Glycoprotein folding in the endoplasmic reticulum: A tale of three chaperones?

  • High S
  • Lecomte F
  • Russell S
 et al. 
  • 45


    Mendeley users who have this article in their library.
  • 121


    Citations of this article.


The endoplasmic reticulum (ER) is a major site of protein synthesis and its inside, or lumen, is a major site of protein folding. The lumen of the ER contains many folding factors and molecular chaperones, which facilitate protein folding by increasing both the rate and the efficiency of this process. Amongst the many ER folding factors, there are three components that specifically modulate the folding glycoproteins bearing N-linked carbohydrate side chains. These components are calnexin, calreticulin and ERp57, and this review focuses on the molecular basis for their capacity to influence glycoprotein folding. Copyright (C) 2000 Federation of European Biochemical Societies.

Author-supplied keywords

  • Calnexin
  • ERp57
  • Endoplasmic reticulum
  • Glycoprotein
  • Molecular chaperone
  • Protein folding

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Get full text


  • Stephen High

  • Fabienne J.L. Lecomte

  • Sarah J. Russell

  • Benjamin M. Abell

  • Jason D. Oliver

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free