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Article

Substrate specificity of the oxidoreductase ERp57 is determined primarily by its interaction with calnexin and calreticulin.

The Journal of biological chemistry - 23 Jan 2009

Jessop Catherine E, Tavender Timothy J, Watkins Rachel H, Chambers Joseph E, Bulleid Neil J

Abstract excerpt

The formation of disulfides within proteins entering the secretory pathway is catalyzed by the protein disulfide isomerase family of endoplasmic reticulum localized oxidoreductases. One such enzyme, ERp57, is thought to catalyze the isomerization of non-native disulfide bonds formed in glycoproteins with unstructured disulfide-rich domains. Here we investigated the mechanism underlying ERp57 specificity toward...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 19054761
DOI: 10.1074/jbc.M808054200
PMCID: PMC2629083

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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