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

doi:10.1074/jbc.M112.414235

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

Department of Chemistry

Research output: Contribution to journal › Article › peer-review

53 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 language	English
Pages (from-to)	4970-4980
Number of pages	11
Journal	Journal of Biological Chemistry
Volume	288
Issue number	7
DOIs	https://doi.org/10.1074/jbc.M112.414235
Publication status	Published - 2013 Feb 15

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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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.",

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PY - 2013/2/15

Y1 - 2013/2/15

N2 - 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.

AB - 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.

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

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