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Article

Denaturational stress induces formation of zinc-deficient monomers of Cu,Zn superoxide dismutase: implications for pathogenesis in amyotrophic lateral sclerosis.

Journal of molecular biology - 7 Nov 2008

Mulligan Vikram Khipple, Kerman Aaron, Ho Sylvia, Chakrabartty Avijit

Abstract excerpt

Mutations in the Cu,Zn superoxide dismutase (SOD1) cause a subset of amyotrophic lateral sclerosis cases. SOD1 is a homodimer in which each monomer binds one copper atom and one zinc atom. Mutation is believed to increase the conformational flexibility of SOD1, giving rise to a misfolded SOD1 population with novel cytotoxic properties. While SOD1's metal ligands affect its stability greatly, little is known about...

Topics

Amyotrophic Lateral Sclerosis
Copper
Dimerization
Guanidine
Humans
Kinetics
Models, Molecular
Mutation
Protein Conformation
Protein Denaturation
Superoxide Dismutase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Thermodynamics

Tryptophan

Zinc

Source

Identifiers

PMID: 18761352
DOI: 10.1016/j.jmb.2008.08.024

Genes

SOD1

Provenance

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

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Denaturational stress induces formation of zinc-deficient monomers of Cu,Zn superoxide dismutase: implications for pathogenesis in amyotrophic lateral sclerosis.PMID 18761352Read ↗

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