Within the cell, several mechanisms exist to maintain homeostasis of the endoplasmic
reticulum (ER). One of the primary mechanisms is the unfolded protein response (UPR). 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 …

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

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 endoplasmic reticulum (ER) has diverse functions, and especially misfolded protein
modification is in the focus of this review paper. With a highly regulatory mechanism, called …

In the endoplasmic reticulum (ER), secretory and membrane proteins are properly folded
and modified, and the failure of these processes leads to ER stress. At the same time …

Endoplasmic reticulum (ER) stress is a hallmark feature of secretory cells and many
diseases, including cancer, neurodegeneration, and diabetes. Adaptation to protein-folding …

This chapter provides an overview of our present understanding of mechanisms of sensing
protein folding status and endoplasmic reticulum (ER) stress in eukaryotic cells. The ER …

The unfolded protein response (UPR) is an essential cell signaling system that detects the
accumulation of misfolded proteins within the endoplasmic reticulum (ER) and initiates a …

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 …