ArticleNucleic acids research2008
Interaction of human tRNA-dihydrouridine synthase-2 with interferon-induced protein kinase PKR.
Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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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.
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Who cites it
24 citing papers in PubMed, 46 citations in OpenAlex.
- The tRNA dihydrouridine synthase DusA has a distinct mechanism in optimizing tRNAs for translation.Nucleic acids research · 2026Article
- IFN alpha inducible protein 27 (IFI27) acts as a positive regulator of PACT-dependent PKR activation after RNA virus infections.PLoS pathogens · 2025Article
- Differential redox sensitivity of tRNA dihydrouridylation.Nucleic acids research · 2024Article
- Analysis of the serum proteome profile of wild stump-tailed macaques (Frontiers in veterinary science · 2024Article
- The Repertoire of RNA Modifications Orchestrates a Plethora of Cellular Responses.International journal of molecular sciences · 2023Review
- Evolutionary Diversity of Dus2 Enzymes Reveals Novel Structural and Functional Features among Members of the RNA Dihydrouridine Synthases Family.Biomolecules · 2022Article
- The Dihydrouridine landscape from tRNA to mRNA: a perspective on synthesis, structural impact and function.RNA biology · 2022Review
- Accurate identification of RNA D modification using multiple features.RNA biology · 2021Article
- Human DICER helicase domain recruits PKR and modulates its antiviral activity.PLoS pathogens · 2021Article
- Naturally occurring modified ribonucleosides.Wiley interdisciplinary reviews. RNA · 2020Review
- FMN reduces Amyloid-β toxicity in yeast by regulating redox status and cellular metabolism.Nature communications · 2020Article
- 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
- Molecular basis for transfer RNA recognition by the double-stranded RNA-binding domain of human dihydrouridine synthase 2.Nucleic acids research · 2019Article
- An extended dsRBD is required for post-transcriptional modification in human tRNAs.Nucleic acids research · 2015Article
- Runs of Homozygosity: Association with Coronary Artery Disease and Gene Expression in Monocytes and Macrophages.American journal of human genetics · 2015Article
- Article
- The stress granule protein G3BP1 recruits protein kinase R to promote multiple innate immune antiviral responses.Journal of virology · 2015Article
- 'Black sheep' that don't leave the double-stranded RNA-binding domain fold.Trends in biochemical sciences · 2014Review
- The PKR activator, PACT, becomes a PKR inhibitor during HIV-1 replication.Retrovirology · 2013Article
- Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of human dihydrouridine synthase.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
PKR is an interferon (IFN)-induced protein kinase, which is involved in regulation of antiviral innate immunity, stress signaling, cell proliferation and programmed cell death. Although a low amount of PKR is expressed ubiquitously in all cell types in the absence of IFNs, PKR expression is induced at transcriptional level by IFN. PKR's enzymatic activity is activated by its binding to one of its activators. Double-stranded (ds) RNA, protein activator PACT and heparin are the three known activators of PKR. Activation of PKR in cells leads to a general block in protein synthesis due to phosphorylation of eIF2alpha on serine 51 by PKR. PKR activation is regulated very tightly in mammalian cells and a prolonged activation of PKR leads to apoptosis. Thus, positive and negative regulation of PKR activation is important for cell viability and function. The studies presented here describe human dihydrouridine synthase-2 (hDUS2) as a novel regulator of PKR. We originally identified hDUS2 as a protein interacting with PACT in a yeast two-hybrid screen. Further characterization revealed that hDUS2 also interacts with PKR through its dsRNA binding/dimerization domain and inhibits its kinase activity. Our results suggest that hDUS2 may act as a novel inhibitor of PKR in cells.
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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.