ArticleJournal of molecular biology2011
Heparin activates PKR by inducing dimerization.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
17 citing papers in PubMed, 31 citations in OpenAlex.
- Contribution of dsRBD2 to PKR Activation.ACS omega · 2021Article
- The Potential Role of Protein Kinase R as a Regulator of Age-Related Neurodegeneration.Frontiers in aging neuroscience · 2021Review
- PKR kinase directly regulates tau expression and Alzheimer's disease-related tau phosphorylation.Brain pathology (Zurich, Switzerland) · 2021Article
- PKR activation by noncanonical ligands: a 5'-triphosphate requirement versus antisense contamination.RNA (New York, N.Y.) · 2019Article
- Structural Basis of Protein Kinase R Autophosphorylation.Biochemistry · 2019Article
- APOL1 risk allele RNA contributes to renal toxicity by activating protein kinase R.Communications biology · 2018Article
- Interaction of PKR with single-stranded RNA.Scientific reports · 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
- Structural analysis of adenovirus VAI RNA defines the mechanism of inhibition of PKR.Biophysical journal · 2015Article
- Activation of the double-stranded RNA-dependent protein kinase PKR by small ubiquitin-like modifier (SUMO).The Journal of biological chemistry · 2014Article
- Domain interactions in adenovirus VAI RNA mediate high-affinity PKR binding.Journal of molecular biology · 2014Article
- mRNA decapping enzyme 1a (Dcp1a)-induced translational arrest through protein kinase R (PKR) activation requires the N-terminal enabled vasodilator-stimulated protein homology 1 (EVH1) domain.The Journal of biological chemistry · 2014Article
- Development of eczema vaccinatum in atopic mouse models and efficacy of MVA vaccination against lethal poxviral infection.PloS one · 2014Article
- Article
- Mechanistic characterization of the 5'-triphosphate-dependent activation of PKR: lack of 5'-end nucleobase specificity, evidence for a distinct triphosphate binding site, and a critical role for the dsRBD.RNA (New York, N.Y.) · 2012Article
- The use of analytical sedimentation velocity to extract thermodynamic linkage.Biophysical chemistry · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Protein kinase R (PKR) is an interferon-induced kinase that plays a pivotal role in the innate immunity pathway. PKR is activated to undergo autophosphorylation upon binding to double-stranded RNAs or RNAs that contain duplex regions. Activated PKR phosphorylates the α subunit of eukaryotic initiation factor 2, thereby inhibiting protein synthesis. PKR is also activated by heparin, a highly sulfated glycosaminoglycan. We have used biophysical methods to define the mechanism of PKR activation by heparin. Heparins as short as hexasaccharide bind strongly to PKR and activate autophosphorylation. In contrast to double-stranded RNA, heparin activates PKR by binding to the kinase domain. Analytical ultracentrifugation measurements support a thermodynamic linkage model where heparin binding allosterically enhances PKR dimerization, thereby activating the kinase. These results indicate that PKR can be activated by small molecules and represents a viable target for the development of novel antiviral agents.
Indexed as
Identifiers
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.