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Article

S-acylation of SOD1, CCS, and a stable SOD1-CCS heterodimer in human spinal cords from ALS and non-ALS subjects.

Scientific reports - 25 Jan 2017

Antinone Sarah E, Ghadge Ghanashyam D, Ostrow Lyle W, Roos Raymond P, Green William N

Abstract excerpt

Previously, we found that human Cu, Zn-superoxide dismutase (SOD1) is S-acylated (palmitoylated) in vitro and in amyotrophic lateral sclerosis (ALS) mouse models, and that S-acylation increased for ALS-causing SOD1 mutants relative to wild type. Here, we use the acyl resin-assisted capture (acyl-RAC) assay to demonstrate S-acylation of SOD1 in human post-mortem spinal cord homogenates from ALS and non-ALS...

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Share to Acylation
Share to Amyotrophic Lateral Sclerosis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Chaperones

Share to Protein Multimerization

Share to Protein Processing, Post-Translational

Share to Protein Stability

Share to Spinal Cord

Share to Superoxide Dismutase-1

Source

Open in PubMed Open full text

Identifiers

PMID: 28120938
DOI: 10.1038/srep41141
PMCID: PMC5264640

Genes

SOD1
CCS

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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