Evidence map›Paper›PMID 28345656›Full record

ArticleNature communications2017

Structure and function of the Zika virus full-length NS5 protein.

Baoyu Zhao, Guanghui Yi, Fenglei Du, Yin-Chih Chuang, Robert C Vaughan, Banumathi Sankaran, C Cheng Kao, Pingwei Li

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers.

0numbers the graph read from it
0cells of the map it votes in
110citing papers in PubMed
26.3field-weighted citation impact, top 1% 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

110 citing papers in PubMed, 215 citations in OpenAlex.

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  20. Envelope Protein-Targeting Zika Virus Entry Inhibitors.International journal of molecular sciences · 2024
    Review

50 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

Baoyu ZhaoDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843, USA.
Guanghui YiDepartment of Molecular and Cellular Biochemistry, Indiana University, Bloomington, Indiana 47405, USA.
Fenglei DuDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843, USA.
Yin-Chih ChuangDepartment of Molecular and Cellular Biochemistry, Indiana University, Bloomington, Indiana 47405, USA.
Robert C VaughanDepartment of Molecular and Cellular Biochemistry, Indiana University, Bloomington, Indiana 47405, USA.
Banumathi SankaranMolecular Biophysics and Integrated Bioimaging, Berkeley Center for Structural Biology, 1 Cyclotron Road, Lawrence Berkeley National Lab, Berkeley 94720, USA.
C Cheng KaoDepartment of Molecular and Cellular Biochemistry, Indiana University, Bloomington, Indiana 47405, USA.
Pingwei LiDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843, USA.
Indiana University Bloomington · USTexas A&M University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The recent outbreak of Zika virus (ZIKV) has infected over 1 million people in over 30 countries. ZIKV replicates its RNA genome using virally encoded replication proteins. Nonstructural protein 5 (NS5) contains a methyltransferase for RNA capping and a polymerase for viral RNA synthesis. Here we report the crystal structures of full-length NS5 and its polymerase domain at 3.0 Å resolution. The NS5 structure has striking similarities to the NS5 protein of the related Japanese encephalitis virus. The methyltransferase contains in-line pockets for substrate binding and the active site. Key residues in the polymerase are located in similar positions to those of the initiation complex for the hepatitis C virus polymerase. The polymerase conformation is affected by the methyltransferase, which enables a more efficiently elongation of RNA synthesis in vitro. Overall, our results will contribute to future studies on ZIKV infection and the development of inhibitors of ZIKV replication.

Indexed as

Crystallography, X-RayMethyltransferasesProtein ConformationRNA CapsRNA-Dependent RNA PolymeraseSubstrate SpecificityViral Nonstructural ProteinsVirus ReplicationZika VirusMethyltransferasesNS5 protein, flavivirusRNA CapsRNA-Dependent RNA PolymeraseViral Nonstructural Proteins

Identifiers

PMID28345656
PMCPMC5378950
OpenAlexW2599913756

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.