Evidence map›Paper›PMID 9334327›Full record

ArticleGenes & development1997

The HIV transactivator TAT binds to the CDK-activating kinase and activates the phosphorylation of the carboxy-terminal domain of RNA polymerase II.

T P Cujec, H Okamoto, K Fujinaga, J Meyer, H Chamberlin, D O Morgan, B M Peterlin

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

94 citing papers in PubMed, 194 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. HIV Transcription Is Independent of Mediator Kinases.AIDS research and human retroviruses · 2019
    Article
  11. Article
  12. Review
  13. Apobec3A maintains HIV-1 latency through recruitment of epigenetic silencing machinery to the long terminal repeat.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  14. Article
  15. Article
  16. The essential and multifunctional TFIIH complex.Protein science : a publication of the Protein Society · 2018
    Review
  17. Article
  18. Review
  19. Article
  20. Article

34 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

T P CujecHoward Hughes Medical Institute, Department of Medicine, University of California at San Francisco, San Franscisco, California USA.
H Okamoto
K Fujinaga
J Meyer
H Chamberlin
D O Morgan
B M Peterlin
Howard Hughes Medical Institute · USUniversity of California, San Francisco · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human immunodeficiency virus encodes the transcriptional transactivator Tat, which binds to the transactivation response (TAR) RNA stem-loop in the viral long terminal repeat (LTR) and increases rates of elongation rather than initiation of transcription by RNA polymerase II (Pol II). In this study, we demonstrate that Tat binds directly to the cyclin-dependent kinase 7 (CDK7), which leads to productive interactions between Tat and the CDK-activating kinase (CAK) complex and between Tat and TFIIH. Tat activates the phosphorylation of the carboxy-terminal domain (CTD) of Pol II by CAK in vitro. The ability of CAK to phosphorylate the CTD can be inhibited specifically by a CDK7 pseudosubstrate peptide that also inhibits transcriptional activation by Tat in vitro and in vivo. We conclude that the phosphorylation of the CTD by CAK is essential for Tat transactivation. Our data identify a cellular protein that interacts with the activation domain of Tat, demonstrate that this interaction is critical for the function of Tat, and provide a mechanism by which Tat increases the processivity of Pol II.

Indexed as

Cyclin-Dependent KinasesTranscriptional ActivationTranscription Factors, TFIIAnimalsCell LineCyclin-Dependent Kinase-Activating KinaseGene Products, tatHumansKineticsModels, ChemicalMutagenesis, Site-DirectedPhosphorylationPolymerase Chain ReactionProtein KinasesProtein Serine-Threonine KinasesRecombinant Fusion Proteinscarboxy-terminal domain kinaseCyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesGene Products, tatProtein KinasesProtein Serine-Threonine KinasesRecombinant Fusion ProteinsRNA Polymerase IITranscription FactorsTranscription Factors, TFIITranscription Factor TFIIH

Identifiers

PMID9334327
PMCPMC316603
OpenAlexW2108857688

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.