Autophosphorylation in the activation loop is required for full kinase activity in vivo of human and yeast eukaryotic initiation factor 2alpha kinases PKR and GCN2
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Characterization of a mutant pancreatic eIF-2alpha kinase, PEK, and co-localization with somatostatin in islet delta cellsCharacterization of a mammalian homolog of the GCN2 eukaryotic initiation factor 2alpha kinaseThe B56alpha regulatory subunit of protein phosphatase 2A is a target for regulation by double-stranded RNA-dependent protein kinase PKRDetection of a novel unglycosylated form of hepatitis C virus E2 envelope protein that is located in the cytosol and interacts with PKRDimerization and release of molecular chaperone inhibition facilitate activation of eukaryotic initiation factor-2 kinase in response to endoplasmic reticulum stressInteraction of human tRNA-dihydrouridine synthase-2 with interferon-induced protein kinase PKRIdentification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational controlA new double-stranded RNA-binding protein that interacts with PKRThe Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKRInhibition of PACT-mediated activation of PKR by the herpes simplex virus type 1 Us11 protein.A mammalian homologue of GCN2 protein kinase important for translational control by phosphorylation of eukaryotic initiation factor-2alphaMolecular basis for PKR activation by PACT or dsRNAModular structure of PACT: distinct domains for binding and activating PKRAssociation of GCN1-GCN20 regulatory complex with the N-terminus of eIF2alpha kinase GCN2 is required for GCN2 activationWest Nile Virus-Induced Interferon Production Is Mediated by the Double-Stranded RNA-Dependent Protein Kinase PKRInterferon-inducible antiviral effectorsYIH1 is an actin-binding protein that inhibits protein kinase GCN2 and impairs general amino acid control when overexpressed.Dimerization by translation initiation factor 2 kinase GCN2 is mediated by interactions in the C-terminal ribosome-binding region and the protein kinase domain.Phosphorylation of initiation factor eIF2 in response to stress conditions is mediated by acidic ribosomal P1/P2 proteins in Saccharomyces cerevisiae.Separate domains in GCN1 for binding protein kinase GCN2 and ribosomes are required for GCN2 activation in amino acid-starved cells.Nuclear factor 90 is a substrate and regulator of the eukaryotic initiation factor 2 kinase double-stranded RNA-activated protein kinaseThe anti-apoptotic function of Hsp70 in the interferon-inducible double-stranded RNA-dependent protein kinase-mediated death signaling pathway requires the Fanconi anemia protein, FANCCPhosphorylation of specific serine residues in the PKR activation domain of PACT is essential for its ability to mediate apoptosisRNA-binding proteins: modular design for efficient functionTwo heme-binding domains of heme-regulated eukaryotic initiation factor-2alpha kinase. N terminus and kinase insertionActivation of double-stranded RNA-activated protein kinase by mild impairment of oxidative metabolism in neuronsAutophosphorylation of heme-regulated eukaryotic initiation factor 2α kinase and the role of the modification in catalysisIMPACT is a developmentally regulated protein in neurons that opposes the eukaryotic initiation factor 2α kinase GCN2 in the modulation of neurite outgrowthPfeIK1, a eukaryotic initiation factor 2alpha kinase of the human malaria parasite Plasmodium falciparum, regulates stress-response to amino-acid starvationCharacterization of phosphopeptides from protein digests using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and nanoelectrospray quadrupole time-of-flight mass spectrometry.Functional characterization of and cooperation between the double-stranded RNA-binding motifs of the protein kinase PKR.Characterization of the hemin-sensitive eukaryotic initiation factor 2alpha kinase from mouse nonerythroid cells.Interaction of double-stranded RNA-dependent protein kinase (PKR) with the death receptor signaling pathway in amyloid beta (Abeta)-treated cells and in APPSLPS1 knock-in miceEnhanced interaction between pseudokinase and kinase domains in Gcn2 stimulates eIF2α phosphorylation in starved cellsThe 3'-untranslated regions of cytoskeletal muscle mRNAs inhibit translation by activating the double-stranded RNA-dependent protein kinase PKR.Phosphoinositide 3-kinases upregulate system xc(-) via eukaryotic initiation factor 2α and activating transcription factor 4 - A pathway active in glioblastomas and epilepsyDecreased ATF4 expression as a mechanism of acquired resistance to long-term amino acid limitation in cancer cellsMechanism of interferon action: identification of essential positions within the novel 15-base-pair KCS element required for transcriptional activation of the RNA-dependent protein kinase pkr geneDiversity in viral anti-PKR mechanisms: a remarkable case of evolutionary convergenceHepatitis C virus envelope protein E2 does not inhibit PKR by simple competition with autophosphorylation sites in the RNA-binding domain.
P2860
Q22008790-12FC170A-DA88-476D-87CE-2D70E6D55E66Q22010589-745171AC-6194-4A6A-B3F2-4FAE1B322A96Q22254335-7B06381D-AAF7-4B77-89E8-567316608AA6Q24292085-A6209254-6C49-4FA6-AA52-7F0737EEF0FEQ24292499-2348E474-14B8-46B5-BD5C-33B14D2EF4C2Q24304341-37141BE2-8BFD-402F-B4CF-780CBDA68C1EQ24522941-FB9FFB4C-38A7-49A5-94E2-5464F3D60CDBQ24524116-2CBF8C15-01DB-4BDA-BFDC-F429B722E028Q24535594-9D8C7505-391C-4B68-9D78-F0617A142E44Q24538727-EE041AA5-2197-4217-ABD3-091857C0F2E8Q24548092-A8A6482D-7926-4560-979D-308F97A4A1FDQ24550949-576476BA-C425-4391-9A85-3E4AC0D195E9Q24551001-402E3961-41B4-411B-95B9-E63D508D07BCQ24600114-AA08E524-C27C-48C2-B187-ACDA96F30E62Q27481501-99043A2E-43B4-40B9-AF2C-8BADDC491099Q27486790-BC4EA5F8-335D-4E75-B59F-88C95C721A88Q27932122-013B3BAC-CBF7-4A78-BE06-3E99F30AF22AQ27934914-1D2BF3EF-3A06-4BBD-A489-29ADA160D552Q27937914-CBBA91F7-2249-4FF7-82EB-6A5960AEE9D3Q27940265-BCF0E55A-3134-4551-983C-A13A6378AAFCQ28204764-FDB3997B-66D7-453A-B79C-C374753E846CQ28210355-888A5FAE-1510-4C2F-A0D8-EC10B995B821Q28264248-973E5B54-FD79-450D-A7BB-5DB7FBA1E4FDQ28300258-DE1D1CEC-E8D0-4797-8C32-33301981C0A4Q28506814-D83CD9FC-B640-4711-A397-B2F0A56FABBAQ28577883-8514EA08-BE36-4831-AF27-D4E2545A640DQ28592351-AEAFCABA-4AFE-4A4A-91D2-078D48F09A2AQ28594198-34DDE65B-FD44-4395-9C07-D466A006E84DQ30042894-24D88390-1DB9-40AE-AC4D-BCB57418BA1EQ30717218-C981A9BF-1994-4AEB-B28A-6349B7E4BC9DQ31778073-452BE255-3C6C-4C11-8752-88E7B8C545C6Q31971317-791D0975-3ABA-4FA9-BFA8-63AEDD395B1EQ33569701-885909C2-B428-4EAF-8EAA-587777CBF89EQ33583677-FA22BEAA-8C01-474E-A2E1-C5BF33F873FDQ33583983-79F3A2B1-1CBD-42C8-A3B9-FB7D7F45A354Q33687799-C1CE3634-F632-416A-A778-C0F3DB24327FQ33689081-3843AF08-4B76-4295-81C4-CAF9FD84BA94Q33786084-4929211E-B1C8-4E77-BC95-979F822F359FQ33818201-B11EA942-3F83-4ACD-BB9D-69DE90B84213Q33836081-7CA5A5AC-75B5-4F2D-B814-8757B8619BD4
P2860
Autophosphorylation in the activation loop is required for full kinase activity in vivo of human and yeast eukaryotic initiation factor 2alpha kinases PKR and GCN2
description
1998 nî lūn-bûn
@nan
1998 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Autophosphorylation in the act ...... or 2alpha kinases PKR and GCN2
@ast
Autophosphorylation in the act ...... or 2alpha kinases PKR and GCN2
@en
type
label
Autophosphorylation in the act ...... or 2alpha kinases PKR and GCN2
@ast
Autophosphorylation in the act ...... or 2alpha kinases PKR and GCN2
@en
prefLabel
Autophosphorylation in the act ...... or 2alpha kinases PKR and GCN2
@ast
Autophosphorylation in the act ...... or 2alpha kinases PKR and GCN2
@en
P2093
P2860
P356
P1476
Autophosphorylation in the act ...... or 2alpha kinases PKR and GCN2
@en
P2093
A G Hinnebusch
D R Taylor
M B Mathews
M T Garcia-Barrio
P R Romano
P2860
P304
P356
10.1128/MCB.18.4.2282
P407
P577
1998-04-01T00:00:00Z