Evidence map›Paper›PMID 23184951›Full record

ArticleThe Journal of biological chemistry2013

ATP hydrolysis enhances RNA recognition and antiviral signal transduction by the innate immune sensor, laboratory of genetics and physiology 2 (LGP2).

Annie M Bruns, Darja Pollpeter, Nastaran Hadizadeh, Sua Myong, John F Marko, Curt M Horvath

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

58 citing papers in PubMed, 90 citations in OpenAlex.

  1. Article
  2. Immune mechanism ofFrontiers in immunology · 2025
    Article
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  8. Article
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  13. Dysregulated Immunity and Immunotherapy after Sepsis.Journal of clinical medicine · 2021
    Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Spatiotemporal dynamics of innate immune signaling via RIG-I-like receptors.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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

6 authors at 2 institutions in 1 country.

Annie M BrunsDepartment of Molecular Biosciences, Physics and Astronomy, Northwestern University, Evanston,Illinois 60208, USA.
Darja Pollpeter
Nastaran Hadizadeh
Sua Myong
John F Marko
Curt M Horvath
Northwestern University · USUniversity of Illinois Urbana-Champaign · US

Funding

CELLULAR &MOLECULAR BASIS OF DISEASE TRAINING PROGRAMT32GM008061 · NIGMS · NORTHWESTERN UNIVERSITY · PI CARTHEW, RICHARD W. · 1985 to 2022
$17.1M
TRANS-NETWORK PROJECTSU54CA143869 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI WIDOM, JONATHAN · 2009 to 2013
$12.8M
New Paradigms in Gene Regulation During Influenza Virus InfectionsU01AI082984 · NIAID · NORTHWESTERN UNIVERSITY · PI HORVATH, CURT M · 2009 to 2013
$3.6M
Helicase Regulation of dsRNA Signaling and Innate Antiviral Immune ResponsesR01AI073919 · NIAID · NORTHWESTERN UNIVERSITY · PI HORVATH, CURT M · 2008 to 2012
$1.8M
NCI NIH HHS 1U54CA143869-01NCI NIH HHS U54 CA143869NIAID NIH HHS R01 AI073919NIAID NIH HHS R01AI073919NIAID NIH HHS U01 AI082984NIAID NIH HHS U01AI082984NIGMS NIH HHS T32 GM008061NIGMS NIH HHS T32GM008061
6 · The paper itself

Abstract

Laboratory of genetics and physiology 2 (LGP2) is a member of the RIG-I-like receptor family of cytoplasmic pattern recognition receptors that detect molecular signatures of virus infection and initiate antiviral signal transduction cascades. The ATP hydrolysis activity of LGP2 is essential for antiviral signaling, but it has been unclear how the enzymatic properties of LGP2 regulate its biological response. Quantitative analysis of the dsRNA binding and enzymatic activities of LGP2 revealed high dsRNA-independent ATP hydrolysis activity. Biochemical assays and single-molecule analysis of LGP2 and mutant variants that dissociate basal from dsRNA-stimulated ATP hydrolysis demonstrate that LGP2 utilizes basal ATP hydrolysis to enhance and diversify its RNA recognition capacity, enabling the protein to associate with intrinsically poor substrates. This property is required for LGP2 to synergize with another RIG-I-like receptor, MDA5, to potentiate IFNβ transcription in vivo during infection with encephalomyocarditis virus or transfection with poly(I:C). These results demonstrate previously unrecognized properties of LGP2 ATP hydrolysis and RNA interaction and provide a mechanistic basis for a positive regulatory role for LGP2 in antiviral signaling.

Indexed as

Immunity, InnateSignal TransductionAdenosine TriphosphateAntiviral AgentsBase SequenceHEK293 CellsHumansHydrolysisMutagenesis, Site-DirectedRNARNA HelicasesAdenosine TriphosphateAntiviral AgentsDHX58 protein, humanRNARNA Helicases

Identifiers

PMID23184951
PMCPMC3543043
OpenAlexW2093755635

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.