Evidence map›Paper›PMID 10559303›Full record

ArticleJournal of virology1999

The residues between the two transformation effector sites of Epstein-Barr virus latent membrane protein 1 are not critical for B-lymphocyte growth transformation.

K M Izumi, E D Cahir McFarland, E A Riley, D Rizzo, Y Chen, E Kieff

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
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 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.9field-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

33 citing papers in PubMed, 83 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Epstein-Barr virus latent genes.Experimental & molecular medicine · 2015
    Review
  12. Article
  13. Review
  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

6 authors at 2 institutions in 1 country.

K M IzumiDepartment of Medicine, Brigham and Women's Hospital, Channing Laboratories, Harvard Medical School, Boston, Massachusetts 02115-5804, USA.
E D Cahir McFarland
E A Riley
D Rizzo
Y Chen
E Kieff
Brigham and Women's Hospital · USHarvard University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Epstein-Barr virus (EBV) latent membrane protein 1 (LMP1) is essential for EBV-mediated transformation of primary B lymphocytes. LMP1 spontaneously aggregates in the plasma membrane and enables two transformation effector sites (TES1 and TES2) within the 200-amino-acid cytoplasmic carboxyl terminus to constitutively engage the tumor necrosis factor receptor (TNFR)-associated factors TRAF1, TRAF2, TRAF3, and TRAF5 and the TNFR-associated death domain proteins TRADD and RIP, thereby activating NF-kappaB and c-Jun N-terminal kinase (JNK). To investigate the importance of the 60% of the LMP1 carboxyl terminus that lies between the TES1-TRAF and TES2-TRADD and -RIP binding sites, an EBV recombinant was made that contains a specific deletion of LMP1 codons 232 to 351. Surprisingly, the deletion mutant was similar to wild-type (wt) LMP1 EBV recombinants in its efficiency in transforming primary B lymphocytes into lymphoblastoid cell lines (LCLs). Mutant and wt EBV-transformed LCLs were similarly efficient in long-term outgrowth and in regrowth after endpoint dilution. Mutant and wt LMP1 proteins were also similar in their constitutive association with TRAF1, TRAF2, TRAF3, TRADD, and RIP. Mutant and wt EBV-transformed LCLs were similar in steady-state levels of Bcl2, JNK, and activated JNK proteins. The wt phenotype of recombinants with LMP1 codons 232 to 351 deleted further demarcates TES1 and TES2, underscores their central importance in B-lymphocyte growth transformation, and provides a new perspective on LMP1 sequence variation between TES1 and TES2.

Indexed as

Cell Transformation, ViralHomeodomain ProteinsTumor Necrosis Factor Receptor-Associated Peptides and ProteinsBinding SitesB-LymphocytesCell DivisionCells, CulturedCodonCytoskeletal ProteinsDNA-Binding ProteinsEpstein-Barr Virus Nuclear AntigensHerpesvirus 4, HumanHumansJNK Mitogen-Activated Protein KinasesMitogen-Activated Protein Kinase 9Mitogen-Activated Protein KinasesCodonCytoskeletal ProteinsDistal-less homeobox proteinsDNA-Binding ProteinsEBV-associated membrane antigen, Epstein-Barr virusEpstein-Barr Virus Nuclear AntigensFLAG peptideHomeodomain ProteinsJNK Mitogen-Activated Protein KinasesMitogen-Activated Protein Kinase 9Mitogen-Activated Protein KinasesNF-kappa BOligopeptidesPeptidesProtein KinasesProteinsRecombinant Fusion ProteinsRNA-Binding ProteinsTes protein, mouseTNF Receptor-Associated Death Domain ProteinTNF Receptor-Associated Factor 1TNF Receptor-Associated Factor 2TNF Receptor-Associated Factor 3Tradd protein, mouseTranscription FactorsTumor Necrosis Factor Receptor-Associated Peptides and ProteinsViral Matrix Proteins

Identifiers

PMID10559303
PMCPMC113040
OpenAlexW2144076363

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.