Evidence map›Paper›PMID 38572740›Full record

ArticleThe Journal of general virology2024

Translational arrest and mRNA decay are independent activities of alphaherpesvirus virion host shutoff proteins.

Lucy Eke, Alistair Tweedie, Sophie Cutts, Emma L Wise, Gillian Elliott

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

Article in The Journal of general virology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Review
  2. 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

5 authors at 1 institution in 1 country.

Lucy EkeSection of Virology, Department of Microbial Sciences, School of Biosciences, University of Surrey, Guildford, UK.
Alistair TweedieSection of Virology, Department of Microbial Sciences, School of Biosciences, University of Surrey, Guildford, UK.
Sophie CuttsSection of Virology, Department of Microbial Sciences, School of Biosciences, University of Surrey, Guildford, UK.
Emma L WiseSection of Virology, Department of Microbial Sciences, School of Biosciences, University of Surrey, Guildford, UK.
Gillian ElliottSection of Virology, Department of Microbial Sciences, School of Biosciences, University of Surrey, Guildford, UK.
University of Surrey · GB

Funding

Medical Research Council MR/T001038/1
6 · The paper itself

Abstract

The herpes simplex virus 1 (HSV1) virion host shutoff (vhs) protein is an endoribonuclease that regulates the translational environment of the infected cell, by inducing the degradation of host mRNA via cellular exonuclease activity. To further understand the relationship between translational shutoff and mRNA decay, we have used ectopic expression to compare HSV1 vhs (vhsH) to its homologues from four other alphaherpesviruses - varicella zoster virus (vhsV), bovine herpesvirus 1 (vhsB), equine herpesvirus 1 (vhsE) and Marek's disease virus (vhsM). Only vhsH, vhsB and vhsE induced degradation of a reporter luciferase mRNA, with poly(A)+

Indexed as

Herpesvirus 1, HumanViral ProteinsDNA HelicasesEndoribonucleasesPoly-ADP-Ribose Binding ProteinsRibonucleasesRNA HelicasesRNA, MessengerRNA Recognition Motif ProteinsRNA StabilityVirionDNA HelicasesEndoribonucleasesPoly-ADP-Ribose Binding ProteinsRibonucleasesRNA HelicasesRNA, MessengerRNA Recognition Motif ProteinsViral ProteinsalphaherpesvirusesBHV1EHV1endoribonucleaseG3BP1HSV1MDVPABPC1poly(A)+ FISHstress granulesvhsVZV

Identifiers

PMID38572740
PMCPMC11083458
OpenAlexW4393948961

What Socratic 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 Socratic graph.