ArticleThe Journal of biological chemistry2016
Cellular Redox Systems Impact the Aggregation of Cu,Zn Superoxide Dismutase Linked to Familial Amyotrophic Lateral Sclerosis.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 25 citations in OpenAlex.
- Linking Superoxide Production and Scavenging in Plant Development.Plant, cell & environment · 2026Review
- Landscapes of missense variant impact for human superoxide dismutase 1.American journal of human genetics · 2025Article
- Redox homeostasis and inflammation in fibroblasts of patients with Friedreich Ataxia: a possible cross talk.Frontiers in molecular neuroscience · 2025Article
- Metabolic Profile and Pathological Alterations in the Muscle of Patients with Early-Stage Amyotrophic Lateral Sclerosis.Biomedicines · 2022Article
- A mitochondrial membrane-bridging machinery mediates signal transduction of intramitochondrial oxidation.Nature metabolism · 2021Article
- Glutaredoxin: Discovery, redox defense and much more.Redox biology · 2021Review
- 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
- Article
- Ebselen as template for stabilization of A4V mutant dimer for motor neuron disease therapy.Communications biology · 2020Article
- Emerging Evidence Highlighting the Importance of Redox Dysregulation in the Pathogenesis of Amyotrophic Lateral Sclerosis (ALS).Frontiers in cellular neuroscience · 2020Article
- Cu/Zn-superoxide dismutase and wild-type like fALS SOD1 mutants produce cytotoxic quantities of HScientific reports · 2019Article
- Vascular Dysfunction Induced by Mercury Exposure.International journal of molecular sciences · 2019Review
- Pathological hydrogen peroxide triggers the fibrillization of wild-type SOD1 via sulfenic acid modification of Cys-111.Cell death & disease · 2018Article
- Dysregulation of MicroRNAs and Target Genes Networks in Peripheral Blood of Patients With Sporadic Amyotrophic Lateral Sclerosis.Frontiers in molecular neuroscience · 2018Article
- Effect of etomidate on the oxidative stress response and levels of inflammatory factors from ischemia-reperfusion injury after tibial fracture surgery.Experimental and therapeutic medicine · 2017Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein misfolding is implicated in neurodegenerative diseases such as ALS, where mutations of superoxide dismutase 1 (SOD1) account for about 20% of the inherited mutations. Human SOD1 (hSOD1) contains four cysteines, including Cys(57) and Cys(146), which have been linked to protein stability and folding via forming a disulfide bond, and Cys(6) and Cys(111) as free thiols. But the roles of the cellular oxidation-reduction (redox) environment in SOD1 folding and aggregation are not well understood. Here we explore the effects of cellular redox systems on the aggregation of hSOD1 proteins. We found that the known hSOD1 mutations G93A and A4V increased the capability of the thioredoxin and glutaredoxin systems to reduce hSOD1 compared with wild-type hSOD1. Treatment with inhibitors of these redox systems resulted in an increase of hSOD1 aggregates in the cytoplasm of cells transfected with mutants but not in cells transfected with wild-type hSOD1 or those containing a secondary C111G mutation. This aggregation may be coupled to changes in the redox state of the G93A and A4V mutants upon mild oxidative stress. These results strongly suggest that the thioredoxin and glutaredoxin systems are the key regulators for hSOD1 aggregation and may play critical roles in the pathogenesis of ALS.
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