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- W2091797397 endingPage "387" @default.
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- W2091797397 abstract "Assembled class I histocompatibility molecules, consisting of heavy chain, beta 2-microglobulin, and peptide ligand, are transported rapidly to the cell surface. In contrast, the intracellular transport of free heavy chains or peptide-deficient heavy chain-beta 2-microglobulin heterodimers is impaired. A 90-kilodalton membrane-bound chaperone of the endoplasmic reticulum (ER), termed calnexin, associates quantitatively with newly synthesized class I heavy chains, but the functions of calnexin in this interaction are unknown. Class I subunits were expressed alone or in combination with calnexin in Drosophila melanogaster cells. Calnexin retarded the intracellular transport of both peptide-deficient heavy chain-beta 2-microglobulin heterodimers and free heavy chains. Calnexin also impeded the rapid intracellular degradation of free heavy chains. The ability of calnexin to protect and retain class I assembly intermediates is likely to contribute to the efficient intracellular formation of class I-peptide complexes." @default.
- W2091797397 created "2016-06-24" @default.
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- W2091797397 date "1994-01-21" @default.
- W2091797397 modified "2023-10-16" @default.
- W2091797397 title "Regulation of MHC Class I Transport by the Molecular Chaperone, Calnexin (p88, IP90)" @default.
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- W2091797397 doi "https://doi.org/10.1126/science.8278813" @default.
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