The Binding of TAPBPR and Tapasin to MHC Class I Is Mutually Exclusive
Author:
Publisher
The American Association of Immunologists
Subject
Immunology,Immunology and Allergy
Reference49 articles.
1. Cloning and functional characterization of a subunit of the transporter associated with antigen processing
2. Roles for Calreticulin and a Novel Glycoprotein, Tapasin, in the Interaction of MHC Class I Molecules with TAP
3. Recruitment of MHC Class I Molecules by Tapasin into the Transporter Associated with Antigen Processing-Associated Complex Is Essential for Optimal Peptide Loading
4. Disulfide Bond Isomerization and the Assembly of MHC Class I-Peptide Complexes
5. Tapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complex
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1. A Chicken Tapasin ortholog can chaperone empty HLA-B∗37:01 molecules independent of other peptide-loading components;Journal of Biological Chemistry;2023-10
2. Introducing Molecular Chaperones into the Causality and Prospective Management of Autoimmune Hepatitis;Digestive Diseases and Sciences;2023-09-27
3. Crystal structures of MHC class I complexes reveal the elusive intermediate conformations explored during peptide editing;Nature Communications;2023-08-18
4. Get into the groove! The influence of TAPBPR on cargo selection;Current Opinion in Immunology;2023-08
5. The ER folding sensor UGGT1 acts on TAPBPR-chaperoned peptide-free MHC I;eLife;2023-06-22
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