Evidence map›Paper›PMID 22355520›Full record

ArticleScientific reports2011

Interplay between NS3 protease and human La protein regulates translation-replication switch of Hepatitis C virus.

Upasana Ray, Saumitra Das

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
31.1field-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

16 citing papers in PubMed, 893 citations in OpenAlex.

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  15. Inhibition of the interaction between NS3 protease and HCV IRES with a small peptide: a novel therapeutic strategy.Molecular therapy : the journal of the American Society of Gene Therapy · 2013
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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

2 authors at 1 institution in 1 country.

Upasana RayDepartment of Microbiology and Cell Biology, Indian Institute of Science , Bangalore-560012, India.
Saumitra Das
Indian Institute of Science Bangalore · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

HCV NS3 protein plays a central role in viral polyprotein processing and RNA replication. We demonstrate that the NS3 protease (NS3(pro)) domain alone can specifically bind to HCV-IRES RNA, predominantly in the SLIV region. The cleavage activity of the NS3 protease domain is reduced upon HCV-RNA binding. More importantly, NS3(pro) binding to the SLIV hinders the interaction of La protein, a cellular IRES-trans acting factor required for HCV IRES-mediated translation, resulting in inhibition of HCV-IRES activity. Although overexpression of both NS3(pro) as well as the full length NS3 protein decreased the level of HCV IRES mediated translation, replication of HCV replicon RNA was enhanced significantly. These observations suggest that the NS3(pro) binding to HCV IRES reduces translation in favor of RNA replication. The competition between the host factor (La) and the viral protein (NS3) for binding to HCV IRES might regulate the molecular switch from translation to replication of HCV.

Indexed as

DEAD-box RNA HelicasesGene Expression Regulation, ViralHepacivirusHumansNucleoside-TriphosphatasePhosphoproteinsProtein BindingProtein BiosynthesisSerine EndopeptidasesViral Nonstructural ProteinsViral ProteasesVirus ReplicationDEAD-box RNA HelicasesLa protein, humanNS3 protein, hepatitis C virusNucleoside-TriphosphatasePhosphoproteinsSerine EndopeptidasesViral Nonstructural ProteinsViral Proteases

Identifiers

PMID22355520
PMCPMC3210691
OpenAlexW2078167976

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.