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 …

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 …

The vast majority of proteins that a cell secretes or displays on its surface first enter the
endoplasmic reticulum (ER), where they fold and assemble. Only properly assembled …

Increased demand on the protein folding capacity of the endoplasmic reticulum (ER)
engages an adaptive reaction known as the unfolded protein response (UPR). The UPR …

The endoplasmic reticulum (ER) is a membranous intracellular organelle and the first
compartment of the secretory pathway. As such, the ER contributes to the production and …

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 …

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 …

Stress induced by accumulation of unfolded proteins at the endoplasmic reticulum (ER) is a
classic feature of secretory cells and is observed in many tissues in human diseases …

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

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 …