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The loading of peptides into the groove of MHC class I molecules prior to antigen presentation is a complex process. In this issue of Cell, Park et al. (2006) show that peptide loading gets a helping hand from a resident ER enzyme called protein disulfide isomerase, a chaperone that has oxidoreductase activity.

Original publication

DOI

10.1016/j.cell.2006.10.001

Type

Journal article

Journal

Cell

Publication Date

10/2006

Volume

127

Pages

249 - 251

Addresses

Cancer Sciences Division, University of Southampton School of Medicine, Southampton SO16 6YD, UK. t.j.elliott@soton.ac.uk

Keywords

Humans, Cytomegalovirus Infections, Sulfhydryl Compounds, Proteasome Endopeptidase Complex, Peptides, Histocompatibility Antigens Class I, Antigen Presentation, Oxidation-Reduction, Protein Disulfide-Isomerases