Evidence map›Paper›PMID 23283942›Full record

ArticleJournal of virology2013

Structure of a VP1-VP3 complex suggests how birnaviruses package the VP1 polymerase.

Mohammad W Bahar, L Peter Sarin, Stephen C Graham, Jances Pang, Dennis H Bamford, David I Stuart, Jonathan M Grimes

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

10 citing papers in PubMed, 25 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 5 institutions in 2 countries.

Mohammad W BaharWellcome Trust Centre for Human Genetics, University of Oxford, Oxford, UK.
L Peter Sarin
Stephen C Graham
Jances Pang
Dennis H Bamford
David I Stuart
Jonathan M Grimes
Diamond Light Source · GBUniversity of Helsinki · FICentre for Human Genetics · GBUniversity of Cambridge · GBUniversity of Oxford · GB

Funding

Medical Research Council G1000099Medical Research Council G1100525Wellcome Trust 075491/Z/04Wellcome Trust 079895Wellcome Trust 090532
6 · The paper itself

Abstract

Infectious pancreatic necrosis virus (IPNV), a member of the family Birnaviridae, infects young salmon, with a severe impact on the commercial sea farming industry. Of the five mature proteins encoded by the IPNV genome, the multifunctional VP3 has an essential role in morphogenesis; interacting with the capsid protein VP2, the viral double-stranded RNA (dsRNA) genome and the RNA-dependent RNA polymerase VP1. Here we investigate one of these VP3 functions and present the crystal structure of the C-terminal 12 residues of VP3 bound to the VP1 polymerase. This interaction, visualized for the first time, reveals the precise molecular determinants used by VP3 to bind the polymerase. Competition binding studies confirm that this region of VP3 is necessary and sufficient for VP1 binding, while biochemical experiments show that VP3 attachment has no effect on polymerase activity. These results indicate how VP3 recruits the polymerase into birnavirus capsids during morphogenesis.

Indexed as

Crystallography, X-RayInfectious pancreatic necrosis virusProtein BindingProtein ConformationRNA-Dependent RNA PolymeraseViral Structural ProteinsRNA-Dependent RNA PolymeraseViral Structural Proteins

Identifiers

PMID23283942
PMCPMC3592137
OpenAlexW2097643677

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.