Evidence map›Paper›PMID 25033909›Full record

ReviewNature reviews. Immunology2014

OAS proteins and cGAS: unifying concepts in sensing and responding to cytosolic nucleic acids.

Veit Hornung, Rune Hartmann, Andrea Ablasser, Karl-Peter Hopfner

Open access · bronzeAbstract readReview
In one paragraph

Review in Nature reviews. Immunology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 208 papers.

0numbers the graph read from it
0cells of the map it votes in
208citing papers in PubMed
10.7field-weighted citation impact, top 1% 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

208 citing papers in PubMed, 330 citations in OpenAlex.

  1. Trial
  2. Trial
  3. Article
  4. Review
  5. Article
  6. iScience · 2026
    Article
  7. Article
  8. Article
  9. Article
  10. Extracellular cGAMP in health and disease.Molecular biomedicine · 2026
    Review
  11. Article
  12. Article
  13. Review
  14. Overexpression ofJournal of clinical medicine · 2026
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. iScience · 2025
    Article

148 more citing papers are in PubMed but not listed here.

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 2 institutions in 2 countries.

Veit HornungInstitute of Molecular Medicine, University Hospital, University of Bonn, Sigmund-Freud-Strasse 25, 53127 Bonn, Germany.
Rune HartmannCentre for Structural Biology, Department of Molecular Biology, Aarhus University, Gustav Wieds Vej 10c, 8000 Aarhus C, Denmark.
Andrea AblasserInstitute of Molecular Medicine, University Hospital, University of Bonn, Sigmund-Freud-Strasse 25, 53127 Bonn, Germany, and the Global Health Institute, École Polytechnique Fédérale de Lausanne, Station 15, CH-1015 Lausanne, Switzerland.
Karl-Peter HopfnerDepartment of Biochemistry and Gene Center, Ludwig-Maximilians-University, Feodor-Lynen-Strasse 25, D-81377 Munich, Germany.
École Polytechnique Fédérale de Lausanne · CHUniversity of Bonn · DE

Funding

TRIM mediated host antiviral responses during influenza virus infectionsU19AI083025 · NIAID · UNIVERSITY OF SOUTHERN CALIFORNIA · PI JUNG, JAE U · 2009 to 2013
$10.0M
NIAID NIH HHS U19 AI083025NIAID NIH HHS U19U19AI083025
6 · The paper itself

Abstract

Recent discoveries in the field of innate immunity have highlighted the existence of a family of nucleic acid-sensing proteins that have similar structural and functional properties. These include the well-known oligoadenylate synthase (OAS) family proteins and the recently identified OAS homologue cyclic GMP-AMP (cGAMP) synthase (cGAS). The OAS proteins and cGAS are template-independent nucleotidyltransferases that, once activated by double-stranded nucleic acids in the cytosol, produce unique classes of 2'-5'-linked second messenger molecules, which - through distinct mechanisms - have crucial antiviral functions. 2'-5'-linked oligoadenylates limit viral propagation through the activation of the enzyme RNase L, which degrades host and viral RNA, and 2'-5'-linked cGAMP activates downstream signalling pathways to induce de novo antiviral gene expression. In this Progress article, we describe the striking functional and structural similarities between OAS proteins and cGAS, and highlight their roles in antiviral immunity.

Indexed as

2',5'-Oligoadenylate SynthetaseAdenine NucleotidesCyclic Guanosine Monophosphate-Adenosine Monophosphate SynthaseCytosolDNAEndoribonucleasesHumansImmunity, InnateNucleotides, CyclicNucleotidyltransferasesOligoribonucleotidesRNARNA, ViralRNA VirusesSecond Messenger SystemsViruses2-5A-dependent ribonuclease2',5'-oligoadenylate2',5'-Oligoadenylate SynthetaseAdenine NucleotidescGAS protein, humancyclic guanosine monophosphate-adenosine monophosphateCyclic Guanosine Monophosphate-Adenosine Monophosphate SynthaseDNAEndoribonucleasesNucleotides, CyclicNucleotidyltransferasesOligoribonucleotidesRNARNA, Viral

Identifiers

PMID25033909
PMCPMC7097587
OpenAlexW2049898530

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.