Association of folding intermediates of glycoproteins with calnexin during protein maturation.

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.

journal_name

Nature

journal_title

Nature

authors

Ou WJ,Cameron PH,Thomas DY,Bergeron JJ

doi

10.1038/364771a0

subject

Has Abstract

pub_date

1993-08-26 00:00:00

pages

771-6

issue

6440

eissn

0028-0836

issn

1476-4687

journal_volume

364

pub_type

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