Evidence map›Paper›PMID 11024139›Full record

ArticleJournal of virology2000

Interaction of Epstein-Barr virus nuclear antigen leader protein (EBNA-LP) with HS1-associated protein X-1: implication of cytoplasmic function of EBNA-LP.

Y Kawaguchi, K Nakajima, M Igarashi, T Morita, M Tanaka, M Suzuki, A Yokoyama, G Matsuda, K Kato, M Kanamori and 1 more

Abstract read
In one paragraph

Article in Journal of virology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

46 citing papers in PubMed, 89 citations in OpenAlex.

  1. Article
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  5. Review
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  7. Intrinsically disordered HAX-1 regulates CaBiochimica et biophysica acta. Biomembranes · 2020
    Article
  8. Article
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  10. Article
  11. High expression of HAX-1 protein is associated with tumor growth in papillary thyroid carcinoma.International journal of clinical and experimental pathology · 2018
    Article
  12. HAX-1 regulates SERCA2a oxidation and degradation.Journal of molecular and cellular cardiology · 2018
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. HAX-1 is overexpressed in hepatocellular carcinoma and promotes cell proliferation.International journal of clinical and experimental pathology · 2015
    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

11 authors at 1 institution in 1 country.

Y KawaguchiDepartment of Tumor Virology, Division of Virology and Immunology, Medical Research Institute, Tokyo Medical and Dental University, Bunkyo-ku, Tokyo 113-8510, Japan.
K Nakajima
M Igarashi
T Morita
M Tanaka
M Suzuki
A Yokoyama
G Matsuda
K Kato
M Kanamori
K Hirai
Tokyo Medical and Dental University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Epstein-Barr virus (EBV) nuclear antigen leader protein (EBNA-LP) consists of W1W2 repeats and a unique C-terminal Y1Y2 domain and has been suggested to play an important role in EBV-induced transformation. To identify the cellular factors interacting with EBNA-LP, we performed a yeast two-hybrid screen, using EBNA-LP cDNA containing four W1W2 repeats as bait and an EBV-transformed human peripheral blood lymphocyte cDNA library as the source of cellular genes. Our results were as follows. (i) All three cDNAs in positive yeast colonies were found to encode the same cellular protein, HS1-associated protein X-1 (HAX-1), which is localized mainly in the cytoplasm and has been suggested to be involved in the regulation of B-cell signal transduction and apoptosis. (ii) Mutational analysis of EBNA-LP revealed that the association with HAX-1 is mediated by the W1W2 repeat domain. (iii) A purified chimeric protein consisting of glutathione S-transferase fused to EBNA-LP specifically formed complexes with HAX-1 transiently expressed in COS-7 cells. (iv) When EBNA-LP and HAX-1 were coexpressed in COS-7 cells, EBNA-LP was specifically coimmunoprecipitated with HAX-1. (v) Careful cell fractionation experiments of an EBV-infected lymphoblastoid cell line revealed that EBNA-LP is localized in the cytoplasm as well as in the nucleus. (vi) When EBNA-LP containing four W1W2 repeats was expressed in COS-7 cells, EBNA-LP was detected mainly in the nucleus by immunofluorescence assay. Interestingly, when EBNA-LP containing a single W1W2 repeat was expressed in COS-7 cells, EBNA-LP was localized predominantly in the cytoplasm and was colocalized with HAX-1. These results indicate that EBNA-LP is in fact present and may have a significant function in the cytoplasm, possibly by interacting with and affecting the function of HAX-1.

Indexed as

Cell Transformation, ViralAdaptor Proteins, Signal TransducingAnimalsCell LineCOS CellsCytoplasmHerpesvirus 4, HumanHumansImmunoblottingPlasmidsPrecipitin TestsProteinsRecombinant Fusion ProteinsTransfectionTwo-Hybrid System TechniquesViral ProteinsAdaptor Proteins, Signal TransducingEBNA-LP protein, Human herpesvirus 4HAX1 protein, humanProteinsRecombinant Fusion ProteinsViral Proteins

Identifiers

PMID11024139
PMCPMC102049
OpenAlexW2103277453

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.