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 …

▪ Abstract In the endoplasmic reticulum (ER), secretory and transmembrane proteins fold into
their native conformation and undergo posttranslational modifications important for their …

Conformational diseases are caused by mutations altering the folding pathway or final
conformation of a protein. Many conformational diseases are caused by mutations in …

Inositol-requiring enzyme type 1 (IRE1) is a serine/threonine kinase acting as one of three
branches of the Unfolded Protein Response (UPR) signaling pathway, which is activated …

Nonstandard abbreviations used: endoplasmic reticulum (ER); unfolded protein response
(UPR); basic leucine zipper (bZIP); UPR element (UPRE); endoplasmic reticulum stress …

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 transcription factor X-box binding protein 1 (XBP-1) is essential for the differentiation of
plasma cells and the unfolded protein response (UPR). Here we show that UPR-induced …

Protein folding in the mitochondria is assisted by nuclear-encoded compartment-specific
chaperones but regulation of the expression of their encoding genes is poorly understood …

The membrane of the endoplasmic reticulum (ER) of a cell forms contacts directly with
mitochondria whereby the contact is referred to as the m itochondrion-a ssociated ER m …

Unfolded proteins in the endoplasmic reticulum (ER) activate the ER transmembrane sensor
Ire1 to trigger the unfolded protein response (UPR), a homeostatic signaling pathway that …