Misfolded, potentially toxic proteins in the lumen and membrane of the endoplasmic
reticulum (ER) are eliminated by proteasomes in the cytosol through ER-associated …

ER-phagy (reticulophagy) defines the degradation of portions of the endoplasmic reticulum
(ER) within lysosomes or vacuoles. It is part of the self-digestion (ie, autophagic) programs …

Insulin synthesis in pancreatic β‐cells is initiated as preproinsulin. Prevailing glucose
concentrations, which oscillate pre‐and postprandially, exert major dynamic variation in …

Many human diseases are associated with mutations causing protein misfolding and
aggregation in the endoplasmic reticulum (ER). ER-associated degradation (ERAD) is a …

ER-phagy, literally endoplasmic reticulum (ER)-eating, defines the constitutive or regulated
clearance of ER portions within metazoan endolysosomes or yeast and plant vacuoles. The …

About 40% of the eukaryotic cell's proteins are inserted co-or post-translationally in the
endoplasmic reticulum (ER), where they attain the native structure under the assistance of …

Background The quality of proteins destined for the secretory pathway is ensured by two
distinct mechanisms in the endoplasmic reticulum (ER): productive folding of newly …

The reversal of thiol oxidation in proteins within the endoplasmic reticulum (ER) is crucial for
protein folding, degradation, chaperone function, and the ER stress response. Our …

Protein disulfide isomerases are thiol oxidoreductase chaperones from thioredoxin
superfamily. As redox folding catalysts from the endoplasmic reticulum (ER), their roles in …

Both basal and glucose-stimulated insulin release occur primarily by insulin secretory
granule exocytosis from pancreatic β cells, and both are needed to maintain normoglycemia …