Structural instability and Cu-dependent pro-oxidant activity acquired by the apo form of mutant SOD1 associated with amyotrophic lateral sclerosis.

doi:10.1021/bi200338h

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Article

Structural instability and Cu-dependent pro-oxidant activity acquired by the apo form of mutant SOD1 associated with amyotrophic lateral sclerosis.

Biochemistry - 24 May 2011

Kitamura Furi, Fujimaki Nobuhiro, Okita Wakana, Hiramatsu Hirotsugu, Takeuchi Hideo

Abstract excerpt

Cu,Zn-superoxide dismutase (SOD1) is a cytosolic antioxidant enzyme, and its mutation has been implicated in amyotrophic lateral sclerosis (ALS), a disease causing a progressive loss of motor neurons. Although the pathogenic mechanism of ALS remains unclear, it is hypothesized that some toxic properties acquired by mutant SOD1 play a role in the development of ALS. We have examined the structural and catalytic...

Topics

Amyotrophic Lateral Sclerosis
Apoproteins
Circular Dichroism
Copper
Disease Progression
Enzyme Stability
Humans
Models, Molecular
Mutant Proteins
Mutation
Protein Multimerization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Structure, Quaternary

Protein Structure, Secondary

Reactive Oxygen Species

Structure-Activity Relationship

Superoxide Dismutase

Superoxide Dismutase-1

Source

Open in PubMed

Identifiers

PMID: 21506602
DOI: 10.1021/bi200338h

Genes

SOD1

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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