ArticleBiophysical journal2015
Structural analysis of adenovirus VAI RNA defines the mechanism of inhibition of PKR.
Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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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.
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Who cites it
18 citing papers in PubMed, 27 citations in OpenAlex.
- Biomolecular phase separation in stress granule assembly and virus infection.Acta biochimica et biophysica Sinica · 2023Article
- Review
- HIV co-opts a cellular antiviral mechanism, activation of stress kinase PKR by its RNA, to enable splicing of rev/tat mRNA.Cell & bioscience · 2023Article
- A little less aggregation a little more replication: Viral manipulation of stress granules.Wiley interdisciplinary reviews. RNA · 2023Review
- Cellular origins of dsRNA, their recognition and consequences.Nature reviews. Molecular cell biology · 2022Review
- Structural Insights into Human Adenovirus Type 4 Virus-Associated RNA I.International journal of molecular sciences · 2022Article
- Structural analyses of an RNA stability element interacting with poly(A).Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Inhibition of PKR by Viruses.Frontiers in microbiology · 2021Review
- Analytical ultracentrifuge: an ideal tool for characterization of non-coding RNAs.European biophysics journal : EBJ · 2020Review
- Review
- Crystal structure of an adenovirus virus-associated RNA.Nature communications · 2019Article
- 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
- Translational Control in Virus-Infected Cells.Cold Spring Harbor perspectives in biology · 2019Review
- Adenovirus VA RNAI Blocks ASC Oligomerization and Inhibits NLRP3 Inflammasome Activation.Frontiers in immunology · 2019Article
- Impact of the structural integrity of the three-way junction of adenovirus VAI RNA on PKR inhibition.PloS one · 2017Article
- SAXS studies of RNA: structures, dynamics, and interactions with partners.Wiley interdisciplinary reviews. RNA · 2016Review
- The Regulatory and Kinase Domains but Not the Interdomain Linker Determine Human Double-stranded RNA-activated Kinase (PKR) Sensitivity to Inhibition by Viral Non-coding RNAs.The Journal of biological chemistry · 2015Article
- Diverse mechanisms evolved by DNA viruses to inhibit early host defenses.Critical reviews in biochemistry and molecular biologyReview
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Protein kinase R (PKR) is activated by dsRNA produced during virus replication and plays a major role in the innate immunity response to virus infection. In response, viruses have evolved multiple strategies to evade PKR. Adenovirus virus-associated RNA-I (VAI) is a short, noncoding transcript that functions as an RNA decoy to sequester PKR in an inactive state. VAI consists of an apical stem-loop, a highly structured central domain, and a terminal stem. Chemical probing and mutagenesis demonstrate that the central domain is stabilized by a pseudoknot. A structural model of VAI was obtained from constraints derived from chemical probing and small angle x-ray scattering (SAXS) measurements. VAI adopts a flat, extended conformation with the apical and terminal stems emanating from a protuberance in the center. This model reveals how the apical stem and central domain assemble to produce an extended duplex that is precisely tuned to bind a single PKR monomer with high affinity, thereby inhibiting activation of PKR by viral dsRNA.
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Registered trials
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.