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 …

The unfolded protein response (UPR) is a mechanism aiming at restoring endoplasmic
reticulum (ER) homeostasis and is likely involved in other adaptive pathways. The UPR is …

Activation of the IRE1/XBP1s signaling arm of the unfolded protein response (UPR) is a
promising strategy to correct defects in endoplasmic reticulum (ER) proteostasis implicated …

The endoplasmic reticulum (ER) is responsible for the synthesis of one-third of the cellular
proteome and is constantly challenged by physiological and environmental situations that …

Environmental stressors disrupt secretory protein folding and proteostasis in the
endoplasmic reticulum (ER), leading to ER stress. The unfolded protein response (UPR) …

The endoplasmic reticulum (ER) stress response is triggered by any condition that disrupts
protein folding and promotes the accumulation of unfolded proteins in the lumen of the …

Accumulation of misfolded proteins in ER activates the unfolded protein response (UPR), a
multifunctional signaling pathway that is important for cell survival. The UPR is regulated by …

Abstract The site-1 and site-2 proteases (S1P and S2P) were identified over 20 years ago,
and the functions of both have been addressed in numerous studies ever since. Whereas …

Maintenance of homeostasis of the endoplasmic reticulum (ER) ensures the balance
between loading of nascent proteins and their secretion. Certain developmental conditions …

Proteostasis is critical for cells to maintain the balance between protein synthesis, quality
control, and degradation. This is particularly important for myeloid cells of the central …