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Article

Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS.

Nature neuroscience - 1 Nov 2010

Bosco Daryl A, Morfini Gerardo, Karabacak N Murat, Song Yuyu, Gros-Louis Francois, Pasinelli Piera, Goolsby Holly, Fontaine Benjamin A, Lemay Nathan, McKenna-Yasek Diane, Frosch Matthew P, Agar Jeffrey N, Julien Jean-Pierre, Brady Scott T, Brown Robert H

Abstract excerpt

Many mutations confer one or more toxic function(s) on copper/zinc superoxide dismutase 1 (SOD1) that impair motor neuron viability and cause familial amyotrophic lateral sclerosis (FALS). Using a conformation-specific antibody that detects misfolded SOD1 (C4F6), we found that oxidized wild-type SOD1 and mutant SOD1 share a conformational epitope that is not present in normal wild-type SOD1. In a subset of human...

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Share to Amyotrophic Lateral Sclerosis
Share to Antibodies, Anti-Idiotypic

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Epitope Mapping

Share to Mass Spectrometry

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Share to Proteostasis Deficiencies

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Source

Open in PubMed Open full text

Identifiers

PMID: 20953194
DOI: 10.1038/nn.2660
PMCID: PMC2967729

Genes

SOD1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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