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Endoplasmic Reticulum-Associated Degradation and Protein Quality Control
2016Approximately one-third of all polypeptides synthesized in eukaryotes are targeted to the endoplasmic reticulum (ER), and once associated with this compartment they are chemically modified. The folding status of the resulting nascent proteins is then surveyed by molecular chaperones and lectins.
Zacchi, L.F. +3 more
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Roles of Ubiquitin in Endoplasmic Reticulum-Associated Protein Degradation (ERAD)
Current Protein & Peptide Science, 2012In the secretory pathway, quality control for the correct folding of proteins is largely occurring in the endoplasmic reticulum (ER), at the earliest possible stage and in an environment where early folding intermediates mix with terminally misfolded species.
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ENDOPLASMIC RETICULUM ASSOCIATED DEGRADATION (ERAD) IN THE LIVER
2019Recent literature has revolutionized our view on the patho-physiological importance and the underlying molecular mechanism of endoplasmic reticulum (ER)-associated degradation (ERAD) in health and disease. Aside from being a downstream element of ER stress response or the unfolded protein response (UPR), ERAD also plays a direct and vital role in ...
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Endoplasmic Reticulum-Associated Protein Degradation
2013R. Bernasconi, M. Molinari
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Endoplasmic Reticulum Degradation Requires Lumen to Cytosol Signaling
Journal of Cell Biology, 2000Richard Gardner, R Y Hampton
exaly