ArticleJournal of molecular biology2006
Mapping of the auto-inhibitory interactions of protein kinase R by nuclear magnetic resonance.
Article in Journal of molecular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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
21 citing papers in PubMed, 32 citations in OpenAlex.
- Contribution of dsRBD2 to PKR Activation.ACS omega · 2021Article
- Backbone resonance assignments of the catalytic and regulatory domains of CaBiomolecular NMR assignments · 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
- Double-Stranded RNA Sensors and Modulators in Innate Immunity.Annual review of immunology · 2019Review
- Development of 1-((1,4-trans)-4-Aryloxycyclohexyl)-3-arylurea Activators of Heme-Regulated Inhibitor as Selective Activators of the Eukaryotic Initiation Factor 2 Alpha (eIF2α) Phosphorylation Arm of the Integrated Endoplasmic Reticulum Stress Response.Journal of medicinal chemistry · 2017Article
- Interaction of PKR with single-stranded RNA.Scientific reports · 2017Article
- Auto-phosphorylation Represses Protein Kinase R Activity.Scientific reports · 2017Article
- Role of the Interdomain Linker in RNA-Activated Protein Kinase Activation.Biochemistry · 2016Article
- Regulation of PKR by RNA: formation of active and inactive dimers.Biochemistry · 2015Article
- Depletion of eIF2·GTP·Met-tRNAi translation initiation complex up-regulates BRCA1 expression in vitro and in vivo.Oncotarget · 2015Article
- Examining weak protein-protein interactions in start codon recognition via NMR spectroscopy.The FEBS journal · 2014Review
- Activation of protein kinase PKR requires dimerization-induced cis-phosphorylation within the activation loop.The Journal of biological chemistry · 2014Article
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- Ligand binding in the conserved interhelical loop of CorA, a magnesium transporter from Mycobacterium tuberculosis.The Journal of biological chemistry · 2009Article
- Analysis of PKR structure by small-angle scattering.Journal of molecular biology · 2009Article
- Mechanism of PKR Activation by dsRNA.Journal of molecular biology · 2008Article
- Interferon-inducible antiviral effectors.Nature reviews. Immunology · 2008Review
- Domain stabilities in protein kinase R (PKR): evidence for weak interdomain interactions.Biochemistry · 2008Article
- RNA-binding proteins: modular design for efficient function.Nature reviews. Molecular cell biology · 2007Review
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
Abstract
The dsRNA-dependent protein kinase (PKR) is a key mediator of the anti-viral and anti-proliferative effects of interferon. Unphosphorylated PKR is characterized by inhibitory interactions between the kinase and RNA binding domains (RBDs), but the structural details of the latent state and its unraveling during activation are not well understood. To study PKR regulation by NMR we assigned a large portion of the backbone resonances of the catalytically inactive K296R kinase domain, and performed (15)N-heteronuclear single quantum coherence (HSQC) titrations of this kinase domain with the RBDs. Chemical shift perturbations in the kinase indicate that RBD2 binds to the substrate eIF2alpha docking site in the kinase C-lobe. Consistent with these results, a mutation in the eIF2alpha docking site, F495A, displays weaker interactions with the RBD. The full-length RBD1+2 binds more strongly to the kinase domain than RBD2 alone. The observed chemical shift changes extend from the eIF2alpha binding site into the kinase N-lobe and inside the active site, consistent with weak interactions between the N-terminal part of the RBD and the kinase.
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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.