Evidence map›Paper›PMID 26371557›Full record

ArticleeLife2015

Establishing the role of ATP for the function of the RIG-I innate immune sensor.

David C Rawling, Megan E Fitzgerald, Anna Marie Pyle

Abstract read
In one paragraph

Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
–field-weighted citation impact
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

41 citing papers in PubMed.

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  15. Enzymatic Noncovalent Synthesis.Chemical reviews · 2020
    Review
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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

3 authors.

David C RawlingDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, United States.
Megan E FitzgeraldDepartment of Molecular, Cellular and Developmental Biology, Howard Hughes Medical Institute, Yale University, New Haven, United States.
Anna Marie PyleDepartment of Molecular, Cellular and Developmental Biology, Yale University, New Haven, United States.

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Retinoic acid-inducible gene I (RIG-I) initiates a rapid innate immune response upon detection and binding to viral ribonucleic acid (RNA). This signal activation occurs only when pathogenic RNA is identified, despite the ability of RIG-I to bind endogenous RNA while surveying the cytoplasm. Here we show that ATP binding and hydrolysis by RIG-I play a key role in the identification of viral targets and the activation of signaling. Using biochemical and cell-based assays together with mutagenesis, we show that ATP binding, and not hydrolysis, is required for RIG-I signaling on viral RNA. However, we show that ATP hydrolysis does provide an important function by recycling RIG-I and promoting its dissociation from non-pathogenic RNA. This activity provides a valuable proof-reading mechanism that enhances specificity and prevents an antiviral response upon encounter with host RNA molecules.

Indexed as

Immunity, InnateSignal TransductionAdenosine TriphosphateCell LineDEAD Box Protein 58DEAD-box RNA HelicasesHumansHydrolysisProtein BindingReceptors, ImmunologicRNA, ViralAdenosine TriphosphateDEAD Box Protein 58DEAD-box RNA HelicasesReceptors, ImmunologicRIGI protein, humanRNA, Viralantiviral signalingbiochemistryimmunologyinnate immunitynoneRIG-I like receptorRNA helicase

Identifiers

PMID26371557
PMCPMC4622095

What OpenQuestion holds

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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.