(Q28204738)

English

Two dimerization domains in the trans-activation response RNA-binding protein (TRBP) individually reverse the protein kinase R inhibition of HIV-1 long terminal repeat expression

scientific article (publication date: 7 September 2001)

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Two dimerization domains in the trans-activation response RNA-binding protein (TRBP) individually reverse the protein kinase R inhibition of HIV-1 long terminal repeat expression (English)

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RNA-binding proteins

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object named as

A Gatignol

12

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author name string

A Daher

1

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M Longuet

2

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D Dorin

3

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F Bois

4

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E Segeral

5

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S Bannwarth

6

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P L Battisti

7

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D F Purcell

8

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R Benarous

9

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C Vaquero

10

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E F Meurs

11

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language of work or name

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publication date

7 September 2001

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Journal of Biological Chemistry

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276

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33899-905

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36

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A compilation of cellular transcription factor interactions with the HIV-1 LTR promoter

1 reference

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Tat as a transcriptional activator and a potential therapeutic target for HIV-1.

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Tat, Tat-associated kinase, and transcription

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Taking a new TAK on tat transactivation

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Transcriptional control: Tat cofactors and transcriptional elongation

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Mechanisms of viral inhibition by interferons.

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Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon

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PKR: a new name and new roles.

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

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

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21 January 2018

Translational control of viral gene expression in eukaryotes

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Translational control by the Epstein-Barr virus small RNA EBER-1. Reversal of the double-stranded RNA-induced inhibition of protein synthesis in reticulocyte lysates

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Tat-responsive region RNA of human immunodeficiency virus 1 can prevent activation of the double-stranded-RNA-activated protein kinase

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HIV-I TAT inhibits PKR activity by both RNA-dependent and RNA-independent mechanisms

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Control of PKR protein kinase by hepatitis C virus nonstructural 5A protein: molecular mechanisms of kinase regulation

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Proteins that interact with PKR.

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HIV-1 Tat directly interacts with the interferon-induced, double-stranded RNA-dependent kinase, PKR

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Oncogenic potential of TAR RNA binding protein TRBP and its regulatory interaction with RNA-dependent protein kinase PKR.

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Expression of hepatitis C virus proteins interferes with the antiviral action of interferon independently of PKR-mediated control of protein synthesis

1 reference

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TAR RNA-binding protein is an inhibitor of the interferon-induced protein kinase PKR

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Double-stranded RNA-activated protein kinase (PKR) is negatively regulated by 60S ribosomal subunit protein L18

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

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Characterization of a human TAR RNA-binding protein that activates the HIV-1 LTR

1 reference

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Characterization of TRBP1 and TRBP2

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Binding properties of newly identified Xenopus proteins containing dsRNA-binding motifs

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Relatedness of an RNA-binding motif in human immunodeficiency virus type 1 TAR RNA-binding protein TRBP to human P1/dsI kinase and Drosophila staufen

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A conserved double-stranded RNA-binding domain

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21 January 2018

Analysis of a binding difference between the two dsRNA-binding domains in TRBP reveals the modular function of a KR-helix motif

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An Arg/Lys-rich core peptide mimics TRBP binding to the HIV-1 TAR RNA upper-stem/loop.

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Genetic mapping in human and mouse of the locus encoding TRBP, a protein that binds the TAR region of the human immunodeficiency virus (HIV-1)

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A testis cytoplasmic RNA-binding protein that has the properties of a translational repressor

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A double-stranded RNA binding protein required for activation of repressed messages in mammalian germ cells

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Expression of TAR RNA-Binding Protein in Baculovirus and Co-Immunoprecipitation with Insect Cell Protein Kinase.

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

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Construction of an improved host strain for two hybrid screening

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Identification of Limiting Steps for Efficient Trans-activation of HIV-1 Promoter by Tat inSaccharomyces cerevisiae

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Human PKR transfected into murine cells stimulates expression of genes under control of the HIV1 or HTLV-I LTR.

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Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes

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Human Sos1: a guanine nucleotide exchange factor for Ras that binds to GRB2

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Tumor suppressor function of the interferon-induced double-stranded RNA-activated protein kinase

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Translational control in mammalian cells

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PKR stimulates NF-kappaB irrespective of its kinase function by interacting with the IkappaB kinase complex.

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JNK2 and IKKbeta are required for activating the innate response to viral infection

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Mechanism of interferon action. Biochemical and genetic evidence for the intermolecular association of the RNA-dependent protein kinase PKR from human cells

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The interferon-inducible double-stranded RNA-activated protein kinase self-associates in vitro and in vivo

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Double-stranded (ds) RNA binding and not dimerization correlates with the activation of the dsRNA-dependent protein kinase (PKR).

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

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Activation of the double-stranded RNA (dsRNA)-activated human protein kinase in vivo in the absence of its dsRNA binding domain

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21 January 2018

Identifiers

10.1074/JBC.M103584200

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