Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1A membrane protein complex mediates retro-translocation from the ER lumen into the cytosolDisulphide production by Ero1α-PDI relay is rapid and effectively regulatedFusion of CHOP to a novel RNA-binding protein in human myxoid liposarcomaHeightened stress response in primary fibroblasts expressing mutant eIF2B genes from CACH/VWM leukodystrophy patientsHeat shock protein 90 modulates the unfolded protein response by stabilizing IRE1alpha.Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3Identification of novel stress-induced genes downstream of chopControl of PERK eIF2alpha kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK.Somatic CALR mutations in myeloproliferative neoplasms with nonmutated JAK2The molecular basis for selective inhibition of unconventional mRNA splicing by an IRE1-binding small moleculeThe gadd and MyD genes define a novel set of mammalian genes encoding acidic proteins that synergistically suppress cell growthTransmission of cell stress from endoplasmic reticulum to mitochondria: enhanced expression of Lon proteaseDivergent effects of PERK and IRE1 signaling on cell viabilityCrystal Structure of P58(IPK) TPR Fragment Reveals the Mechanism for its Molecular Chaperone Activity in UPRFlavonol Activation Defines an Unanticipated Ligand-Binding Site in the Kinase-RNase Domain of IRE1The structure of the PERK kinase domain suggests the mechanism for its activationSignal integration in the endoplasmic reticulum unfolded protein responseHuman 75-kDa DNA-pairing protein is identical to the pro-oncoprotein TLS/FUS and is able to promote D-loop formationPerk is essential for translational regulation and cell survival during the unfolded protein responseRearrangement of the transcription factor gene CHOP in myxoid liposarcomas with t(12;16)(q13;p11)IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNAA novel effector domain from the RNA-binding protein TLS or EWS is required for oncogenic transformation by CHOPCharacterization of the CHOP breakpoints and fusion transcripts in myxoid liposarcomas with the 12;16 translocationTLS (FUS) binds RNA in vivo and engages in nucleo-cytoplasmic shuttlingTLS (translocated-in-liposarcoma) is a high-affinity interactor for steroid, thyroid hormone, and retinoid receptorsStress-induced phosphorylation and activation of the transcription factor CHOP (GADD153) by p38 MAP KinaseCHOP, a novel developmentally regulated nuclear protein that dimerizes with transcription factors C/EBP and LAP and functions as a dominant-negative inhibitor of gene transcriptionProtein translation and folding are coupled by an endoplasmic-reticulum-resident kinaseExpression patterns of the human sarcoma-associated genes FUS and EWS and the genomic structure of FUSA selective inhibitor of eIF2alpha dephosphorylation protects cells from ER stressERAD inhibitors integrate ER stress with an epigenetic mechanism to activate BH3-only protein NOXA in cancer cellsArsenite-inducible RNA-associated protein (AIRAP) protects cells from arsenite toxicityIncreased sensitivity to dextran sodium sulfate colitis in IRE1beta-deficient miceHyperhomocysteinemia and function of the endoplasmic reticulumModulation of Innate Immune Signalling by Lipid-Mediated MAVS Transmembrane Domain OligomerizationMammalian stress granules represent sites of accumulation of stalled translation initiation complexesCotranslocational degradation protects the stressed endoplasmic reticulum from protein overloadRegulated translation initiation controls stress-induced gene expression in mammalian cellsActivating transcription factor 3 is integral to the eukaryotic initiation factor 2 kinase stress response
P50
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P50
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Professor of Cellular Pathophy ...... at the University of Cambridge
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David Ron
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David Ron
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David Ron
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David Ron
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David Ron
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no2008168350
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0000-0002-3014-5636
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1955-01-01T00:00:00Z
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lccn-no2008168350