The unfolded protein response (UPR) is activated by endoplasmic reticulum (ER) stress and
is designed to restore cellular homeostasis through multiple intracellular signalling …

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 …

Unfolded stress response (UPR) is a conserved cellular pathway involved in protein quality
control to maintain homeostasis under different conditions and disease states characterized …

A variety of cell intrinsic or extrinsic stresses evoke perturbations in the folding environment
of the endoplasmic reticulum (ER), collectively known as ER stress. Adaptation to stress and …

The endoplasmic reticulum (ER) is the principal cellular organelle in which correct folding
and maturation of transmembrane, secretory, and ER-resident proteins occur. Research …

Proteins requiring post‐translational modifications such as N‐linked glycosylation are
processed in the endoplasmic reticulum (ER). A diverse array of cellular stresses can lead to …

The accumulation of unfolded proteins in the endoplasmic reticulum (ER) activates a
signaling cascade known as the unfolded protein response (UPR). Although activation of the …

Background The unfolded protein response (UPR) is a major signalling cascade acting in
the quality control of protein folding in the endoplasmic reticulum (ER). The cascade is …

The endoplasmic reticulum (ER) is the site for folding of membrane and secreted proteins in
the cell. Physiological or pathological processes that disturb protein folding in the ER cause …

Stress induced by accumulation of misfolded proteins in the endoplasmic reticulum is
observed in many physiological and pathological conditions. To cope with endoplasmic …