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• W2131609927 endingPage "358" @default.
• W2131609927 startingPage "323" @default.
• W2131609927 abstract "Classical class I molecules assemble in the endoplasmic reticulum (ER) with peptides mostly generated from cytosolic proteins by the proteasome. The activity of the proteasome can be modulated by a variety of accessory protein complexes. A subset of the proteasome beta-subunits (LMP2, LMP7, and MECL-1) and one of the accessory complexes, PA28, are upregulated by gamma-interferon and affect the generation of peptides to promote more efficient antigen recognition. The peptides are translocated into the ER by the transporter associated with antigen processing (TAP). A transient complex containing a class I heavy chain-beta 2 microglobulin (beta 2 m) dimer is assembled onto the TAP molecule by successive interactions with the ER chaperones calnexin and calreticulin and a specialized molecule, tapasin. Peptide binding releases the class I-beta 2 m dimer for transport to the cell surface, while lack of binding results in proteasome-mediated degradation. The products of certain nonclassical MHC-linked class I genes bind peptides in a similar way. A homologous set of beta 2 m-associated membrane glycoproteins, the CD1 molecules, appears to bind lipid-based ligands within the endocytic pathway." @default.
• W2131609927 created "2016-06-24" @default.
• W2131609927 creator A5025998259 @default.
• W2131609927 creator A5065397632 @default.
• W2131609927 date "1998-04-01" @default.
• W2131609927 modified "2023-10-17" @default.
• W2131609927 title "MECHANISMS OF MHC CLASS I–RESTRICTED ANTIGEN PROCESSING" @default.
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