Physical association between STAT1 and the interferon-inducible protein kinase PKR and implications for interferon and double-stranded RNA signaling pathways - Test2 - elhamkhani - TriplyDB

Physical association between STAT1 and the interferon-inducible protein kinase PKR and implications for interferon and double-stranded RNA signaling pathways

Physical association between STAT1 and the interferon-inducible protein kinase PKR and implications for interferon and double-stranded RNA signaling pathways

http://www.wikidata.org/entity/Q24532129

about

The B56alpha regulatory subunit of protein phosphatase 2A is a target for regulation by double-stranded RNA-dependent protein kinase PKR Endoplasmic reticulum stress induces p53 cytoplasmic localization and prevents p53-dependent apoptosis by a pathway involving glycogen synthase kinase-3beta PACT, a protein activator of the interferon-induced protein kinase, PKR.Homologous regions of the alpha subunit of eukaryotic translational initiation factor 2 (eIF2alpha) and the vaccinia virus K3L gene product interact with the same domain within the dsRNA-activated protein kinase (PKR)Regulation of interferon-induced protein kinase PKR: modulation of P58IPK inhibitory function by a novel protein, P52rIPK Protein kinase PKR is required for platelet-derived growth factor signaling of c-fos gene expression via Erks and Stat3.Inhibition of PACT-mediated activation of PKR by the herpes simplex virus type 1 Us11 protein.Molecular basis for PKR activation by PACT or dsRNA Modular structure of PACT: distinct domains for binding and activating PKR RAX, the PKR activator, sensitizes cells to inflammatory cytokines, serum withdrawal, chemotherapy, and viral infection Impact of protein kinase PKR in cell biology: from antiviral to antiproliferative action The double-stranded RNA activated protein kinase PKR physically associates with the tumor suppressor p53 protein and phosphorylates human p53 on serine 392 in vitro Nuclear factor 90 is a substrate and regulator of the eukaryotic initiation factor 2 kinase double-stranded RNA-activated protein kinase Stimulation of interferon regulatory factor-1 by prolactin Enhanced antiviral and antiproliferative properties of a STAT1 mutant unable to interact with the protein kinase PKR The direct binding of the catalytic subunit of protein phosphatase 1 to the PKR protein kinase is necessary but not sufficient for inactivation and disruption of enzyme dimer formation Phosphorylation of specific serine residues in the PKR activation domain of PACT is essential for its ability to mediate apoptosis Serine 18 phosphorylation of RAX, the PKR activator, is required for PKR activation and consequent translation inhibition Activation of target-tissue immune-recognition molecules by double-stranded polynucleotides PKR regulates proliferation, differentiation, and survival of murine hematopoietic stem/progenitor cells Signal transducer and activator of transcription-1 is critical for apoptosis in macrophages subjected to endoplasmic reticulum stress in vitro and in advanced atherosclerotic lesions in vivo.The human papilloma virus (HPV)-18 E6 oncoprotein physically associates with Tyk2 and impairs Jak-STAT activation by interferon-alpha.Stat1 phosphorylation determines Ras oncogenicity by regulating p27 kip1 Requirement of PKR dimerization mediated by specific hydrophobic residues for its activation by double-stranded RNA and its antigrowth effects in yeast Mechanism 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 gene Double-stranded RNA-activated protein kinase (PKR) is negatively regulated by 60S ribosomal subunit protein L18 Serine phosphorylation of STATs.Double-stranded-RNA-activated protein kinase PKR enhances transcriptional activation by tumor suppressor p53 Antisense RNA: function and fate of duplex RNA in cells of higher eukaryotes.The protein kinase PKR: a molecular clock that sequentially activates survival and death programs.Increased expression of the dsRNA-activated protein kinase PKR in breast cancer promotes sensitivity to doxorubicin Double-stranded RNA-dependent protein kinase phosphorylation of the alpha-subunit of eukaryotic translation initiation factor 2 mediates apoptosis.Phosphorylation of STAT-1 serine 727 is prolonged in HLA-B27-expressing human monocytic cells.Controlling activation of the RNA-dependent protein kinase by siRNAs using site-specific chemical modification The antitumor effects of IFN-alpha are abrogated in a STAT1-deficient mouse Inhibitor of κB kinase epsilon (IKK(epsilon)), STAT1, and IFIT2 proteins define novel innate immune effector pathway against West Nile virus infection Interferons induce tyrosine phosphorylation of the eIF2alpha kinase PKR through activation of Jak1 and Tyk2.Enhanced phosphorylation of STAT-1 is dependent on double-stranded RNA-dependent protein kinase signaling in HLA-B27-expressing U937 monocytic cells.Translational control in T lymphocytes.Effects of length and location on the cellular response to double-stranded RNA.

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Physical association between STAT1 and the interferon-inducible protein kinase PKR and implications for interferon and double-stranded RNA signaling pathways

http://www.wikidata.org/entity/Q24532129

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1997 nî lūn-bûn

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1997 թուականի Մարտին հրատարակուած գիտական յօդուած

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1997 թվականի մարտին հրատարակված գիտական հոդված

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1997年の論文

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1997年学术文章

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1997年学术文章

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1997年学术文章

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Physical association between S ...... tranded RNA signaling pathways

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Physical association between S ...... tranded RNA signaling pathways

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Physical association between S ...... tranded RNA signaling pathways

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Physical association between S ...... tranded RNA signaling pathways

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Physical association between S ...... tranded RNA signaling pathways

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The EMBO Journal

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Physical association between S ...... tranded RNA signaling pathways

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Cuddihy AR

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Decker T

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Hauser H

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Kirchhoff S

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Koromilas AE

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Li S

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Tam NW

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Wong AH

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Yang YL

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P2860

Subunit of an alpha-interferon-responsive transcription factor is related to interferon regulatory factor and Myb families of DNA-binding proteins

Phosphorylated interferon-alpha receptor 1 subunit (IFNaR1) acts as a docking site for the latent form of the 113 kDa STAT2 protein

The SH2 domains of Stat1 and Stat2 mediate multiple interactions in the transduction of IFN-alpha signals

Kinase-negative mutants of JAK1 can sustain interferon-gamma-inducible gene expression but not an antiviral state

Double-stranded-RNA-dependent protein kinase and TAR RNA-binding protein form homo- and heterodimers in vivo

Interferon activation of the transcription factor Stat91 involves dimerization through SH2-phosphotyrosyl peptide interactions

In vitro activation of the transcription factor ISGF3 by interferon alpha involves a membrane-associated tyrosine phosphatase and tyrosine kinase

Maximal activation of transcription by Stat1 and Stat3 requires both tyrosine and serine phosphorylation

A single phosphotyrosine residue of Stat91 required for gene activation by interferon-gamma

Requirement of serine phosphorylation for formation of STAT-promoter complexes

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1291-1304

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10.1093/EMBOJ/16.6.1291

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6

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16

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1997-03-01T00:00:00Z

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14083499

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9135145

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1169727

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