Evidence map›Paper›PMID 26439734›Full record

ArticleScientific reports2015

Kinetic characterization of trans-proteolytic activity of Chikungunya virus capsid protease and development of a FRET-based HTS assay.

Megha Aggarwal, Rajesh Sharma, Pravindra Kumar, Manmohan Parida, Shailly Tomar

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
5.0field-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

17 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. The evolution of chikungunya virus circulating in Indonesia: Sequence analysis of the orf2 gene encoding the viral structural proteins.International microbiology : the official journal of the Spanish Society for Microbiology · 2023
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Dimethyl sulfoxide reduces the stability but enhances catalytic activity of the main SARS-CoV-2 protease 3CLpro.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  10. Review
  11. ArthritogenicLife (Basel, Switzerland) · 2021
    Review
  12. Functional Study of the Retrotransposon-Derived Human PEG10 Protease.International journal of molecular sciences · 2020
    Article
  13. Article
  14. Multi-core-shell composite SnOEnvironmental science and pollution research international · 2019
    Article
  15. Review
  16. Review
  17. 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

5 authors at 2 institutions in 1 country.

Megha AggarwalDepartment of Biotechnology, Indian Institute of Technology Roorkee, Roorkee-247667, India.
Rajesh SharmaDepartment of Biotechnology, Indian Institute of Technology Roorkee, Roorkee-247667, India.
Pravindra KumarDepartment of Biotechnology, Indian Institute of Technology Roorkee, Roorkee-247667, India.
Manmohan ParidaDivision of Virology, Defence Research and Development Establishment, Gwalior 474002, India.
Shailly TomarDepartment of Biotechnology, Indian Institute of Technology Roorkee, Roorkee-247667, India.
Indian Institute of Technology Roorkee · INDefence Research and Development Establishment · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chikungunya virus (CHIKV) capsid protein (CVCP) is a serine protease that possesses cis-proteolytic activity essential for the structural polyprotein processing and plays a key role in the virus life cycle. CHIKV being an emerging arthropod-borne pathogenic virus, is a public health concern worldwide. No vaccines or specific antiviral treatment is currently available for chikungunya disease. Thus, it is important to develop inhibitors against CHIKV enzymes to block key steps in viral reproduction. In view of this, CVCP was produced recombinantly and purified to homogeneity. A fluorescence resonance energy transfer (FRET)-based proteolytic assay was developed for high throughput screening (HTS). A FRET peptide substrate (DABCYL-GAEEWSLAIE-EDANS) derived from the cleavage site present in the structural polyprotein of CVCP was used. The assay with a Z' factor of 0.64 and coefficient of variation (CV) is 8.68% can be adapted to high throughput format for automated screening of chemical libraries to identify CVCP specific protease inhibitors. Kinetic parameters Km and kcat/Km estimated using FRET assay were 1.26 ± 0.34 μM and 1.11 × 10(3) M(-1) sec(-1) respectively. The availability of active recombinant CVCP and cost effective fluorogenic peptide based in vitro FRET assay may serve as the basis for therapeutics development against CHIKV.

Indexed as

Fluorescence Resonance Energy TransferCapsid ProteinsChikungunya FeverChikungunya virusCloning, MolecularHigh-Throughput Screening AssaysHumansKineticsModels, MolecularPeptide HydrolasesProtease InhibitorsProtein ConformationCapsid ProteinsPeptide HydrolasesProtease Inhibitors

Identifiers

PMID26439734
PMCPMC4593962
OpenAlexW2411577186

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.