Evidence map›Paper›PMID 20682079›Full record

ArticleJournal of biomedical science2010

Enterovirus type 71 2A protease functions as a transcriptional activator in yeast.

Chee-Hing Yang, Hui-Chun Li, Jeng-Geng Jiang, Che-Fang Hsu, Yi-Jen Wang, Meng-Jiun Lai, Yue-Li Juang, Shih-Yen Lo

Open access · diamondAbstract readComparative Study
In one paragraph

Article in Journal of biomedical science, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.7field-weighted citation impact, top 14% 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

21 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Analysis of the Complete Genomes of Enterovirus 71 Subtypes in China.The Canadian journal of infectious diseases & medical microbiology = Journal canadien des maladies infectieuses et de la microbiologie medicale · 2021
    Article
  5. Review
  6. Review
  7. Article
  8. Enterovirus A71 Proteins: Structure and Function.Frontiers in microbiology · 2018
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Studying coronavirus-host protein interactions.Methods in molecular biology (Clifton, N.J.) · 2015
    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

8 authors at 1 institution in 1 country.

Chee-Hing YangDepartment of Laboratory Medicine and Biotechnology, Tzu Chi University, Hualien, Taiwan.
Hui-Chun Li
Jeng-Geng Jiang
Che-Fang Hsu
Yi-Jen Wang
Meng-Jiun Lai
Yue-Li Juang
Shih-Yen Lo
Tzu Chi University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enterovirus type 71 (EV71) 2A protease exhibited strong transcriptional activity in yeast cells. The transcriptional activity of 2A protease was independent of its protease activity. EV71 2A protease retained its transcriptional activity after truncation of 40 amino acids at the N-terminus but lost this activity after truncation of 60 amino acids at the N-terminus or deletion of 20 amino acids at the C-terminus. Thus, the acidic domain at the C-terminus of this protein is essential for its transcriptional activity. Indeed, deletion of amino acids from 146 to 149 (EAME) in this acidic domain lost the transcriptional activity of EV71 2A protein though still retained its protease activity. EV71 2A protease was detected both in the cytoplasm and nucleus using confocal microscopy analysis. Coxsackie virus B3 2A protease also exhibited transcriptional activity in yeast cells. As expected, an acidic domain in the C-terminus of Coxsackie virus B3 2A protease was also identified. Truncation of this acidic domain resulted in the loss of transcriptional activity. Interestingly, this acidic region of poliovirus 2A protease is critical for viral RNA replication. The transcriptional activity of the EV71 or Coxsackie virus B3 2A protease should play a role in viral replication and/or pathogenesis.

Indexed as

Amino Acid SequenceBlotting, WesternCysteine EndopeptidasesEnterovirus A, HumanEnterovirus B, HumanHeLa CellsHumansMicroscopy, ConfocalReverse Transcriptase Polymerase Chain ReactionSequence DeletionTrans-ActivatorsTwo-Hybrid System TechniquesViral ProteinsVirus ReplicationYeastsCysteine Endopeptidasespicornain 2A, PicornavirusTrans-ActivatorsViral Proteins

Identifiers

PMID20682079
PMCPMC2923119
OpenAlexW2121971955

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.