Disulfide scrambling describes the oligomer formation of superoxide dismutase (SOD1) proteins in the familial form of amyotrophic lateral sclerosis

Keisuke Toichi, Koji Yamanaka, Yoshiaki Furukawa

Research output: Contribution to journalArticle

43 Citations (Scopus)

Abstract

Background: Cu, Zn-superoxide dismutase (SOD1) possesses a highly conserved intramolecular disulfide bond. Results: Structural destabilization of SOD1 scrambles the intramolecular disulfide to form cross-linked oligomers with an intermolecular disulfide bond. Conclusion: Disulfide scrambling is a key to understand the folding/misfolding process of SOD1. Significance: A disulfide-scrambling model provides a molecular pathomechanism describing the formation of disulfide-linked SOD1 oligomers in amyotrophic lateral sclerosis.

Original languageEnglish
Pages (from-to)4970-4980
Number of pages11
JournalJournal of Biological Chemistry
Volume288
Issue number7
DOIs
Publication statusPublished - 2013 Feb 15

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Oligomers
Disulfides
Superoxide Dismutase
Proteins
Amyotrophic Lateral Sclerosis
Superoxide Dismutase-1
Amyotrophic lateral sclerosis 1

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

Disulfide scrambling describes the oligomer formation of superoxide dismutase (SOD1) proteins in the familial form of amyotrophic lateral sclerosis. / Toichi, Keisuke; Yamanaka, Koji; Furukawa, Yoshiaki.

In: Journal of Biological Chemistry, Vol. 288, No. 7, 15.02.2013, p. 4970-4980.

Research output: Contribution to journalArticle

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