Association of folding intermediates of glycoproteins with calnexin during protein maturation
- 1 August 1993
- journal article
- Published by Springer Nature in Nature
- Vol. 364 (6440) , 771-776
- https://doi.org/10.1038/364771a0
Abstract
Calnexin, an endoplasmic reticulum transmembrane protein, represents a new type of molecular chaperone that selectively associates in a transient fashion with newly synthesized monomeric glycoproteins in HepG2 cells. Calnexin only recognizes glycoproteins when they are incompletely folded. Dissociation of glycoproteins from calnexin occurs at different rates and is related to the time taken for their folding, which may then initiate their differential transport rates from the endoplasmic reticulum.Keywords
This publication has 36 references indexed in Scilit:
- The major histocompatibility complex class I antigen-binding protein p88 is the product of the calnexin gene.Proceedings of the National Academy of Sciences, 1992
- The endoplasmic reticulum as a protein-folding compartmentTrends in Cell Biology, 1992
- Endoplasmic reticulum resident protein of 90 kilodaltons associates with the T- and B-cell antigen receptors and major histocompatibility complex antigens during their assembly.Proceedings of the National Academy of Sciences, 1992
- Protein folding in the cellNature, 1992
- Folding of influenza hemagglutinin in the endoplasmic reticulum.The Journal of cell biology, 1991
- Protein Oligomerization in the Endoplasmic ReticulumAnnual Review of Cell Biology, 1989
- Control of Protein Exit from the Endoplasmic ReticulumAnnual Review of Cell Biology, 1989
- Hepatoma secretory proteins migrate from rough endoplasmic reticulum to Golgi at characteristic ratesNature, 1983
- Homology between the primary structure of α-fetoprotein, deduced from a complete cDNA sequence, and serum albuminNature, 1981
- Human Hepatocellular Carcinoma Cell Lines Secrete the Major Plasma Proteins and Hepatitis B Surface AntigenScience, 1980