The Molecular Chaperone Calnexin Binds Glc1Man9GlcNAc2 Oligosaccharide as an Initial Step in Recognizing Unfolded Glycoproteins
Open Access
- 1 March 1995
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 270 (9) , 4697-4704
- https://doi.org/10.1074/jbc.270.9.4697
Abstract
No abstract availableKeywords
This publication has 41 references indexed in Scilit:
- 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
- Calnexin retains unassembled major histocompatibility complex class I free heavy chains in the endoplasmic reticulum.The Journal of Experimental Medicine, 1994
- Kinetics and affinity of reactions between an antigen-specific T cell receptor and peptide-MHC complexesImmunity, 1994
- Calnexin: a membrane-bound chaperone of the endoplasmic reticulumTrends in Biochemical Sciences, 1994
- Regulation of MHC Class I Transport by the Molecular Chaperone, Calnexin (p88, IP90)Science, 1994
- Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigmCell, 1994
- Class II histocompatibility molecules associate with calnexin during assembly in the endoplasmic reticulumInternational Immunology, 1994
- Biology of Animal LectinsAnnual Review of Cell Biology, 1993
- Lumenal proteins of the mammalian endoplasmic reticulum are required to complete protein translocationCell, 1993
- Participation of a novel 88-kD protein in the biogenesis of murine class I histocompatibility molecules.The Journal of cell biology, 1991