The heavy chain of neonatal Fc receptor for IgG is sequestered in endoplasmic reticulum by forming oligomers in the absence of β2-microglobulin association
- 1 November 2002
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 367 (3), 703-714
- https://doi.org/10.1042/bj20020200
Abstract
No abstract availableKeywords
This publication has 47 references indexed in Scilit:
- Tryptophan- and Dileucine-based Endocytosis Signals in the Neonatal Fc ReceptorPublished by Elsevier ,2001
- Crystal Structure and Immunoglobulin G Binding Properties of the Human Major Histocompatibility Complex-Related Fc Receptor,Biochemistry, 2000
- β2-microglobulin–deficient Mice Are Resistant to Bullous PemphigoidThe Journal of Experimental Medicine, 1997
- β2-Microglobulin and calnexin can independently promote folding and disulfide bond formation in class I histocompatibility proteinsMolecular Immunology, 1997
- A Method for Isolation and Purification of Specific Antibodies to a Protein Fused to the GSTAnalytical Biochemistry, 1996
- β2‐microglobulin with an endoplasmic reticulum retention signal increases the surface expression of folded class I major histocompatibility complex moleculesEuropean Journal of Immunology, 1995
- A major histocompatibility complex class I-related Fc receptor for IgG on rat hepatocytes.Journal of Clinical Investigation, 1995
- β 2 -Microglobulin-Independent MHC Class Ib Molecule Expressed by Human Intestinal EpitheliumScience, 1994
- Calnexin retains unassembled major histocompatibility complex class I free heavy chains in the endoplasmic reticulum.The Journal of Experimental Medicine, 1994
- Lack of HLA class I antigen expression by melanoma cells SK-MEL-33 caused by a reading frameshift in beta 2-microglobulin messenger RNA.Journal of Clinical Investigation, 1993