ArticleBiochemistry2015
Regulation of PKR by RNA: formation of active and inactive dimers.
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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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.
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.
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Who cites it
18 citing papers in PubMed, 29 citations in OpenAlex.
- PACT prevents aberrant activation of PKR by endogenous dsRNA without sequestration.Nature communications · 2025Article
- Therapeutic application of circular RNA aptamers in a mouse model of psoriasis.Nature biotechnology · 2025Article
- RNA recognition by PKR during DNA virus infection.Journal of medical virology · 2024Review
- Innate immune responses to RNA: sensing and signaling.Frontiers in immunology · 2024Review
- RNA Modification in Inflammatory Bowel Diseases.Biomedicines · 2022Review
- Contribution of dsRBD2 to PKR Activation.ACS omega · 2021Article
- Mucosal immunity and tRNA, tRF, and tiRNA.Journal of molecular medicine (Berlin, Germany) · 2021Review
- The Potential Role of Protein Kinase R as a Regulator of Age-Related Neurodegeneration.Frontiers in aging neuroscience · 2021Review
- Analysis of nonideality: insights from high concentration simulations of sedimentation velocity data.European biophysics journal : EBJ · 2020Article
- Structural Basis of Protein Kinase R Autophosphorylation.Biochemistry · 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
- Double-Stranded RNA Sensors and Modulators in Innate Immunity.Annual review of immunology · 2019Review
- Defects in interferon pathways as potential biomarkers of sensitivity to oncolytic viruses.Reviews in medical virology · 2018Review
- Interaction of PKR with single-stranded RNA.Scientific reports · 2017Article
- Mechanism of Protein Kinase R Inhibition by Human Cytomegalovirus pTRS1.Journal of virology · 2017Article
- Activation of PKR by short stem-loop RNAs containing single-stranded arms.RNA (New York, N.Y.) · 2016Article
- Role of the Interdomain Linker in RNA-Activated Protein Kinase Activation.Biochemistry · 2016Article
- Oncogenes: The Passport for Viral Oncolysis Through PKR Inhibition.Biomarkers in cancer · 2016Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
PKR is a member of the eIF2α family of protein kinases that inhibit translational initiation in response to stress stimuli and functions as a key mediator of the interferon-induced antiviral response. PKR contains a dsRNA binding domain that binds to duplex regions present in viral RNAs, resulting in kinase activation and autophosphorylation. An emerging theme in the regulation of protein kinases is the allosteric linkage of dimerization and activation. The PKR kinase domain forms a back-to-back parallel dimer that is implicated in activation. We have developed a sensitive homo-Förster resonance energy transfer assay for kinase domain dimerization to directly probe the relationship among RNA binding, activation, and dimerization. In the case of perfect duplex RNAs, dimerization is correlated with activation and dsRNAs containing 30 bp or more efficiently induce kinase domain dimerization and activation. However, more complex duplex RNAs containing a 10-15 bp 2'-O-methyl RNA barrier produce kinase dimers but do not activate. Similarly, inactivating mutations within the PKR dimer interface that disrupt key electrostatic and hydrogen binding interactions fail to abolish dimerization. Our data support a model in which activating RNAs induce formation of a back-to-back parallel PKR kinase dimer whereas nonactivating RNAs either fail to induce dimerization or produce an alternative, inactive dimer configuration, providing an additional mechanism for distinguishing between host and pathogen RNA.
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What OpenQuestion holds
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.