Degradation of the interferon-induced 68,000-M(r) protein kinase by poliovirus requires RNA
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Summary
A hypothetical model depicting possible mechanisms of P68 degradation in poliovirus-infected cells is presented and it is found that preincubation of cell extracts with the synthetic dsRNA poly(I-C) largely prevented P68 proteolysis, providing additional evidence for the critical role of RNA.
- Type
- article
- Published
- 1993-02-01
- Cited by
- 89
- References
- 81
- Access
- Open access
- OpenAlex
- https://openalex.org/W1931351062
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:29395487
Keywords
Biology, Proteolysis, RNA, Proteases, Molecular biology
References
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- 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
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- The cellular 68,000-Mr protein kinase is highly autophosphorylated and activated yet significantly degraded during poliovirus infection: implications for translational regulation
- Autophosphorylation of the protein kinase dependent on double-stranded RNA.
- Role for the P4 amino acid residue in substrate utilization by the poliovirus 3CD proteinase
- Influenza virus regulates protein synthesis during infection by repressing autophosphorylation and activity of the cellular 68,000-Mr protein kinase
- Proteolysis of the p220 component of the cap-binding protein complex is not sufficient for complete inhibition of host cell protein synthesis after poliovirus infection
Cited by
- Mechanisms of viral inhibition by interferons.
- Identification of the Major Phosphorylation Site of the Hepatitis C Virus H Strain NS5A Protein as Serine 2321*
- 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
- Pathogenic Viruses: Smart Manipulators of the Interferon System
- Evading the interferon response: hepatitis C virus and the interferon-induced protein kinase, PKR.
- Chapter 9 Viral Strategies to Subvert the Mammalian Translation Machinery
- Endoplasmic reticulum stress is induced and modulated by enterovirus 71
- Enteroviruses and myocarditis: viral pathogenesis through replication, cytokine induction, and immunopathogenicity.
- Mammalian cell stress responses during Semliki Forest virus infection
- A late adenovirus factor induces eIF-4E dephosphorylation and inhibition of cell protein synthesis
- Cleavage of Poly(A)-Binding Protein by Enterovirus Proteases Concurrent with Inhibition of Translation In Vitro
- Cleavage of RasGAP and Phosphorylation of Mitogen-Activated Protein Kinase in the Course of Coxsackievirus B3 Replication
- Translation of Viral mRNA without Active eIF2: The Case of Picornaviruses
- 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
- Tipping the Balance: Antagonism of PKR Kinase and ADAR1 Deaminase Functions by Virus Gene Products
- Interferon, Mx, and viral countermeasures
- Inhibition of PKR by RNA and DNA viruses.
- Coxsackievirus-Induced Pancreatitis
- Theiler’s virus strain-dependent induction of innate immune responses in RAW264.7 macrophages and its influence on viral clearance versus viral persistence
- Virus strategies for evasion of the host response to infection.
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