Evidence map›Paper›PMID 20943890›Full record

ArticleThe Journal of general virology2011

Amino acid changes within the Bunyamwera virus nucleocapsid protein differentially affect the mRNA transcription and RNA replication activities of assembled ribonucleoprotein templates.

Cheryl T Walter, Diana F Costa Bento, Ana Guerrero Alonso, John N Barr

Open access · hybridAbstract read
In one paragraph

Article in The Journal of general virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

25 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
  2. Article
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  7. Emerging Tick-BorneMicroorganisms · 2023
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  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Modulation of Potassium Channels Inhibits Bunyavirus Infection.The Journal of biological chemistry · 2016
    Article
  18. Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Cheryl T WalterInstitute for Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK.
Diana F Costa Bento
Ana Guerrero Alonso
John N Barr
University of Leeds · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

The genome of Bunyamwera virus (BUNV) comprises three RNA segments that are encapsidated by the virus-encoded nucleocapsid (N) protein to form ribonucleoprotein (RNP) complexes. These RNPs are the functional templates for RNA synthesis by the virus-encoded RNA-dependent RNA polymerase (RdRp). We investigated the roles of conserved positively charged N-protein amino acids in RNA binding, in oligomerization to form model RNPs and in generating RNP templates active for both RNA replication and mRNA transcription. We identified several residues that performed important roles in RNA binding, and furthermore showed that a single amino acid change can differentially affect the ability of the resulting RNP templates to regulate the transcription and replication activities of the RdRp. These results indicate that the BUNV N protein possesses functions outside of its primary role of RNA encapsidation.

Indexed as

Transcription, GeneticVirus ReplicationAmino Acid SubstitutionBunyamwera virusHumansNucleocapsid ProteinsProtein MultimerizationRibonucleoproteinsRNA-Dependent RNA PolymeraseRNA, MessengerN protein, Bunyamwera bunyavirusNucleocapsid ProteinsRibonucleoproteinsRNA-Dependent RNA PolymeraseRNA, Messenger

Identifiers

PMID20943890
PMCPMC3052533
OpenAlexW2164028270

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.