Evidence map›Paper›PMID 24965468›Full record

ArticleJournal of virology2014

The linker region of NS3 plays a critical role in the replication and infectivity of hepatitis C virus.

Andrew Kohlway, Nathan Pirakitikulr, Steve C Ding, Feng Yang, Dahai Luo, Brett D Lindenbach, Anna M Pyle

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

17 citing papers in PubMed, 21 citations in OpenAlex.

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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

7 authors at 1 institution in 1 country.

Andrew KohlwayDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut, USA.
Nathan PirakitikulrDepartment of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut, USA.
Steve C DingDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut, USA.
Feng YangDepartment of Microbial Pathogenesis, Yale University, New Haven, Connecticut, USA.
Dahai LuoDepartment of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut, USA.
Brett D LindenbachDepartment of Microbial Pathogenesis, Yale University, New Haven, Connecticut, USA.
Anna M PyleDepartment of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut, USA Department of Chemistry, Yale University, New Haven, Connecticut, USA Howard Hughes Medical Institute, Yale University, New Haven, Connecticut, USA anna.pyle@yale.edu.
Yale University · US

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007205 · NIGMS · YALE UNIVERSITY · PI KAZMIERCZAK, BARBARA I · 1985 to 2019
$42.9M
Yale University Clinical and Translational Science Award ProgramUL1TR000142 · NCATS · YALE UNIVERSITY · PI SHERWIN, ROBERT S · 2012 to 2015
$31.8M
Skill Development for Diverse Scientific Careers: A New Course Predoctoral Program in Cellular and Molecular BiologyT32GM007223 · NIGMS · YALE UNIVERSITY · PI BASERGA, SUSAN J · 1985 to 2019
$31.0M
Structure and function of the HCV replication complexR01AI089826 · NIAID · YALE UNIVERSITY · PI LINDENBACH, BRETT D., PYLE, ANNA MARIE · 2010 to 2014
$2.9M
Howard Hughes Medical InstituteNCATS NIH HHS UL1 TR000142NIAID NIH HHS R01 AI089826NIAID NIH HHS R01AI89826NIGMS NIH HHS T32 GM007205NIGMS NIH HHS T32 GM007223
6 · The paper itself

Abstract

Hepatitis C virus (HCV) NS3-4A is required for viral replication and assembly. We establish that virus assembly is sensitive to mutations in the linker region between the helicase and protease domains of NS3-4A. However, we find that the protease cleavage, RNA binding, and unwinding rates of NS3 are minimally affected in vitro. Thus, we conclude that the NS3 linker is critical for mediating protein-protein interactions and dynamic control rather than for modulating the enzymatic functions of NS3-4A.

Indexed as

Virus ReplicationAmino Acid MotifsAmino Acid SequenceCarrier ProteinsDEAD-box RNA HelicasesHepacivirusHepatitis CHumansIntracellular Signaling Peptides and ProteinsMolecular Sequence DataNucleoside-TriphosphataseProtein BindingSequence AlignmentSerine EndopeptidasesViral Nonstructural ProteinsViral ProteasesCarrier ProteinsDEAD-box RNA HelicasesIntracellular Signaling Peptides and ProteinsNS3 protein, hepatitis C virusNS4A cofactor peptide, Hepatitis C virusNucleoside-TriphosphataseSerine EndopeptidasesViral Nonstructural ProteinsViral Proteases

Identifiers

PMID24965468
PMCPMC4178846
OpenAlexW2169701242

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.