Accumulation of unfolded proteins in the endoplasmic reticulum (ER) activates the unfolded
protein response (UPR). In mammalian cells, UPR signals generated by several ER …

Apoptosis triggered by endoplasmic reticulum (ER) stress is associated with rapid
attenuation of the IRE1α and ATF6 pathways but persistent activation of the PERK branch of …

Alterations in cellular homeostasis that affect protein folding in the endoplasmic reticulum
(ER) trigger a signaling pathway known as the unfolded protein response (UPR). The …

The unfolded protein response is an adaptive stress response that responds to the
imbalance between the entry of newly synthesized unfolded proteins and the inherent …

Endoplasmic reticulum (ER) stress is a hallmark feature of secretory cells and many
diseases, including cancer, neurodegeneration, and diabetes. Adaptation to protein-folding …

Disruptions of the endoplasmic reticulum (ER) that perturb protein folding cause ER stress
and elicit an unfolded protein response (UPR) that involves translational and transcriptional …

The accumulation of unfolded proteins in the endoplasmic reticulum (ER) triggers the
unfolded protein response (UPR) through the activation of specialized sensors including …

Perturbations in endoplasmic reticulum (ER) homeostasis, including depletion of Ca 2+ or
altered redox status, induce ER stress due to protein accumulation, misfolding and …

The endoplasmic reticulum (ER) is an essential organelle involved in many cellular
functions including protein folding and secretion, lipid biosynthesis, and calcium …

Numerous genetic and environmental insults impede the ability of cells to properly fold and
posttranslationally modify secretory and transmembrane proteins in the endoplasmic …