A new unfolded protein response has been discovered that is distinct from the heat shock response and protects mammalian cells from proteotoxic stress.

A unique form of regulation has been observed in the unfolded protein response of S. pombe, along with a novel mechanism of post-transcriptional mRNA processing.

Endoplasmic reticulum stress in yeast activates not only the UPR but also Rpn4, promoting the clearance of misfolded proteins from the cytosol as part of a modular cross-compartment stress response.

The chaperone protein BiP forms complexes with Ire1 and Perk that dissociate when unfolded proteins bind to BiP to activate the unfolded protein response in the ER.

ER-stress sensing mechanism of the unfolded protein response sensor/transducer IRE1 is conserved from yeast to mammals, where in mammals, unfolded protein binding to IRE1's ER lumenal domain is coupled to its oligomerization and activation through an allosteric conformational change.

A herpesvirus harnesses the unfolded protein response to regulate its own life cycle, revealing an unexpected role of XBP1u as a potent repressor of the most important viral promoter.

The unfolded protein response regulates neuronal dendrite morphogenesis by controlling the folding of a transmembrane leucine-rich repeat (LRR) protein.

RNA decay is used at multiple points in the budding yeast unfolded protein response to regulate its suppression and activation, and possibly its attenuation.

Ceapins enable selective pharmacological inhibition of the cytoprotective transcriptional response to endoplasmic reticulum stress through ATF6α without affecting other branches of the unfolded protein response.

Estrogen is a systemic factor that promotes hematopoietic regeneration by activating the unfolded protein responses.