Evidence map›Paper›PMID 39981948›Full record

ArticleProtein science : a publication of the Protein Society2025

A robust fluorogenic substrate for chikungunya virus protease (nsP2) activity.

Sparsh Makhaik, Wioletta Rut, Shruti Choudhary, Tulsi Upadhyay, Chenzhou Hao, Michael Westberg, Cedric Bobst, Euna Yoo, Jasna Fejzo, Michael Z Lin and 4 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Review
  2. A robust fluorogenic substrate for chikungunya virus protease (nsP2) activity.Protein science : a publication of the Protein Society · 2025
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors.

Sparsh MakhaikDepartment of Chemistry, University of Massachusetts, Amherst, Massachusetts, USA.ORCID 0000-0001-7622-1502
Wioletta RutDepartment of Chemical Biology and Bioimaging, Wroclaw University of Science and Technology, Wroclaw, Poland.ORCID 0000-0003-1261-5566
Shruti ChoudharyDepartment of Biochemistry and Molecular Biotechnology, University of Massachusetts Chan Medical School, Worcester, Massachusetts, USA.
Tulsi UpadhyayDepartment of Pathology, Stanford University School of Medicine, Stanford, California, USA.
Chenzhou HaoDepartment of Neurobiology, Stanford University, Stanford, California, USA.ORCID 0000-0001-6803-7270
Michael WestbergDepartment of Neurobiology, Stanford University, Stanford, California, USA.ORCID 0000-0002-2312-5282
Cedric BobstMass Spectrometry Core Facility, Institute of Applied Life Sciences, University of Massachusetts, Amherst, Massachusetts, USA.ORCID 0009-0001-2680-1100
Euna YooChemical Biology Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, Maryland, USA.ORCID 0000-0001-5982-1979
Jasna FejzoBiomolecular NMR Core Facility, Institute for Applied Life Sciences (IALS), University of Massachusetts, Amherst, Massachusetts, USA.
Michael Z LinDepartment of Neurobiology, Stanford University, Stanford, California, USA.ORCID 0000-0002-0492-1961
Matthew BogyoDepartment of Pathology, Stanford University School of Medicine, Stanford, California, USA.ORCID 0000-0003-3753-4412
Paul ThompsonDepartment of Biochemistry and Molecular Biotechnology, University of Massachusetts Chan Medical School, Worcester, Massachusetts, USA.ORCID 0000-0002-1621-3372
Marcin DragDepartment of Chemical Biology and Bioimaging, Wroclaw University of Science and Technology, Wroclaw, Poland.ORCID 0000-0001-8510-1967
Jeanne A HardyDepartment of Chemistry, University of Massachusetts, Amherst, Massachusetts, USA.ORCID 0000-0002-3406-7997

Funding

Chemical probes to decipher PAD biologyR35GM118112 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI Paul R Thompson · 2016 to 2026
$9.5M
CIHR PS 162417Foundation for Polish Science TEAM/2017-4/32NIGMS NIH HHS R35 GM118112
6 · The paper itself

Abstract

Chikungunya virus (CHIKV) is an emerging pathogen with pandemic potential. CHIKV infection in humans is transmitted by mosquitoes and induces common symptoms of high fever, arthralgia and myalgia. Because no specific antiviral drugs for treatment of CHIKV infection are available, drug development remains a central goal. The chikungunya virus protease from nsP2 (CHIKVP) has emerged as a key drug target due to its indispensable role in viral replication via cleavage of the viral polyprotein. To date, effective tools for screening for CHIKVP inhibitors that reflect the most critical polyprotein cleavage sites have been lacking, hampering drug-development efforts. We found that the recognition ability of CHIKVP is sensitive to the length of peptide substrates. In this study, we report a robust fluorogenic substrate comprising a 15-mer peptide derived from the nsP3/4 junction from the CHIKV polyprotein. This peptide is flanked by an ACC-Lys(dnp) donor-quencher pair. Our new substrate acc-CHIK

Indexed as

Chikungunya virusCysteine EndopeptidasesFluorescent DyesPeptidesChikungunya FeverHumansSubstrate SpecificityCysteine EndopeptidasesFluorescent DyesnsP2 proteinasePeptidesalphavirus proteaseamino carbamoyl coumarin FRET donorcysteine proteasedinitrophenyl quencherfluorescent substrate design principlesfluorogenic substrateFRET protease reporterpolyprotein junction mimicproteasevirus

Identifiers

PMID39981948
PMCPMC11843719

What OpenQuestion holds

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Registered trials

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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.