H., Lin, S.-L., Huang, C., Lu, F., Chiu, P., Huang, W., Lai, T., & Lin, C. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-150741 · Cited by 50
Nanoceria: Synthesis and Biomedical Applications
Sahu, T., Bisht, S. S., Das, K. R., & Kerkar, S. (2013) · Current Nanoscience · doi:10.2174/15734137113099990084 · Cited by 50
Fibroblast glutamate transport in aging and in AD: correlations with disease severity
Zoia, C., Tagliabue, E., Isella, V., Begni, B., Fumagalli, L., Brighina, L., Appollonio, I. M., Racchi, M., & Ferrarese, C. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.07.007 · Cited by 50
Dysfunctional Nucleus Tractus Solitarius: Its Crucial Role in Promoting Neuropathogentic Cascade of Alzheimer’s Dementia—A Novel Hypothesis
Daulatzai, M. A. (2012) · Neurochemical Research · doi:10.1007/s11064-011-0680-2 · Cited by 49
Protective effects of Glycyrrhiza uralensis Fisch. on the cognitive deficits caused by β-amyloid peptide 25–35 in young mice
Ahn, J., Um, M. Y., Choi, W., Kim, S., & Ha, T. Y. (2006) · Biogerontology · doi:10.1007/s10522-006-9023-0 · Cited by 50
Metallo‐ROS in Alzheimer's Disease: Oxidation of Neurotransmitters by CuII‐β‐Amyloid and Neuropathology of the Disease
da Silva, G. F. Z., & Ming, L. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200604421 · Cited by 50
γ‐Glutamylcysteine ethyl ester protection of proteins from Aβ(1–42)‐mediated oxidative stress in neuronal cell culture: A proteomics approach
Debra Boyd-kimball, A., Rukhsana Sultana, A., Poon, H. F., Abdul, H. M., Lynn, B. C., Klein, J. B., & Butterfield, D. A. (2005) · Journal of Neuroscience Research · doi:10.1002/jnr.20393 · Cited by 50
Targeting NADPH Oxidase and Phospholipases A2 in Alzheimer’s Disease
Simonyi, Á., He, Y., Sheng, W., Sun, A. Y., Wood, W. G., Weisman, G. A., & Sun, G. Y. (2010) · Molecular Neurobiology · doi:10.1007/s12035-010-8107-7 · Cited by 51
The Triggering Receptor Expressed on Myeloid Cells 2: “TREM-ming” the Inflammatory Component Associated with Alzheimer's Disease
Rohn, T. T. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/860959 · Cited by 51
Interaction of amyloid β peptides with redox active heme cofactor: Relevance to Alzheimer's disease
Pramanik, D., Ghosh, C., Mukherjee, S., & Dey, S. G. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.02.025 · Cited by 50
Amyloid β Peptide Conformational Changes in the Presence of a Lipid Membrane System
Accardo, A., Shalabaeva, V., Cotte, M., Burghammer, M. C., Krahne, R., Riekel, C., & Dante, S. (2014) · Langmuir · doi:10.1021/la500145r · Cited by 49
Formation of Tau Inclusions in Knock-in Mice with Familial Alzheimer Disease (FAD) Mutation of Presenilin 1 (PS1)
Tanemura, K., Chui, D.-H., Fukuda, T., Murayama, M., Park, J.-M., Akagi, T., Tatebayashi, Y., Miyasaka, T., Kimura, T., Hashikawa, T., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509145200 · Cited by 48
Amyloid β-peptide preconditioning reduces glutamate-induced neurotoxicity by promoting endocytosis of NMDA receptor
Goto, Y., Niidome, T., Akaike, A., Kihara, T., & Sugimoto, H. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.10.030 · Cited by 49
Cerebrometabolic abnormalities in Alzheimer's disease
Blass, J. P. (2003) · Neurological Research · doi:10.1179/016164103101201995 · Cited by 49
Dihydroxybenzoic acids as free radical scavengers: mechanisms, kinetics, and trends in activity
Pérez‐González, A., Galano, A., & Alvarez-Idaboy, J. R. (2014) · New Journal of Chemistry · doi:10.1039/c4nj00071d · Cited by 48
Synthesis and biological evaluation of new spirooxindoles with embedded pharmacophores
Mathusalini, S., Arasakumar, T., Lakshmi, K., Lin, C., Mohan, P. S., Ramnath, M. G., & Thirugnanasampandan, R. (2016) · New Journal of Chemistry · doi:10.1039/c6nj00534a · Cited by 48
In vivo protection of synaptosomes from oxidative stress mediated by Fe2+/H2O2 or 2,2-azobis-(2-amidinopropane) dihydrochloride by the glutathione mimetic tricyclodecan-9-yl-xanthogenate
Gururaj Joshi, A., Rukhsana Sultana, A., Marzia Perluigi, A., & Butterfield, D. A. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.12.027 · Cited by 48
Increased susceptibility to amyloid toxicity in familial Alzheimer's fibroblasts
Cecchi, C., Fiorillo, C., Baglioni, S., Pensalfini, A., Bagnoli, S., Nacmias, B., Sorbi, S., Nosi, D., Relini, A., & Liguri, G. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.05.014 · Cited by 48
Neuroprotective Effects of Hydrated Fullerene C60: Cortical and Hippocampal EEG Interplay in an Amyloid-Infused Rat Model of Alzheimer's Disease
Vorobyov, V., Kaptsov, V., Gordon, R. Y., Makarova, E. G., Podolski, I. Y., & Sengpiel, F. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-142469 · Cited by 47
New Markers of Oxidative Damage to Macromolecules
Čolak, E. (2008) · Journal of Medical Biochemistry · doi:10.2478/v10011-007-0049-x · Cited by 47
Altered Metabolomic Profiles May Be Associated with Sevoflurane-Induced Neurotoxicity in Neonatal Rats
Liu, B., Gu, Y., Xiao, H., Lei, X., Liang, W., & Zhang, J. (2015) · Neurochemical Research · doi:10.1007/s11064-015-1529-x · Cited by 47
Influence of the Environment on the Protective Effects of Guaiacol Derivatives against Oxidative Stress: Mechanisms, Kinetics, and Relative Antioxidant Activity
Galano, A., León‐Carmona, J. R., & Alvarez-Idaboy, J. R. (2012) · The Journal of Physical Chemistry B · doi:10.1021/jp302810w · Cited by 49
Proteolytic degradation of heat shock protein A2 occurs in response to oxidative stress in male germ cells of the mouse
Bromfield, E. G., Aitken, R. J., McLaughlin, E. A., & Nixon, B. (2016) · Molecular Human Reproduction · doi:10.1093/molehr/gaw074 · Cited by 47
Current Therapeutic Molecules and Targets in Neurodegenerative Diseases Based on in silico Drug Design
Sehgal, S. A., Hammad, M. A., Tahir, R. A., Akram, H. N., & Ahmad, F. (2018) · Current Neuropharmacology · doi:10.2174/1570159x16666180315142137 · Cited by 47
MoO3−x nanodots with dual enzyme mimic activities as multifunctional modulators for amyloid assembly and neurotoxicity
Han, Q., Wang, X., Liu, X., Zhang, Y., Cai, S., Cui, Q., Wang, C., & Yang, R. (2018) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2018.12.093 · Cited by 46
Transition metal complexes as imaging or therapeutic agents for neurodegenerative diseases
Ma, D., Wu, C., Li, G., Yung, T.-L., & Leung, C. (2020) · Journal of Materials Chemistry B · doi:10.1039/c9tb02669j · Cited by 47
Neuroprotective effects of p62(SQSTM1)-engineered lactic acid bacteria in Alzheimer’s disease: a pre-clinical study
Cecarini, V., Bonfili, L., Gogoi, O., Lawrence, S., Venanzi, F. M., Azevedo, V., Mancha-Agresti, P. D. C., Drumond, M. M., Rossi, G., Berardi, S., et al. (2020) · Aging · doi:10.18632/aging.103900 · Cited by 49
Despite its role in assembly, methionine 35 is not necessary for amyloid β‐protein toxicity
Maiti, P., Lomakin, A., Benedek, G. B., & Bitan, G. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06692.x · Cited by 46
YAP accelerates Aβ25–35-induced apoptosis through upregulation of Bax expression by interaction with p73
Zhang, H., Wu, S., & Xing, D. (2011) · APOPTOSIS · doi:10.1007/s10495-011-0608-y · Cited by 47
Recent Advances in Targeting Transition Metals (Copper, Iron, and Zinc) in Alzheimer’s Disease
Singh, R., Panghal, A., Jadhav, K., Thakur, A., Verma, R. K., Singh, C., Goyal, M., Kumar, J., & Namdeo, A. G. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04256-8 · Cited by 50
Normal aging in rats and pathological aging in human Alzheimer’s disease decrease FAAH activity: Modulation by cannabinoid agonists
Pascual, A. C., Martín-Moreno, A. M., Giusto, N. M., CEBALLOS, M. L. D., & Pasquaré, S. J. (2014) · Experimental Gerontology · doi:10.1016/j.exger.2014.10.011 · Cited by 46
Aβ-AGE aggravates cognitive deficit in rats via RAGE pathway
Chen, C., Li, X.-H., Tu, Y., Sun, H.-T., Liang, H., Cheng, S., & Zhang, S. (2013) · Neuroscience · doi:10.1016/j.neuroscience.2013.10.056 · Cited by 46
Protective effects of compound FLZ on beta-amyloid peptide-(25-35)-induced mouse hippocampal injury and learning and memory impairment1
Fang, F., & Liu, G.-T. (2006) · Acta Pharmacologica Sinica · doi:10.1111/j.1745-7254.2006.00347.x · Cited by 46
Early and Persistent O-GlcNAc Protein Modification in the Streptozotocin Model of Alzheimer’s Disease
dos Santos, J. P. A., Vizuete, A. F. K., Hansen, F., Biasibetti, R., & Gonçalves, C. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170211 · Cited by 46
Amyloid peptides in different assembly states and related effects on isolated and cellular proteasomes
Cecarini, V., Bonfili, L., Amici, M., Angeletti, M., Keller, J. N., & Eleuteri, A. M. (2008) · Brain Research · doi:10.1016/j.brainres.2008.03.003 · Cited by 46
Low molecular weight thiol amides attenuate MAPK activity and protect primary neurons from Aβ(1–42) toxicity
Bartov, O., Rukhsana Sultana, A., Butterfield, D. A., & Atlas, D. (2006) · Brain Research · doi:10.1016/j.brainres.2005.10.079 · Cited by 46
RETRACTED ARTICLE: Quercetin Exhibits α7nAChR/Nrf2/HO-1-Mediated Neuroprotection Against STZ-Induced Mitochondrial Toxicity and Cognitive Impairments in Experimental Rodents
Singh, N. K., & Garabadu, D. (2021) · Neurotoxicity Research · doi:10.1007/s12640-021-00410-5 · Cited by 45
Retracted
Cholesterol Potentiates β-Amyloid-Induced Toxicity in Human Neuroblastoma Cells: Involvement of Oxidative Stress
Ferrera, P., Mercado-Gómez, O. F., Silva-Aguilar, M., Valverde, M., & Arias, C. (2008) · Neurochemical Research · doi:10.1007/s11064-008-9623-y · Cited by 46
Protective role of N-trans-feruloyltyramine against β-amyloid peptide-induced neurotoxicity in rat cultured cortical neurons
Thangnipon, W., Suwanna, N., Kitiyanant, N., Soi‐ampornkul, R., Tuchinda, P., Munyoo, B., & Nobsathian, S. (2012) · Neuroscience Letters · doi:10.1016/j.neulet.2012.02.047 · Cited by 45
Galanthamine decreases genotoxicity and cell death induced by β-amyloid peptide in SH-SY5Y cell line
Ordoñez, W. O. C., Aristizábal-Pachón, A. F., Montaldi, A. P. D. L., Sakamoto‐Hojo, E. T., & Takahashi, C. S. (2016) · NeuroToxicology · doi:10.1016/j.neuro.2016.10.013 · Cited by 43
Androgens, ApoE, and Alzheimer's Disease
Raber, J. (2004) · Science of Aging Knowledge Environment · doi:10.1126/sageke.2004.11.re2 · Cited by 48
Endothelial leakiness elicited by amyloid protein aggregation
Li, Y., Ni, N., Lee, M., Wei, W., Andrikopoulos, N., Käkinen, A., Davis, T. P., Song, Y., Ding, F., Leong, D. T., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-44814-1 · Cited by 52
Neuroprotective effect of purple rice extract and its constituent against amyloid beta-induced neuronal cell death in SK-N-SH cells
Thummayot, S., Tocharus, C., Pinkaew, D., Viwatpinyo, K., Sringarm, K., & Tocharus, J. (2014) · NeuroToxicology · doi:10.1016/j.neuro.2014.10.010 · Cited by 44
Chronic oxidative damage together with genome repair deficiency in the neurons is a double whammy for neurodegeneration: Is damage response signaling a potential therapeutic target?
Wang, H., Dharmalingam, P., Vasquez, V., Mitra, J., Boldogh, I. R., Rao, K. S. J., Kent, T. A., MITRA, S. P., & Hegde, M. L. (2016) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2016.09.005 · Cited by 46
Inhibition of human islet amyloid polypeptide aggregation and cellular toxicity by oleuropein and derivatives from olive oil
Châari, A. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.06.170 · Cited by 44
Oxidation of methionine 35 reduces toxicity of the amyloid beta-peptide(1–42) in neuroblastoma cells (IMR-32) via enzyme methionine sulfoxide reductase A expression and function
Misiti, F., Clementi, M. E., & Giardina, B. (2010) · Neurochemistry International · doi:10.1016/j.neuint.2010.01.002 · Cited by 44
Spirulina maxima extract prevents cell death through BDNF activation against amyloid beta 1-42 (Aβ 1-42 ) induced neurotoxicity in PC12 cells
Koh, E.-J., Kim, K.-J., Choi, J., Kang, D.-H., & Lee, B.-Y. (2018) · Neuroscience Letters · doi:10.1016/j.neulet.2018.02.057 · Cited by 43
Age-associated temporal decline in butyrate-producing bacteria plays a key pathogenic role in the onset and progression of neuropathology and memory deficits in 3×Tg-AD mice
Chilton, P. M., Ghare, S. S., Charpentier, B. T., Myers, S., Rao, A. V., Petrosino, J. F., Hoffman, K. L., Greenwell, J. C., Tyagi, N., Behera, J., et al. (2024) · Gut Microbes · doi:10.1080/19490976.2024.2389319 · Cited by 45
Amyloid-β Inhibits Thrombospondin 1 Release From Cultured Astrocytes: Effects on Synaptic Protein Expression
Rao, K. V. R., Curtis, K. M., Johnstone, J. T., & Norenberg, M. D. (2013) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31829bd082 · Cited by 43
Protective Effect of Mangosteen Extract against β-Amyloid-Induced Cytotoxicity, Oxidative Stress and Altered Proteome in SK-N-SH Cells
Moongkarndi, P., Srisawat, C., Saetun, P., Jantaravinid, J., Peerapittayamongkol, C., Soi‐ampornkul, R., Junnu, S., Sinchaikul, S., Chen, S., Charoensilp, P., et al. (2010) · Journal of Proteome Research · doi:10.1021/pr100049v · Cited by 43
Hypoxia-Induced Degenerative Protein Modifications Associated with Aging and Age-Associated Disorders
Adav, S. S., & Sze, S. K. (2020) · Aging and Disease · doi:10.14336/ad.2019.0604 · Cited by 44
2-Propargylamino-naphthoquinone derivatives as multipotent agents for the treatment of Alzheimer’s disease
Mezeiová, E., Janočková, J., Andrýs, R., Soukup, O., Kobrlová, T., Múčková, Ľ., Pejchal, J., Šimunková, M. M., Handl, J., Micankova, P., et al. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.113112 · Cited by 42
Nanogold induces anti-inflammation against oxidative stress induced in human neural stem cells exposed to amyloid-beta peptide
Chiang, M., Nicol, C. J. B., Lin, C., Chen, S., Yen, C., & Huang, R. (2021) · Neurochemistry International · doi:10.1016/j.neuint.2021.104992 · Cited by 44
Safflower yellow reduces lipid peroxidation, neuropathology, tau phosphorylation and ameliorates amyloid β-induced impairment of learning and memory in rats
Ma, Q., Ruan, Y., Xu, H. Y., Shi, X., Wang, Z., & Hu, Y. (2015) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2015.10.004 · Cited by 43
Diterpenes: Advances in Neurobiological Drug Research
Islam, M. T., da Silva, C. B., de Alencar, M. V. O. B., Paz, M. F. C. J., Almeida, F. R. D. C., & Cavalcante, A. A. D. C. M. (2016) · Phytotherapy Research · doi:10.1002/ptr.5609 · Cited by 42
Disturbances in the control of capillary flow in an aged APPswe/PS1ΔE9 model of Alzheimer's disease
Gutiérrez‐Jiménez, E., Angleys, H., Rasmussen, P. M., West, M. J., Catalini, L., Iversen, N., Jensen, M. S., Frische, S., & Østergaard, L. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.10.006 · Cited by 44
Stress and Alzheimer’s disease
Escher, C. M., Sannemann, L., & Jessen, F. (2019) · Journal of Neural Transmission · doi:10.1007/s00702-019-01988-z · Cited by 47
Theoretical study on the peroxyl radicals scavenging activity of esculetin and its regeneration in aqueous solution
Medina, M. E., Galano, A., & Alvarez-Idaboy, J. R. (2013) · Physical Chemistry Chemical Physics · doi:10.1039/c3cp53889c · Cited by 42
Antioxidant activity of fraxetin and its regeneration in aqueous media. A density functional theory study
Medina, M. E., Iuga, C., & Alvarez-Idaboy, J. R. (2014) · RSC Advances · doi:10.1039/c4ra08394f · Cited by 42
The Senescence Hypothesis of Disease Progression in Alzheimer Disease: an Integrated Matrix of Disease Pathways for FAD and SAD
Hunter, S., Arendt, T., & Brayne, C. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8445-3 · Cited by 41
Details of the antioxidant mechanism of hydroxycinnamic acids
Shang, Y., Liu, B.-Y., & Zhao, M. (2015) · Czech Journal of Food Sciences · doi:10.17221/611/2014-cjfs · Cited by 41
S-metolachlor promotes oxidative stress in green microalga Parachlorella kessleri - A potential environmental and health risk for higher organisms
Maronić, D. Š., Čamagajevac, I. Š., Horvatić, J., Pfeiffer, T. Ž., Stević, F., Žarković, N., Waeg, G., & Jaganjac, M. (2018) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2018.04.433 · Cited by 41
Role of selenoprotein P in Alzheimer's disease.
Takemoto, A. S., Berry, M. J., & Bellinger, F. P. (2010) · PubMed · Cited by 41
4-O-methylhonokiol attenuated β-amyloid-induced memory impairment through reduction of oxidative damages via inactivation of p38 MAP kinase
Lee, Y. K., Choi, I. S., Ban, J. O., Lee, H. J., Lee, U. S., Han, S., Jung, J., Kim, Y. H., Kim, K. H., Oh, K., et al. (2010) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2010.04.002 · Cited by 41
Age-related loss of phospholipid asymmetry in APP /APP x PS-1 /PS-1 human double mutant knock-in mice: Relevance to Alzheimer disease
Lange, M. L. B., Clair, D. K. S., Markesbery, W. R., Studzinski, C. M., Murphy, M. P., & Butterfield, D. A. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.01.004 · Cited by 41
Neuroprotective Effects of PARP Inhibitors in Drosophila Models of Alzheimer’s Disease
Maggiore, A., Casale, A. M., Toscanelli, W., Cappucci, U., Rotili, D., Grieco, M., Gagné, J.-P., Poirier, G. G., d’Erme, M., & Piacentini, L. (2022) · Cells · doi:10.3390/cells11081284 · Cited by 40
The close relationship between trace elements (Cu, Fe, Zn, Se, Rb, Si, Cr, and V) and Alzheimer's disease: Research progress and insights
Mao, Y., Zhang, L., Zhang, C., Qin, L., Liao, X., & Zhao, L. (2025) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2025.127692 · Cited by 43
Alzheimer’s disease and the ‘ABSENT’ hypothesis: mechanism for amyloid β endothelial and neuronal toxicity
Roy, S. S., & Rauk, A. (2005) · Medical Hypotheses · doi:10.1016/j.mehy.2004.08.031 · Cited by 38
The Cys Sense: Thiol Redox Switches Mediate Life Cycles of Cellular Proteins
Radzinski, M., Oppenheim, T., Metanis, N., & Reichmann, D. (2021) · Biomolecules · doi:10.3390/biom11030469 · Cited by 38
A free radical‐generating system induces the cholesterol biosynthesis pathway: a role in Alzheimer's disease
Recuero, M., Vicente, M. C., Martı́nez-Garcı́a, A., Ramos, M. C., Carmona‐Sáez, P., Sastre, I., Aldudo, J., Vilella, E., Frank, A., Bullido, M. J., et al. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00457.x · Cited by 42
Amyloid-Beta Peptide 1-42 Causes Microtubule Deregulation through N-methyl-D-aspartate Receptors in Mature Hippocampal Cultures
Mota, S. I., Ferreira, I. L., Pereira, C., Oliveira, C. R., & Rego, A. C. (2012) · Current Alzheimer Research · doi:10.2174/156720512802455322 · Cited by 42
Sustained Activation of Glial Cell Epidermal Growth Factor Receptor by Bis(thiosemicarbazonato) Metal Complexes Is Associated with Inhibition of Protein Tyrosine Phosphatase Activity
Price, K. A., Caragounis, A., Paterson, B. M., Filiz, G., Volitakis, I., Masters, C. L., Barnham, K. J., Donnelly, P. S., Crouch, P. J., & White, A. R. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm9007938 · Cited by 40
Quantitative Phosphoproteomic Analyses of the Inferior Parietal Lobule from Three Different Pathological Stages of Alzheimer’s Disease
Triplett, J. C., Swomley, A. M., Cai, J., Klein, J. B., & Butterfield, D. A. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-150417 · Cited by 40
Effects of the single point genetic mutation D54G on muscle creatine kinase activity, structure and stability
Feng, S., Zhao, T., Hai‐Meng, Z. H. O. U., & Yan, Y. (2006) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2006.09.004 · Cited by 39
Protective Effects of Fibroblast Growth Factor 21 Against Amyloid-Beta1–42-Induced Toxicity in SH-SY5Y Cells
Amiri, M., Braidy, N., & Aminzadeh, M. (2018) · Neurotoxicity Research · doi:10.1007/s12640-018-9914-2 · Cited by 38
Prevention of Neurodegenerative Damage to the Brain in Rats in Experimental Alzheimer’s Disease by Adaptation to Hypoxia
Manukhina, E. B., Goryacheva, A. V., Barskov, I. V., Викторов, И. В., Guseva, A. A., Pshennikova, M. G., Khomenko, I. P., Mashina, S. Y., Pokidyshev, D. A., & Malyshev, I. Y. (2010) · Neuroscience and Behavioral Physiology · doi:10.1007/s11055-010-9320-6 · Cited by 41
The Dying of the Light: Mitochondrial Failure in Alzheimer's Disease
Young, K. J., McArdle, M. J., & Bennett, J. P. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-111487 · Cited by 39
Modulation of Amyloid β Peptide1-42 Cytotoxicity and Aggregation in Vitro by Glucose and Chondroitin Sulfate
Fernàndez‐Busquets, X., Ponce, J., Bravo, R., Arimon, M., Martiáñez, T., Gella, A., Cladera, J., & Durany, N. (2010) · Current Alzheimer Research · doi:10.2174/156720510791383787 · Cited by 38
The Protective Effects of PSM-04 Against Beta Amyloid-Induced Neurotoxicity in Primary Cortical Neurons and an Animal Model of Alzheimer’s Disease
Park, H., Kang, S., Nam, E., Suh, Y., & Chang, K. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00002 · Cited by 38
From reactive species to disease development: Effect of oxidants and antioxidants on the cellular biomarkers
Andrés, C. M. C., de la Lastra, J. M. P., Andrés, C., Plou, F. J., & Pérez‐Lebeña, E. (2023) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.23455 · Cited by 44
Effects of chemical chaperones on oxidative stress and detergent-insoluble species formation following conditional expression of amyloid precursor protein carboxy-terminal fragment
Woltjer, R. L., McMahan, W., Milatović, D., Kjerulf, J. D., Shie, F., Rung, L. G., Montine, K. S., & Montine, T. J. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.10.003 · Cited by 38
Protective potential of naringenin and its nanoformulations in redox mechanisms of injury and disease
Mehranfard, N., Ghasemi, M., Rajabian, A., & Ansari, L. (2023) · Heliyon · doi:10.1016/j.heliyon.2023.e22820 · Cited by 40
Disulfide-Rich Cyclic Peptides from Clitoria ternatea Protect against β-Amyloid Toxicity and Oxidative Stress in Transgenic Caenorhabditis elegans
Kalmankar, N. V., Hari, H., Sowdhamini, R., & Venkatesan, R. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00033 · Cited by 37
Hyperhomocysteinemia in Alzheimer's Disease: The Hen and the Egg?
Farkas, M., Keskitalo, S., Smith, D. E. C., Bain, N., Semmler, A., Ineichen, B. V., Smulders, Y. M., Blom, H. J., Kulic, L., & Linnebank, M. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-121378 · Cited by 36
Self-Assembled Monolayers of Aβ peptides on Au Electrodes: An Artificial Platform for Probing the Reactivity of Redox Active Metals and Cofactors Relevant to Alzheimer’s Disease
Pramanik, D., Sengupta, K., Mukherjee, S., Dey, S. G., & Dey, A. (2012) · Journal of the American Chemical Society · doi:10.1021/ja303930f · Cited by 36
A mechanistic link between oxidative stress and membrane mediated amyloidogenesis revealed by infrared spectroscopy
Komatsu, H., Liu, L., Murray, I. V. J., & Axelsen, P. H. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.05.026 · Cited by 36
Amyloid beta enhances cytosolic phospholipase A2 level and arachidonic acid release via nitric oxide in APP-transfected PC12 cells.
Chalimoniuk, M., Stolecka‐Warzecha, A., Cąkała, M., Hauptmann, S., Schulz, K., Lipka, U., Leuner, K., Eckert, A., Muller, W. E., & Strosznajder, J. B. (2007) · Acta Biochimica Polonica · doi:10.18388/abp.2007_3235 · Cited by 35
Docosahexaenoic acid withstands the Aβ25-35-induced neurotoxicity in SH-SY5Y cells
Hashimoto, M., Katakura, M., Hossain, S., Rahman, A., Shimada, T., & Shido, O. (2010) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2009.11.005 · Cited by 36
Identification of human presequence protease (hPreP) agonists for the treatment of Alzheimer's disease
Vangavaragu, J. R., Valasani, K. R., Gan, X., & Yan, S. S. (2014) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2014.02.046 · Cited by 35
Investigation on the Role of BDNF in the Benefits of Blueberry Extracts for the Improvement of Learning and Memory in Alzheimer’s Disease Mouse Model
Tan, L., Yang, H., Pang, W., Li, H., Liu, W., Sun, S., Song, N., Zhang, W., & Jiang, Y. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-151108 · Cited by 35
Protective role of rosmarinic acid on amyloid beta 42-induced echoic memory decline: Implication of oxidative stress and cholinergic impairment
Kantar, D., Hidişoğlu, E., Ocak, G. A., Er, H., Acun, A. D., & Yargıçoğlu, P. (2018) · Neurochemistry International · doi:10.1016/j.neuint.2018.04.008 · Cited by 34

Authors: Allan Butterfield, D.
Venue: Free Radical Research
Publisher: Informa UK Limited
Published: 2002-01
Volume: 36
Issue: 12
Pages: 1307-1313
ISSN: 1029-2470 (ISSN-L)
1071-5762
DOI: 10.1080/1071576021000049890
OpenAlex: W2153767421
Cited by: 786
References: 58
Citations by year: 2026: 12 · 2025: 20 · 2024: 18 · 2023: 21 · 2022: 24 · 2021: 34 · 2020: 26 · 2019: 28 · 2018: 30 · 2017: 32 · 2016: 45 · 2015: 43 · 2014: 42 · 2013: 39 · 2012: 42
FWCI: 18.78
Type: journal article
Language: en
Open access: closed
Locations: Free Radical Research (publishedVersion)
PubMed (publishedVersion)
Funders: University of Kentucky
National Institute on Aging (P01AG010836, P01AG005119, AG 10836, AG12423, AG0 5119, R01AG012423)
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 › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: amyloid beta peptide 1-42, oxidative stress, neurotoxicity, Alzheimer's disease, protein oxidation, lipid peroxidation, nitrotyrosine, vitamin E, hippocampal neurons, synaptosomes, apolipoprotein E, APOE ε4, amyloid fibril formation, neurodegeneration, lipid bilayers
MeSH terms: Alzheimer Disease, Amino Acid Sequence, Animals, Brain, Humans, Lipid Bilayers, Methionine, Molecular Sequence Data, Neurons, Peptide Fragments, Peptides, Free Radical Scavengers, Amyloid beta-Peptides, Reactive Oxygen Species, Protein Structure, Tertiary, 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

Amyloid β-peptide (1-42)-induced Oxidative Stress and Neurotoxicity: Implications for Neurodegeneration in Alzheimer's Disease Brain. A Review

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks