The endoplasmic reticulum (ER) is an important site for protein folding and maturation in
eukaryotes. The cellular requirement to synthesize proteins within the ER is matched by its …

An accumulation of unfolded or misfolded proteins in the endoplasmic reticulum (ER) leads
to stress conditions. To mitigate such circumstances, stressed cells activate a homeostatic …

Coupling of structure-specific in vivo chemical modification to next-generation sequencing is
transforming RNA secondary structure studies in living cells. The dominant strategy for …

Most of the secreted and plasma membrane proteins are synthesized on membrane-bound
ribosomes on the endoplasmic reticulum (ER). They require engagement of ER-resident …

The unfolded protein response (UPR) is a conserved homeostatic program that is activated
by misfolded proteins in the lumen of the endoplasmic reticulum (ER). Recently, it became …

Secretory and transmembrane proteins enter the endoplasmic reticulum (ER) as unfolded
proteins and exit as either folded proteins in transit to their target organelles or as misfolded …

When unfolded proteins accumulate to irremediably high levels within the endoplasmic
reticulum (ER), intracellular signaling pathways called the unfolded protein response (UPR) …

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 …

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 …

The ability to ensure proteostasis is critical for maintaining proper cell function and
organismal viability but is mitigated by aging. We analyzed the role of the endoplasmic …