Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control - Test2 - elhamkhani - TriplyDB

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

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

http://www.wikidata.org/entity/Q24522941

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Characterization of a mutant pancreatic eIF-2alpha kinase, PEK, and co-localization with somatostatin in islet delta cells Characterization of a mammalian homolog of the GCN2 eukaryotic initiation factor 2alpha kinase Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress 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 Protein synthesis and endoplasmic reticulum stress can be modulated by the hepatitis C virus envelope protein E2 through the eukaryotic initiation factor 2alpha kinase PERK Transcriptional regulation of the Ufm1 conjugation system in response to disturbance of the endoplasmic reticulum homeostasis and inhibition of vesicle trafficking p58IPK is an inhibitor of the eIF2α kinase GCN2 and its localization and expression underpin protein synthesis and ER processing capacity Heat shock protein 90 modulates the unfolded protein response by stabilizing IRE1alpha.Differential regulation of endoplasmic reticulum stress by protein tyrosine phosphatase 1B and T cell protein tyrosine phosphatase Activation of hepatitis B virus S promoter by a cell type-restricted IRE1-dependent pathway induced by endoplasmic reticulum stress Distinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein response Endoplasmic reticulum stress: cell life and death decisions.The mRNA of the translationally controlled tumor protein P23/TCTP is a highly structured RNA, which activates the dsRNA-dependent protein kinase PKR Regulation of protein synthesis by hypoxia via activation of the endoplasmic reticulum kinase PERK and phosphorylation of the translation initiation factor eIF2alpha.Control of PERK eIF2alpha kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK.A mammalian homologue of GCN2 protein kinase important for translational control by phosphorylation of eukaryotic initiation factor-2alpha Identification of domains and residues within the epsilon subunit of eukaryotic translation initiation factor 2B (eIF2Bepsilon) required for guanine nucleotide exchange reveals a novel activation function promoted by eIF2B complex formation Association of GCN1-GCN20 regulatory complex with the N-terminus of eIF2alpha kinase GCN2 is required for GCN2 activation Endoplasmic reticulum stress and the inflammatory basis of metabolic disease Nrf2 is a direct PERK substrate and effector of PERK-dependent cell survival Cellular interplay between neurons and glia: toward a comprehensive mechanism for excitotoxic neuronal loss in neurodegeneration IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response Japanese encephalitis virus infection initiates endoplasmic reticulum stress and an unfolded protein response Regulation of Stress Responses and Translational Control by Coronavirus Endoplasmic reticulum stress: a novel mechanism and therapeutic target for cardiovascular diseases The unfolded protein response in neurodegenerative diseases: a neuropathological perspective Emerging functions of the unfolded protein response in immunity Endoplasmic reticulum stress and type 2 diabetes Advancing animal models of human type 1 diabetes by engraftment of functional human tissues in immunodeficient mice Endoplasmic reticulum stress and diabetic cardiomyopathy Protein tyrosine phosphatase 1B deficiency potentiates PERK/eIF2α signaling in brown adipocytes XBP1 mitigates aminoglycoside-induced endoplasmic reticulum stress and neuronal cell death.Protective coupling of mitochondrial function and protein synthesis via the eIF2α kinase GCN-2 Coronavirus gene 7 counteracts host defenses and modulates virus virulence The unfolded protein response represses differentiation through the RPD3-SIN3 histone deacetylase Separate domains in GCN1 for binding protein kinase GCN2 and ribosomes are required for GCN2 activation in amino acid-starved cells.ER Stress-Mediated Signaling: Action Potential and Ca(2+) as Key Players Tumor progression and the different faces of the PERK kinase PERK mediates cell-cycle exit during the mammalian unfolded protein response

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

http://www.wikidata.org/entity/Q24522941

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1998 nî lūn-bûn

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1998 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

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1998 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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1998年の論文

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1998年論文

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Identification and characteriz ...... olved in translational control

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Identification and characteriz ...... olved in translational control

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Identification and characteriz ...... olved in translational control

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Identification and characteriz ...... olved in translational control

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Identification and characteriz ...... olved in translational control

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Identification and characteriz ...... olved in translational control

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Identification and characteriz ...... olved in translational control

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Identification and characteriz ...... olved in translational control

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J Liang

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P2860

Identification of double-stranded RNA-binding domains in the interferon-induced double-stranded RNA-activated p68 kinase

Isolation of the gene encoding the Drosophila melanogaster homolog of the Saccharomyces cerevisiae GCN2 eIF-2alpha kinase

Mammalian eukaryotic initiation factor 2 alpha kinases functionally substitute for GCN2 protein kinase in the GCN4 translational control mechanism of yeast

Autophosphorylation sites participate in the activation of the double-stranded-RNA-activated protein kinase PKR

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

Phosphorylation of initiation factor 2 alpha by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast.

Identification of positive-acting domains in GCN2 protein kinase required for translational activation of GCN4 expression.

Suppression of ribosomal reinitiation at upstream open reading frames in amino acid-starved cells forms the basis for GCN4 translational control

Histidyl-tRNA synthetase-related sequences in GCN2 protein kinase regulate in vitro phosphorylation of eIF-2.

Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification

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10.1128/MCB.18.12.7499

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12

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18

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1998-12-01T00:00:00Z

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9819435

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109330

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