ArticleJournal of molecular biology2014
Domain interactions in adenovirus VAI RNA mediate high-affinity PKR binding.
Article in Journal of molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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The trial behind it
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Who cites it
13 citing papers in PubMed, 18 citations in OpenAlex.
- African swine fever virus L11L interferes with antiviral responses by targeting the IRF3 and PKR.Cellular and molecular life sciences : CMLS · 2025Article
- The role of circular RNAs in autoimmune diseases: Potential diagnostic biomarkers and therapeutic targets.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Review
- Article
- Insights Into the Involvement of Circular RNAs in Autoimmune Diseases.Frontiers in immunology · 2021Review
- Environmental, Neuro-immune, and Neuro-oxidative Stress Interactions in Chronic Fatigue Syndrome.Molecular neurobiology · 2020Review
- Review
- The search for a PKR code-differential regulation of protein kinase R activity by diverse RNA and protein regulators.RNA (New York, N.Y.) · 2019Review
- Adenovirus VA RNAI Blocks ASC Oligomerization and Inhibits NLRP3 Inflammasome Activation.Frontiers in immunology · 2019Article
- MicroRNAs as Important Players in Host-Adenovirus Interactions.Frontiers in microbiology · 2017Review
- Article
- Structural analysis of adenovirus VAI RNA defines the mechanism of inhibition of PKR.Biophysical journal · 2015Article
- Dissection of the adenoviral VA RNAI central domain structure reveals minimum requirements for RNA-mediated inhibition of PKR.The Journal of biological chemistry · 2014Article
- Antiviral innate immunity: editorial overview.Journal of molecular biology · 2014Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Protein kinase R (PKR) is a component of the innate immunity antiviral pathway. PKR is activated upon binding to double-stranded RNA (dsRNA) to undergo dimerization and autophosphorylation. Adenovirus-associated RNA I (VAI) is a short, non-coding transcript whose major function is to inhibit the activity of PKR. VAI contains three domains: an apical stem-loop, a highly structured central domain, and a terminal stem. Previous studies have localized PKR binding to the apical stem and to the central domain. However, the molecular mechanism for inhibition of PKR is not known. We have characterized the stoichiometry and affinity of PKR binding to VAI and several domain constructs using analytical ultracentrifugation and correlated VAI binding and PKR inhibition. Although PKR binding to simple dsRNAs is not regulated by divalent ion, analysis of the interaction of the isolated dsRNA binding domain with VAI reveals that the binding affinity is enhanced by divalent ion. Dissection of VAI into its constituent domains indicates that none of the isolated domains retains the PKR binding affinity or inhibitory potency of the full-length RNA. PKR is capable of binding the isolated terminal stem, but deletion of this domain from VAI does not affect PKR binding or inhibition. These results indicate that both the apical stem and the central domain are required to form a high-affinity PKR binding site. Our data support a model whereby VAI functions as a PKR inhibitor because it binds a monomer tightly but does not facilitate dimerization.
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Registered trials
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