Evidence map›Paper›PMID 12195020›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2002

Epstein-Barr virus EBNA2 blocks Nur77- mediated apoptosis.

Jae Myun Lee, Kyoung-Ho Lee, Magdalena Weidner, Barbara A Osborne, S Diane Hayward

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

44 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. Article
  3. Controversy and multiple roles of the solitary nucleus receptor Nur77 in disease and physiology.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Review
  4. Multiple sclerosis and infection: history, EBV, and the search for mechanism.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Review
  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 4 institutions in 2 countries.

Jae Myun LeeDepartment of Pharmacology and Molecular Sciences, Johns Hopkins School of Medicine, 1650 Orleans Street, Baltimore, MD 21231, USA.
Kyoung-Ho Lee
Magdalena Weidner
Barbara A Osborne
S Diane Hayward
Johns Hopkins University · USLaboratory of Molecular Genetics · PLSidney Kimmel Comprehensive Cancer Center · USUniversity of Massachusetts Amherst · US

Funding

BIOCHEMISTRY, CELLULAR AND MOLECULAR BIOLOGY PROGRAMT32GM007445 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREEN, RACHEL · 1985 to 2021
$24.1M
REGULATION OF REPLICATION AND LATENCY BY EBV EBNASR01CA042245 · NCI · JOHNS HOPKINS UNIVERSITY · PI HAYWARD, S DIANE · 1986 to 2002
$871k
NCI NIH HHS R01 CA042245NCI NIH HHS R01 CA42245NIGMS NIH HHS 5 T32 GM07445NIGMS NIH HHS T32 GM007445PHS HHS R01 A47922
6 · The paper itself

Abstract

Epstein-Barr virus infection in vitro immortalizes primary B cells. EBNA2 is an Epstein-Barr virus-encoded transcriptional transactivator that mimics the effects of activated Notch signaling and is essential for this proliferative response. An assay using Sindbis virus (SV) as a cell death inducer revealed that, like Notch, EBNA2 also has antiapoptotic activity. We show that Nur77 is a mediator of SV-induced cell death and that EBNA2 antiapoptotic activity results from interaction with Nur77. EBNA2 colocalized with Nur77 in transfected cells and coprecipitated with Nur77 in IB4 B cells. EBNA2 binds to Nur77 through sequences in the EBNA2 amino acid 123-147 conserved domain and an EBNA2 mutant unable to bind Nur77 also lost the ability to protect cells from SV-induced apoptosis. EBNA2 exerted its antideath function by retaining Nur77 in the nucleus and preventing Nur77 from targeting mitochondria in response to apoptotic stimuli. Thus, targeting of Nur77 can be added to the list of strategies used by viruses to counter apoptosis.

Indexed as

Receptors, Cell SurfaceAnimalsApoptosisCell LineCell NucleusCricetinaeDNA-Binding ProteinsEpstein-Barr Virus Nuclear AntigensFluorescent Antibody TechniqueHerpesvirus 4, HumanMembrane ProteinsMiceNuclear Receptor Subfamily 4, Group A, Member 1Precipitin TestsProtein TransportReceptor, Notch1DNA-Binding ProteinsEBNA-2 protein, Human herpesvirus 4Epstein-Barr Virus Nuclear AntigensMembrane ProteinsNotch1 protein, mouseNR4A1 protein, humanNr4a1 protein, mouseNuclear Receptor Subfamily 4, Group A, Member 1Receptor, Notch1Receptors, Cell SurfaceReceptors, Cytoplasmic and NuclearReceptors, SteroidTranscription FactorsViral Proteins

Identifiers

PMID12195020
PMCPMC129362
OpenAlexW2137336327

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.