TY - JOUR
T1 - Disulfide scrambling describes the oligomer formation of superoxide dismutase (SOD1) proteins in the familial form of amyotrophic lateral sclerosis
AU - Toichi, Keisuke
AU - Yamanaka, Koji
AU - Furukawa, Yoshiaki
N1 - Copyright:
Copyright 2013 Elsevier B.V., All rights reserved.
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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U2 - 10.1074/jbc.M112.414235
DO - 10.1074/jbc.M112.414235
M3 - Article
C2 - 23264618
AN - SCOPUS:84874086845
VL - 288
SP - 4970
EP - 4980
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 7
ER -