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-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 …

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

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

The endoplasmic reticulum (ER) is the cellular site of newly synthesized secretory and
membrane proteins. Such proteins must be properly folded and posttranslationally modified …

The efficient functioning of the endoplasmic reticulum (ER) is essential for most cellular
activities and survival. Conditions that interfere with ER function lead to the accumulation …

The endoplasmic reticulum is an organelle with multiple functions. The synthesis of
transmembrane proteins and proteins that are to be secreted occurs in this organelle. Many …

Inability to meet protein folding demands within the endoplasmic reticulum (ER) activates the
unfolded protein response (UPR), a signaling pathway with both adaptive and apoptotic …

The endoplasmic-reticulum (ER) stress response constitutes a cellular process that is
triggered by a variety of conditions that disturb folding of proteins in the ER. Eukaryotic cells …

Increased demands on the protein folding capacity of the endoplasmic reticulum (ER) trigger
the unfolded protein response (UPR). Comprised of a tripartite signaling system, the UPR …