ArticleJournal of molecular biology2011
Structural and thermodynamic effects of post-translational modifications in mutant and wild type Cu, Zn superoxide dismutase.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
22 citing papers in PubMed, 48 citations in OpenAlex.
- The effect of aging on post-translational modifications of wild-type human SOD1 and the A5V ALS mutant.GeroScience · 2026Article
- Direct observation of prion-like propagation of protein misfolding templated by pathogenic mutants.Nature chemical biology · 2024Article
- Toxic SOD1 trimers are off-pathway in the formation of amyloid-like fibrils in ALS.Biophysical journal · 2022Article
- Computational Insights into the Unfolding of a Destabilized Superoxide Dismutase 1 Mutant.Biology · 2021Article
- β-Methylamino-L-alanine substitution of serine in SOD1 suggests a direct role in ALS etiology.PLoS computational biology · 2019Article
- RNA Fibers as Optimized Nanoscaffolds for siRNA Coordination and Reduced Immunological Recognition.Advanced functional materials · 2018Article
- Partially native intermediates mediate misfolding of SOD1 in single-molecule folding trajectories.Nature communications · 2017Article
- A Structural Model for Vinculin Insertion into PIPStructure (London, England : 1993) · 2017Article
- Discovery of Age-Related Protein Folding Stability Differences in the Mouse Brain Proteome.Journal of proteome research · 2016Article
- A Phosphomimetic Mutation Stabilizes SOD1 and Rescues Cell Viability in the Context of an ALS-Associated Mutation.Structure (London, England : 1993) · 2016Article
- Global analysis of protein folding thermodynamics for disease state characterization.Journal of proteome research · 2015Article
- Genotype-property patient-phenotype relations suggest that proteome exhaustion can cause amyotrophic lateral sclerosis.PloS one · 2015Article
- Oxidation of the tryptophan 32 residue of human superoxide dismutase 1 caused by its bicarbonate-dependent peroxidase activity triggers the non-amyloid aggregation of the enzyme.The Journal of biological chemistry · 2014Article
- Non-native soluble oligomers of Cu/Zn superoxide dismutase (SOD1) contain a conformational epitope linked to cytotoxicity in amyotrophic lateral sclerosis (ALS).Biochemistry · 2014Article
- Computational approaches to understanding protein aggregation in neurodegeneration.Journal of molecular cell biology · 2014Review
- Competitive binding of natural amphiphiles with graphene derivatives.Scientific reports · 2013Article
- Local unfolding of Cu, Zn superoxide dismutase monomer determines the morphology of fibrillar aggregates.Journal of molecular biology · 2012Article
- Abnormal SDS-PAGE migration of cytosolic proteins can identify domains and mechanisms that control surfactant binding.Protein science : a publication of the Protein Society · 2012Article
- An over-oxidized form of superoxide dismutase found in sporadic amyotrophic lateral sclerosis with bulbar onset shares a toxic mechanism with mutant SOD1.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Amyotrophic lateral sclerosis: update and new developments.Degenerative neurological and neuromuscular disease · 2012Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Aggregation of Cu,Zn superoxide dismutase (SOD1) is implicated in amyotrophic lateral sclerosis. Glutathionylation and phosphorylation of SOD1 is omnipresent in the human body, even in healthy individuals, and has been shown to increase SOD1 dimer dissociation, which is the first step on the pathway toward SOD1 aggregation. We found that post-translational modification of SOD1, especially glutathionylation, promotes dimer dissociation. We discovered an intermediate state in the pathway to dissociation, a conformational change that involves a "loosening" of the β-barrels and a loss or shift of dimer interface interactions. In modified SOD1, this intermediate state is stabilized as compared to unmodified SOD1. The presence of post-translational modifications could explain the environmental factors involved in the speed of disease progression. Because post-translational modifications such as glutathionylation are often induced by oxidative stress, post-translational modification of SOD1 could be a factor in the occurrence of sporadic cases of amyotrophic lateral sclerosis, which represent 90% of all cases of the disease.
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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.