Evidence map›Paper›PMID 12525665›Full record

ArticleJournal of virology2003

Protein phosphatase 2A enhances activation of human immunodeficiency virus type 1 by phorbol myristate acetate.

Neil E Faulkner, Brian R Lane, Paul J Bock, David M Markovitz

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

16 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Insights into the HIV Latency and the Role of Cytokines.Pathogens (Basel, Switzerland) · 2019
    Review
  4. SIV-Mediated Synaptic Dysfunction Is Associated with an Increase in Synapsin Site 1 Phosphorylation and Impaired PP2A Activity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2019
    Article
  5. Review
  6. Review
  7. A Highly Convergent Total Synthesis of Leustroducsin B.Journal of the American Chemical Society · 2015
    Article
  8. Article
  9. P-TEFb- the final frontier.Cell division · 2009
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. 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

4 authors at 1 institution in 1 country.

Neil E FaulknerCellular and Molecular Biology Program. Division of Infectious Diseases, Department of Internal Medicine, University of Michigan Medical Center, Ann Arbor, Michigan 48109-0640, USA.
Brian R Lane
Paul J Bock
David M Markovitz
University of Michigan–Ann Arbor · US

Funding

MICHIGAN MEDICAL SCIENTIST TRAINING PROGRAMT32GM007863 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI COLLINS, KATHLEEN L. · 1985 to 2024
$38.3M
Molecular Mechanisms of Microbial Pathogenesis Training ProgramT32AI007528 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI CARRUTHERS, VERNON BRUCE · 1998 to 2024
$6.8M
REGULATION OF HIV2 TRANSCRIPTION BY THE PETS FACTORR01AI036685 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MARKOVITZ, DAVID MICHAEL · 1994 to 2002
$929k
NIAID NIH HHS AI07528NIAID NIH HHS AI 36685NIAID NIH HHS T32 AI007528NIGMS NIH HHS T32 GM007863NIGMS NIH HHS T32 GM07863
6 · The paper itself

Abstract

The viral replication rate in patients infected with human immunodeficiency virus type 1 (HIV-1) is controlled in part by regulation of the transcription of viral genes. The rate of transcription is determined by a complex interplay between cellular and viral proteins and the promoter elements found in the long terminal repeats. Protein phosphatase 2A (PP2A) is a phosphoprotein that plays important roles in the regulation of signal transduction and cell growth. In this report, we demonstrate that overexpression of the catalytic subunit of protein phosphatase 2A (PP2Ac) increases the basal activity of the HIV-1 promoter and, especially, enhances the promoter's response to the protein kinase C (PKC) activator 12-O-tetradecanoyl phorbol-13-acetate (PMA). Additionally, ectopic PP2Ac enhances activation of HIV-1 provirus by PMA. Okadaic acid, a potent inhibitor of PP2A, markedly reduces both HIV-1 enhancer and proviral activation. Fostriecin, a PP2A inhibitor which has been used as an antineoplastic agent in clinical trials, is also able to inhibit PMA-stimulated HIV-1 proviral activation. These observations demonstrate a role for the important cellular phosphatase PP2A in HIV-1 transcription and replication and also suggest that PKC can potentiate the activity of PP2A. PP2A is a potential target for therapeutic intervention in patients infected with HIV-1.

Indexed as

AlkenesHIV-1HumansOkadaic AcidPhosphoprotein PhosphatasesPolyenesPromoter Regions, GeneticProtein Kinase CProtein Phosphatase 2PyronesTetradecanoylphorbol AcetateTumor Necrosis Factor-alphaU937 CellsVirus ActivationAlkenesfostriecinOkadaic AcidPhosphoprotein PhosphatasesPolyenesProtein Kinase CProtein Phosphatase 2PyronesTetradecanoylphorbol AcetateTumor Necrosis Factor-alpha

Identifiers

PMID12525665
PMCPMC140936
OpenAlexW2159428489

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.