Evidence map›Paper›PMID 25794939›Full record

ReviewCytokine2015

LGP2 synergy with MDA5 in RLR-mediated RNA recognition and antiviral signaling.

Annie M Bruns, Curt M Horvath

Abstract readReview
In one paragraph

Review in Cytokine, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

68 citing papers in PubMed, 114 citations in OpenAlex.

  1. Article
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  3. Article
  4. Review
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  9. Article
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  11. Review
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  13. IFN-Induced PARPs-Sensors of Foreign Nucleic Acids?Pathogens (Basel, Switzerland) · 2023
    Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. Review
  20. Article

8 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

2 authors at 1 institution in 1 country.

Annie M BrunsDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA. Electronic address: annie0311@u.northwestern.edu.
Curt M HorvathDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA.
Northwestern University · US

Funding

Tumor Environment and Metastasis (TEAM) Research ProgramP30CA060553 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Daniela E Matei · 1993 to 2026
$153.9M
CELLULAR &MOLECULAR BASIS OF DISEASE TRAINING PROGRAMT32GM008061 · NIGMS · NORTHWESTERN UNIVERSITY · PI CARTHEW, RICHARD W. · 1985 to 2022
$17.1M
Molecular Basis-Paramyxovirus-induced STAT DegradationR01AI050707 · NIAID · NORTHWESTERN UNIVERSITY · PI HORVATH, CURT M · 2002 to 2012
$3.3M
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 P30 CA060553NIAID NIH HHS AI073919NIAID NIH HHS AI50707NIAID NIH HHS R01 AI050707NIAID NIH HHS R01 AI073919NIGMS NIH HHS T32 GM008061NIGMS NIH HHS T32GM008061
6 · The paper itself

Abstract

Mammalian cells have the ability to recognize virus infection and mount a powerful antiviral response. Pattern recognition receptor proteins detect molecular signatures of virus infection and activate antiviral signaling. The RIG-I-like receptor (RLR) proteins are expressed in the cytoplasm of nearly all cells and specifically recognize virus-derived RNA species as a molecular feature discriminating the pathogen from the host. The RLR family is composed of three homologous proteins, RIG-I, MDA5, and LGP2. All RLRs have the ability to detect virus-derived dsRNA and hydrolyze ATP, but display individual differences in enzymatic activity, intrinsic ability to recognize RNA, and mechanisms of activation. Emerging evidence suggests that MDA5 and RIG-I utilize distinct mechanisms to form oligomeric complexes along dsRNA. Aligning of their signaling domains creates a platform capable of propagating and amplifying antiviral signaling responses. LGP2 with intact ATP hydrolysis is critical for the MDA5-mediated antiviral response, but LGP2 lacks the domains essential for activation of antiviral signaling, leaving the role of LGP2 in antiviral signaling unclear. Recent studies revealed a mechanistic basis of synergy between LGP2 and MDA5 leading to enhanced antiviral signaling. This review briefly summarizes the RLR system, and focuses on the relationship between LGP2 and MDA5, describing in detail how these two proteins work together to detect foreign RNA and generate a fully functional antiviral response.

Indexed as

AnimalsDEAD Box Protein 58DEAD-box RNA HelicasesHumansInterferon-Induced Helicase, IFIH1Receptors, ImmunologicRNA, Double-StrandedRNA HelicasesRNA, ViralSignal TransductionDEAD Box Protein 58DEAD-box RNA HelicasesDHX58 protein, humanIFIH1 protein, humanInterferon-Induced Helicase, IFIH1Receptors, ImmunologicRIGI protein, humanRNA, Double-StrandedRNA HelicasesRNA, ViralAntiviral immunityLGP2MDA5RIG-I-like receptors

Identifiers

PMID25794939
PMCPMC4475439
OpenAlexW1993063850

What OpenQuestion holds

Textmetadata
LicenceTDM
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.