Evidence map›Paper›PMID 42337180›Full record

ArticleArchives of virology2026

Structural insights into DENV-2 NS2B-NS3 protease and inhibition by glutathione-coated gold nanocluster.

Haojia Zhu, Wenchao Niu, Yuancong Xu, Zhaoyang Li, Dongfang Xia, Sixu Chen, Botao Zhang, Junshuai Wang, Huai Yang, Xueyun Gao and 4 more

Abstract read
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In one paragraph

Article in Archives of virology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

14 authors.

Haojia Zhu *College of Chemistry and Life Science, Beijing University of Technology, Beijing, 100124, China.
Wenchao Niu *Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing, 100049, China.
Yuancong XuCollege of Chemistry and Life Science, Beijing University of Technology, Beijing, 100124, China.
Zhaoyang LiCollege of Chemistry and Life Science, Beijing University of Technology, Beijing, 100124, China.
Dongfang XiaCollege of Chemistry and Life Science, Beijing University of Technology, Beijing, 100124, China.
Sixu ChenCollege of Chemistry and Life Science, Beijing University of Technology, Beijing, 100124, China.
Botao ZhangCollege of Chemistry and Life Science, Beijing University of Technology, Beijing, 100124, China.
Junshuai WangCollege of Chemistry and Life Science, Beijing University of Technology, Beijing, 100124, China.
Huai YangCollege of Chemistry and Life Science, Beijing University of Technology, Beijing, 100124, China.
Xueyun GaoCollege of Chemistry and Life Science, Beijing University of Technology, Beijing, 100124, China.
Yuanyuan ChenThe Research Platform for Protein Sciences, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing, 100101, China.
Yong GongBeijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing, 100049, China. yonggong@ihep.ac.cn.
Peng CaoCollege of Chemistry and Life Science, Beijing University of Technology, Beijing, 100124, China. pengcao@bjut.edu.cn.
Yubai ZhouCollege of Chemistry and Life Science, Beijing University of Technology, Beijing, 100124, China. zhouyubai@bjut.edu.cn.ORCID http://orcid.org/0000-0003-1066-7071

Funding

Beijing Municipal Commission of Education KZ202210005001
6 · The paper itself

Abstract

Dengue virus (DENV) continues to pose a significant global health threat, with increasing infection rates and limited treatment options. The viral NS2B-NS3 protease (NS2B-NS3pro), a highly conserved two-component enzyme essential for polyprotein processing and replication, is a key target for antiviral drug development. Here, we report the 2.25 Å-resolution crystal structure of DENV serotype 2 (DENV-2) NS2B-NS3pro, in which a PEG fragment is bound within a solvent-exposed pocket between β10, β11, β14 and β15 of NS3. This structure reveals a previously unrecognized solvent-exposed PEG-binding pocket, which may represent a putative ligand-binding surface for future validation and inhibitor-design studies. We also show that the glutathione-coated gold nanocluster (GSH-AuNC) directly inhibits DENV-2 NS2B-NS3pro. Bio-layer interferometry and fluorescence-based protease assays indicate that the nanocluster binds NS2B-NS3pro with a dissociation constant of 15.64 µM and inhibits its catalytic activity with an IC

Indexed as

Dengue VirusGlutathioneGoldMetal NanoparticlesViral Nonstructural ProteinsViral Protease InhibitorsDEAD-box RNA HelicasesDengueEscherichia coliMolecular Dynamics SimulationNucleoside-TriphosphataseProtein ConformationRecombinant Fusion ProteinsSerine EndopeptidasesViral ProteasesDEAD-box RNA HelicasesGlutathioneGoldnonstructural protein 2B, Dengue virusNS3 protein, flavivirusNucleoside-TriphosphataseRecombinant Fusion ProteinsSerine EndopeptidasesViral Nonstructural ProteinsViral Protease InhibitorsViral Proteases

Identifiers

PMID42337180

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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.