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Article

SOD1 gains pro-oxidant activity upon aberrant oligomerization: change in enzymatic activity by intramolecular disulfide bond cleavage.

Scientific reports - 11 Jul 2022

Yamazaki Kosuke, Tahara Shinya, Ohyama Takumi, Kuroi Kunisato, Nakabayashi Takakazu

Abstract excerpt

Copper-zinc superoxide dismutase (SOD1) has been proposed as one of the causative proteins of amyotrophic lateral sclerosis (ALS). The accumulation of non-native conformers, oligomers, and aggregates of SOD1 in motor neurons is considered responsible for this disease. However, it remains unclear which specific feature of these species induces the onset of ALS. In this study, we showed that disulfide-linked...

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Identifiers

PMID: 35817830
DOI: 10.1038/s41598-022-15701-w
PMCID: PMC9273606

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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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