… unfolded/misfolded proteins directly bind to the amino-terminal luminal domain of Ire1 p to
induce dimerization. A recent study showed that unfolded proteins … with unfolded proteins in …

… by the abnormal accumulation of unfolded or misfolded proteins at the endoplasmic …
unfolded protein response (UPR), a signal transduction pathway that senses the fidelity of protein …

… These pathways are called the unfolded protein response (UPR). In this review, we briefly
summarize principles of protein folding and molecular chaperone function important for a …

… mechanism to prevent further accumulation of unfolded proteins… unfolded protein response
(UPR). The UPR detects the build-up of unfolded or misfolded proteins and adjust the protein …

… proteins. Perturbations that alter ER homeostasis can lead to accumulation of unfolded proteins
… an intracellular signaling pathway – the unfolded protein response(UPR). The UPR is an …

… secreted proteins. Here we review our current understanding of how an unfolded protein …
, and how downstream events in this stress response are regulated. We propose a model in …

… /unfolded proteins in the ER. To maintain ER homeostasis, eukaryotic cells have evolved the
unfolded protein response … oxidative stress, and inflammatory response pathways. The UPR …

… response known as the unfolded protein response (UPR). Three major stress sensors control
UPR-dependent responses: inositol-requiring enzyme 1α (IRE1α), protein kinase … proteins …

… protein folding by an inbuilt quality control system involving both the ER and the Golgi apparatus.
Unfolded or misfolded proteins … proteins can also trigger the unfolded protein response (…

… Unfolded protein response (UPR) is an important genomic response to endoplasmic …
During the UPR, accumulated unfolded protein is either correctly refolded, or unsuccessfully …