Association of folding intermediates of glycoproteins with calnexin during protein maturation View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1993-08

AUTHORS

Wei-Jia Ou, Pamela H. Cameron, David Y. Thomas, John J. M. Bergeron

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. More... »

PAGES

771-776

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/364771a0

DOI

http://dx.doi.org/10.1038/364771a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1010850274

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8102790


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