Identification of Specific Glycoforms of Major Histocompatibility Complex Class I Heavy Chains Suggests That Class I Peptide Loading Is an Adaptation of the Quality Control Pathway Involving Calreticulin and ERp57-Reference-Cited by-同舟云学术

Identification of Specific Glycoforms of Major Histocompatibility Complex Class I Heavy Chains Suggests That Class I Peptide Loading Is an Adaptation of the Quality Control Pathway Involving Calreticulin and ERp57

Published:2002-11 Issue:48 Volume:277 Page:46415-46423
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Radcliffe Catherine M.,Diedrich Gundo,Harvey David J.,Dwek Raymond A.,Cresswell Peter,Rudd Pauline M.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference38 articles.

1. MECHANISMS OF MHC CLASS I–RESTRICTED ANTIGEN PROCESSING

2. Efficient dissociation of the p88 chaperone from major histocompatibility complex class I molecules requires both beta 2-microglobulin and peptide.

3. The Role of ERp57 in Disulfide Bond Formation during the Assembly of Major Histocompatibility Complex Class I in a Synchronized Semipermeabilized Cell Translation System

4. Species-specific differences in chaperone interaction of human and mouse major histocompatibility complex class I molecules.

5. Roles for Calreticulin and a Novel Glycoprotein, Tapasin, in the Interaction of MHC Class I Molecules with TAP

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