Evidence map›Paper›PMID 18343826›Full record

ArticleThe Journal of general virology2008

Epstein-Barr virus nuclear antigen (EBNA) 3A induces the expression of and interacts with a subset of chaperones and co-chaperones.

Paul Young, Emma Anderton, Kostas Paschos, Rob White, Martin J Allday

Open access · greenAbstract read
In one paragraph

Article in The Journal of general virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

27 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Epstein-Barr virus nuclear antigen 3A partially coincides with EBNA3C genome-wide and is tethered to DNA through BATF complexes.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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 1 institution in 1 country.

Paul YoungDepartment of Virology, Imperial College London, St Mary's Campus, Norfolk Place, London W2 1PG, UK.
Emma AndertonDepartment of Virology, Imperial College London, St Mary's Campus, Norfolk Place, London W2 1PG, UK.
Kostas PaschosDepartment of Virology, Imperial College London, St Mary's Campus, Norfolk Place, London W2 1PG, UK.
Rob WhiteDepartment of Virology, Imperial College London, St Mary's Campus, Norfolk Place, London W2 1PG, UK.
Martin J AlldayDepartment of Virology, Imperial College London, St Mary's Campus, Norfolk Place, London W2 1PG, UK.
Imperial College London · GB

Funding

Wellcome Trust WT056822Wellcome Trust WT077489
6 · The paper itself

Abstract

Viral nuclear oncoproteins EBNA3A and EBNA3C are essential for the efficient immortalization of B cells by Epstein-Barr virus (EBV) in vitro and it is assumed that they play an essential role in viral persistence in the human host. In order to identify cellular genes regulated by EBNA3A expression, cDNA encoding EBNA3A was incorporated into a recombinant adenoviral vector. Microarray analysis of human diploid fibroblasts infected with either adenovirus EBNA3A or an empty control adenovirus consistently showed an EBNA3A-specific induction of mRNA corresponding to the chaperones Hsp70 and Hsp70B/B' and co-chaperones Bag3 and DNAJA1/Hsp40. Analysis of infected fibroblasts by real-time quantitative RT-PCR and Western blotting confirmed that EBNA3A, but not EBNA3C, induced expression of Hsp70, Hsp70B/B', Bag3 and DNAJA1/Hsp40. This was also confirmed in a stable, inducible expression system. EBNA3A activated transcription from the Hsp70B promoter, but not multimerized heat-shock elements in transient transfection assays, consistent with specific chaperone and co-chaperone upregulation. Co-immunoprecipitation experiments suggest that EBNA3A can form a complex with the chaperone/co-chaperone proteins in both adenovirus-infected cells and EBV-immortalized lymphoblastoid cell lines. Consistent with this, induction of EBNA3A resulted in redistribution of Hsp70 from the cytoplasm to the nucleus. EBNA3A therefore specifically induces (and then interacts with) all of the factors necessary for an active Hsp70 chaperone complex.

Indexed as

Active Transport, Cell NucleusAdaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsCell LineCell NucleusCell Transformation, ViralEpstein-Barr Virus Nuclear AntigensHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHSP72 Heat-Shock ProteinsHumansPromoter Regions, GeneticTranscriptional ActivationUp-RegulationAdaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsBAG3 protein, humanDNAJA1 protein, humanEBNA-3A antigenEpstein-Barr Virus Nuclear AntigensHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHSP72 Heat-Shock ProteinsHSPA7 protein, human

Identifiers

PMID18343826
PMCPMC2885026
OpenAlexW2152523857

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.