HIV-1 Tat acts as a processivity factor in vitro in conjunction with cellular elongation factors
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Tat-SF1 protein associates with RAP30 and human SPT5 proteinsEvidence that P-TEFb alleviates the negative effect of DSIF on RNA polymerase II-dependent transcription in vitroThe cellular factor TRP-185 regulates RNA polymerase II binding to HIV-1 TAR RNACA150, a nuclear protein associated with the RNA polymerase II holoenzyme, is involved in Tat-activated human immunodeficiency virus type 1 transcriptionTwo human homologues of Saccharomyces cerevisiae SWI2/SNF2 and Drosophila brahma are transcriptional coactivators cooperating with the estrogen receptor and the retinoic acid receptorCloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifsThe type 1 human immunodeficiency virus Tat binding protein is a transcriptional activator belonging to an additional family of evolutionarily conserved genesCharacterization of a family of related cellular transcription factors which can modulate human immunodeficiency virus type 1 transcription in vitroDSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologsTranscriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoterPurification of a Tat-associated kinase reveals a TFIIH complex that modulates HIV-1 transcriptionSpt5 cooperates with human immunodeficiency virus type 1 Tat by preventing premature RNA release at terminator sequencesRelief of two built-In autoinhibitory mechanisms in P-TEFb is required for assembly of a multicomponent transcription elongation complex at the human immunodeficiency virus type 1 promoterTat-dependent occlusion of the HIV poly(A) siteHuman immunodeficiency virus type 1 Tat increases the expression of cleavage and polyadenylation specificity factor 73-kilodalton subunit modulating cellular and viral expressionSpecific binding of RNA polymerase II to the human immunodeficiency virus trans-activating region RNA is regulated by cellular cofactors and TatHuman immunodeficiency virus type-1 Tat is an integral component of the activated transcription-elongation complexInhibition of HIV-1 Tat-mediated LTR transactivation and HIV-1 infection by anti-Tat single chain intrabodiesNovel mechanism and factor for regulation by HIV-1 TatThe HIV-1 Tat cellular coactivator Tat-SF1 is a general transcription elongation factorTrans-activation by human immunodeficiency virus Tat protein requires the C-terminal domain of RNA polymerase IIThe HIV transactivator TAT binds to the CDK-activating kinase and activates the phosphorylation of the carboxy-terminal domain of RNA polymerase IIBinding of basal transcription factor TFIIH to the acidic activation domains of VP16 and p53Visna virus Tat protein: a potent transcription factor with both activator and suppressor domainsThe human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzymeThree functional classes of transcriptional activation domainA human primary T-lymphocyte-derived human immunodeficiency virus type 1 Tat-associated kinase phosphorylates the C-terminal domain of RNA polymerase II and induces CAK activityLentivirus Tat proteins specifically associate with a cellular protein kinase, TAK, that hyperphosphorylates the carboxyl-terminal domain of the large subunit of RNA polymerase II: candidate for a Tat cofactorInteraction of human immunodeficiency virus type 1 Tat with a unique site of TFIID inhibits negative cofactor Dr1 and stabilizes the TFIID-TFIIA complexMutations in the carboxy-terminal domain of TBP affect the synthesis of human immunodeficiency virus type 1 full-length and short transcripts similarlyFunctional interaction between the HIV transactivator Tat and the transcriptional coactivator PC4 in T cellsHIV-1 Tat protein-mediated transactivation of the HIV-1 long terminal repeat promoter is potentiated by a novel nuclear Tat-interacting protein of 110 kDa, Tip110Regulation of carboxyl-terminal domain phosphatase by HIV-1 tat proteinAssociation of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexesA novel LBP-1-mediated restriction of HIV-1 transcription at the level of elongation in vitroThe human immunodeficiency virus type 1 Tat antagonist, Ro 5-3335, predominantly inhibits transcription initiation from the viral promoterInhibition of type 1 human immunodeficiency virus replication by a tat antagonist to which the virus remains sensitive after prolonged exposure in vitroMechanisms of HIV-1 to escape from the host immune surveillance.A novel glutamine-RNA interaction identified by screening libraries in mammalian cells.RNA recognition by arginine-rich peptide motifs.
P2860
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P2860
HIV-1 Tat acts as a processivity factor in vitro in conjunction with cellular elongation factors
description
1992 nî lūn-bûn
@nan
1992 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
HIV-1 Tat acts as a processivi ...... th cellular elongation factors
@ast
HIV-1 Tat acts as a processivi ...... th cellular elongation factors
@en
HIV-1 Tat acts as a processivi ...... th cellular elongation factors
@nl
type
label
HIV-1 Tat acts as a processivi ...... th cellular elongation factors
@ast
HIV-1 Tat acts as a processivi ...... th cellular elongation factors
@en
HIV-1 Tat acts as a processivi ...... th cellular elongation factors
@nl
prefLabel
HIV-1 Tat acts as a processivi ...... th cellular elongation factors
@ast
HIV-1 Tat acts as a processivi ...... th cellular elongation factors
@en
HIV-1 Tat acts as a processivi ...... th cellular elongation factors
@nl
P2093
P356
P1433
P1476
HIV-1 Tat acts as a processivi ...... th cellular elongation factors
@en
P2093
P304
P356
10.1101/GAD.6.4.655
P407
P577
1992-04-01T00:00:00Z