Evidence map›Paper›PMID 25217590›Full record

ArticleNucleic acids research2014

The RIG-I ATPase core has evolved a functional requirement for allosteric stabilization by the Pincer domain.

David C Rawling, Andrew S Kohlway, Dahai Luo, Steve C Ding, Anna Marie Pyle

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

20 citing papers in PubMed, 27 citations in OpenAlex.

  1. Biochemical and structural basis of Dicer helicase function unveiled by resurrecting ancient proteins.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  18. OASes and STING: adaptive evolution in concert.Genome biology and evolution · 2015
    Article
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  20. 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

5 authors at 2 institutions in 1 country.

David C RawlingDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
Andrew S KohlwayDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
Dahai LuoDepartment of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520, USA Department of Chemistry, Yale University, New Haven, CT 06520, USA.
Steve C DingDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
Anna Marie PyleDepartment of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520, USA Howard Hughes Medical Institute, Chevy Chase, MD 20815, USA Department of Chemistry, Yale University, New Haven, CT 06520, USA anna.pyle@yale.edu.
Yale University · USHoward Hughes Medical Institute · US

Funding

Skill Development for Diverse Scientific Careers: A New Course Predoctoral Program in Cellular and Molecular BiologyT32GM007223 · NIGMS · YALE UNIVERSITY · PI BASERGA, SUSAN J · 1985 to 2019
$31.0M
Howard Hughes Medical InstituteNIGMS NIH HHS T32 GM007223
6 · The paper itself

Abstract

Retinoic acid-inducible gene I (RIG-I) is a pattern recognition receptor expressed in metazoan cells that is responsible for eliciting the production of type I interferons and pro-inflammatory cytokines upon detection of intracellular, non-self RNA. Structural studies of RIG-I have identified a novel Pincer domain composed of two alpha helices that physically tethers the C-terminal domain to the SF2 helicase core. We find that the Pincer plays an important role in mediating the enzymatic and signaling activities of RIG-I. We identify a series of mutations that additively decouple the Pincer motif from the ATPase core and show that this decoupling results in impaired signaling. Through enzymological and biophysical analysis, we further show that the Pincer domain controls coupled enzymatic activity of the protein through allosteric control of the ATPase core. Further, we show that select regions of the HEL1 domain have evolved to potentiate interactions with the Pincer domain, resulting in an adapted ATPase cleft that is now responsive to adjacent domains that selectively bind viral RNA.

Indexed as

Adenosine TriphosphatasesAllosteric RegulationBiocatalysisDEAD Box Protein 58DEAD-box RNA HelicasesHEK293 CellsHumansInterferon-betaProtein BindingProtein StabilityProtein Structure, TertiaryReceptors, ImmunologicRNAAdenosine TriphosphatasesDEAD Box Protein 58DEAD-box RNA HelicasesInterferon-betaReceptors, ImmunologicRIGI protein, humanRNA

Identifiers

PMID25217590
PMCPMC4191399
OpenAlexW2127832771

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.