ArticleMolecular neurodegeneration2013
Features of wild-type human SOD1 limit interactions with misfolded aggregates of mouse G86R Sod1.
Article in Molecular neurodegeneration, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Diverse effects of coexpression of human SOD1 variants on motor neuron disease.Human molecular genetics · 2025Article
- Improvements of Paraquat Treatment in Liquid Media for Behavior and Neurodegenerative Tests.microPublication biology · 2025Article
- The role of exosomes in adult neurogenesis: implications for neurodegenerative diseases.Neural regeneration research · 2024Review
- Tryptophan residue 32 in human Cu-Zn superoxide dismutase modulates prion-like propagation and strain selection.PloS one · 2020Article
- Quantum chemical and molecular mechanics studies on the assessment of interactions between resveratrol and mutant SOD1 (G93A) protein.Journal of computer-aided molecular design · 2018Article
- Relationship between mutant Cu/Zn superoxide dismutase 1 maturation and inclusion formation in cell models.Journal of neurochemistry · 2017Article
- Interaction between dimer interface residues of native and mutated SOD1 protein: a theoretical study.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Article
- Metal-deficient aggregates and diminished copper found in cells expressing SOD1 mutations that cause ALS.Frontiers in aging neuroscience · 2014Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Mutations in the gene encoding superoxide dismutase 1 (SOD1) account for about 20% of the cases of familial amyotrophic lateral sclerosis (fALS). It is well established that mutations in SOD1, associated with fALS, heighten the propensity of the protein to misfold and aggregate. Although aggregation appears to be a factor in the toxicity of mutant SOD1s, the precise nature of this toxicity has not been elucidated. A number of other studies have now firmly established that raising the levels of wild-type (WT) human SOD1 (hSOD1) proteins can in some manner augment the toxicity of mutant hSOD1 proteins. However, a recent study demonstrated that raising the levels of WT-hSOD1 did not affect disease in mice that harbor a mouse Sod1 gene (mSod1) encoding a well characterized fALS mutation (G86R). In the present study, we sought a potential explanation for the differing effects with WT-hSOD1 on the toxicity of mutant hSOD1 versus mutant mSod1. In the cell culture models used here, we observe poor interactions between WT-hSOD1 and misfolded G86R-mSod1, possibly explaining why over-expression of WT-hSOD1 does not synergize with mutant mSod1 to accelerate the course of the disease in mice.
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