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 …

The unfolded protein response (UPR) is a signal transduction network activated by inhibition
of protein folding in the endoplasmic reticulum (ER). The UPR coordinates adaptive …

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 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 …

The unfolded protein response (UPR) is an intracellular signaling pathway that is activated
by the accumulation of unfolded proteins in the endoplasmic reticulum (ER). UPR activation …

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 …

Numerous environmental, physiological, and pathological insults disrupt protein-folding
homeostasis in the endoplasmic reticulum (ER), referred to as ER stress. Eukaryotic cells …

The unfolded protein response (UPR) is a conserved, intracellular signaling pathway
activated by endoplasmic reticulum (ER) stress. In mammalian cells, the UPR is controlled …

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

Since its discovery more than 25 years ago, great progress has been made in our
understanding of the unfolded protein response (UPR), a homeostatic mechanism that …