The hepatitis C virus NS5A protein binds to members of the Src family of tyrosine kinases and regulates kinase activity
about
Human butyrate-induced transcript 1 interacts with hepatitis C virus NS5A and regulates viral replicationA single-amino-acid mutation in hepatitis C virus NS5A disrupting FKBP8 interaction impairs viral replicationHepatitis C virus NS5A inhibits mixed lineage kinase 3 to block apoptosisA Rab-GAP TBC domain protein binds hepatitis C virus NS5A and mediates viral replicationHuman VAP-B is involved in hepatitis C virus replication through interaction with NS5A and NS5BHepatitis C virus NS5A protein interacts with phosphatidylinositol 4-kinase type IIIalpha and regulates viral propagationEffect of ethanol on innate antiviral pathways and HCV replication in human liver cells.Hepatitis C virus molecular evolution: transmission, disease progression and antiviral therapyModeling HCV disease in animals: virology, immunology and pathogenesis of HCV and GBV-B infectionsHepatitis C virus NS5A-mediated activation of phosphoinositide 3-kinase results in stabilization of cellular beta-catenin and stimulation of beta-catenin-responsive transcriptionIdentification of Residues Required for RNA Replication in Domains II and III of the Hepatitis C Virus NS5A ProteinHepatitis C virus NS5A protein binds the SH3 domain of the Fyn tyrosine kinase with high affinity: mutagenic analysis of residues within the SH3 domain that contribute to the interactionHepatitis C Virus Diversity and Evolution in the Full Open-Reading Frame during Antiviral TherapySuppression of a pro-apoptotic K+ channel as a mechanism for hepatitis C virus persistenceA Conserved Proline between Domains II and III of Hepatitis C Virus NS5A Influences both RNA Replication and Virus AssemblyThe promiscuous binding of the Fyn SH3 domain to a peptide from the NS5A proteinVinexin β Interacts with Hepatitis C Virus NS5A, Modulating Its Hyperphosphorylation To Regulate Viral Propagation.Hepatitis C virus NS5A protein blocks epidermal growth factor receptor degradation via a proline motif- dependent interactionHepatitis C virus NS5A is able to competitively displace c-Myc from the Bin1 SH3 domain in vitro.HCV NS5A protein containing potential ligands for both Src homology 2 and 3 domains enhances autophosphorylation of Src family kinase Fyn in B cells.c-Src is required for complex formation between the hepatitis C virus-encoded proteins NS5A and NS5B: a prerequisite for replication.State and role of SRC family kinases in replication of herpes simplex virus 1.Applications of computer-aided approaches in the development of hepatitis C antiviral agents.Identification of human kinases involved in hepatitis C virus replication by small interference RNA library screening.Ribavirin resistance in hepatitis C virus replicon-containing cell lines conferred by changes in the cell line or mutations in the replicon RNA.Antiviral stilbene 1,2-diamines prevent initiation of hepatitis C virus RNA replication at the outset of infection.Expanding the proteome of an RNA virus by phosphorylation of an intrinsically disordered viral protein.All three domains of the hepatitis C virus nonstructural NS5A protein contribute to RNA binding.Analysis of functional differences between hepatitis C virus NS5A of genotypes 1-7 in infectious cell culture systems.Insights into the complexity and functionality of hepatitis C virus NS5A phosphorylation.An overview of HCV molecular biology, replication and immune responses.Hepatitis C Virus Particle Assembly Involves Phosphorylation of NS5A by the c-Abl Tyrosine Kinase.Regulation of neuronal proapoptotic potassium currents by the hepatitis C virus nonstructural protein 5A.Host cell targets in HCV therapy: novel strategy or proven practice?Interaction of Hepatitis C virus proteins with pattern recognition receptorsVirus-specific mechanisms of carcinogenesis in hepatitis C virus associated liver cancerFunctional differences in hepatitis C virus nonstructural (NS) 3/4A- and 5A-specific T cell responsesViral proteins and Src family kinases: Mechanisms of pathogenicity from a "liaison dangereuse".The PP4R1 sub-unit of protein phosphatase PP4 is essential for inhibition of NF-κB by merkel polyomavirus small tumour antigen.Hydrophobic triaryl-substituted β-lactams as activity-based probes for profiling eukaryotic enzymes and host-pathogen interactions.
P2860
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P2860
The hepatitis C virus NS5A protein binds to members of the Src family of tyrosine kinases and regulates kinase activity
description
2004 nî lūn-bûn
@nan
2004 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի մարտին հրատարակված գիտական հոդված
@hy
2004年の論文
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2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
The hepatitis C virus NS5A pro ...... and regulates kinase activity
@ast
The hepatitis C virus NS5A pro ...... and regulates kinase activity
@en
The hepatitis C virus NS5A pro ...... and regulates kinase activity
@en-gb
The hepatitis C virus NS5A pro ...... and regulates kinase activity
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type
label
The hepatitis C virus NS5A pro ...... and regulates kinase activity
@ast
The hepatitis C virus NS5A pro ...... and regulates kinase activity
@en
The hepatitis C virus NS5A pro ...... and regulates kinase activity
@en-gb
The hepatitis C virus NS5A pro ...... and regulates kinase activity
@nl
prefLabel
The hepatitis C virus NS5A pro ...... and regulates kinase activity
@ast
The hepatitis C virus NS5A pro ...... and regulates kinase activity
@en
The hepatitis C virus NS5A pro ...... and regulates kinase activity
@en-gb
The hepatitis C virus NS5A pro ...... and regulates kinase activity
@nl
P50
P921
P3181
P356
P1476
The hepatitis C virus NS5A pro ...... and regulates kinase activity
@en
P2093
Andrew Street
Katherine Crowder
P3181
P356
10.1099/VIR.0.19691-0
P407
P577
2004-03-01T00:00:00Z