Evidence map›Paper›PMID 26760998›Full record

ReviewInternational journal of molecular sciences2016

The Roles of RNase-L in Antimicrobial Immunity and the Cytoskeleton-Associated Innate Response.

Heather J Ezelle, Krishnamurthy Malathi, Bret A Hassel

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

30 citing papers in PubMed, 49 citations in OpenAlex.

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  20. Zika virus employs the host antiviral RNase L protein to support replication factory assembly.Proceedings of the National Academy of Sciences of the United States of America · 2021
    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

3 authors at 3 institutions in 1 country.

Heather J EzelleMarlene and Stewart Greenebaum Cancer Center, University of Maryland School of Medicine, Baltimore, MD 21201, USA. hezelle@som.umaryland.edu.
Krishnamurthy MalathiDepartment of Biological Sciences, University of Toledo, Toledo, OH 43606, USA. Malathi.Krishnamurthy@utoledo.edu.
Bret A HasselMarlene and Stewart Greenebaum Cancer Center, University of Maryland School of Medicine, Baltimore, MD 21201, USA. bhassel@som.umaryland.edu.
University of Maryland Marlene and Stewart Greenebaum Comprehensive Cancer CenterUniversity of Toledo · USVeterans Health Administration · US

Funding

Role of small RNAs in innate immunity and inflammationR15AI089518 · NIAID · UNIVERSITY OF TOLEDO · PI KRISHNAMURTHY, MALATHI · 2010 to 2010
$430k
NIAID NIH HHS AI089518NIAID NIH HHS R15 AI089518
6 · The paper itself

Abstract

The interferon (IFN)-regulated endoribonuclease RNase-L is involved in multiple aspects of the antimicrobial innate immune response. It is the terminal component of an RNA cleavage pathway in which dsRNA induces the production of RNase-L-activating 2-5A by the 2'-5'-oligoadenylate synthetase. The active nuclease then cleaves ssRNAs, both cellular and viral, leading to downregulation of their expression and the generation of small RNAs capable of activating retinoic acid-inducible gene-I (RIG-I)-like receptors or the nucleotide-binding oligomerization domain-like receptor 3 (NLRP3) inflammasome. This leads to IFNβ expression and IL-1β activation respectively, in addition to broader effects on immune cell function. RNase-L is also one of a growing number of innate immune components that interact with the cell cytoskeleton. It can bind to several cytoskeletal proteins, including filamin A, an actin-binding protein that collaborates with RNase-L to maintain the cellular barrier to viral entry. This antiviral activity is independent of catalytic function, a unique mechanism for RNase-L. We also describe here the interaction of RNase-L with the E3 ubiquitin ligase and scaffolding protein, ligand of nump protein X (LNX), a regulator of tight junction proteins. In order to better understand the significance and context of these novel binding partners in the antimicrobial response, other innate immune protein interactions with the cytoskeleton are also discussed.

Indexed as

Immunity, InnateAnimalsBacteriaBacterial InfectionsCytoskeletonEndoribonucleasesHumansVirus DiseasesViruses2-5A-dependent ribonucleaseEndoribonucleasesactincytoskeletonfilamin Ainflammasomeinnate immunityinterferonLNXRNase-L

Identifiers

PMID26760998
PMCPMC4730318
OpenAlexW2226402689

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.