Endoplasmic reticulum quality control (ERQC) pathways comprising chaperones, folding
enzymes, and degradation factors ensure the fidelity of ER protein folding and trafficking to …

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 unfolded protein response (UPR) is a highly conserved pathway that allows the cell to
manage endoplasmic reticulum (ER) stress that is imposed by the secretory demands …

Life is stressful. Organisms are repeatedly exposed to stressors that disrupt protein
homeostasis (proteostasis), resulting in protein misfolding and aggregation. To sense and …

Tumors that express detectable levels of the product of the ESR1 gene (estrogen receptor-α;
ERα) represent the single largest molecular subtype of breast cancer. More women …

Endoplasmic reticulum (ER) stress sensors use a related luminal domain to monitor the
unfolded protein load and convey the signal to downstream effectors, signaling an unfolded …

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 …

▪ Abstract From a process involved in cell wall synthesis in archaea and some bacteria, N-
linked glycosylation has evolved into the most common covalent protein modification in …

The accumulation of unfolded proteins in the lumen of the endoplasmic reticulum (ER)
induces a coordinated adaptive program called the unfolded protein response (UPR). The …

Multiple myeloma (MM) is an incurable plasma cell malignancy. The 26S proteasome
inhibitor, bortezomib, selectively induces apoptosis in MM cells; however, the nature of its …