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Article

Local unfolding in a destabilized, pathogenic variant of superoxide dismutase 1 observed with H/D exchange and mass spectrometry.

The Journal of biological chemistry - 30 Jun 2006

Shaw Bryan Francis, Durazo Armando, Nersissian Aram M, Whitelegge Julian P, Faull Kym F, Valentine Joan Selverstone

Abstract excerpt

Hydrogen exchange monitored by mass spectrometry has been used to study the structural behavior of the pathogenic A4V variant of superoxide dismutase 1 (SOD1) in the metal-free (apo) form. Mass spectrometric data revealed that in the disulfide-intact (S-S) form, the A4V variant is destabilized at residues 50-53, in the disulfide subloop of the dimer interface, but many other regions of the A4V protein exhibited...

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Source

Identifiers

PMID: 16644738
DOI: 10.1074/jbc.M600623200

Genes

SOD1

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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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