ArticleJournal of molecular biology2009
Analysis of PKR structure by small-angle scattering.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers, 1 of them a synthesis that pooled it.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
31 citing papers in PubMed, 1 synthesis or guideline pooled it, 47 citations in OpenAlex.
- Comprehensive analysis of regulated cell death pathways: intrinsic disorder, protein-protein interactions, and cross-pathway communication.Apoptosis : an international journal on programmed cell death · 2025Pooled it
- Toward unraveling molecular grammars for dsRNA-binding proteins: substrate recognition to binding mechanisms.BMB reports · 2025Review
- Structural Characteristics and Properties of the RNA-Binding Protein hnRNPK at Multiple Physical States.International journal of molecular sciences · 2025Article
- Host species-specific activity of the poxvirus PKR inhibitors E3 and K3 mediate host range function.Journal of virology · 2024Article
- RNA recognition by PKR during DNA virus infection.Journal of medical virology · 2024Review
- Contribution of dsRBD2 to PKR Activation.ACS omega · 2021Article
- Analytical ultracentrifuge: an ideal tool for characterization of non-coding RNAs.European biophysics journal : EBJ · 2020Review
- 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
- Interaction of PKR with single-stranded RNA.Scientific reports · 2017Article
- Impact of the structural integrity of the three-way junction of adenovirus VAI RNA on PKR inhibition.PloS one · 2017Article
- Order, Disorder, and Everything in Between.Molecules (Basel, Switzerland) · 2016Review
- Measurement of protein size in concentrated solutions by small angle X-ray scattering.Protein science : a publication of the Protein Society · 2016Article
- 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
- 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
- Regulation of PKR by RNA: formation of active and inactive dimers.Biochemistry · 2015Article
- Structural Insights into High Density Lipoprotein: Old Models and New Facts.Frontiers in pharmacology · 2015Review
- Classification of intrinsically disordered regions and proteins.Chemical reviews · 2014Review
- The eIF2α kinases: their structures and functions.Cellular and molecular life sciences : CMLS · 2013Review
- Recognition of viral RNA stem-loops by the tandem double-stranded RNA binding domains of PKR.RNA (New York, N.Y.) · 2013Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Protein kinase R (PKR) is a key component of the interferon antiviral defense pathway. Upon binding double-stranded RNA, PKR undergoes autophosphorylation reactions that activate the kinase. PKR contains an N-terminal double-stranded RNA binding domain, which consists of two tandem double-stranded RNA binding motifs, and a C-terminal kinase domain. We have used small-angle X-ray scattering and small-angle neutron scattering to define the conformation of latent PKR in solution. Guinier analysis indicates a radius of gyration of about 35 A. The p(r) distance distribution function exhibits a peak near 30 A, with a broad shoulder extending to longer distances. Good fits to the scattering data require models that incorporate multiple compact and extended conformations of the two interdomain linker regions. Thus, PKR belongs to the growing family of proteins that contain intrinsically unstructured regions. We propose that the flexible linkers may allow PKR to productively dimerize upon interaction with RNA activators that have diverse structures.
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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.