β2-Microglobulin and calnexin can independently promote folding and disulfide bond formation in class I histocompatibility proteins
- 1 April 1997
- journal article
- Published by Elsevier in Molecular Immunology
- Vol. 34 (5) , 401-408
- https://doi.org/10.1016/s0161-5890(97)00045-x
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- Roles for Calreticulin and a Novel Glycoprotein, Tapasin, in the Interaction of MHC Class I Molecules with TAPImmunity, 1996
- MHC class I molecules form ternary complexes with calnexin and TAP and undergo peptide-regulated interaction with TAP via their extracellular domains.The Journal of Experimental Medicine, 1996
- Calnexin Influences Folding of Human Class I Histocompatibility Proteins but Not Their Assembly with β2-MicroglobulinJournal of Biological Chemistry, 1995
- Specificity in chaperonin-mediated protein foldingNature, 1995
- An unstable beta 2-microglobulin: major histocompatibility complex class I heavy chain intermediate dissociates from calnexin and then is stabilized by binding peptide.The Journal of Experimental Medicine, 1994
- Folding of VSV G Protein: Sequential Interaction with BiP and CalnexinScience, 1994
- Calnexin retains unassembled major histocompatibility complex class I free heavy chains in the endoplasmic reticulum.The Journal of Experimental Medicine, 1994
- MHC class l/β2-microglobulin complexes associate with TAP transporters before peptide bindingNature, 1994
- A molecular model of MHC class-I-restricted antigen processingImmunology Today, 1992
- Participation of a novel 88-kD protein in the biogenesis of murine class I histocompatibility molecules.The Journal of cell biology, 1991