Evidence map›Paper›PMID 18566585›Full record

ArticleThe EMBO journal2008

The structure of P-TEFb (CDK9/cyclin T1), its complex with flavopiridol and regulation by phosphorylation.

Sonja Baumli, Graziano Lolli, Edward D Lowe, Sonia Troiani, Luisa Rusconi, Alex N Bullock, Judit E Debreczeni, Stefan Knapp, Louise N Johnson

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 203 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
203citing papers in PubMed, 1 pooled it
9.9field-weighted citation impact, top 1% of its field
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

203 citing papers in PubMed, 1 synthesis or guideline pooled it, 349 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Article
  4. Article
  5. Structural basis for P-TEFb association with BRD4.bioRxiv : the preprint server for biology · 2026
    Article
  6. Targeting CDKs in the RNAPII transcription cycle.Nature reviews. Drug discovery · 2026
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Targeting CDK9 with Molegro Virtual Docker.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

143 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

9 authors at 3 institutions in 2 countries.

Sonja BaumliLaboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, Oxford, UK.
Graziano Lolli
Edward D Lowe
Sonia Troiani
Luisa Rusconi
Alex N Bullock
Judit E Debreczeni
Stefan Knapp
Louise N Johnson
University of Oxford · GBGenomics (United Kingdom) · GBNerviano Medical Sciences · IT

Funding

Biotechnology and Biological Sciences Research CouncilMedical Research Council G0400957Medical Research Council G0701166Wellcome Trust
6 · The paper itself

Abstract

The positive transcription elongation factor b (P-TEFb) (CDK9/cyclin T (CycT)) promotes mRNA transcriptional elongation through phosphorylation of elongation repressors and RNA polymerase II. To understand the regulation of a transcriptional CDK by its cognate cyclin, we have determined the structures of the CDK9/CycT1 and free cyclin T2. There are distinct differences between CDK9/CycT1 and the cell cycle CDK CDK2/CycA manifested by a relative rotation of 26 degrees of CycT1 with respect to the CDK, showing for the first time plasticity in CDK cyclin interactions. The CDK9/CycT1 interface is relatively sparse but retains some core CDK-cyclin interactions. The CycT1 C-terminal helix shows flexibility that may be important for the interaction of this region with HIV TAT and HEXIM. Flavopiridol, an anticancer drug in phase II clinical trials, binds to the ATP site of CDK9 inducing unanticipated structural changes that bury the inhibitor. CDK9 activity and recognition of regulatory proteins are governed by autophosphorylation. We show that CDK9/CycT1 autophosphorylates on Thr186 in the activation segment and three C-terminal phosphorylation sites. Autophosphorylation on all sites occurs in cis.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCyclin-Dependent Kinase 9CyclinsCyclin TFlavonoidsHumansModels, MolecularMolecular Sequence DataPhosphorylationPiperidinesSequence AlignmentalvocidibCCNT1 protein, humanCCNT2 protein, humanCDK9 protein, humanCyclin-Dependent Kinase 9CyclinsCyclin TFlavonoidsPiperidines

Identifiers

PMID18566585
PMCPMC2486423
OpenAlexW2103608656

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.