著者

古川 良明

出版者

一般社団法人 日本生物物理学会

雑誌

生物物理 (ISSN:05824052)

巻号頁・発行日

vol.60, no.6, pp.338-341, 2020 (Released:2020-11-28)

参考文献数

20

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Mutations in the gene coding Cu/Zn-superoxide dismutase (SOD1) are known to cause amyotrophic lateral sclerosis (ALS), a neurodegenerative disease with no cures. SOD1 is a highly stable enzyme where copper and zinc ions bind and a disulfide bond forms, but is also known to accumulate as misfolded forms in spinal motoneurons of ALS. A key to understand such pathological changes in SOD1 is the contribution of metal binding as well as disulfide formation to the conformational stability of SOD1. In this review, I will summarize mechanisms of SOD1 misfolding in ALS where the metal binding and/or disulfide formation go awry.