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Article

SOD1 mutations targeting surface hydrogen bonds promote amyotrophic lateral sclerosis without reducing apo-state stability.

The Journal of biological chemistry - 18 Jun 2010

Byström Roberth, Andersen Peter M, Gröbner Gerhard, Oliveberg Mikael

Abstract excerpt

In good accord with the protein aggregation hypothesis for neurodegenerative diseases, ALS-associated SOD1 mutations are found to reduce structural stability or net repulsive charge. Moreover there are weak indications that the ALS disease progression rate is correlated with the degree of mutational impact on the apoSOD1 structure. A bottleneck for obtaining more conclusive information about these...

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Share to Amyotrophic Lateral Sclerosis
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 20189984
DOI: 10.1074/jbc.M109.086074
PMCID: PMC2885233

Genes

SOD1

Provenance

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