Abstract
There is significant evidence that, in neurodegenerative disorders, oxidative stress in the brain is fundamental to the pathophysiology and progression of such conditions, among which is Alzheimer disease (AD) [...]
David Allan Butterfield
Abstract
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Oxidative damage in neurodegeneration: Roles in the pathogenesis and progression of Alzheimer disease
10.1152/physrev.00030.2022 · 2024
10.1093/acprof:oso/9780198717478.001.0001
10.1093/acprof:oso/9780198717478.001.0001
Oxidative stress, glucose dysmetabolism and Alzheimer disease
10.1038/s41583-019-0132-6 · 2019
Role of 4-hydroxy-2-nonenal (HNE) in the pathogenesis of Alzheimer disease and other selected age-related neurodegenerative disorders
10.1016/j.freeradbiomed.2016.10.490 · 2017
10.3390/life10070101
10.3390/life10070101
Energetics and oxidative stress in synaptic plasticity and neurodegenerative disorders
10.1385/nmm:2:2:215 · 2002
Protein oxidation
10.1111/j.1749-6632.2000.tb06187.x · 2000
10.3390/antiox13050574
10.3390/antiox13050574
Protein oxidation and peroxidation
10.1042/bj20151227 · 2016
Protein oxidation processes in aging brain
10.1016/s1566-3124(08)60057-7 · 1997
The superoxide radical switch in the biology of nitric oxide and peroxynitrite
10.1152/physrev.00005.2022 · 2022
Lipid peroxidation in aging brain and Alzheimer’s disease
10.1016/s0891-5849(02)00807-9 · 2002
Brain lipid peroxidation and Alzheimer disease: Synergy between the Butterfield and Mattson laboratories
10.1016/j.arr.2020.101049 · 2020
Oxidative damage to mitochondrial DNA is increased in Alzheimer’s disease
10.1002/ana.410360510 · 1994
Nucleic acid oxidation in Alzheimer disease
10.1016/j.freeradbiomed.2008.01.002 · 2008
Alzheimer’s disease—synergistic effects of glucose deficit, oxidative stress and advanced glycation endproducts
10.1007/s007020050069 · 1998
Common neurodegenerative pathways in obesity, diabetes, and Alzheimer’s disease
10.1016/j.bbadis.2016.04.017 · 2017
Superoxide dismutase activity, oxidative damage, and mitochondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosis
10.1111/j.1471-4159.1993.tb07478.x · 1993
Redox proteomics analysis of oxidatively modified proteins in G93A-SOD1 transgenic mice-a model of familial amyotrophic lateral sclerosis
10.1016/j.freeradbiomed.2005.03.030 · 2005
Manganese superoxide dismutase regulation and cancer
10.1016/j.freeradbiomed.2012.03.009 · 2012
Oxidative and nitrosative modifications of biliverdin reductase in the brain of subjects with Alzheimer disease and mild cognitive impairment
10.3233/jad-2011-110092 · 2011
Heme oxygenase-1 posttranslational modifications in the brain of subjects with Alzheimer disease and mild cognitive impairment
10.1016/j.freeradbiomed.2012.03.020 · 2012
Bach1 overexpression in Down syndrome correlates with the alteration of the HO-1/BVR-A system: Insights for transition to Alzheimer’s disease
10.3233/jad-141254 · 2015
Apolipoprotein E: Cholesterol transport protein with expanding role in cell biology
10.1126/science.3283935 · 1988
Binding of human apolipoprotein E to synthetic amyloid beta peptide: Isoform-specific effects and implications for late-onset Alzheimer disease
10.1073/pnas.90.17.8098 · 1993
Apolipoprotein E and oxidative stress with relevance to Alzheimer’s disease
10.1016/j.nbd.2020.104795 · 2020
Transcription-coupled DNA repair: Two decades of progress and surprises
10.1038/nrm2549 · 2008
The Association between Mushroom Consumption and Mild Cognitive Impairment: A Community-Based Cross-Sectional Study in Singapore
10.3233/jad-180959 · 2019
Ergothioneine levels in an elderly population decrease with age and incidence of cognitive decline; a risk factor for neurodegeneration?
10.1016/j.bbrc.2016.07.074 · 2016
Low plasma ergothioneine levels are associated with neurodegeneration and cerebrovascular disease in dementia
10.1016/j.freeradbiomed.2021.10.019 · 2021
Are age-related neurodegenerative diseases caused by a lack of the diet-derived compound ergothioneine?
10.1016/j.freeradbiomed.2024.03.009 · 2024
Association between levels of trimethylamine N-oxide and cognitive dysfunction: A systematic review and meta-analysis
10.7717/peerj.20000 · 2025
The glial glutamate transporter, GLT-1, is oxidatively modified by 4-hydroxy-2-nonenal in the Alzheimer’s disease brain: The role of Abeta1-42
10.1046/j.1471-4159.2001.00451.x · 2001
Impairment of Biliverdin Reductase-A Promotes Brain Insulin Resistance in Alzheimer Disease: A New Paradigm
10.1016/j.freeradbiomed.2015.12.012 · 2016
Biliverdin reductase-A: A novel drug target for atorvastatin in a dog pre-clinical model of Alzheimer disease
10.1111/j.1471-4159.2011.07538.x · 2012
10.3389/fphar.2025.1473796
10.3389/fphar.2025.1473796
In vivo protective effects of ferulic acid ethyl ester against amyloid-beta peptide 1-42-induced oxidative stress
10.1002/jnr.20879 · 2006
Benfotiamine and Cognitive Decline in Alzheimer’s Disease: Results of a Randomized Placebo-Controlled Phase IIa Clinical Trial
10.3233/jad-200896 · 2020
Benfotiamine and Cognitive Decline in Alzheimer’s Disease: Results of a Randomized Placebo-Controlled Phase IIa Clinical Trial
10.3233/jad-200896 · doi-reference
In vivo protective effects of ferulic acid ethyl ester against amyloid-beta peptide 1-42-induced oxidative stress
10.1002/jnr.20879 · doi-reference
10.3389/fphar.2025.1473796
10.3389/fphar.2025.1473796 · doi-reference
Biliverdin reductase-A: A novel drug target for atorvastatin in a dog pre-clinical model of Alzheimer disease
10.1111/j.1471-4159.2011.07538.x · doi-reference
Impairment of Biliverdin Reductase-A Promotes Brain Insulin Resistance in Alzheimer Disease: A New Paradigm
10.1016/j.freeradbiomed.2015.12.012 · doi-reference
The glial glutamate transporter, GLT-1, is oxidatively modified by 4-hydroxy-2-nonenal in the Alzheimer’s disease brain: The role of Abeta1-42
10.1046/j.1471-4159.2001.00451.x · doi-reference
Association between levels of trimethylamine N-oxide and cognitive dysfunction: A systematic review and meta-analysis
10.7717/peerj.20000 · doi-reference
Are age-related neurodegenerative diseases caused by a lack of the diet-derived compound ergothioneine?
10.1016/j.freeradbiomed.2024.03.009 · doi-reference
Low plasma ergothioneine levels are associated with neurodegeneration and cerebrovascular disease in dementia
10.1016/j.freeradbiomed.2021.10.019 · doi-reference
Ergothioneine levels in an elderly population decrease with age and incidence of cognitive decline; a risk factor for neurodegeneration?
10.1016/j.bbrc.2016.07.074 · doi-reference
The Association between Mushroom Consumption and Mild Cognitive Impairment: A Community-Based Cross-Sectional Study in Singapore
10.3233/jad-180959 · doi-reference
Transcription-coupled DNA repair: Two decades of progress and surprises
10.1038/nrm2549 · doi-reference
Apolipoprotein E and oxidative stress with relevance to Alzheimer’s disease
10.1016/j.nbd.2020.104795 · doi-reference
Binding of human apolipoprotein E to synthetic amyloid beta peptide: Isoform-specific effects and implications for late-onset Alzheimer disease
10.1073/pnas.90.17.8098 · doi-reference
Apolipoprotein E: Cholesterol transport protein with expanding role in cell biology
10.1126/science.3283935 · doi-reference
Bach1 overexpression in Down syndrome correlates with the alteration of the HO-1/BVR-A system: Insights for transition to Alzheimer’s disease
10.3233/jad-141254 · doi-reference
Heme oxygenase-1 posttranslational modifications in the brain of subjects with Alzheimer disease and mild cognitive impairment
10.1016/j.freeradbiomed.2012.03.020 · doi-reference
Oxidative and nitrosative modifications of biliverdin reductase in the brain of subjects with Alzheimer disease and mild cognitive impairment
10.3233/jad-2011-110092 · doi-reference
Manganese superoxide dismutase regulation and cancer
10.1016/j.freeradbiomed.2012.03.009 · doi-reference
Redox proteomics analysis of oxidatively modified proteins in G93A-SOD1 transgenic mice-a model of familial amyotrophic lateral sclerosis
10.1016/j.freeradbiomed.2005.03.030 · doi-reference
Superoxide dismutase activity, oxidative damage, and mitochondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosis
10.1111/j.1471-4159.1993.tb07478.x · doi-reference
Common neurodegenerative pathways in obesity, diabetes, and Alzheimer’s disease
10.1016/j.bbadis.2016.04.017 · doi-reference
Alzheimer’s disease—synergistic effects of glucose deficit, oxidative stress and advanced glycation endproducts
10.1007/s007020050069 · doi-reference
Nucleic acid oxidation in Alzheimer disease
10.1016/j.freeradbiomed.2008.01.002 · doi-reference
Oxidative damage to mitochondrial DNA is increased in Alzheimer’s disease
10.1002/ana.410360510 · doi-reference
Brain lipid peroxidation and Alzheimer disease: Synergy between the Butterfield and Mattson laboratories
10.1016/j.arr.2020.101049 · doi-reference
Lipid peroxidation in aging brain and Alzheimer’s disease
10.1016/s0891-5849(02)00807-9 · doi-reference
The superoxide radical switch in the biology of nitric oxide and peroxynitrite
10.1152/physrev.00005.2022 · doi-reference
Protein oxidation processes in aging brain
10.1016/s1566-3124(08)60057-7 · doi-reference
Protein oxidation and peroxidation
10.1042/bj20151227 · doi-reference
10.3390/antiox13050574
10.3390/antiox13050574 · doi-reference
Protein oxidation
10.1111/j.1749-6632.2000.tb06187.x · doi-reference
Energetics and oxidative stress in synaptic plasticity and neurodegenerative disorders
10.1385/nmm:2:2:215 · doi-reference
10.3390/life10070101
10.3390/life10070101 · doi-reference
Role of 4-hydroxy-2-nonenal (HNE) in the pathogenesis of Alzheimer disease and other selected age-related neurodegenerative disorders
10.1016/j.freeradbiomed.2016.10.490 · doi-reference
Oxidative stress, glucose dysmetabolism and Alzheimer disease
10.1038/s41583-019-0132-6 · doi-reference
10.1093/acprof:oso/9780198717478.001.0001
10.1093/acprof:oso/9780198717478.001.0001 · doi-reference
Oxidative damage in neurodegeneration: Roles in the pathogenesis and progression of Alzheimer disease
10.1152/physrev.00030.2022 · doi-reference