ArticleNeurochemical research2012
Oxidative modification of cysteine 111 promotes disulfide bond-independent aggregation of SOD1.
Article in Neurochemical research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 41 citations in OpenAlex.
- Covalent Modulation of Protein Misfolding and Aggregation Processes in the Context of Neurodegenerative Diseases.Archiv der Pharmazie · 2026Review
- Oxidative denaturation of Cu/Zn-superoxide dismutase associated with neurodegenerative diseases.Protein science : a publication of the Protein Society · 2025Article
- The Underestimated Role of Iron in Frontotemporal Dementia: A Narrative Review.International journal of molecular sciences · 2024Review
- Axonopathy Underlying Amyotrophic Lateral Sclerosis: Unraveling Complex Pathways and Therapeutic Insights.Neuroscience bulletin · 2024Review
- Oxidative Cysteine Post Translational Modifications Drive the Redox Code Underlying Neurodegeneration and Amyotrophic Lateral Sclerosis.Antioxidants (Basel, Switzerland) · 2024Review
- Oxidized SOD1 accelerates cellular senescence in neural stem cells.Stem cell research & therapy · 2024Article
- Selective removal of misfolded SOD1 delays disease onset in a mouse model of amyotrophic lateral sclerosis.Cellular and molecular life sciences : CMLS · 2023Article
- Review
- Hydrogen Peroxide and Amyotrophic Lateral Sclerosis: From Biochemistry to Pathophysiology.Antioxidants (Basel, Switzerland) · 2021Review
- Erythrocytes of Little Ground Squirrels Undergo Reversible Oxidative Stress During Arousal From Hibernation.Frontiers in physiology · 2021Article
- Novel Selenium-based compounds with therapeutic potential for SOD1-linked amyotrophic lateral sclerosis.EBioMedicine · 2020Article
- Cross-talk between redox signalling and protein aggregation.Biochemical Society transactions · 2020Review
- Oxidative Stress in Amyotrophic Lateral Sclerosis: Pathophysiology and Opportunities for Pharmacological Intervention.Oxidative medicine and cellular longevity · 2020Review
- SOD1-positive aggregate accumulation in the CNS predicts slower disease progression and increased longevity in a mutant SOD1 mouse model of ALS.Scientific reports · 2019Article
- Redox Signaling by Reactive Electrophiles and Oxidants.Chemical reviews · 2018Review
- Pathological hydrogen peroxide triggers the fibrillization of wild-type SOD1 via sulfenic acid modification of Cys-111.Cell death & disease · 2018Article
- Overexpression of Human SOD1 Leads to Discrete Defects in the Cerebellar Architecture in the Mouse.Frontiers in neuroanatomy · 2017Article
- Article
- Aggregation propensities of superoxide dismutase G93 hotspot mutants mirror ALS clinical phenotypes.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Identification of a misfolded region in superoxide dismutase 1 that is exposed in amyotrophic lateral sclerosis.The Journal of biological chemistry · 2014Article
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Authors and funding
8 authors at 5 institutions in 3 countries.
Funding
Abstract
Converging evidence indicates that SOD1 aggregation is a common feature of mutant SOD1-linked fALS, and seems to be directly related to the gain-of-function toxic property. However, the mechanism inducing the aggregation is not understood. To study the contribution of oxidative modification of cysteine residues in SOD1 aggregation, we systematically examined the redox state of SOD1 cysteine residues in the G37R transgenic mouse model at different stages of the disease and under oxidative stress induced by H₂O₂. Our data suggest that under normal circumstance, cysteine 111 residue in SOD1 is free; however, under oxidative stress, it is prone to oxidative modification by providing the thiolate anion (S-). With the progression of the disease, increased levels of oxidative insults facilitated the oxidation of thiol groups of cysteine residues; human mutant SOD1 could generate an upper shift band in reducing SDS-PAGE, which turned out to be a Cys111-peroxidized SOD1 species. We also detected the formation of SOD1 multimers at different stages of the disease, and found that accumulated oxidative stress facilitated the formation of aggregates, which were not mediated by disulfide bond. This oxidative modification of cysteine 111 therefore promotes the formation of disulfide bond-independent aggregation of SOD1.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.