Misfolding of Cu/Zn-Superoxide Dismutase in Neurodegenerative Diseases

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  • FURUKAWA Yoshiaki
    Lab. for Mechanistic Chemistry of Biomolecules, Department of Chemistry, Keio University

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  • 神経変性疾患における銅・亜鉛スーパーオキシドディスムターゼのミスフォールディング
  • シンケイ ヘンセイ シッカン ニ オケル ドウ ・ アエン スーパーオキシドディスムターゼ ノ ミスフォールディング

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Abstract

<p>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.</p>

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  • Seibutsu Butsuri

    Seibutsu Butsuri 60 (6), 338-341, 2020

    The Biophysical Society of Japan General Incorporated Association

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