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 …

The secretory capacity of a cell is constantly challenged by physiological demands and
pathological perturbations. To adjust and match the protein-folding capacity of the …

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

Cells operate a signaling network termed the unfolded protein response (UPR) to monitor
protein-folding capacity in the endoplasmic reticulum (ER). Inositol-requiring enzyme 1 …

In cells experiencing unrelieved endoplasmic reticulum (ER) stress, the ER transmembrane
kinase/endoribonuclease (RNase)—IRE1α—endonucleolytically degrades ER-localized …

Endoplasmic reticulum (ER)-associated degradation (ERAD) represents a principle quality
control mechanism to clear misfolded proteins in the ER; however, its physiological …

Maintenance of endoplasmic reticulum (ER) proteostasis is controlled by a dynamic
signaling network known as the unfolded protein response (UPR). IRE1α is a major UPR …

Lipid droplets (LDs) are cellular organelles critical for lipid homeostasis, with intramyocyte
LD accumulation implicated in metabolic disorder-associated heart diseases. Here we …

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 …