Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1.
Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress.
XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor.
Complementary signaling pathways regulate the unfolded protein response and are required for C. elegans development.
Heat shock protein 90 modulates the unfolded protein response by stabilizing IRE1alpha.
Structure and intermolecular interactions of the luminal dimerization domain of human IRE1alpha.
JAB1 participates in unfolded protein responses by association and dissociation with IRE1.
Synoviolin promotes IRE1 ubiquitination and degradation in synovial fibroblasts from mice with collagen-induced arthritis.
USP14 inhibits ER-associated degradation via interaction with IRE1alpha.
BAX inhibitor-1 is a negative regulator of the ER stress sensor IRE1alpha.
Unconventional splicing of XBP1 mRNA occurs in the cytoplasm during the mammalian unfolded protein response.
A crucial role for RACK1 in the regulation of glucose-stimulated IRE1alpha activation in pancreatic beta cells.
HSP72 protects cells from ER stress-induced apoptosis via enhancement of IRE1alpha-XBP1 signaling through a physical interaction.
Structure of the Ire1 autophosphorylation complex and implications for the unfolded protein response.
The unfolded protein response: integrating stress signals through the stress sensor IRE1α.
Ursolic acid induces ER stress response to activate ASK1-JNK signaling and induce apoptosis in human bladder cancer T24 cells.
PARP16 is a tail-anchored endoplasmic reticulum protein required for the PERK- and IRE1α-mediated unfolded protein response.
Vascular endothelial cell growth-activated XBP1 splicing in endothelial cells is crucial for angiogenesis.
Using an in situ proximity ligation assay to systematically profile endogenous protein-protein interactions in a pathway network.
Yip1A, a novel host factor for the activation of the IRE1 pathway of the unfolded protein response during Brucella infection.
XBP 1-Deficiency Abrogates Neointimal Lesion of Injured Vessels Via Cross Talk With the PDGF Signaling.
Compounds Triggering ER Stress Exert Anti-Melanoma Effects and Overcome BRAF Inhibitor Resistance.
A critical role of DDRGK1 in endoplasmic reticulum homoeostasis via regulation of IRE1α stability.
A J-Protein Co-chaperone Recruits BiP to Monomerize IRE1 and Repress the Unfolded Protein Response.
A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells.
IRE1 dimer autophosphorylates
IRE1 binds IRE1 forming dimer
IRE1:BiP dissociates in response to unfolded protein
IRE1alpha hydrolyzes Xbp1 mRNA and Xbp1 mRNA is spliced