ArticleProtein science : a publication of the Protein Society2018
Atomic structures of corkscrew-forming segments of SOD1 reveal varied oligomer conformations.
Article in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Gangliosides GM3 And GD3 Modulate Insulin Aggregation Pathways and Reduce Cytotoxicity Through Structural Remodeling.bioRxiv : the preprint server for biology · 2026Article
- Distinct amyloid fibril structures formed by ALS-causing SOD1 mutants G93A and D101N.EMBO reports · 2025Article
- Amyloid fibril structures and ferroptosis activation induced by ALS-causing SOD1 mutations.Science advances · 2024Article
- Review
- SOD1 gains pro-oxidant activity upon aberrant oligomerization: change in enzymatic activity by intramolecular disulfide bond cleavage.Scientific reports · 2022Article
- Atomic view of an amyloid dodecamer exhibiting selective cellular toxic vulnerability in acute brain slices.Protein science : a publication of the Protein Society · 2022Article
- Prionoids in amyotrophic lateral sclerosis.Brain communications · 2022Review
- Exploring amyloid oligomers with peptide model systems.Current opinion in chemical biology · 2021Review
- Direct Observation of β-Barrel Intermediates in the Self-Assembly of Toxic SOD1Journal of chemical information and modeling · 2021Article
- Prion-Like Propagation of Protein Misfolding and Aggregation in Amyotrophic Lateral Sclerosis.Frontiers in molecular neuroscience · 2019Article
- Structural Properties and Interaction Partners of Familial ALS-Associated SOD1 Mutants.Frontiers in neurology · 2019Review
- Tryptophan 32-mediated SOD1 aggregation is attenuated by pyrimidine-like compounds in living cells.Scientific reports · 2018Article
- Repurposing Triphenylmethane Dyes to Bind to Trimers Derived from Aβ.Journal of the American Chemical Society · 2018Article
- Are Amyloid Fibrils RNA-Traps? A Molecular Dynamics Perspective.Frontiers in molecular biosciences · 2018Article
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5 authors.
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Abstract
The aggregation cascade of disease-related amyloidogenic proteins, terminating in insoluble amyloid fibrils, involves intermediate oligomeric states. The structural and biochemical details of these oligomers have been largely unknown. Here we report crystal structures of variants of the cytotoxic oligomer-forming segment residues 28-38 of the ALS-linked protein, SOD1. The crystal structures reveal three different architectures: corkscrew oligomeric structure, nontwisting curved sheet structure and a steric zipper proto-filament structure. Our work highlights the polymorphism of the segment 28-38 of SOD1 and identifies the molecular features of amyloidogenic entities.
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