The endoplasmic reticulum (ER) plays role in the maintenance of numerous aspects of
cellular and organismal homeostasis by folding, modifying, and exporting nascent secretory …

The unfolded protein response (UPR) plays a central role in regulating endoplasmic
reticulum (ER) and global cellular physiology in response to pathologic ER stress. The UPR …

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 …

The stress sensors ATF6, IRE1, and PERK monitor deviations from homeostatic conditions
in the endoplasmic reticulum (ER), a protein biogenesis compartment of eukaryotic cells …

The inability of cells to properly fold, modify and assemble secretory and transmembrane
proteins leads to accumulation of misfolded proteins in the endoplasmic reticulum (ER) …

Unfolded proteins and other conditions affecting endoplasmic reticulum (ER) homeostasis
cause ER stress. The cell reacts to ER stress by activation of the unfolded protein response …

The unfolded protein response (UPR) regulates gene expression in response to stress in the
endoplasmic reticulum (ER). We determined the transcriptional scope of the UPR using DNA …

The endoplasmic reticulum (ER) is a critical organelle for protein synthesis, folding and
modification, and lipid synthesis and calcium storage. Dysregulation of ER functions leads to …

Accumulation of unfolded proteins in the endoplasmic reticulum (ER) causes a state of
cellular stress known as ER stress. The cells respond to ER stress by activating the unfolded …

Perturbance of endoplasmic reticulum (ER) function, either by the mutant proteins not folding
correctly, or by an excessive accumulation of proteins in the organelle, will lead to the …