Evidence map›Paper›PMID 22767259›Full record

ArticleRNA biology2012

Architecture and regulation of negative-strand viral enzymatic machinery.

Philip J Kranzusch, Sean P J Whelan

Open access · bronzeAbstract read
In one paragraph

Article in RNA biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

13 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Common and unique features of viral RNA-dependent polymerases.Cellular and molecular life sciences : CMLS · 2014
    Review
  8. Article
  9. Current progress in antiviral strategies.Trends in pharmacological sciences · 2014
    Review
  10. Bunyamwera virus possesses a distinct nucleocapsid protein to facilitate genome encapsidation.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  11. The polymerase of negative-stranded RNA viruses.Current opinion in virology · 2013
    Review
  12. Review
  13. Review
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.

Philip J KranzuschDepartment of Microbiology & Immunobiology, Harvard Medical School, Boston, MA, USA.
Sean P J Whelan
Harvard University · US

Funding

Treatments for Nipah Virus InfectionU54AI057159 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI KASPER, DENNIS L. · 2003 to 2013
$113.7M
RNA Processing in Non-Segmented Minus-Strand RNA VirusesR37AI059371 · NIAID · WASHINGTON UNIVERSITY · PI WHELAN, SEAN PJ · 2015 to 2024
$5.4M
RNA Processing in Non-Segmented Minus-Strand RNA VirusesR01AI059371 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WHELAN, SEAN PJ · 2005 to 2015
$3.9M
NIAID NIH HHS AI057159NIAID NIH HHS AI059371NIAID NIH HHS R01 AI059371NIAID NIH HHS R37 AI059371NIAID NIH HHS U54 AI057159
6 · The paper itself

Abstract

Negative-strand (NS) RNA viruses initiate infection with a unique polymerase complex that mediates both mRNA transcription and subsequent genomic RNA replication. For nearly all NS RNA viruses, distinct enzymatic domains catalyzing RNA polymerization and multiple steps of 5' mRNA cap formation are contained within a single large polymerase protein (L). While NS RNA viruses include a variety of emerging human and agricultural pathogens, the enzymatic machinery driving viral replication and gene expression remains poorly understood. Recent insights with Machupo virus and vesicular stomatitis virus have provided the first structural information of viral L proteins, and revealed how the various enzymatic domains are arranged into a conserved architecture shared by both segmented and nonsegmented NS RNA viruses. In vitro systems reconstituting RNA synthesis from purified components provide new tools to understand the viral replicative machinery, and demonstrate the arenavirus matrix protein regulates RNA synthesis by locking a polymerase-template complex. Inhibition of gene expression by the viral matrix protein is a distinctive feature also shared with influenza A virus and nonsegmented NS RNA viruses, possibly illuminating a conserved mechanism for coordination of viral transcription and polymerase packaging.

Indexed as

AnimalsHumansProtein Structure, TertiaryRNA-Dependent RNA PolymeraseRNA, ViralRNA VirusesViral ProteinsVirus AssemblyVirus ReplicationRNA-Dependent RNA PolymeraseRNA, ViralViral Proteins

Identifiers

PMID22767259
PMCPMC3495737
OpenAlexW1975813005

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.