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Article

Atomic structures of corkscrew-forming segments of SOD1 reveal varied oligomer conformations.

Protein science : a publication of the Protein Society - 1 Jul 2018

Sangwan Smriti, Sawaya Michael R, Murray Kevin A, Hughes Michael P, Eisenberg David S

Abstract excerpt

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...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 29453800
DOI: 10.1002/pro.3391
PMCID: PMC6032342

Genes

SOD1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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