Evidence map›Paper›PMID 15096509›Full record

ArticleThe Journal of biological chemistry2004

The hepatitis E virus open reading frame 3 protein activates ERK through binding and inhibition of the MAPK phosphatase.

Anindita Kar-Roy, Hasan Korkaya, Ruchi Oberoi, Sunil Kumar Lal, Shahid Jameel

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

45 citing papers in PubMed, 84 citations in OpenAlex.

  1. Review
  2. Genetic Evolution of Hepatitis E Virus.Advances in experimental medicine and biology · 2023
    Review
  3. Characteristics and Functions of HEV Proteins.Advances in experimental medicine and biology · 2023
    Article
  4. Structural aspects of hepatitis E virus.Archives of virology · 2022
    Review
  5. Review
  6. Review
  7. Structural and molecular biology of hepatitis E virus.Computational and structural biotechnology journal · 2021
    Review
  8. Review
  9. Stem Cell-Derived Culture Models of Hepatitis E Virus Infection.Cold Spring Harbor perspectives in medicine · 2019
    Review
  10. Hepatitis E Virus Genome Structure and Replication Strategy.Cold Spring Harbor perspectives in medicine · 2019
    Review
  11. Article
  12. Article
  13. Hepatitis E virus: advances and challenges.Nature reviews. Gastroenterology & hepatology · 2018
    Review
  14. Article
  15. Article
  16. Review
  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.

Anindita Kar-RoyVirology Group, International Centre for Genetic Engineering and Biotechnology, New Delhi 110067, India.
Hasan Korkaya
Ruchi Oberoi
Sunil Kumar Lal
Shahid Jameel
International Centre for Genetic Engineering and Biotechnology · IN

Funding

Wellcome Trust 063171
6 · The paper itself

Abstract

The hepatitis E virus causes acute viral hepatitis endemic in much of the developing world and is a serious public health problem. However, due to the lack of an in vitro culture system or a small animal model, its biology and pathogenesis are poorly understood. We have shown earlier that the ORF3 protein (pORF3) of hepatitis E virus activates ERK, a member of the MAPK superfamily. Here we have explored the mechanism of pORF3-mediated ERK activation and demonstrated it to be independent of the Raf/MEK pathway. Using biochemical assays, yeast two-hybrid analysis, and intracellular fluorescence resonance energy transfer we showed that pORF3 binds Pyst1, a prototypic member of the ERK-specific MAPK phosphatase. The binding regions in the two proteins were mapped to the N terminus of pORF3 and a central portion of Pyst1. Expression of pORF3 protected ERK from the inhibitory effects of ectopically expressed Pyst1. This is the first example of a viral protein regulating ERK activation by inhibition of its cognate dual specificity phosphatase.

Indexed as

Cell Cycle ProteinsJNK Mitogen-Activated Protein KinasesPhosphoprotein PhosphatasesAnimalsBlotting, WesternCell LineCOS CellsCytoplasmDual Specificity Phosphatase 1Dual Specificity Phosphatase 6Enzyme ActivationEnzyme InhibitorsFluorescence Resonance Energy TransferGlutathione TransferaseImmediate-Early ProteinsMAP Kinase Kinase 4Cell Cycle ProteinsDual Specificity Phosphatase 1Dual Specificity Phosphatase 6Enzyme InhibitorsGlutathione TransferaseImmediate-Early ProteinsJNK Mitogen-Activated Protein KinasesMAP Kinase Kinase 4Mitogen-Activated Protein Kinase KinasesMitogen-Activated Protein KinasesORF3 protein, Hepatitis E virusPhosphoprotein PhosphatasesPhosphoric Monoester HydrolasesProtein Phosphatase 1Protein Tyrosine PhosphatasesViral Proteins

Identifiers

PMID15096509
PMCPMC2441640
OpenAlexW2080062813

What OpenQuestion holds

Textmetadata
LicenceTDM
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.