Regulation of the interferon-induced PKR: can viruses cope?
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Summary
PKR may regulate cell growth and proliferation in uninfected cells, suggesting that it also participates in the antiproliferative arm of the interferon response.
- Type
- review
- Published
- 1995-02-01
- Cited by
- 193
- References
- 21
- OpenAlex
- https://openalex.org/W2049444392
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:34735039
Keywords
Protein kinase R, Interferon, Biology, EIF-2 kinase, Virology
References
- Adenovirus VAI RNA complexes with the 68 000 Mr protein kinase to regulate its autophosphorylation and activity.
- Characterization and regulation of the 58,000-dalton cellular inhibitor of the interferon-induced, dsRNA-activated protein kinase.
- The integrity of the stem structure of human immunodeficiency virus type 1 Tat-responsive sequence of RNA is required for interaction with the interferon-induced 68,000-Mr protein kinase
- Recombinant vaccinia virus K3L gene product prevents activation of double-stranded RNA-dependent, initiation factor 2 alpha-specific protein kinase.
- Translational stimulation by reovirus polypeptide sigma 3: substitution for VAI RNA and inhibition of phosphorylation of the alpha subunit of eukaryotic initiation factor 2
- Degradation of the interferon-induced 68,000-M(r) protein kinase by poliovirus requires RNA
- The 58,000-dalton cellular inhibitor of the interferon-induced double-stranded RNA-activated protein kinase (PKR) is a member of the tetratricopeptide repeat family of proteins
- Chromosomal assignment of the interferon-inducible double-stranded RNA-dependent protein kinase (PRKR) to human chromosome 2p21-p22 and mouse chromosome 17 E2.
- Control of the interferon-induced 68-kilodalton protein kinase by the HIV-1 tat gene product.
- HIV-1 TAR RNA has an intrinsic ability to activate interferon-inducible enzymes.
- Blockage of NF-kappa B signaling by selective ablation of an mRNA target by 2-5A antisense chimeras.
- Identification of a conserved motif that is necessary for binding of the vaccinia virus E3L gene products to double-stranded RNA.
- Comparative analysis of the regulation of the interferon-inducible protein kinase PKR by Epstein-Barr virus RNAs EBER-1 and EBER-2 and adenovirus VAI RNA.
- Games viruses play: a strategic initiative against the interferon-induced dsRNA activated 68,000 Mr protein kinase
- Adenovirus VAI RNA is required for efficient translation of viral mRNAs at late times after infection.
- Mechanism of interferon action motif I of the interferon-induced, RNA-dependent protein kinase (PKR) is sufficient to mediate RNA-binding activity.
- Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase.
- Epstein-Barr virus-encoded small RNAs (EBERs) do not modulate interferon effects in infected lymphocytes
- Two RNA-binding motifs in the double-stranded RNA-activated protein kinase, DAI.
- Functional expression and RNA binding analysis of the interferon-induced, double-stranded RNA-activated, 68,000-Mr protein kinase in a cell-free system
Cited by
- Maturation, Activation, and Protection of Dendritic Cells Induced by Double-stranded RNA
- PACT, a Stress-modulated Cellular Activator of Interferon-induced Double-stranded RNA-activated Protein Kinase, PKR*
- The Herpes Simplex Virus Type 1 US11 Protein Interacts with Protein Kinase R in Infected Cells and Requires a 30-Amino-Acid Sequence Adjacent to a Kinase Substrate Domain
- Interferon action and the double-stranded RNA-dependent enzymes ADAR1 adenosine deaminase and PKR protein kinase.
- Structural insight into the protective role of P58(IPK) during unfolded protein response.
- Evading the interferon response: hepatitis C virus and the interferon-induced protein kinase, PKR.
- PKR in innate immunity, cancer, and viral oncolysis.
- Innate immunity and hepatitis C virus: eluding the host cell defense.
- Tamoxifen enhances interferon-regulated gene expression in breast cancer cells
- Regulation of translational initiation during cellular responses to stress.
- Silencing African horsesickness virus VP7 protein expression in vitro by RNA interference
- Plant Gene Silencing
- Double-stranded RNA-activated protein kinase interacts with apoptosis signal-regulating kinase 1. Implications for apoptosis signaling pathways.
- 'Omics investigations of HIV and SIV pathogenesis and innate immunity.
- Formation of α-Pal/Max Heterodimers Synergistically Activates the eIF2-α Promoter*
- A diminished activation capacity of the interferon-inducible protein kinase PKR in human T lymphocytes.
- Enhanced Antiviral and Antiproliferative Properties of a STAT1 Mutant Unable to Interact with the Protein Kinase PKR*
- RNA interference: a new and powerful tool for functional genomic analysis
- Double-Stranded-RNA-Activated Protein Kinase PKR Enhances Transcriptional Activation by Tumor Suppressor p53
- Modulation of Interferon (IFN)-inducible Gene Expression by Retinoic Acid
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