Evidence map›Paper›PMID 10618435›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

Epstein-Barr virus nuclear protein 2 interacts with p300, CBP, and PCAF histone acetyltransferases in activation of the LMP1 promoter.

L Wang, S R Grossman, E Kieff

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 119 papers.

0numbers the graph read from it
0cells of the map it votes in
119citing papers in PubMed
8.3field-weighted citation impact, top 2% 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

119 citing papers in PubMed, 216 citations in OpenAlex.

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  13. Role of Virus-Induced Host Cell Epigenetic Changes in Cancer.International journal of molecular sciences · 2021
    Review
  14. Review
  15. Review
  16. Burkitt Lymphomas Evolve to Escape Dependencies on Epstein-Barr Virus.Frontiers in cellular and infection microbiology · 2020
    Review
  17. Review
  18. Review
  19. Article
  20. Review

59 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

3 authors at 1 institution in 1 country.

L WangProgram in Virology, Department of Medicine Brigham and Women's Hospital, Harvard Medical School, Channing Laboratory, 181 Longwood Avenue, Boston, MA 02115, USA.
S R Grossman
E Kieff
Dana-Farber Brigham Cancer Center · US

Funding

Epstein-Barr Virus Nuclear Proteins in B Cell Growth TransformationR01CA047006 · NCI · BRIGHAM AND WOMEN'S HOSPITAL · PI ZHAO, BO · 2002 to 2021
$12.1M
MOLECULAR BIOLOGY OF EPSTEIN-BARR VIRUS INFECTIONR35CA047006 · NCI · BRIGHAM AND WOMEN'S HOSPITAL · PI KIEFF, ELLIOTT D · 1987 to 2000
$1.6M
NCI NIH HHS CA47006NCI NIH HHS R01 CA047006NCI NIH HHS R35 CA047006
6 · The paper itself

Abstract

The Epstein-Barr virus (EBV) nuclear protein 2 (EBNA2) and herpes simplex virion protein 16 (VP16) acidic domains that mediate transcriptional activation now are found to have affinity for p300, CBP, and PCAF histone acetyltransferases (HATs). Transcriptionally inactive point mutations in these domains lack affinity for p300, CBP, or PCAF. P300 and CBP copurify with the principal HAT activities that bind to EBNA2 or VP16 acidic domains through velocity sedimentation and anion-exchange chromatography. EBNA2 binds to both the N- and C-terminal domains of p300 and coimmune-precipitates from transfected 293T cells with p300. In EBV-infected Akata Burkitt's tumor cells that do not express the EBV encoded oncoproteins EBNA2 or LMP1, p300 expression enhances the ability of EBNA2 to up-regulate LMP1 expression. Through its intrinsic HAT activity, PCAF can further potentiate the p300 effect. In 293 T cells, P300 and CBP (but not PCAF) can also coactivate transcription mediated by the EBNA2 or VP16 acidic domains and HAT-negative mutants of p300 have partial activity. Thus, the EBNA2 and VP16 acidic domains can utilize the intrinsic HAT or scaffolding properties of p300 to activate transcription.

Indexed as

Epstein-Barr Virus Nuclear AntigensSaccharomyces cerevisiae ProteinsAcetyltransferasesBurkitt LymphomaCell Cycle ProteinsCREB-Binding ProteinDNA-Binding ProteinsFungal ProteinsGene Expression Regulation, ViralGenes, ReporterHerpes Simplex Virus Protein Vmw65Herpesvirus 4, HumanHistone AcetyltransferasesHumansMutationNuclear ProteinsAcetyltransferasesCell Cycle ProteinsCREB-Binding ProteinCREBBP protein, humanDNA-Binding ProteinsEBNA-2 protein, Human herpesvirus 4EBV-associated membrane antigen, Epstein-Barr virusEpstein-Barr Virus Nuclear AntigensFungal ProteinsGAL4 protein, S cerevisiaeHerpes Simplex Virus Protein Vmw65Histone AcetyltransferasesNuclear Proteinsp300-CBP-Associated Factorp300-CBP Transcription FactorsSaccharomyces cerevisiae ProteinsTrans-ActivatorsTranscription FactorsViral Matrix ProteinsViral Proteins

Identifiers

PMID10618435
PMCPMC26680
OpenAlexW2018571726

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.