HLA-B27 Misfolding Is Associated with Aberrant Intermolecular Disulfide Bond Formation (Dimerization) in the Endoplasmic Reticulum-Reference-Cited by-同舟云学术

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HLA-B27 Misfolding Is Associated with Aberrant Intermolecular Disulfide Bond Formation (Dimerization) in the Endoplasmic Reticulum

Published:2002-06 Issue:26 Volume:277 Page:23459-23468
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Dangoria Nandita S.,DeLay Monica L.,Kingsbury Daniel J.,Mear John P.,Uchanska-Ziegler Barbara,Ziegler Andreas,Colbert Robert A.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference68 articles.

1. Setting the Standards: Quality Control in the Secretory Pathway

2. The nature of the MHC class I peptide loading complex

3. Thiol oxidation and reduction in MHC-restricted antigen processing and presentation

4. Mutation of the α2 domain disulfide bridge of the class I molecule HLA-A∗0201 Effect on maturation and peptide presentation

5. ERp57 Functions as a Subunit of Specific Complexes Formed with the ER Lectins Calreticulin and Calnexin

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