Evidence map›Paper›PMID 26182358›Full record

ArticleBioscience reports2015

Full length and protease domain activity of chikungunya virus nsP2 differ from other alphavirus nsP2 proteases in recognition of small peptide substrates.

Chonticha Saisawang, Pornpan Sillapee, Kwanhathai Sinsirimongkol, Sukathida Ubol, Duncan R Smith, Albert J Ketterman

Open access · goldAbstract read
In one paragraph

Article in Bioscience reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
4.6field-weighted citation impact, top 5% 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

20 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Microbiology spectrum · 2026
    Article
  4. Article
  5. Article
  6. A robust fluorogenic substrate for chikungunya virus protease (nsP2) activity.Protein science : a publication of the Protein Society · 2025
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Chikungunya vaccines in development.Human vaccines & immunotherapeutics · 2016
    Review
  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 1 institution in 1 country.

Chonticha SaisawangInstitute of Molecular Biosciences, Mahidol University, Salaya Campus, Thailand.
Pornpan SillapeeInstitute of Molecular Biosciences, Mahidol University, Salaya Campus, Thailand.
Kwanhathai SinsirimongkolInstitute of Molecular Biosciences, Mahidol University, Salaya Campus, Thailand.
Sukathida UbolCenter for Emerging and Neglected Infectious Diseases, Mahidol University, Thailand Department of Microbiology, Faculty of Science, Mahidol University, Bangkok, Thailand.
Duncan R SmithInstitute of Molecular Biosciences, Mahidol University, Salaya Campus, Thailand Center for Emerging and Neglected Infectious Diseases, Mahidol University, Thailand.
Albert J KettermanInstitute of Molecular Biosciences, Mahidol University, Salaya Campus, Thailand albertketterman@yahoo.com.
Mahidol University · TH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alphavirus nsP2 proteins are multifunctional and essential for viral replication. The protease role of nsP2 is critical for virus replication as only the virus protease activity is used for processing of the viral non-structural polypeptide. Chikungunya virus is an emerging disease problem that is becoming a world-wide health issue. We have generated purified recombinant chikungunya virus nsP2 proteins, both full length and a truncated protease domain from the C-terminus of the nsP2 protein. Enzyme characterization shows that the protease domain alone has different properties compared with the full length nsP2 protease. We also show chikungunya nsP2 protease possesses different substrate specificity to the canonical alphavirus nsP2 polyprotein cleavage specificity. Moreover, the chikungunya nsP2 also appears to differ from other alphavirus nsP2 in its distinctive ability to recognize small peptide substrates.

Indexed as

AlphavirusChikungunya virusCysteine EndopeptidasesCysteine Proteinase InhibitorsEnzyme StabilityKineticsPeptidesProtein DomainsProtein EngineeringRecombinant ProteinsSubstrate SpecificityViral ProteinsCysteine EndopeptidasesCysteine Proteinase InhibitorsnsP2 proteinasePeptidesRecombinant ProteinsViral Proteinsalphaviruschikungunya viruscysteine proteasenon-structural protein 2 (nsP2)

Identifiers

PMID26182358
PMCPMC4445351
OpenAlexW2033288485

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.