Hepatitis C virus envelope protein E2 does not inhibit PKR by simple competition with autophosphorylation sites in the RNA-binding domain.
about
Detection of a novel unglycosylated form of hepatitis C virus E2 envelope protein that is located in the cytosol and interacts with PKRProtein synthesis and endoplasmic reticulum stress can be modulated by the hepatitis C virus envelope protein E2 through the eukaryotic initiation factor 2alpha kinase PERKNew antiviral pathway that mediates hepatitis C virus replicon interferon sensitivity through ADAR1Genetic Diversity Underlying the Envelope Glycoproteins of Hepatitis C Virus: Structural and Functional Consequences and the Implications for Vaccine DesignPKR-dependent mechanisms of gene expression from a subgenomic hepatitis C virus clone.Inhibition of the protein kinase PKR by the internal ribosome entry site of hepatitis C virus genomic RNAViral Determinants of Resistance to Treatment in Patients with Hepatitis CHepatitis C virus RNA: Dinucleotide frequencies and cleavage by RNase LThe anti-apoptotic function of Hsp70 in the interferon-inducible double-stranded RNA-dependent protein kinase-mediated death signaling pathway requires the Fanconi anemia protein, FANCCThe direct binding of the catalytic subunit of protein phosphatase 1 to the PKR protein kinase is necessary but not sufficient for inactivation and disruption of enzyme dimer formationPhosphorylation of the RNA-dependent protein kinase regulates its RNA-binding activity.Induction and evasion of innate antiviral responses by hepatitis C virus.Unactivated PKR exists in an open conformation capable of binding nucleotidesViruses and the type I interferon antiviral system: induction and evasion.Development of prophylactic and therapeutic vaccines against hepatitis C virus.dsRNA-dependent protein kinase PKR and its role in stress, signaling and HCV infection.Intrahepatic gene expression during chronic hepatitis C virus infection in chimpanzees.Tinkering with translation: protein synthesis in virus-infected cells.Impact of hepatitis C virus heterogeneity on interferon sensitivity: an overview.Newcastle disease virus (NDV)-based assay demonstrates interferon-antagonist activity for the NDV V protein and the Nipah virus V, W, and C proteinsRole of the Interdomain Linker in RNA-Activated Protein Kinase ActivationAnalysis of monomeric and dimeric phosphorylated forms of protein kinase R.Mutations in the E2-PePHD region of hepatitis C virus type 1b in patients with hepatocellular carcinoma.Binding of double-stranded RNA to protein kinase PKR is required for dimerization and promotes critical autophosphorylation events in the activation loop.Roles of protein kinase R in cancer: Potential as a therapeutic target.
P2860
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P2860
Hepatitis C virus envelope protein E2 does not inhibit PKR by simple competition with autophosphorylation sites in the RNA-binding domain.
description
2001 nî lūn-bûn
@nan
2001 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Hepatitis C virus envelope pro ...... tes in the RNA-binding domain.
@ast
Hepatitis C virus envelope pro ...... tes in the RNA-binding domain.
@en
type
label
Hepatitis C virus envelope pro ...... tes in the RNA-binding domain.
@ast
Hepatitis C virus envelope pro ...... tes in the RNA-binding domain.
@en
prefLabel
Hepatitis C virus envelope pro ...... tes in the RNA-binding domain.
@ast
Hepatitis C virus envelope pro ...... tes in the RNA-binding domain.
@en
P2093
P2860
P1433
P1476
Hepatitis C virus envelope pro ...... tes in the RNA-binding domain.
@en
P2093
A G Hinnebusch
D R Taylor
M B Mathews
P R Romano
P2860
P304
P356
10.1128/JVI.75.3.1265-1273.2001
P50
P577
2001-02-01T00:00:00Z