Evidence map›Paper›PMID 27770702›Full record

ArticleVirology2017

Modulation of HCV replication and translation by ErbB3 binding protein1 isoforms.

Priya Mishra, Updesh Dixit, Ashutosh K Pandey, Alok Upadhyay, Virendra N Pandey

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Virology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.2field-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

0 citing papers in PubMed, 9 citations in OpenAlex.

No citing paper in PubMed yet.

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

5 authors at 1 institution in 1 country.

Priya MishraDepartment of Microbiology, Biochemistry, and Molecular Genetics, Rutgers New Jersey Medical School, Rutgers, The State University of New Jersey, Newark, NJ 07103, USA.
Updesh DixitDepartment of Microbiology, Biochemistry, and Molecular Genetics, Rutgers New Jersey Medical School, Rutgers, The State University of New Jersey, Newark, NJ 07103, USA.
Ashutosh K PandeyDepartment of Microbiology, Biochemistry, and Molecular Genetics, Rutgers New Jersey Medical School, Rutgers, The State University of New Jersey, Newark, NJ 07103, USA.
Alok UpadhyayDepartment of Microbiology, Biochemistry, and Molecular Genetics, Rutgers New Jersey Medical School, Rutgers, The State University of New Jersey, Newark, NJ 07103, USA.
Virendra N PandeyDepartment of Microbiology, Biochemistry, and Molecular Genetics, Rutgers New Jersey Medical School, Rutgers, The State University of New Jersey, Newark, NJ 07103, USA. Electronic address: vnp22@njms.rutgers.edu.
Rutgers, The State University of New Jersey · US

Funding

Proteomics of HCV Replication ComplexR21AI073703 · NIAID · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI PANDEY, VIRENDRA NATH · 2009 to 2010
$429k
FUSE Binding Protein As a Cellular Effector of HCV ReplicationR21DK083560 · NIDDK · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI PANDEY, VIRENDRA NATH · 2010 to 2011
$427k
NIAID NIH HHS R21 AI073703NIDDK NIH HHS R21 DK083560
6 · The paper itself

Abstract

We recently identified a cell-factor, ErbB3 binding protein 1 (Ebp-1), which specifically interacts with the viral RNA genome and modulates HCV replication and translation. Ebp1 has two isoforms, p48, and p42, that result from differential splicing. We found that both isoforms interact with HCV proteins NS5A and NS5B, as well as cell-factor PKR. The p48 isoform, which localizes in the cytoplasm and nuclei, promoted HCV replication, whereas the shorter p42 isoform, which resides exclusively in the cytoplasm, strongly inhibited HCV replication. Transient expression of individual isoforms in Ebp1-knockdown MH14 cells confirmed that the p48 isoform promotes HCV replication, while the p42 isoform inhibits it. We found that Ebp1-p42 significantly enhanced autophosphorylation of PKR, while Ebp1-p48 isoform strongly inhibited it. We propose that modulation of autophosphorylation of PKR by p48 isoform is an important mechanism whereby the HCV virus escapes innate antiviral immune responses by circumventing p42-mediated inhibition of its replication.

Indexed as

Virus ReplicationCell Line, TumorDNA ReplicationeIF-2 KinaseHepacivirusHepatitis CHumansKeratin-20PhosphorylationProtein BiosynthesisProtein IsoformsEIF2AK2 protein, humaneIF-2 KinaseKeratin-20KRT20 protein, humanProtein IsoformsEbp1isoformsErbB3 binding protein1HCV replicationPKR activation

Identifiers

PMID27770702
PMCPMC5831692
OpenAlexW2535478722

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.