Evidence map›Paper›PMID 23874742›Full record

ArticlePloS one2013

Hepatitis C virus non-structural protein 3 interacts with cytosolic 5'(3')-deoxyribonucleotidase and partially inhibits its activity.

Chiu-Ping Fang, Zhi-Cheng Li, Chee-Hing Yang, Ju-Chien Cheng, Yung-Ju Yeh, Tsai-Hsia Sun, Hui-Chun Li, Yue-Li Juang, Shih-Yen Lo

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. 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
0.3field-weighted citation impact, top 39% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Studying coronavirus-host protein interactions.Methods in molecular biology (Clifton, N.J.) · 2015
    Article
  2. 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

9 authors at 2 institutions in 1 country.

Chiu-Ping FangDepartment of Laboratory Medicine and Biotechnology, Tzu Chi University, Hualien, Taiwan.
Zhi-Cheng Li
Chee-Hing Yang
Ju-Chien Cheng
Yung-Ju Yeh
Tsai-Hsia Sun
Hui-Chun Li
Yue-Li Juang
Shih-Yen Lo
Tzu Chi University · TWChina Medical University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Infection with hepatitis C virus (HCV) is etiologically involved in liver cirrhosis, hepatocellular carcinoma and B-cell lymphomas. It has been demonstrated previously that HCV non-structural protein 3 (NS3) is involved in cell transformation. In this study, a yeast two-hybrid screening experiment was conducted to identify cellular proteins interacting with HCV NS3 protein. Cytosolic 5'(3')-deoxyribonucleotidase (cdN, dNT-1) was found to interact with HCV NS3 protein. Binding domains of HCV NS3 and cellular cdN proteins were also determined using the yeast two-hybrid system. Interactions between HCV NS3 and cdN proteins were further demonstrated by co-immunoprecipitation and confocal analysis in cultured cells. The cellular cdN activity was partially repressed by NS3 protein in both the transiently-transfected and the stably-transfected systems. Furthermore, HCV partially repressed the cdN activity while had no effect on its protein expression in the systems of HCV sub-genomic replicons and infectious HCV virions. Deoxyribonucleotidases are present in most mammalian cells and involve in the regulation of intracellular deoxyribonucleotides pools by substrate cycles. Control of DNA precursor concentration is essential for the maintenance of genetic stability. Reduction of cdN activity would result in the imbalance of DNA precursor concentrations. Thus, our results suggested that HCV partially reduced the cdN activity via its NS3 protein and this may in turn cause diseases.

Indexed as

5'-NucleotidaseCell LineCytosolDEAD-box RNA HelicasesEnzyme ActivationHepacivirusHumansNucleoside-TriphosphataseProtein BindingSerine EndopeptidasesTwo-Hybrid System TechniquesViral Nonstructural ProteinsViral ProteasesVirus Replication5'(3')-nucleotidase5'-NucleotidaseDEAD-box RNA HelicasesNS3 protein, hepatitis C virusNucleoside-TriphosphataseSerine EndopeptidasesViral Nonstructural ProteinsViral Proteases

Identifiers

PMID23874742
PMCPMC3706368
OpenAlexW2038533269

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.