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 …

The endoplasmic reticulum (ER) is an important site for protein folding and maturation in
eukaryotes. The cellular requirement to synthesize proteins within the ER is matched by its …

Most of the secreted and plasma membrane proteins are synthesized on membrane-bound
ribosomes on the endoplasmic reticulum (ER). They require engagement of ER-resident …

The unfolded protein response (UPR) is a conserved homeostatic program that is activated
by misfolded proteins in the lumen of the endoplasmic reticulum (ER). Recently, it became …

The endoplasmic reticulum (ER) produces the vast majority of all proteins secreted into the
extracellular space, including hormones and cytokines, as well as cell surface receptors and …

Secretory and transmembrane proteins enter the endoplasmic reticulum (ER) as unfolded
proteins and exit as either folded proteins in transit to their target organelles or as misfolded …

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) detects the accumulation of unfolded proteins in the
endoplasmic reticulum (ER) and adjusts the protein-folding capacity to the needs of the cell …

The endoplasmic reticulum (ER) responds to the accumulation of unfolded proteins in its
lumen (ER stress) by activating intracellular signal transduction pathways—cumulatively …

Perturbations in endoplasmic reticulum (ER) homeostasis, including depletion of Ca 2+ or
altered redox status, induce ER stress due to protein accumulation, misfolding and …