An accumulation of misfolded proteins in the endoplasmic reticulum (ER) triggers the
unfolded protein response (UPR) mediated via the activation of three transmembrane …

One of the early cellular responses to endoplasmic reticulum (ER) stress is the activation of
the unfolded protein response (UPR). ER stress and the UPR are both implicated in …

Protein misfolding in the endoplasmic reticulum (ER) activates a set of intracellular signaling
pathways, collectively termed the Unfolded Protein Response (UPR). UPR signaling …

The endoplasmic reticulum (ER) is a principal site for folding and maturation of
transmembrane, secretory and ER-resident proteins. Perturbations that alter ER …

Endoplasmic reticulum (ER) stress activates a set of signaling pathways, collectively termed
the unfolded protein response (UPR). The three UPR branches (IRE1, PERK, and ATF6) …

In response to an accumulation of unfolded proteins in the endoplasmic reticulum (ER)
lumen, three ER transmembrane signaling proteins, inositol-requiring enzyme 1 (IRE1) …

The unfolded protein response (UPR) is an adaptive stress response in which cells recover
from the accumulation of unfolded or misfolded proteins in the endoplasmic reticulum (ER) …

Protein-folding stress at the endoplasmic reticulum (ER) is a salient feature of specialized
secretory cells and is also involved in the pathogenesis of many human diseases. ER stress …

The kinases PERK and IRE1 alleviate endoplasmic reticulum (ER) stress by orchestrating
the unfolded protein response (UPR). If stress mitigation fails, PERK promotes cell death by …

A diverse array of cellular stresses can lead to accumulation of misfolded or unfolded
proteins in endoplasmic reticulum (ER), which subsequently elicits ER stress. Inositol …