Deficiencies in the protein-folding capacity of the endoplasmic reticulum (ER) in all
eukaryotic cells lead to ER stress and trigger the unfolded protein response (UPR),,. ER …

Aberrant folding of proteins in the endoplasmic reticulum activates the bifunctional
transmembrane kinase/endoribonuclease Ire1. Ire1 excises an intron from HAC1 messenger …

The unfolded protein response (UPR), caused by stress, matches the folding capacity of
endoplasmic reticulum (ER) to the load of client proteins in the organelle,. In yeast …

Eukaryotic cells control the levels of molecular chaperones and folding enzymes in the
endoplasmic reticulum (ER) by a transcriptional induction process termed the unfolded …

The unfolded protein response (UPR) activates Ire1, an endoplasmic reticulum (ER) resident
transmembrane kinase and ribonuclease (RNase), in response to ER stress. We used an in …

Accumulation of misfolded proteins in the lumen of the endoplasmic reticulum (ER) activates
the unfolded protein response (UPR). Ire1, an ER-resident transmembrane kinase/RNase …

Under conditions of endoplasmic reticulum (ER) stress, mammalian cells induce both
translational repression and the unfolded protein response that transcriptionally activates …

In yeast, the transmembrane protein kinase/endoribonuclease Ire1p activated by
endoplasmic reticulum stress cleaves HAC1 mRNA, leading to production of the …

An intracellular signaling from the endoplasmic reticulum (ER) to the nucleus, called the
unfolded protein response (UPR), is activated when unfolded proteins are accumulated in …

Genetic analysis of the cellular adaptation to malfolded proteins in the endoplasmic
reticulum (the unfolded protein response–UPR) has revealed a novel signaling pathway …