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Article

The redox activity of ERp57 is not essential for its functions in MHC class I peptide loading.

Proceedings of the National Academy of Sciences of the United States of America - 29 Jul 2008

Peaper David R, Cresswell Peter

Abstract excerpt

ERp57 is an oxidoreductase that, in conjunction with calnexin and calreticulin, assists disulfide bond formation in folding glycoproteins. ERp57 also forms a mixed disulfide with the MHC class I-specific chaperone tapasin, and this dimeric conjugate edits the peptide repertoire bound by MHC class...

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Share to B-Lymphocytes
Share to Genes, MHC Class I
Share to Membrane Transport Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Oxidation-Reduction

Share to Oxidoreductases

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Identifiers

PMID: 18650385
DOI: 10.1073/pnas.0805044105
PMCID: PMC2483232

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-18650385-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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The redox activity of ERp57 is not essential for its functions in MHC class I peptide loading.PMID 18650385Read ↗

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