ArticleProceedings of the National Academy of Sciences of the United States of America2017
Atomic structure of a toxic, oligomeric segment of SOD1 linked to amyotrophic lateral sclerosis (ALS).
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 118 citations in OpenAlex.
- Usefulness ofInternational journal of molecular sciences · 2026Article
- Toxic mechanisms of amyloid oligomers and therapeutic strategies.Protein science : a publication of the Protein Society · 2026Review
- Distinct amyloid fibril structures formed by ALS-causing SOD1 mutants G93A and D101N.EMBO reports · 2025Article
- A structure-guided antibody detects SOD1 oligomers in diverse ALS genotypes.bioRxiv : the preprint server for biology · 2025Article
- Emerging biophysical origins and pathogenic implications of amyloid oligomers.Nature communications · 2025Review
- The Ile35 Residue of the ALS-Associated Mutant SOD1 Plays a Crucial Role in the Intracellular Aggregation of the Molecule.Molecular neurobiology · 2025Article
- Amyloid fibril structures and ferroptosis activation induced by ALS-causing SOD1 mutations.Science advances · 2024Article
- Cryo-EM confirms a common fibril fold in the heart of four patients with ATTRwt amyloidosis.Communications biology · 2024Article
- Amyloidogenic regions in beta-strands II and III modulate the aggregation and toxicity of SOD1 in living cells.Open biology · 2024Article
- Cryo-EM confirms a common fibril fold in the heart of four patients with ATTRwt amyloidosis.bioRxiv : the preprint server for biology · 2024Article
- Protein aggregation and therapeutic strategies in SOD1- and TDP-43- linked ALS.Frontiers in molecular biosciences · 2024Review
- Characterizing proteomic and transcriptomic features of missense variants in amyotrophic lateral sclerosis genes.Brain : a journal of neurology · 2023Article
- Zebrafish as a Model Organism for Studying Pathologic Mechanisms of Neurodegenerative Diseases and other Neural Disorders.Cellular and molecular neurobiology · 2023Review
- Probing differences among Aβ oligomers with two triangular trimers derived from Aβ.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Nanoscale imaging of individual amyloid aggregates extracted from brains of Alzheimer and Parkinson patients reveals presence of lipids in α-synuclein but not in amyloid βProtein science : a publication of the Protein Society · 2023Article
- Remodeling of astrocyte secretome in amyotrophic lateral sclerosis: uncovering novel targets to combat astrocyte-mediated toxicity.Translational neurodegeneration · 2022Review
- SOD1 gains pro-oxidant activity upon aberrant oligomerization: change in enzymatic activity by intramolecular disulfide bond cleavage.Scientific reports · 2022Article
- Cryo-EM structure of an amyloid fibril formed by full-length human SOD1 reveals its conformational conversion.Nature communications · 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
Corrections and comments
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Authors and funding
18 authors at 6 institutions in 1 country.
Funding
Abstract
Fibrils and oligomers are the aggregated protein agents of neuronal dysfunction in ALS diseases. Whereas we now know much about fibril architecture, atomic structures of disease-related oligomers have eluded determination. Here, we determine the corkscrew-like structure of a cytotoxic segment of superoxide dismutase 1 (SOD1) in its oligomeric state. Mutations that prevent formation of this structure eliminate cytotoxicity of the segment in isolation as well as cytotoxicity of the ALS-linked mutants of SOD1 in primary motor neurons and in a
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