Evidence map›Paper›PMID 15994762›Full record

ArticleJournal of virology2005

Stimulation of hepatitis C virus (HCV) nonstructural protein 3 (NS3) helicase activity by the NS3 protease domain and by HCV RNA-dependent RNA polymerase.

Chen Zhang, Zhaohui Cai, Young-Chan Kim, Ranjith Kumar, Fenghua Yuan, Pei-Yong Shi, Cheng Kao, Guangxiang Luo

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

38 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
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  15. Article
  16. The intraviral protein interaction network of hepatitis C virus.Molecular & cellular proteomics : MCP · 2014
    Article
  17. Article
  18. Review
  19. Hepatitis C virus RNA replication.Current topics in microbiology and immunology · 2013
    Review
  20. 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 1 country.

Chen ZhangDepartment of Microbiology, Immunology and Molecular Genetics, University of Kentucky College of Medicine, 800 Rose Street, Lexington, KY 40536, USA.
Zhaohui Cai
Young-Chan Kim
Ranjith Kumar
Fenghua Yuan
Pei-Yong Shi
Cheng Kao
Guangxiang Luo
University of Kentucky · USTexas A&M University · USNew York State Department of Health · US

Funding

Cis-acting RNA elements in hepatitis C virus replicationR01AI051592 · NIAID · UNIVERSITY OF KENTUCKY · PI LUO, GUANGXIANG GEORGE · 2003 to 2007
$1.3M
Molecular Dissection of Hepatitis C Virus ReplicaseR01CA093712 · NCI · UNIVERSITY OF KENTUCKY · PI LUO, GUANGXIANG GEORGE · 2002 to 2006
$1.3M
NCI NIH HHS CA093712NCI NIH HHS R01 CA093712NIAID NIH HHS R01 AI051592
6 · The paper itself

Abstract

Hepatitis C virus (HCV) nonstructural protein 3 (NS3) possesses multiple enzyme activities. The N-terminal one-third of NS3 primarily functions as a serine protease, while the remaining two-thirds of NS3 serve as a helicase and nucleoside triphosphatase. Whether the multiple enzyme activities of NS3 are functionally interdependent and/or modulated by other viral NS proteins remains unclear. We performed biochemical studies to examine the functional interdependence of the NS3 protease and helicase domains and the modulation of NS3 helicase by NS5B, an RNA-dependent RNA polymerase (RdRp). We found that the NS3 protease domain of the full-length NS3 (NS3FL) enhances the NS3 helicase activity. Additionally, HCV RdRp stimulates the NS3FL helicase activity by more than sevenfold. However, the helicase activity of the NS3 helicase domain was unaffected by HCV RdRp. Glutathione S-transferase pull-down as well as fluorescence anisotropy results revealed that the NS3 protease domain is required for specific NS3 and NS5B interaction. These findings suggest that HCV RdRp regulates the functions of NS3 during HCV replication. In contrast, NS3FL does not increase NS5B RdRp activity in vitro, which is contrary to a previously published report that the HCV NS3 enhances NS5B RdRp activity.

Indexed as

DEAD-box RNA HelicasesNucleoside-TriphosphataseRecombinant ProteinsRNA-Dependent RNA PolymeraseRNA HelicasesRNA, ViralSerine EndopeptidasesSpectrometry, FluorescenceViral Nonstructural ProteinsViral ProteasesDEAD-box RNA HelicasesNS3 protein, hepatitis C virusNS-5 protein, hepatitis C virusNucleoside-TriphosphataseRecombinant ProteinsRNA-Dependent RNA PolymeraseRNA HelicasesRNA, ViralSerine EndopeptidasesViral Nonstructural ProteinsViral Proteases

Identifiers

PMID15994762
PMCPMC1168731
OpenAlexW2109191027

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.