Phosphorylation of the alpha subunit of eukaryotic initiation factor 2 is required for activation of NF-kappaB in response to diverse cellular stresses. - Wikidata - wikimedia - TriplyDB

Phosphorylation of the alpha subunit of eukaryotic initiation factor 2 is required for activation of NF-kappaB in response to diverse cellular stresses.

Phosphorylation of the alpha subunit of eukaryotic initiation factor 2 is required for activation of NF-kappaB in response to diverse cellular stresses.

http://www.wikidata.org/entity/Q35169632

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Endoplasmic reticulum stress-activated C/EBP homologous protein enhances nuclear factor-kappaB signals via repression of peroxisome proliferator-activated receptor gamma Hepatitis C virus NS2 protease inhibits host cell antiviral response by inhibiting IKKε and TBK1 functions Mutations linked to leukoencephalopathy with vanishing white matter impair the function of the eukaryotic initiation factor 2B complex in diverse ways Angptl4 protects against severe proinflammatory effects of saturated fat by inhibiting fatty acid uptake into mesenteric lymph node macrophages Endoplasmic reticulum stress and the inflammatory basis of metabolic disease Expression of the pro-angiogenic factors vascular endothelial growth factor and interleukin-8/CXCL8 by human breast carcinomas is responsive to nutrient deprivation and endoplasmic reticulum stress Novel concepts on pregnancy clocks and alarms: redundancy and synergy in human parturition Role for the Unfolded Protein Response in Heart Disease and Cardiac Arrhythmias The unfolded protein response in multiple sclerosis Endoplasmic Reticulum Stress in the Diabetic Kidney, the Good, the Bad and the Ugly Hepatitis C virus comes for dinner: How the hepatitis C virus interferes with autophagy Emerging functions of the unfolded protein response in immunity The role of glucosamine-induced ER stress in diabetic atherogenesis The unfolded protein response in retinal vascular diseases: implications and therapeutic potential beyond protein folding Role of endoplasmic reticulum stress in the pathogenesis of nonalcoholic fatty liver disease Drosophila as a model for unfolded protein response research Endoplasmic reticulum stress and the related signaling networks in severe asthma Micro(RNA)managing endoplasmic reticulum stress Crystal Structures of GCN2 Protein Kinase C-terminal Domains Suggest Regulatory Differences in Yeast and Mammals Crosstalk between the unfolded protein response and NF-κB-mediated inflammation in the progression of chronic kidney disease Oxidative stress, unfolded protein response, and apoptosis in developmental toxicity Tumor progression and the different faces of the PERK kinase Inflammation and cellular stress: a mechanistic link between immune-mediated and metabolically driven pathologies Induction of Bcl-2 expression by hepatitis B virus pre-S2 mutant large surface protein resistance to 5-fluorouracil treatment in Huh-7 cells UPR-induced resistance to etoposide is downstream of PERK and independent of changes in topoisomerase IIα levels Activating transcription factor 3 is integral to the eukaryotic initiation factor 2 kinase stress response PERK and GCN2 contribute to eIF2alpha phosphorylation and cell cycle arrest after activation of the unfolded protein response pathway Endoplasmic reticulum stress and unfolded protein response in renal pathophysiology: Janus faces New Concepts in Alpha-1 Antitrypsin Deficiency Disease Mechanisms.Loss of p24 function in Drosophila melanogaster causes a stress response and increased levels of NF-kappaB-regulated gene products.ER stress depresses NF-kappaB activation in mesangial cells through preferential induction of C/EBP beta Endocannabinoid receptors gene expression in morbidly obese women with nonalcoholic fatty liver disease.Transcriptional and post-transcriptional regulation of proangiogenic factors by the unfolded protein response.Coronavirus infection, ER stress, apoptosis and innate immunity Stressed to death: targeting endoplasmic reticulum stress response induced apoptosis in gliomas.Expression profiling after activation of amino acid deprivation response in HepG2 human hepatoma cells Endoplasmic reticulum stress pathway PERK-eIF2α confers radioresistance in oropharyngeal carcinoma by activating NF-κB.eIF2alpha phosphorylation tips the balance to apoptosis during osmotic stress.TRAM1 is involved in disposal of ER membrane degradation substrates.Proteomic snapshot of breast cancer cell cycle: G1/S transition point.

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P2860

Phosphorylation of the alpha subunit of eukaryotic initiation factor 2 is required for activation of NF-kappaB in response to diverse cellular stresses.

http://www.wikidata.org/entity/Q35169632

description

2003 nî lūn-bûn

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2003 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի օգոստոսին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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name

Phosphorylation of the alpha s ...... to diverse cellular stresses.

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Phosphorylation of the alpha s ...... to diverse cellular stresses.

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type

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Phosphorylation of the alpha s ...... to diverse cellular stresses.

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Phosphorylation of the alpha s ...... to diverse cellular stresses.

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Phosphorylation of the alpha s ...... to diverse cellular stresses.

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Phosphorylation of the alpha s ...... to diverse cellular stresses.

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MCB.23.16.5651-5663.2003

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Molecular and Cellular Biology

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Phosphorylation of the alpha s ...... to diverse cellular stresses.

@en

P2093

Barbara C McGrath

http://www.w3.org/2001/XMLSchema#string

Donalyn Scheuner

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Douglas R Cavener

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Hao-Yuan Jiang

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Randal J Kaufman

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Ronald C Wek

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Sheree A Wek

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P2860

Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta

Pancreatic eukaryotic initiation factor-2alpha kinase (PEK) homologues in humans, Drosophila melanogaster and Caenorhabditis elegans that mediate translational control in response to endoplasmic reticulum stress

Dimerization and release of molecular chaperone inhibition facilitate activation of eukaryotic initiation factor-2 kinase in response to endoplasmic reticulum stress

Selection of optimal kappa B/Rel DNA-binding motifs: interaction of both subunits of NF-kappa B with DNA is required for transcriptional activation

Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control

A mammalian homologue of GCN2 protein kinase important for translational control by phosphorylation of eukaryotic initiation factor-2alpha

NF-kappaB induces expression of the Bcl-2 homologue A1/Bfl-1 to preferentially suppress chemotherapy-induced apoptosis

The prosurvival Bcl-2 homolog Bfl-1/A1 is a direct transcriptional target of NF-kappaB that blocks TNFalpha-induced apoptosis

The histidyl-tRNA synthetase-related sequence in the eIF-2 alpha protein kinase GCN2 interacts with tRNA and is required for activation in response to starvation for different amino acids

NF-kappaB-mediated up-regulation of Bcl-x and Bfl-1/A1 is required for CD40 survival signaling in B lymphocytes

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5651-5663

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10.1128/MCB.23.16.5651-5663.2003

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16

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23

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2003-08-01T00:00:00Z

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phosphorylation

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166326

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