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 (Q28204738)

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scientific article (publication date: 7 September 2001)

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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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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

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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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36

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33899-905

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

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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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Translational control of viral gene expression in eukaryotes

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

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

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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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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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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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10.1074/JBC.M103584200

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