Quality control in the endoplasmic reticulum.

By M. Michalak. Seminars in Cell and Developmental Biology, 2010

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Protein quality control in the early secretory pathway (2008, background): “Protein QC (Box 1) is intimately linked to the processes of folding (Ellgaard and Helenius, 2003; Sitia and Braakman, 2003).”
The Role of the PERK/eIF2α/ATF4/CHOP Signaling Pathway in Tumor Progression During Endoplasmic Reticulum Stress (2016, background): “The ER has a quality control system to eliminate unfolded or misfolded proteins from the secretory pathway and exports only the properly folded proteins to their final destinations [14].”
One step at a time: endoplasmic reticulum-associated degradation (2008, background): “To ensure that the ER assembly line manufactures products that meet the needs of the cell, secreted proteins are subject to ER quality control (ERQC”
Glycosyltransferase complexes in eukaryotes: long-known, prevalent but still unrecognized (2015, background): “The Glc 3-Man 9 GlcNAc 2 core structure is subject to trimming by aglucosidases I and II, yielding Glc 2 Man 9 GlcNAc 2 and Glc 1 Man 9 GlcNAc 2 structures, the latter of which serves for ER quality control by ER chaperones Erp57, calnexin and calreticulin [25] [26] [27] .”