Evidence map›Paper›PMID 10364292›Full record

ArticleJournal of virology1999

Human and rodent transcription elongation factor P-TEFb: interactions with human immunodeficiency virus type 1 tat and carboxy-terminal domain substrate.

Y Ramanathan, S M Reza, T M Young, M B Mathews, T Pe'ery

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

22 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. P-TEFb as A Promising Therapeutic Target.Molecules (Basel, Switzerland) · 2020
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

5 authors at 2 institutions in 1 country.

Y RamanathanDepartment of Biochemistry and Molecular Biology, New Jersey Medical School, University of Medicine and Dentistry of New Jersey, Newark, New Jersey 07103, USA.
S M Reza
T M Young
M B Mathews
T Pe'ery
Rutgers New Jersey Medical SchoolRutgers, The State University of New Jersey · US

Funding

REGULATION OF HIV1 GENE EXPRESSION BY TAT AND TARR01AI031802 · NIAID · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI MATHEWS, MICHAEL B · 1992 to 2001
$642k
NIAID NIH HHS AI 31802
6 · The paper itself

Abstract

The human immunodeficiency virus type 1 transcriptional regulator Tat increases the efficiency of elongation, and complexes containing the cellular kinase CDK9 have been implicated in this process. CDK9 is part of the Tat-associated kinase TAK and of the elongation factor P-TEFb (positive transcription elongation factor-b), which consists minimally of CDK9 and cyclin T. TAK and P-TEFb are both able to phosphorylate the carboxy-terminal domain (CTD) of RNA polymerase II, but their relationships to one another and to the stimulation of elongation by Tat are not well characterized. Here we demonstrate that human cyclin T1 (but not cyclin T2) interacts with the activation domain of Tat and is a component of TAK as well as of P-TEFb. Rodent (mouse and Chinese hamster) cyclin T1 is defective in Tat binding and transactivation, but hamster CDK9 interacts with human cyclin T1 to give active TAK in hybrid cells containing human chromosome 12. Although TAK is phosphorylated on both serine and threonine residues, it specifically phosphorylates serine 5 in the CTD heptamer. TAK is found in the nuclear and cytoplasmic fractions of human cells as a large complex (approximately 950 kDa). Magnesium or zinc ions are required for the association of Tat with the kinase. We suggest a model in which Tat first interacts with P-TEFb to form the TAK complex that engages with TAR RNA and the elongating transcription complex, resulting in hyperphosphorylation of the CTD on serine 5 residues.

Indexed as

Amino Acid SequenceAnimalsCationsCell LineCHO CellsCricetinaeCyclin-Dependent Kinase 9Cyclin-Dependent KinasesCyclinsCyclin TGene Products, tatHIV-1HumansMagnesiumMiceMolecular Sequence DataCationsCCNT1 protein, humanCcnt1 protein, mouseCDK9 protein, humanCdk9 protein, mouseCyclin-Dependent Kinase 9Cyclin-Dependent KinasesCyclinsCyclin TGene Products, tatMagnesiumPositive Transcriptional Elongation Factor BProtein Serine-Threonine KinasesRecombinant Fusion ProteinsRNA Polymerase IISerinetat Gene Products, Human Immunodeficiency VirusThreonine

Identifiers

PMID10364292
PMCPMC112601
OpenAlexW1518524366

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.