A Role for Protein Disulfide Isomerase in the Early Folding and Assembly of MHC Class I Molecules-Reference-Cited by-同舟云学术

A Role for Protein Disulfide Isomerase in the Early Folding and Assembly of MHC Class I Molecules

Published:2009-10 Issue:10 Volume:11 Page:2553-2561
ISSN:1523-0864
Container-title:Antioxidants & Redox Signaling
language:en
Short-container-title:Antioxidants & Redox Signaling

Author:

Kang Kwonyoon¹,Park Boyoun¹,Oh Changhoon¹,Cho Kwangmin¹²,Ahn Kwangseog¹

Affiliation:

1. National Creative Research Center for Antigen Presentation, Department of Biological Sciences, Seoul National University, Seoul, South Korea.

2. College of Life Sciences, Korea University, Seoul, South Korea.

Publisher

Mary Ann Liebert Inc

Subject

Cell Biology,Clinical Biochemistry,Molecular Biology,Physiology,Biochemistry,Cell Biology,Clinical Biochemistry,Molecular Biology,Physiology,Biochemistry

Link

http://www.liebertpub.com/doi/pdf/10.1089/ars.2009.2465

Reference41 articles.

1. Assembly and export of MHC class I peptide ligands

2. The N-terminal region of tapasin is required to stabilize the MHC class I loading complex

3. Formation of a Major Histocompatibility Complex Class I Tapasin Disulfide Indicates a Change in Spatial Organization of the Peptide-loading Complex during Assembly

4. ERdj5, an Endoplasmic Reticulum (ER)-resident Protein Containing DnaJ and Thioredoxin Domains, Is Expressed in Secretory Cells or following ER Stress

5. Characterization of the active site cysteine residues of the thioredoxin-like domains of protein disulfide isomerase

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