Stoichiometry of HLA Class II-Invariant Chain Oligomers
Author:
Publisher
Public Library of Science (PLoS)
Subject
Multidisciplinary
Reference58 articles.
1. Invariant Chain Trimers Are Sequestered in the Rough Endoplasmic Reticulum in the Absence of Association with HLA Class II Antigens.;MS Marks;J Cell Biol,1990
2. Invariant chain made in Escherichia coli has an exposed N-terminal segment that blocks antigen binding to HLA-DR1 and a trimeric C-terminal segment that binds empty HLA-DR1.;S-J Park;Proc Natl Acad Sci USA,1995
3. Structure of a trimeric domain of the MHC class II-associated chaperonin and targeting protein Ii.;A Jasanoff;EMBO J,1998
4. The CLIP region of invariant chain plays a critical role in regulating major histocompatibility complex class II folding, transport, and peptide occupancy.;P Romagnoli;J Exp Med,1994
5. In Vivo and In Vitro Formation and Dissociation of HLA-DR Complexes with Invariant Chain-Derived Peptides.;RR Avva;Immunity,1994
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