When protein folding in the endoplasmic reticulum (ER) is disrupted by alterations in
homeostasis in the ER lumen, eucaryotic cells activate a series of signal transduction …

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 …

▪ Abstract In the endoplasmic reticulum (ER), secretory and transmembrane proteins fold into
their native conformation and undergo posttranslational modifications important for their …

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 …

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 …

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 …

Simple Summary The unfolded protein response (UPR) is the cells' way of maintaining the
balance of protein folding in the endoplasmic reticulum, which is the section of the cell …

The unfolded protein response (UPR) is an ensemble of signal transduction pathways that
respond to perturbations in the oxidative, pro-folding environment of the endoplasmic …

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

Cells respond to the accumulation of unfolded proteins by activating signal transduction
cascades that improve protein folding. One example of such a cascade is the unfolded …