about
Alu elements as regulators of gene expressionThe B56alpha regulatory subunit of protein phosphatase 2A is a target for regulation by double-stranded RNA-dependent protein kinase PKRLatently expressed human herpesvirus 8-encoded interferon regulatory factor 2 inhibits double-stranded RNA-activated protein kinase.The kinase DYRK phosphorylates protein-synthesis initiation factor eIF2Bepsilon at Ser539 and the microtubule-associated protein tau at Thr212: potential role for DYRK as a glycogen synthase kinase 3-priming kinaseDimerization 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 PKRNucleophosmin interacts with and inhibits the catalytic function of eukaryotic initiation factor 2 kinase PKRThe C-terminal, third conserved motif of the protein activator PACT plays an essential role in the activation of double-stranded-RNA-dependent protein kinase (PKR)Protein kinase PKR is required for platelet-derived growth factor signaling of c-fos gene expression via Erks and Stat3.ICP0 prevents RNase L-independent rRNA cleavage in herpes simplex virus type 1-infected cellsThe 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.The mRNA of the translationally controlled tumor protein P23/TCTP is a highly structured RNA, which activates the dsRNA-dependent protein kinase PKRMolecular basis for PKR activation by PACT or dsRNAModular structure of PACT: distinct domains for binding and activating PKRFAST is a survival protein that senses mitochondrial stress and modulates TIA-1-regulated changes in protein expressionDEQOR: a web-based tool for the design and quality control of siRNAsThe double-stranded RNA-binding protein, PACT, is required for postnatal anterior pituitary proliferationSmall silencing RNAs: an expanding universeRAX, the PKR activator, sensitizes cells to inflammatory cytokines, serum withdrawal, chemotherapy, and viral infectionp53-independent endoplasmic reticulum stress-mediated cytotoxicity of a Newcastle disease virus strain in tumor cell linesImpact of protein kinase PKR in cell biology: from antiviral to antiproliferative actionAdeno-associated viruses can induce phosphorylation of eIF2alpha via PKR activation, which can be overcome by helper adenovirus type 5 virus-associated RNARNA interference: learning gene knock-down from cell physiologyNaïve T Cell Homeostasis Regulated by Stress Responses and TCR SignalingImmunology in the clinic review series; focus on type 1 diabetes and viruses: how viral infections modulate beta cell functionMechanisms of RNA-induced toxicity in CAG repeat disordersDevelopment of eczema vaccinatum in atopic mouse models and efficacy of MVA vaccination against lethal poxviral infectionRegulation of mRNA Translation and Cellular Signaling by Hepatitis C Virus Nonstructural Protein NS5ARegulation of PKR and IRF-1 during hepatitis C virus RNA replication.PKR-dependent mechanisms of gene expression from a subgenomic hepatitis C virus clone.PKR and RNase L Contribute to Protection against Lethal West Nile Virus Infection by Controlling Early Viral Spread in the Periphery and Replication in NeuronsAlternate rRNA secondary structures as regulators of translationDistinct Z-DNA binding mode of a PKR-like protein kinase containing a Z-DNA binding domain (PKZ)An Evolutionary View of the Arms Race between Protein Kinase R and Large DNA VirusesInfluence of host resistance on viral adaptation: hepatitis C virus as a case studyThe anti-apoptotic function of Hsp70 in the interferon-inducible double-stranded RNA-dependent protein kinase-mediated death signaling pathway requires the Fanconi anemia protein, FANCCTranslation inhibition in apoptosis: caspase-dependent PKR activation and eIF2-alpha phosphorylationmTOR/p70S6k signalling alteration by Abeta exposure as well as in APP-PS1 transgenic models and in patients with Alzheimer's diseasePhosphorylation of specific serine residues in the PKR activation domain of PACT is essential for its ability to mediate apoptosis
P2860
Q22065977-D83174B6-DBCB-4A08-8DE6-0F899E0ABCC0Q22254335-DC28DAB5-1A06-4712-908D-381BF9B2BA22Q24290751-9020D2AD-756E-488B-8F7C-D477C3AE184BQ24291138-D735EDBA-1F78-4F2C-B498-98973A1C9DC4Q24292499-A5018045-B8F1-4C9F-979A-345932CEC32CQ24304341-C9CDBDD0-81FC-4651-B1D2-0CBC20C9C773Q24311493-EB6DF4A7-82B8-4241-B936-09184E1B7E42Q24534342-86F4DC9B-9440-4AC7-A3FC-3284E0FE7D15Q24535156-2FAA5831-06D5-478F-863E-C32D07D062C3Q24535541-910BBB65-4F90-485C-981E-8F3C9F4B4803Q24535594-0736A623-AA7F-4FD9-858B-EFA73EF1A52EQ24538727-75484104-BAF6-469B-863D-EE8CCB8C301FQ24540098-891333A3-8BD0-49F2-9EB5-B9843D916C81Q24550949-7A0AC9FB-1FD6-4B3F-A33B-33759E9CCA83Q24551001-BB8B38A9-5E2D-49A8-A24C-B0B55462B845Q24559757-0143B372-879A-490E-B6C8-9B9978778F05Q24562112-B201A3F3-DA01-4E44-A999-8EFA181DBB3EQ24653603-90296B0B-96B4-4A7B-AF44-A896F9613E5CQ24653997-ADF08F20-06DC-4FDC-8DAD-AF9D046FFA34Q24671766-9E4183DC-EE8F-45A2-A74E-67F247B3E9BBQ24672443-57A7F94E-69E2-4C7A-A3B0-6B927A85F690Q24672548-1E0CC078-950F-4E74-963A-AFBE3010A61DQ24681740-2FD67891-536C-40E1-B898-58A0B804E263Q24799925-80E5B994-A43D-4397-AE35-D78530B39A83Q26770670-81CC66C4-E804-47F7-8E81-145A43F3EAC7Q26825327-3E015CD5-D5A2-4A60-B64E-820592F310AAQ26860030-9ABEF882-99A2-4754-AD95-6AC4BBFE4411Q27321985-DC71E1B6-22F0-441C-99F2-6FE5DFDCCDD7Q27469918-3EE32E31-C635-45EC-A659-CEA610258644Q27472373-DA83FE66-0052-440F-806F-E5033D4A83DFQ27472907-3224E94B-4116-4AB3-8052-59FED5E7854AQ27473291-A5AF18BF-27A0-4B61-919E-26FBF4E9E9D1Q27666479-A4F65D8C-7399-4D8F-8C2B-3F88D9256F39Q27682673-9D1A831E-2283-4E57-A8AF-C056B7F8617FQ28067827-0DE39DF3-FB67-44CF-8C77-40A9103C0405Q28087595-830433D8-57A7-4025-B232-BD27FEC329A3Q28210355-1BD397B3-695E-484F-A439-3A409B6F9386Q28216131-9A781968-704E-489D-9B71-57AF33A29D58Q28256208-C9C572C7-9E11-4689-8AB9-F570236A5B90Q28264248-A65C9AE0-4F25-423A-98AA-7635487281BE
P2860
description
1999 nî lūn-bûn
@nan
1999 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
PKR; a sentinel kinase for cellular stress
@ast
PKR; a sentinel kinase for cellular stress
@en
PKR; a sentinel kinase for cellular stress
@nl
type
label
PKR; a sentinel kinase for cellular stress
@ast
PKR; a sentinel kinase for cellular stress
@en
PKR; a sentinel kinase for cellular stress
@nl
prefLabel
PKR; a sentinel kinase for cellular stress
@ast
PKR; a sentinel kinase for cellular stress
@en
PKR; a sentinel kinase for cellular stress
@nl
P3181
P356
P1433
P1476
PKR; a sentinel kinase for cellular stress
@en
P2093
B R Williams
P2888
P304
P3181
P356
10.1038/SJ.ONC.1203127
P407
P577
1999-11-01T00:00:00Z
P5875
P6179
1004663973