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- W2167688505 abstract "MHC class I molecules expressed in a calreticulin-deficient cell line (K42) assembled with β 2-microglobulin (β2-m) normally, but their subsequent loading with optimal peptides was defective. Suboptimally loaded class I molecules were released into the secretory pathway. This occurred despite the ability of newly synthesized class I to interact with the transporter associated with antigen processing (TAP) loading complex. The efficiency of peptide loading was reduced by 50%–80%, and impaired T cell recognition was observed for three out of four antigens tested. The peptide-loading function was specific to calreticulin, since the defect in K42 could be rectified by transfection with calreticulin but not a soluble form of calnexin, which shares its lectin-like activity." @default.
- W2167688505 created "2016-06-24" @default.
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- W2167688505 date "2002-01-01" @default.
- W2167688505 modified "2023-10-13" @default.
- W2167688505 title "Assembly and Antigen-Presenting Function of MHC Class I Molecules in Cells Lacking the ER Chaperone Calreticulin" @default.
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- W2167688505 doi "https://doi.org/10.1016/s1074-7613(01)00260-6" @default.
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