Evidence map›Paper›PMID 30569868›Full record

ReviewMedicinal chemistry (Shariqah (United Arab Emirates))2019

Structural Variability in the RLR-MAVS Pathway and Sensitive Detection of Viral RNAs.

Qiu-Xing Jiang

Abstract readReview
In one paragraph

Review in Medicinal chemistry (Shariqah (United Arab Emirates)), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. SARS-CoV-2-Specific Immune Response and the Pathogenesis of COVID-19.International journal of molecular sciences · 2022
    Review
  9. Single-Run Catalysis and Kinetic Control of Human Telomerase Holoenzyme.Advances in experimental medicine and biology · 2022
    Review
  10. Review
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

1 author.

Qiu-Xing JiangDepartment of Microbiology and Cell Science, University of Florida, Gainesville, FL 32611, United States.

Funding

The Southeastern Consortium for Microscopy of MacroMolecular MachinesU24GM116788 · NIGMS · FLORIDA STATE UNIVERSITY · PI AGBANDJE-MCKENNA, MAVIS, BULLITT, ESTHER · 2016 to 2020
$4.6M
Molecular Mechanisms of the RNAi/MicroRNA PathwaysR01GM111367 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI JIANG, QIU-XING, LIU, QINGHUA · 2015 to 2018
$1.4M
Structural study of a Kv channel in different conformations in membranesR01GM093271 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI JIANG, QIU-XING · 2010 to 2013
$1.2M
Obtaining 3D structures with subnanogram macromoleculesR01GM088745 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI JIANG, QIU-XING · 2009 to 2012
$1.0M
An 8K camera for the cryoEM at UT Southwestern Medical CenterS10RR027972 · NCRR · UT SOUTHWESTERN MEDICAL CENTER · PI JIANG, QIU-XING · 2011 to 2011
$600k
Chemically engineered bilayers for cryoEM imaging of membrane proteins in continuous membranesR21GM131231 · NIGMS · UNIVERSITY OF FLORIDA · PI PAZ, AVIV · 2019 to 2020
$476k
NCRR NIH HHS S10 RR027972NIGMS NIH HHS R01 GM088745NIGMS NIH HHS R01 GM093271NIGMS NIH HHS R01 GM111367NIGMS NIH HHS R21 GM131231NIGMS NIH HHS U24 GM116788
6 · The paper itself

Abstract

Cells need high-sensitivity detection of non-self molecules in order to fight against pathogens. These cellular sensors are thus of significant importance to medicinal purposes, especially for treating novel emerging pathogens. RIG-I-like receptors (RLRs) are intracellular sensors for viral RNAs (vRNAs). Their active forms activate mitochondrial antiviral signaling protein (MAVS) and trigger downstream immune responses against viral infection. Functional and structural studies of the RLR-MAVS signaling pathway have revealed significant supramolecular variability in the past few years, which revealed different aspects of the functional signaling pathway. Here I will discuss the molecular events of RLR-MAVS pathway from the angle of detecting single copy or a very low copy number of vRNAs in the presence of non-specific competition from cytosolic RNAs, and review key structural variability in the RLR / vRNA complexes, the MAVS helical polymers, and the adapter-mediated interactions between the active RLR / vRNA complex and the inactive MAVS in triggering the initiation of the MAVS filaments. These structural variations may not be exclusive to each other, but instead may reflect the adaptation of the signaling pathways to different conditions or reach different levels of sensitivity in its response to exogenous vRNAs.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsHumansProtein BindingProtein DomainsRNA HelicasesRNA, ViralSignal TransductionAdaptor Proteins, Signal TransducingMAVS protein, humanRNA HelicasesRNA, ViralCryo-electron microscopyexogenous microorganismsNMR techniqueRLR and MAVSviral RNAs.X-ray crystallography

Identifiers

PMID30569868
PMCPMC6858087

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Registered trials

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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.