The Protein Kinase/Endoribonuclease IRE1α That Signals the Unfolded Protein Response Has a Luminal N-terminal Ligand-independent Dimerization Domain
Open Access
- 1 May 2002
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 277 (21) , 18346-18356
- https://doi.org/10.1074/jbc.m112454200
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- 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 StressJournal of Biological Chemistry, 2001
- Tripartite Management of Unfolded Proteins in the Endoplasmic ReticulumCell, 2000
- Coupling of Stress in the ER to Activation of JNK Protein Kinases by Transmembrane Protein Kinase IRE1Science, 2000
- Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-βNature, 2000
- A Role for Presenilin-1 in Nuclear Accumulation of Ire1 Fragments and Induction of the Mammalian Unfolded Protein ResponseCell, 1999
- Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controlsGenes & Development, 1999
- Identification of the cis-Acting Endoplasmic Reticulum Stress Response Element Responsible for Transcriptional Induction of Mammalian Glucose-regulated ProteinsJournal of Biological Chemistry, 1998
- INTRACELLULAR SIGNALING FROM THE ENDOPLASMIC RETICULUM TO THE NUCLEUSAnnual Review of Cell and Developmental Biology, 1998
- Cloning of mammalian Ire1 reveals diversity in the ER stress responsesThe EMBO Journal, 1998
- A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cellsGenes & Development, 1998