ArticleThe EMBO journal1997
Physical association between STAT1 and the interferon-inducible protein kinase PKR and implications for interferon and double-stranded RNA signaling pathways.
Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 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.
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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
67 citing papers in PubMed, 175 citations in OpenAlex.
- Deciphering the dialogue between the bovine blastocyst and the uterus: embryo-induced alterations in extracellular vesicle protein content from an ex vivo model and the in vivo environment.Journal of animal science and biotechnology · 2025Article
- SFX-01 is therapeutic against myeloproliferative disorders caused by activating mutations in Shp2.EMBO molecular medicine · 2025Article
- The dsRNA-dependent kinase (PKR) inhibits the growth ofParasitology · 2025Article
- IFN alpha inducible protein 27 (IFI27) acts as a positive regulator of PACT-dependent PKR activation after RNA virus infections.PLoS pathogens · 2025Article
- PKR associates with 4.1R to promote anchorage-independent growth of hepatocellular carcinoma and lead to poor prognosis.Scientific reports · 2024Article
- Long non-coding RNA GRASLND links melanoma differentiation and interferon-gamma response.Frontiers in molecular biosciences · 2024Article
- HSV-1 Triggers an Antiviral Transcriptional Response during Viral Replication That Is Completely Abrogated in PKRPathogens (Basel, Switzerland) · 2023Article
- Adaptive duplication and genetic diversification of protein kinase R contribute to the specificity of bat-virus interactions.Science advances · 2022Article
- Hepatitis C Virus Nonstructural Protein 5A Interacts with Immunomodulatory Kinase IKKε to Negatively Regulate Innate Antiviral Immunity.Molecules and cells · 2022Article
- Article
- LincRNA-EPS impairs host antiviral immunity by antagonizing viral RNA-PKR interaction.EMBO reports · 2022Article
- UBR5 promotes tumor immune evasion through enhancing IFN-γ-inducedTheranostics · 2022Article
- A tale of two proteins: PACT and PKR and their roles in inflammation.The FEBS journal · 2021Review
- Viral pathogen-induced mechanisms to antagonize mammalian interferon (IFN) signaling pathway.Cellular and molecular life sciences : CMLS · 2021Review
- PKR kinase directly regulates tau expression and Alzheimer's disease-related tau phosphorylation.Brain pathology (Zurich, Switzerland) · 2021Article
- Inhibition of the IFN Response by Bluetongue Virus: The Story So Far.Frontiers in microbiology · 2021Review
- Review
- Long non-coding RNAeLife · 2020Article
- An integrated stress response via PKR suppresses HER2+ cancers and improves trastuzumab therapy.Nature communications · 2019Article
- Protein Kinase R Is Constitutively Expressed in the Human Pancreas.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2019Article
7 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The interferon-inducible double-stranded RNA protein kinase PKR controls protein synthesis through the phosphorylation of eukaryotic translation initiation factor (eIF)-2. In addition to its demonstrated role in translational control, several reports have suggested a transcriptional role for PKR. Here we report that PKR is involved in IFN- and dsRNA-signaling pathways by modulating the function of the signal transducer and activator of transcription STAT1. We also show that PKR associates with STAT1 in mouse and human cells. The association is not a kinase-substrate interaction since STAT1 phosphorylation is not modified by PKR in vitro or in vivo. In addition, the formation of the PKR-STAT1 complex is not dependent upon the enzymatic activity of PKR but does require the dsRNA-binding domain of PKR. Moreover, there is a concomitant decrease in PKR-STAT1 interaction and increase in STAT1 DNA binding in response to IFNs or dsRNA. These findings suggest that PKR plays an important role in IFN and dsRNA-signaling pathways by modulating the transcriptional function of STAT1.
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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.