Phosphorylation of eIF2α at serine 51 is an important determinant of cell survival and adaptation to glucose deficiency.
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Could the eIF2α-Independent Translation Be the Achilles Heel of Cancer?Stress granules in the viral replication cycleSuppression of ribosomal function triggers innate immune signaling through activation of the NLRP3 inflammasomePhosphorylation of Eukaryotic Initiation Factor-2α during Stress and Encystation in Entamoeba Species.Gene expression changes leading extreme alkaline tolerance in Amur ide (Leuciscus waleckii) inhabiting soda lake.Translation elongation factor 1A mutants with altered actin bundling activity show reduced aminoacyl-tRNA binding and alter initiation via eIF2α phosphorylation.OSU-03012 sensitizes breast cancers to lapatinib-induced cell killing: a role for Nck1 but not Nck2.A novel role for Tm7sf2 gene in regulating TNFα expressionActivating transcription factor 4, a mediator of the integrated stress response, is increased in the dorsal root ganglia following painful facet joint distraction.Protein kinase GCN2 mediates responses to glyphosate in Arabidopsis.IRES-mediated translation of cellular messenger RNA operates in eIF2α- independent manner during stress.Inhibition of PI3K/mTOR leads to adaptive resistance in matrix-attached cancer cells.KDEL receptor 1 regulates T-cell homeostasis via PP1 that is a key phosphatase for ISR.The PERK-eIF2α phosphorylation arm is a pro-survival pathway of BCR-ABL signaling and confers resistance to imatinib treatment in chronic myeloid leukemia cells.LKB1 inactivation dictates therapeutic response of non-small cell lung cancer to the metabolism drug phenforminAnti-leukemic mechanisms of pegylated arginase I in acute lymphoblastic T-cell leukemia.Phosphorylation of eIF2α attenuates statin-induced apoptosis by inhibiting the stabilization and translocation of p53 to the mitochondriaActivation status of integrated stress response pathways in neurones and astrocytes of HIV-associated neurocognitive disorders (HAND) cortex.Repression of global protein synthesis by Eif1a-like genes that are expressed specifically in the two-cell embryos and the transient Zscan4-positive state of embryonic stem cells.eIF2α phosphorylation bypasses premature senescence caused by oxidative stress and pro-oxidant antitumor therapies.Molecular signal networks and regulating mechanisms of the unfolded protein response.Translational and posttranslational regulation of XIAP by eIF2α and ATF4 promotes ER stress-induced cell death during the unfolded protein response.Control of oncogenesis by eIF2α phosphorylation: implications in PTEN and PI3K-Akt signaling and tumor treatment.Cell death induced by endoplasmic reticulum stress.Evidence for eIF2α phosphorylation-independent effects of GSK2656157, a novel catalytic inhibitor of PERK with clinical implications.ATF4 mediates necrosis induced by glucose deprivation and apoptosis induced by 2-deoxyglucose in the same cells.Glucose Deprivation Induces ATF4-Mediated Apoptosis through TRAIL Death Receptors.Conversion of 2-deoxyglucose-induced growth inhibition to cell death in normoxic tumor cells.HDAC pharmacological inhibition promotes cell death through the eIF2α kinases PKR and GCN2.eIF2α phosphorylation is required to prevent hepatocyte death and liver fibrosis in mice challenged with a high fructose diet.Definition of genetic events directing the development of distinct types of brain tumors from postnatal neural stem/progenitor cellsPhosphorylation of the translation initiation factor eIF2α at serine 51 determines the cell fate decisions of Akt in response to oxidative stressSchlafen2 mutation unravels a role for chronic ER stress in the loss of T cell quiescence.Cross-talk between protein synthesis, energy metabolism and autophagy in cancer.Dysregulation of mRNA translation and energy metabolism in cancer.PKR activation and eIF2α phosphorylation mediate human globin mRNA splicing at spliceosome assembly.Overexpression of Tobacco GCN2 Stimulates Multiple Physiological Changes Associated With Stress Tolerance.GCN2 controls the cellular checkpoint: potential target for regulating inflammation.
P2860
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P2860
Phosphorylation of eIF2α at serine 51 is an important determinant of cell survival and adaptation to glucose deficiency.
description
2010 nî lūn-bûn
@nan
2010 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Phosphorylation of eIF2α at se ...... ptation to glucose deficiency.
@ast
Phosphorylation of eIF2α at se ...... ptation to glucose deficiency.
@en
Phosphorylation of eIF2α at se ...... ptation to glucose deficiency.
@nl
type
label
Phosphorylation of eIF2α at se ...... ptation to glucose deficiency.
@ast
Phosphorylation of eIF2α at se ...... ptation to glucose deficiency.
@en
Phosphorylation of eIF2α at se ...... ptation to glucose deficiency.
@nl
prefLabel
Phosphorylation of eIF2α at se ...... ptation to glucose deficiency.
@ast
Phosphorylation of eIF2α at se ...... ptation to glucose deficiency.
@en
Phosphorylation of eIF2α at se ...... ptation to glucose deficiency.
@nl
P2093
P2860
P356
P1476
Phosphorylation of eIF2α at se ...... aptation to glucose deficiency
@en
P2093
Andreas I Papadakis
Antonis E Koromilas
Donalyn Scheuner
Hala Muaddi
Maria Hatzoglou
Mithu Majumder
Philippos Peidis
Randal J Kaufman
P2860
P304
P356
10.1091/MBC.E10-01-0023
P577
2010-07-21T00:00:00Z