Modular structure of PACT: distinct domains for binding and activating PKR - Wikidata - wikimedia - TriplyDB

Modular structure of PACT: distinct domains for binding and activating PKR

Modular structure of PACT: distinct domains for binding and activating PKR

http://www.wikidata.org/entity/Q24551001

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The role of PACT in the RNA silencing pathway Interaction of human tRNA-dihydrouridine synthase-2 with interferon-induced protein kinase PKR Mutual antagonism between the Ebola virus VP35 protein and the RIG-I activator PACT determines infection outcome The 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)Inhibition of PACT-mediated activation of PKR by the herpes simplex virus type 1 Us11 protein.RDE-4 preferentially binds long dsRNA and its dimerization is necessary for cleavage of dsRNA to siRNA.A role of the double-stranded RNA-binding protein PACT in mouse ear development and hearing Molecular basis for PKR activation by PACT or dsRNA The double-stranded RNA-binding protein, PACT, is required for postnatal anterior pituitary proliferation 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 Processing of pre-microRNAs by the Dicer-1-Loquacious complex in Drosophila cells A novel role for RAX, the cellular activator of PKR, in synergistically stimulating SV40 large T antigen-dependent gene expression Nuclear factor 90 is a substrate and regulator of the eukaryotic initiation factor 2 kinase double-stranded RNA-activated protein kinase 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 Interaction between RAX and PKR modulates the effect of ethanol on protein synthesis and survival of neurons Missense mutation in the second RNA binding domain reveals a role for Prkra (PACT/RAX) during skull development Proapoptotic protein PACT is expressed at high levels in colonic epithelial cells in mice Induced folding in RNA recognition by Arabidopsis thaliana DCL1 An RNA-dependent protein kinase is involved in tunicamycin-induced apoptosis and Alzheimer's disease.JAZ mediates G1 cell-cycle arrest and apoptosis by positively regulating p53 transcriptional activity.An antiviral response directed by PKR phosphorylation of the RNA helicase A dsRNA Binding Domain of PKR Is Proteolytically Released by Enterovirus A71 to Facilitate Viral Replication.The role of PACT in mediating gene induction, PKR activation, and apoptosis in response to diverse stimuli Functional selection of shRNA loops from randomized retroviral libraries PACT and PKR: turning on NF-kappa B in the absence of virus.Viruses, endoplasmic reticulum stress, and interferon responses.Distinguishable in vitro binding mode of monomeric TRBP and dimeric PACT with siRNA dsRNA binding protein PACT/RAX in gene silencing, development and diseases.PACT/RAX regulates the migration of cerebellar granule neurons in the developing cerebellum.Viruses and the type I interferon antiviral system: induction and evasion.Organization and functions of interacting domains for signaling by protein-protein interactions.Cross-species comparative analysis of Dicer proteins during Sindbis virus infection.Stress granules regulate double-stranded RNA-dependent protein kinase activation through a complex containing G3BP1 and Caprin1.Expression of PACT is regulated by Sp1 transcription factor.The double-stranded-RNA-binding motif: interference and much more.Altered activation of protein kinase PKR and enhanced apoptosis in dystonia cells carrying a mutation in PKR activator protein PACT.The multiple functions of TRBP, at the hub of cell responses to viruses, stress, and cancer.Regulation of PACT-Mediated Protein Kinase Activation by the OV20.0 Protein of Orf Virus.

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Modular structure of PACT: distinct domains for binding and activating PKR

http://www.wikidata.org/entity/Q24551001

description

2001 nî lūn-bûn

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2001 թուականի Մարտին հրատարակուած գիտական յօդուած

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2001 թվականի մարտին հրատարակված գիտական հոդված

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2001年の論文

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2001年論文

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2001年論文

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2001年論文

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2001年論文

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2001年论文

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Modular structure of PACT: distinct domains for binding and activating PKR

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Modular structure of PACT: distinct domains for binding and activating PKR

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Modular structure of PACT: distinct domains for binding and activating PKR

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Modular structure of PACT: distinct domains for binding and activating PKR

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Modular structure of PACT: distinct domains for binding and activating PKR

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Modular structure of PACT: distinct domains for binding and activating PKR

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Modular structure of PACT: distinct domains for binding and activating PKR

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Modular structure of PACT: distinct domains for binding and activating PKR

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Modular structure of PACT: distinct domains for binding and activating PKR

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MCB.21.6.1908-1920.2001

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Molecular and Cellular Biology

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Modular structure of PACT: distinct domains for binding and activating PKR

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P2093

G C Sen

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

J Qin

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P2860

DRBP76, a double-stranded RNA-binding nuclear protein, is phosphorylated by the interferon-induced protein kinase, PKR

PACT, a protein activator of the interferon-induced protein kinase, PKR.

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

A conserved double-stranded RNA-binding domain

PKR; a sentinel kinase for cellular stress

RAX, a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling

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

The emerging role of the interferon-induced PKR protein kinase as an apoptotic effector: a new face of death?

Requirement of PKR dimerization mediated by specific hydrophobic residues for its activation by double-stranded RNA and its antigrowth effects in yeast

Double-stranded RNA-independent dimerization of interferon-induced protein kinase PKR and inhibition of dimerization by the cellular P58IPK inhibitor.

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1908-20

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scholarly article

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2141720

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10.1128/MCB.21.6.1908-1920.2001

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6

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21

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2001-03-01T00:00:00Z

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24488883

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11238927

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86773

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