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Article

Structural basis of Cu, Zn-superoxide dismutase amyloid fibril formation involves interaction of multiple peptide core regions.

Journal of biochemistry - 1 Feb 2016

Ida Masataka, Ando Mizuho, Adachi Masayuki, Tanaka Asumi, Machida Kodai, Hongo Kunihiro, Mizobata Tomohiro, Yamakawa Miho Yoshida, Watanabe Yasuhiro, Nakashima Kenji, Kawata Yasushi

Abstract excerpt

Cu, Zn-superoxide dismutase (SOD1), an enzyme implicated in the progression of familial amyotrophic lateral sclerosis (fALS), forms amyloid fibrils under certain experimental conditions. As part of our efforts to understand ALS pathogenesis, in this study we found that reduction of the intramolecular disulfide bond destabilized the tertiary structure of metal free wild-type SOD1 and greatly enhanced fibril...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 26319711
DOI: 10.1093/jb/mvv091
PMCID: PMC4948195

Genes

SOD1

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