Proteins synthesized in the endoplasmic reticulum (ER) are properly folded with the
assistance of ER chaperones. Malfolded proteins are disposed of by ER‐associated protein …

The extracellular space is an environment hostile to unmodified polypeptides. For this
reason, many eukaryotic proteins destined for exposure to this environment through …

A substantial fraction of eukaryotic gene products are synthesized by ribosomes attached at
the cytosolic face of the endoplasmic reticulum (ER) membrane. These polypeptides enter …

Rising interest in the mechanism and function of the proteasomes and the ubiquitin system
revealed that it is hard to find any aspect of the cellular metabolic network that is not directly …

Filamentous fungi are commonly used in the fermentation industry for the large-scale
production of proteins–mainly industrial enzymes. Recent advances in fungal genomics and …

The endoplasmic reticulum (ER) is the site of folding for proteins that are resident in the ER
or that are destined for the Golgi, endosomes, lysosomes, the plasma membrane, or …

Glycosylation of asparagine residues in Asn-x-Ser/Thr motifs is a common covalent
modification of proteins in the lumen of the endoplasmic reticulum (ER). By substantially …

The majority of proteins that traverse the secretory pathway receive asparagine (Asn)-linked
glycosylations. Glycans are bulky hydrophilic modifications that serve a variety of structural …

Plasma cells producing high levels of paraprotein are dependent on the unfolded protein
response (UPR) and chaperone proteins to ensure correct protein folding and cell survival …

Proteins expressed in the endoplasmic reticulum (ER) are covalently modified by co-
translational addition of pre-assembled core glycans (glucose3-mannose9-N …