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 …

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

Stress induced by the accumulation of unfolded proteins in the endoplasmic reticulum (ER)
is a feature of specialized secretory cells and is also observed in many diseases, including …

Inositol-requiring enzyme 1 (IRE1) is the most conserved transducer of the unfolded protein
response (UPR), a homeostatic response that preserves proteostasis. Intriguingly, via its …

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 …

Effector mechanisms of the unfolded protein response (UPR) in the endoplasmic reticulum
(ER) are well-characterised, but how ER proteostasis is sensed is less well understood …

Intestinal goblet cells are secretory cells specialized in the production of mucins, and as
such are challenged by the need for efficient protein folding. Goblet cells express Inositol …

The endoplasmic reticulum (ER) is involved in the development of insulin resistance and
progression to type 2 diabetes mellitus (T2DM). Disruption of ER homeostasis leads to ER …

Proteins are notorious for their unpleasant behavior—continually at risk of misfolding,
collecting damage, aggregating, and causing toxicity and disease. To counter these …

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 …