The eukaryotic heat shock response is an ancient and highly conserved transcriptional
program that results in the immediate synthesis of a battery of cytoprotective genes in the …

Protein disulphide bonds are formed in the endoplasmic reticulum of eukaryotic cells and
the periplasmic space of prokaryotic cells. The main pathways that catalyse the formation of …

The transcription of genes encoding soluble proteins that reside in the endoplasmic
reticulum (ER) is induced when unfolded proteins accumulate in the ER. Thus, an …

Disulfide bond formation is probably involved in the biogenesis of approximately one third of
human proteins. A central player in this essential process is protein disulfide isomerase or …

In eukaryotic cells, the accumulation of unfolded proteins in the endoplasmic reticulum (ER)
triggers a signaling pathway from the ER to the nucleus. Several yeast mutants defective in …

A variety of debilitating diseases including diabetes, Alzheimer's, Huntington's, Parkinson's,
and prion-based diseases are linked to stress within the endoplasmic reticulum (ER). Using …

Protein disulphide isomerase (PDI) has been known for many years to assist in the folding of
proteins containing disulphide bonds, but the exact mechanism by which it achieves this is …

We describe a conserved yeast gene, ERO1, that is induced by the unfolded protein
response and encodes a novel glycoprotein required for oxidative protein folding in the ER …

The mammalian protein disulphide-isomerase (PDI) family encompasses several highly
divergent proteins that are involved in the processing and maturation of secretory proteins in …

Background: Accumulation of unfolded proteins in the endoplasmic reticulum (ER) triggers
the transcriptional induction of molecular chaperones and folding enzymes localized in the …