Double-stranded-RNA-dependent protein kinase and TAR RNA-binding protein form homo- and heterodimers in vivo
about
Mammalian staufen is a double-stranded-RNA- and tubulin-binding protein which localizes to the rough endoplasmic reticulumOrganization of the human tarbp2 gene reveals two promoters that are repressed in an astrocytic cell lineInteraction of human tRNA-dihydrouridine synthase-2 with interferon-induced protein kinase PKRIn vitro reconstitution of the human RISC-loading complexPACT, a protein activator of the interferon-induced protein kinase, PKR.The RNA-binding region of human TRBP interacts with microRNA precursors through two independent domainsA new double-stranded RNA-binding protein that interacts with PKRThe double-stranded RNA-binding protein Staufen is incorporated in human immunodeficiency virus type 1: evidence for a role in genomic RNA encapsidationADAR1 interacts with NF90 through double-stranded RNA and regulates NF90-mediated gene expression independently of RNA editingPhysical association between STAT1 and the interferon-inducible protein kinase PKR and implications for interferon and double-stranded RNA signaling pathwaysMolecular mapping of the determinants involved in human Staufen-ribosome associationThe 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)The 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 human sequence homologue of Staufen is an RNA-binding protein that is associated with polysomes and localizes to the rough endoplasmic reticulumImpact of protein kinase PKR in cell biology: from antiviral to antiproliferative actionMicroRNAs: molecular features and role in cancerTRBP and eIF6 homologue in Marsupenaeus japonicus play crucial roles in antiviral responseControl of PKR protein kinase by hepatitis C virus nonstructural 5A protein: molecular mechanisms of kinase regulation.Analysis of a binding difference between the two dsRNA-binding domains in TRBP reveals the modular function of a KR-helix motifTwo dimerization domains in the trans-activation response RNA-binding protein (TRBP) individually reverse the protein kinase R inhibition of HIV-1 long terminal repeat expressionTranslation inhibition in apoptosis: caspase-dependent PKR activation and eIF2-alpha phosphorylationThe Tat protein of human immunodeficiency virus type 1 is a substrate and inhibitor of the interferon-induced, virally activated protein kinase, PKRNF90 in posttranscriptional gene regulation and microRNA biogenesisTwo heme-binding domains of heme-regulated eukaryotic initiation factor-2alpha kinase. N terminus and kinase insertionFunctional characterization of and cooperation between the double-stranded RNA-binding motifs of the protein kinase PKR.Double-stranded RNA-activated protein kinase PKR of fishes and amphibians: varying the number of double-stranded RNA binding domains and lineage-specific duplications.Human Herpesvirus 6A Exhibits Restrictive Propagation with Limited Activation of the Protein Kinase R-eIF2α Stress Pathway.Regulation of the RNA-dependent protein kinase by triple helix formationB-myb promoter retargeting of herpes simplex virus gamma34.5 gene-mediated virulence toward tumor and cycling cellsAGO2 Negatively Regulates Type I Interferon Signaling Pathway by Competition Binding IRF3 with CBP/p300.Recognition of siRNA asymmetry by TAR RNA binding protein.Requirement of PKR dimerization mediated by specific hydrophobic residues for its activation by double-stranded RNA and its antigrowth effects in yeastInhibition of double-stranded RNA-dependent protein kinase PKR by vaccinia virus E3: role of complex formation and the E3 N-terminal domain.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 geneDouble-stranded RNA-independent dimerization of interferon-induced protein kinase PKR and inhibition of dimerization by the cellular P58IPK inhibitor.Induction of caspase-dependent apoptosis in cultured cells by the avian coronavirus infectious bronchitis virus.Double-stranded RNA-activated protein kinase (PKR) is negatively regulated by 60S ribosomal subunit protein L18Oncogenic potential of TAR RNA binding protein TRBP and its regulatory interaction with RNA-dependent protein kinase PKR.Translational control of viral gene expression in eukaryotes
P2860
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P2860
Double-stranded-RNA-dependent protein kinase and TAR RNA-binding protein form homo- and heterodimers in vivo
description
1995 nî lūn-bûn
@nan
1995 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
name
Double-stranded-RNA-dependent ...... homo- and heterodimers in vivo
@ast
Double-stranded-RNA-dependent ...... homo- and heterodimers in vivo
@en
Double-stranded-RNA-dependent ...... homo- and heterodimers in vivo
@nl
type
label
Double-stranded-RNA-dependent ...... homo- and heterodimers in vivo
@ast
Double-stranded-RNA-dependent ...... homo- and heterodimers in vivo
@en
Double-stranded-RNA-dependent ...... homo- and heterodimers in vivo
@nl
prefLabel
Double-stranded-RNA-dependent ...... homo- and heterodimers in vivo
@ast
Double-stranded-RNA-dependent ...... homo- and heterodimers in vivo
@en
Double-stranded-RNA-dependent ...... homo- and heterodimers in vivo
@nl
P2093
P2860
P3181
P356
P1476
Double-stranded-RNA-dependent ...... homo- and heterodimers in vivo
@en
P2093
F C Serluca
G P Cosentino
M B Mathews
N Sonenberg
S Venkatesan
P2860
P304
P3181
P356
10.1073/PNAS.92.21.9445
P407
P577
1995-10-10T00:00:00Z