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  • Title: Protein folding in the endoplasmic reticulum.
    Author: Braakman I, Hebert DN.
    Journal: Cold Spring Harb Perspect Biol; 2013 May 01; 5(5):a013201. PubMed ID: 23637286.
    Abstract:
    In this article, we will cover the folding of proteins in the lumen of the endoplasmic reticulum (ER), including the role of three types of covalent modifications: signal peptide removal, N-linked glycosylation, and disulfide bond formation, as well as the function and importance of resident ER folding factors. These folding factors consist of classical chaperones and their cochaperones, the carbohydrate-binding chaperones, and the folding catalysts of the PDI and proline cis-trans isomerase families. We will conclude with the perspective of the folding protein: a comparison of characteristics and folding and exit rates for proteins that travel through the ER as clients of the ER machinery.
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