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 | |
| Publication status | Published - 2013 Feb 15 |
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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 journal › Article
}
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
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.
UR - http://www.scopus.com/inward/record.url?scp=84874086845&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84874086845&partnerID=8YFLogxK
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 -