Cellular stress induced by the abnormal accumulation of unfolded or misfolded proteins at
the endoplasmic reticulum (ER) is emerging as a possible driver of human diseases …

Simple Summary The unfolded protein response (UPR) is the cells' way of maintaining the
balance of protein folding in the endoplasmic reticulum, which is the section of the cell …

The secretory capacity of a cell is constantly challenged by physiological demands and
pathological perturbations. To adjust and match the protein-folding capacity of the …

Endoplasmic reticulum (ER)-associated degradation (ERAD) and the unfolded protein
response (UPR) are two key quality-control machineries in the cell. ERAD is responsible for …

Stress induced by accumulation of misfolded proteins in the endoplasmic reticulum is
observed in many physiological and pathological conditions. To cope with endoplasmic …

Stress-signaling pathways are evolutionarily conserved and play an important role in the
maintenance of homeostasis. These pathways are also critical for adaptation to new cellular …

Endoplasmic reticulum (ER) calcium signaling is implicated in a myriad of coordinated
cellular processes. The ER calcium content is tightly regulated as it allows a favorable …

Inositol-requiring enzyme 1 (IRE1) is the most conserved transducer of the unfolded protein
response (UPR), a homeostatic response that preserves proteostasis. Intriguingly, via its …

The ability to respond to perturbations in endoplasmic reticulum (ER) function is a
fundamentally important property of all cells, but ER stress can also lead to apoptosis. In …

The endoplasmic reticulum (ER) functions to properly fold and process secreted and
transmembrane proteins. Environmental and genetic factors that disrupt ER function cause …