HIV-1 Tat protein promotes formation of more-processive elongation complexes.
about
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 RNAA cofactor, TIP30, specifically enhances HIV-1 Tat-activated transcriptionCA150, a nuclear protein associated with the RNA polymerase II holoenzyme, is involved in Tat-activated human immunodeficiency virus type 1 transcriptionCloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifsRole of flanking E box motifs in human immunodeficiency virus type 1 TATA element functionDSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologsPITALRE, the catalytic subunit of TAK, is required for human immunodeficiency virus Tat transactivation in vivo.Transcriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoterAnalysis of the effect of natural sequence variation in Tat and in cyclin T on the formation and RNA binding properties of Tat-cyclin T complexes.Purification of a Tat-associated kinase reveals a TFIIH complex that modulates HIV-1 transcriptionTranscription elongation factor P-TEFb mediates Tat activation of HIV-1 transcription at multiple stagesSpt5 cooperates with human immunodeficiency virus type 1 Tat by preventing premature RNA release at terminator sequencesThe transcription elongation factor CA150 interacts with RNA polymerase II and the pre-mRNA splicing factor SF1Relief 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 promoterNMR structure of a biologically active peptide containing the RNA-binding domain of human immunodeficiency virus type 1 TatTat-dependent occlusion of the HIV poly(A) siteSpecific 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 factorThe Drosophila 7SK snRNP and the essential role of dHEXIM in developmentThe 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 domainRegulation of human immunodeficiency virus type 1 and cytokine gene expression in myeloid cells by NF-kappa B/Rel transcription factorsIn vitro and in vivo binding of human immunodeficiency virus type 1 Tat protein and Sp1 transcription factorA 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 similarlyThe human immunodeficiency virus Tat proteins specifically associate with TAK in vivo and require the carboxyl-terminal domain of RNA polymerase II for functionPhosphorylation of HIV Tat by PKR increases interaction with TAR RNA and enhances transcriptionHIV restriction in quiescent CD4⁺ T cellsCircularization of the HIV-1 RNA genomeStructure of HIV-1 TAR RNA in the absence of ligands reveals a novel conformation of the trinucleotide bulge
P2860
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P2860
HIV-1 Tat protein promotes formation of more-processive elongation complexes.
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年学术文章
@wuu
1991年学术文章
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1991年学术文章
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1991年学术文章
@zh-my
1991年学术文章
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1991年學術文章
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1991年學術文章
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1991年學術文章
@zh-hant
name
HIV-1 Tat protein promotes formation of more-processive elongation complexes.
@ast
HIV-1 Tat protein promotes formation of more-processive elongation complexes.
@en
type
label
HIV-1 Tat protein promotes formation of more-processive elongation complexes.
@ast
HIV-1 Tat protein promotes formation of more-processive elongation complexes.
@en
prefLabel
HIV-1 Tat protein promotes formation of more-processive elongation complexes.
@ast
HIV-1 Tat protein promotes formation of more-processive elongation complexes.
@en
P2860
P1433
P1476
HIV-1 Tat protein promotes formation of more-processive elongation complexes.
@en
P2093
R A Marciniak
P2860
P304
P407
P577
1991-12-01T00:00:00Z