Evidence map›Paper›PMID 25477390›Full record

ArticleNucleic acids research2015

A novel RNA molecular signature for activation of 2'-5' oligoadenylate synthetase-1.

Virginia K Vachon, Brenda M Calderon, Graeme L Conn

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.5field-weighted citation impact, top 34% 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

18 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
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  4. Article
  5. Review
  6. Review
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  8. Article
  9. Role of helical structure and dynamics in oligoadenylate synthetase 1 (OAS1) mismatch tolerance and activation by short dsRNAs.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. HeterozygousScience immunology · 2021
    Observational
  11. Review
  12. Article
  13. Review
  14. Recent Developments in mRNA-Based Protein Supplementation Therapy to Target Lung Diseases.Molecular therapy : the journal of the American Society of Gene Therapy · 2019
    Review
  15. Article
  16. Article
  17. Article
  18. 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

3 authors at 1 institution in 1 country.

Virginia K VachonDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA Microbiology and Molecular Genetics (MMG) Program, Graduate Division of Biological and Biomedical Sciences, Emory University School of Medicine, Atlanta, GA 30322, USA.
Brenda M CalderonDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA Biochemistry, Cell and Developmental Biology (BCDB) Program, Graduate Division of Biological and Biomedical Sciences, Emory University School of Medicine, Atlanta, GA 30322, USA.
Graeme L ConnDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA gconn@emory.edu.ORCID http://orcid.org/0000-0002-2419-380X
Emory University · US

Funding

Training Program in Biochemistry, Cell and Molecular BiologyT32GM008367 · NIGMS · EMORY UNIVERSITY · PI BOISE, LAWRENCE H., CORBETT, ANITA H. · 1990 to 2019
$5.6M
Structural studies of PKR regulation by viral non-coding RNAR21AI097803 · NIAID · EMORY UNIVERSITY · PI CONN, GRAEME L · 2012 to 2013
$391k
NIAID NIH HHS R21-AI097803NIGMS NIH HHS T32 GM008367NIGMS NIH HHS T32-GM008367
6 · The paper itself

Abstract

Human 2'-5' oligoadenylate synthetase-1 (OAS1) is central in innate immune system detection of cytoplasmic double-stranded RNA (dsRNA) and promotion of host antiviral responses. However, the molecular signatures that promote OAS1 activation are currently poorly defined. We show that the 3'-end polyuridine sequence of viral and cellular RNA polymerase III non-coding transcripts is critical for their optimal activation of OAS1. Potentiation of OAS1 activity was also observed with a model dsRNA duplex containing an OAS1 activation consensus sequence. We determined that the effect is attributable to a single appended 3'-end residue, is dependent upon its single-stranded nature with strong preference for pyrimidine residues and is mediated by a highly conserved OAS1 residue adjacent to the dsRNA binding surface. These findings represent discovery of a novel signature for OAS1 activation, the 3'-single-stranded pyrimidine (3'-ssPy) motif, with potential functional implications for OAS1 activity in its antiviral and other anti-proliferative roles.

Indexed as

2',5'-Oligoadenylate SynthetaseEnzyme ActivationHumansMutagenesisNucleotide MotifsPyrimidinesRNA, Double-StrandedRNA, UntranslatedRNA, Viral2',5'-Oligoadenylate SynthetaseOAS1 protein, humanPyrimidinesRNA, Double-StrandedRNA, UntranslatedRNA, Viral

Identifiers

PMID25477390
PMCPMC4288181
OpenAlexW2076787708

What OpenQuestion holds

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LicenceCC BY
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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.