Evidence map›Paper›PMID 30770398›Full record

ReviewRNA (New York, N.Y.)2019

The search for a PKR code-differential regulation of protein kinase R activity by diverse RNA and protein regulators.

Charles Bou-Nader, Jackson M Gordon, Frances E Henderson, Jinwei Zhang

Open access · bronzeAbstract readReview
In one paragraph

Review in RNA (New York, N.Y.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
3.5field-weighted citation impact, top 6% 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

43 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
  2. Journal of chemical information and modeling · 2025
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  16. mRNA-Based Nanomedicine: A New Strategy for Treating Infectious Diseases and Beyond.European journal of drug metabolism and pharmacokinetics · 2023
    Review
  17. Review
  18. Article
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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

4 authors at 1 institution in 1 country.

Charles Bou-NaderLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, Maryland 20892, USA.
Jackson M GordonLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, Maryland 20892, USA.
Frances E HendersonLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, Maryland 20892, USA.
Jinwei ZhangLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, Maryland 20892, USA.ORCID 0000-0002-2114-173X
National Institute of Diabetes and Digestive and Kidney Diseases · US

Funding

Noncoding RNA structures and interactions in cellular stress responses and immunityZIADK075136 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI ZHANG, JINWEI · 2016 to 2025
$23.2M
The Center for HIV RNA Studies (CRNA)U54GM103297 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SUMMERS, MICHAEL FINLEY · 2017 to 2018
$10.2M
NIGMS NIH HHS U54 GM103297
6 · The paper itself

Abstract

The interferon-inducible protein kinase R (PKR) is a key component of host innate immunity that restricts viral replication and propagation. As one of the four eIF2α kinases that sense diverse stresses and direct the integrated stress response (ISR) crucial for cell survival and proliferation, PKR's versatile roles extend well beyond antiviral defense. Targeted by numerous host and viral regulators made of RNA and proteins, PKR is subject to multiple layers of endogenous control and external manipulation, driving its rapid evolution. These versatile regulators include not only the canonical double-stranded RNA (dsRNA) that activates the kinase activity of PKR, but also highly structured viral, host, and artificial RNAs that exert a full spectrum of effects. In this review, we discuss our deepening understanding of the allosteric mechanism that connects the regulatory and effector domains of PKR, with an emphasis on diverse structured RNA regulators in comparison to their protein counterparts. Through this analysis, we conclude that much of the mechanistic details that underlie this RNA-regulated kinase await structural and functional elucidation, upon which we can then describe a "PKR code," a set of structural and chemical features of RNA that are both descriptive and predictive for their effects on PKR.

Indexed as

Allosteric RegulationAnimalsBase SequenceBinding SiteseIF-2 KinaseGene Expression RegulationHost-Pathogen InteractionsHumansImmunity, InnateInterferonsProtein BindingProtein Interaction Domains and MotifsProtein Structure, SecondaryRNA, Double-StrandedRNA, UntranslatedVirus DiseasesEIF2AK2 protein, humaneIF-2 KinaseInterferonsRNA, Double-StrandedRNA, Untranslatedallosteric regulationantiviral defenseinnate immunitynoncoding RNAPKR

Identifiers

PMID30770398
PMCPMC6467004
OpenAlexW2913822211

What OpenQuestion holds

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LicenceCC BY-NC
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.