Endoplasmic reticulum stress-independent activation of unfolded protein response kinases by a small molecule ATP-mimic

Allosteric Inhibition of the IRE1α RNase Preserves Cell Viability and Function during Endoplasmic Reticulum Stress

(2014) Rajarshi Ghosh et al.   CELL

XBP1 promotes triple-negative breast cancer by controlling the HIF1α pathway

(2014) Xi Chen et al.   NATURE

Structure and mechanism of action of the hydroxy–aryl–aldehyde class of IRE1 endoribonuclease inhibitors

(2014) Mario Sanches et al.   Nature Communications

Xbp1s-Negative Tumor B Cells and Pre-Plasmablasts Mediate Therapeutic Proteasome Inhibitor Resistance in Multiple Myeloma

(2013) Chungyee Leung-Hagesteijn et al.   CANCER CELL

RAF Inhibitors Activate the MAPK Pathway by Relieving Inhibitory Autophosphorylation

(2013) Matthew Holderfield et al.   CANCER CELL

Oral Treatment Targeting the Unfolded Protein Response Prevents Neurodegeneration and Clinical Disease in Prion-Infected Mice

(2013) J. A. Moreno et al.   Science Translational Medicine

Structural Basis of the Unfolded Protein Response

(2012) Alexei Korennykh et al.   Annual Review of Cell and Developmental Biology

Discovery of 7-Methyl-5-(1-{[3-(trifluoromethyl)phenyl]acetyl}-2,3-dihydro-1H-indol-5-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine (GSK2606414), a Potent and Selective First-in-Class Inhibitor of Protein Kinase R (PKR)-like Endoplasmic Reticulum Kinase (PERK)

(2012) Jeffrey M. Axten et al.   JOURNAL OF MEDICINAL CHEMISTRY

Divergent allosteric control of the IRE1α endoribonuclease using kinase inhibitors

(2012) Likun Wang et al.   Nature Chemical Biology

The Evolution of Protein Kinase Inhibitors from Antagonists to Agonists of Cellular Signaling

(2011) Arvin C. Dar et al.   Annual Review of Biochemistry

Cofactor-mediated conformational control in the bifunctional kinase/RNase Ire1

(2011) Alexei V Korennykh et al.   BMC BIOLOGY

Homeostatic adaptation to endoplasmic reticulum stress depends on Ire1 kinase activity

(2011) Claudia Rubio et al.   JOURNAL OF CELL BIOLOGY

Unfolded Proteins Are Ire1-Activating Ligands That Directly Induce the Unfolded Protein Response

(2011) B. M. Gardner et al.   SCIENCE

RAF inhibitors transactivate RAF dimers and ERK signalling in cells with wild-type BRAF

(2010) Poulikos I. Poulikakos et al.   NATURE

RAF inhibitors prime wild-type RAF to activate the MAPK pathway and enhance growth

(2010) Georgia Hatzivassiliou et al.   NATURE

Mammalian endoplasmic reticulum stress sensor IRE1 signals by dynamic clustering

(2010) H. Li et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Positive contribution of ERdj5/JPDI to endoplasmic reticulum protein quality control in the salivary gland

(2009) Akira Hosoda et al.   BIOCHEMICAL JOURNAL

A dimerization-dependent mechanism drives RAF catalytic activation

(2009) Thanashan Rajakulendran et al.   NATURE

Small Molecule Recognition of c-Src via the Imatinib-Binding Conformation

(2008) Arvin C. Dar et al.   CHEMISTRY & BIOLOGY

Tuning a Three-Component Reaction For Trapping Kinase Substrate Complexes

(2008) Alexander V. Statsuk et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

The unfolded protein response signals through high-order assembly of Ire1

(2008) Alexei V. Korennykh et al.   NATURE