A Metal-Free, Disulfide Oxidized Form of Superoxide Dismutase 1 as a Primary Misfolded Species with Prion-Like Properties in the Extracellular Environments Surrounding Motor Neuron-Like Cells

A Metal-Free, Disulfide Oxidized Form of Superoxide Dismutase 1 as a Primary Misfolded Species with Prion-Like Properties in the Extracellular Environments Surrounding Motor Neuron-Like Cells

Superoxide dismutase 1 (SOD1) is a metalloenzyme with high structural stability, but a lack of Cu and Zn ions decreases its stability and enhances the likelihood of misfolding, which is a pathological hallmark of amyotrophic lateral sclerosis (ALS). A growing body of evidence has demonstrated that m...

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Bibliographic Details
Main Authors: Chika Takashima, Yasuhiro Kosuge, Masahisa Inoue, Shin-Ichi Ono, Eiichi Tokuda
Format: Article
Language:English
Published: MDPI AG 2021-04-01
Series:International Journal of Molecular Sciences
Subjects:
amyotrophic lateral sclerosis
superoxide dismutase 1
extracellular environment
prion-like property
protein misfolding
Online Access:https://www.mdpi.com/1422-0067/22/8/4155

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