Evidence map›Paper›PMID 24905202›Full record

ReviewJournal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research2014

Viral phosphodiesterases that antagonize double-stranded RNA signaling to RNase L by degrading 2-5A.

Robert H Silverman, Susan R Weiss

Open access · greenAbstract readReview
In one paragraph

Review in Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
3.9field-weighted citation impact, top 5% 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

54 citing papers in PubMed, 72 citations in OpenAlex.

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  19. Zika virus employs the host antiviral RNase L protein to support replication factory assembly.Proceedings of the National Academy of Sciences of the United States of America · 2021
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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

2 authors at 2 institutions in 1 country.

Robert H Silverman1 Department of Cancer Biology, Lerner Research Institute , Cleveland Clinic, Cleveland, Ohio.
Susan R Weiss
Cleveland Clinic Lerner College of Medicine · USUniversity of Pennsylvania · US

Funding

Control of Viral Pathogenesis by Regulation of 2-5A LevelsR01AI104887 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI SILVERMAN, ROBERT H., WEISS, SUSAN R · 2013 to 2023
$7.6M
REGULATION OF 2-5A-DEPENDENT RNASE LEVELS OF INTERFERONR01CA044059 · NCI · HENRY M. JACKSON FDN FOR THE ADV MIL/MED · PI SILVERMAN, ROBERT H. · 1986 to 2015
$6.1M
Murine coronavirus neurovirulence: role of type I interferon responseR01NS081008 · NINDS · UNIVERSITY OF PENNSYLVANIA · PI WEISS, SUSAN R · 2012 to 2016
$1.7M
NCI NIH HHS R01 CA44059NIAID NIH HHS R01 AI104887NINDS NIH HHS R01 NS081001NINDS NIH HHS R01 NS081008
6 · The paper itself

Abstract

The host interferon (IFN) antiviral response involves a myriad of diverse biochemical pathways that disrupt virus replication cycles at many different levels. As a result, viruses have acquired and evolved genes that antagonize the host antiviral proteins. IFNs inhibit viral infections in part through the 2',5'-oligoadenylate (2-5A) synthetase (OAS)/RNase L pathway. OAS proteins are pathogen recognition receptors that exist at different basal levels in different cell types and that are IFN inducible. Upon activation by the pathogen-associated molecular pattern viral double-stranded RNA, certain OAS proteins synthesize 2-5A from ATP. 2-5A binds to the antiviral enzyme RNase L causing its dimerization and activation. Recently, disparate RNA viruses, group 2a betacoronaviruses, and group A rotaviruses, have been shown to produce proteins with 2',5'-phosphodiesterase (PDE) activities that eliminate 2-5A thereby evading the antiviral activity of the OAS/RNase L pathway. These viral proteins are members of the eukaryotic-viral LigT-like group of 2H phosphoesterases, so named for the presence of 2 conserved catalytic histidine residues. Here, we will review the biochemistry, biology, and implications of viral and cellular 2',5'-PDEs that degrade 2-5A. In addition, we discuss alternative viral and cellular strategies for limiting the activity of OAS/RNase L.

Indexed as

Signal Transduction2',5'-Oligoadenylate SynthetaseAnimalsEndoribonucleasesHumansPhosphoric Diester HydrolasesRNA, Double-StrandedViruses2-5A-dependent ribonuclease2',5'-Oligoadenylate SynthetaseEndoribonucleasesPhosphoric Diester HydrolasesRNA, Double-Stranded

Identifiers

PMID24905202
PMCPMC4046343
OpenAlexW2334973813

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.