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A cofactor, TIP30, specifically enhances HIV-1 Tat-activated transcription
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title
A cofactor, TIP30, specifically enhances HIV-1 Tat-activated transcription
(English)
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main subject
HIV-1 Tat interactive protein 2
1 reference
stated in
GOA release 2020-03-11
regulation of transcription by RNA polymerase II
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stated in
GOA release 2020-03-11
author name string
H Xiao
series ordinal
1
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Y Tao
series ordinal
2
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J Greenblatt
series ordinal
3
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R G Roeder
series ordinal
4
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language of work or name
English
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publication date
3 March 1998
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published in
Proceedings of the National Academy of Sciences of the United States of America
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volume
95
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issue
5
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page(s)
2146-51
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cites work
The HIV transactivator TAT binds to the CDK-activating kinase and activates the phosphorylation of the carboxy-terminal domain of RNA polymerase II
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CA150, a nuclear protein associated with the RNA polymerase II holoenzyme, is involved in Tat-activated human immunodeficiency virus type 1 transcription
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Purification of a Tat-associated kinase reveals a TFIIH complex that modulates HIV-1 transcription
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Three human RNA polymerase III-specific subunits form a subcomplex with a selective function in specific transcription initiation
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The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme
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The human immunodeficiency virus Tat proteins specifically associate with TAK in vivo and require the carboxyl-terminal domain of RNA polymerase II for function
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Three functional classes of transcriptional activation domain
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Binding of basal transcription factor TFIIH to the acidic activation domains of VP16 and p53
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Novel mechanism and factor for regulation by HIV-1 Tat
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Identification of a novel human zinc finger protein that specifically interacts with the activation domain of lentiviral Tat proteins
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Molecular cloning and characterization of a cellular protein that interacts with the human immunodeficiency virus type 1 Tat transactivator and encodes a strong transcriptional activation domain
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A cDNA for a protein that interacts with the human immunodeficiency virus Tat transactivator
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TAK, an HIV Tat-associated kinase, is a member of the cyclin-dependent family of protein kinases and is induced by activation of peripheral blood lymphocytes and differentiation of promonocytic cell lines
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P-TEFb kinase is required for HIV Tat transcriptional activation in vivo and in vitro
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Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain
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Requirements for RNA polymerase II carboxyl-terminal domain for activated transcription of human retroviruses human T-cell lymphotropic virus I and HIV-1
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Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat
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Cloning and characterization of human TAF20/15. Multiple interactions suggest a central role in TFIID complex formation
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A human RNA polymerase II complex associated with SRB and DNA-repair proteins
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19 March 2017
Identification of a cellular protein that specifically interacts with the essential cysteine region of the HIV-1 Tat transactivator
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Direct interaction of human TFIID with the HIV-1 transactivator tat
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Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes
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Transcription elongation factor P-TEFb is required for HIV-1 tat transactivation in vitro
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Transcriptional activation by recruitment
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Control of RNA polymerase II elongation potential by a novel carboxyl-terminal domain kinase
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Control of RNA initiation and elongation at the HIV-1 promoter
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Species-specific interaction of the glutamine-rich activation domains of Sp1 with the TATA box-binding protein
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27 September 2017
Transcriptional activation in vitro by the human immunodeficiency virus type 1 Tat protein: evidence for specific interaction with a coactivator(s).
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27 September 2017
Unique TATA-binding protein-containing complexes and cofactors involved in transcription by RNA polymerases II and III.
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27 September 2017
Regulation of transcriptional elongation by RNA polymerase II.
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The location of cis-acting regulatory sequences in the human T cell lymphotropic virus type III (HTLV-III/LAV) long terminal repeat
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Activation of yeast polymerase II transcription by herpesvirus VP16 and GAL4 derivatives in vitro
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HIV-1 Tat protein trans-activates transcription in vitro
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27 September 2017
tat regulates binding of the human immunodeficiency virus trans-activating region RNA loop-binding protein TRP-185.
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PubMed Central
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27 September 2017
HIV-1 Tat protein promotes formation of more-processive elongation complexes
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27 September 2017
Two distinct nuclear transcription factors recognize loop and bulge residues of the HIV-1 TAR RNA hairpin
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27 September 2017
c-myc reverses neu-induced transformed morphology by transcriptional repression
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27 September 2017
The specificity of the human immunodeficiency virus type 2 transactivator is different from that of human immunodeficiency virus type 1.
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Bicistronic vector for the creation of stable mammalian cell lines that predisposes all antibiotic-resistant cells to express recombinant protein.
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Specific interaction of the human immunodeficiency virus Tat proteins with a cellular protein kinase.
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30 May 2018
Inhibition of in vivo and in vitro transcription by monoclonal antibodies prepared against wheat germ RNA polymerase II that react with the heptapeptide repeat of eukaryotic RNA polymerase II.
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30 May 2018
Presence of a potent transcription activating sequence in the p53 protein
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30 May 2018
The HIV-1 Tat protein activates transcription from an upstream DNA-binding site: implications for Tat function
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retrieved
21 January 2018
Identifiers
DOI
10.1073/PNAS.95.5.2146
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2996752
ADS bibcode
1998PNAS...95.2146X
0 references
OpenCitations bibliographic resource ID
2996752
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2996752
PMC publication ID
19278
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2996752
PubMed publication ID
9482853
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2996752
ResearchGate publication ID
13748495
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