The accumulation of misfolded proteins in the endoplasmic reticulum (ER) leads to ER
stress, resulting in activation of the unfolded protein response (UPR) that aims to restore …

Protein-folding stress at the endoplasmic reticulum (ER) is a salient feature of specialized
secretory cells and is also involved in the pathogenesis of many human diseases. ER stress …

The vast majority of proteins that a cell secretes or displays on its surface first enter the
endoplasmic reticulum (ER), where they fold and assemble. Only properly assembled …

Highly sophisticated mechanisms that modulate protein structure and function, which involve
synthesis and degradation, have evolved to maintain cellular homeostasis. Perturbations in …

IRE1α (inositol requiring enzyme 1 alpha) is one of the main transducers of the unfolded
protein response (UPR). IRE1α plays instrumental protumoral roles in several cancers, and …

Accumulation of unfolded or misfolded proteins in the endoplasmic reticulum (ER) leads to
ER stress, which is characteristic of cells with high level of secretory activity and implicated …

The unfolded protein response (UPR) is a network of intracellular signaling pathways that
maintain the protein-folding capacity of the endoplasmic reticulum (ER) in 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) …

Inositol-requiring transmembrane kinase endoribonuclease-1α (IRE1α) is the most
prominent and evolutionarily conserved unfolded protein response (UPR) signal transducer …

Protein kinases are known primarily for their ability to phosphorylate protein substrates,
which constitutes an essential biological process. Recently, compelling evidence has …