Evidence map›Paper›PMID 35891424›Full record

ArticleViruses2022

Dynamic Interactions of Post Cleaved NS2B Cofactor and NS3 Protease Identified by Integrative Structural Approaches.

Jun-Ping Quek, Zheng Ser, Bing Liang Alvin Chew, Xin Li, Lili Wang, Radoslaw M Sobota, Dahai Luo, Wint Wint Phoo

Open access · goldAbstract read
In one paragraph

Article in Viruses, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

11 citing papers in PubMed, 19 citations in OpenAlex.

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  11. Protein Abundance of Drug Transporters in Human Hepatitis C Livers.International journal of molecular sciences · 2022
    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 3 institutions in 2 countries.

Jun-Ping QuekLee Kong Chian School of Medicine, Nanyang Technological University, EMB 03-07, 59 Nanyang Drive, Singapore 636921, Singapore.ORCID 0000-0002-3827-8580
Zheng SerFunctional Proteomics Laboratory, SingMass National Laboratory, Institute of Molecular and Cell Biology, Agency for Science, Technology and Research, 61 Biopolis Drive, #07-03, Singapore 138673, Singapore.ORCID 0000-0003-4297-7525
Bing Liang Alvin ChewLee Kong Chian School of Medicine, Nanyang Technological University, EMB 03-07, 59 Nanyang Drive, Singapore 636921, Singapore.ORCID 0000-0002-2748-9366
Xin LiSingMass National Laboratory, Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Blk S2, #02, Singapore 117543, Singapore.
Lili WangSingMass National Laboratory, Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Blk S2, #02, Singapore 117543, Singapore.
Radoslaw M SobotaFunctional Proteomics Laboratory, SingMass National Laboratory, Institute of Molecular and Cell Biology, Agency for Science, Technology and Research, 61 Biopolis Drive, #07-03, Singapore 138673, Singapore.
Dahai LuoLee Kong Chian School of Medicine, Nanyang Technological University, EMB 03-07, 59 Nanyang Drive, Singapore 636921, Singapore.
Wint Wint PhooFunctional Proteomics Laboratory, SingMass National Laboratory, Institute of Molecular and Cell Biology, Agency for Science, Technology and Research, 61 Biopolis Drive, #07-03, Singapore 138673, Singapore.
Agency for Science, Technology and Research · SGNanyang Technological University · SGNational University of Singapore · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Diseases caused by flaviviruses such as dengue virus (DENV) and West Nile Virus (WNV), are a serious threat to public health. The flavivirus single-stranded RNA genome is translated into a polyprotein which is cleaved into three structural proteins and seven non-structural proteins by the viral and cellular proteases. Non-structural (NS) protein 3 is a multifunctional protein that has N-terminal protease and C-terminal helicase domains. The NS3 protease requires co-factor NS2B for enzymatic activity and folding. Due to its essential role in viral replication, NS2B-NS3 protease is an attractive target for antiviral drugs. Despite the availability of crystal structures, dynamic interactions of the N- and C-termini of NS2B co-factor have been elusive due to their flexible fold. In this study, we employ integrative structural approaches combined with biochemical assays to elucidate the dynamic interactions of the flexible DENV4 NS2B and NS3 N- and C-termini. We captured the crystal structure of self-cleaved DENV4 NS2B

Indexed as

FlavivirusZika VirusZika Virus InfectionCatalytic DomainHumansPeptide HydrolasesRNA HelicasesSerine EndopeptidasesViral Nonstructural ProteinsPeptide HydrolasesRNA HelicasesSerine EndopeptidasesViral Nonstructural Proteinscross-linking mass spectrometrydengue feverdengue virusDENVNS2B-NS3 proteaseviral proteaseX-ray crystallography

Identifiers

PMID35891424
PMCPMC9323329
OpenAlexW4283747628

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.