Modulation of hepatitis C virus NS5A hyperphosphorylation by nonstructural proteins NS3, NS4A, and NS4B
about
The lipid kinase phosphatidylinositol-4 kinase III alpha regulates the phosphorylation status of hepatitis C virus NS5AApolipoprotein E likely contributes to a maturation step of infectious hepatitis C virus particles and interacts with viral envelope glycoproteinsHepatitis C virus RNA replication is regulated by FKBP8 and Hsp90Polo-like kinase 1 is involved in hepatitis C virus replication by hyperphosphorylating NS5AHuman VAP-B is involved in hepatitis C virus replication through interaction with NS5A and NS5BPhosphorylation of hepatitis C virus nonstructural protein 5A modulates its protein interactions and viral RNA replicationNew treatment strategies for hepatitis C infectionThe modulation of apoptosis by oncogenic virusesComplete translation of the hepatitis C virus genome in vitro: membranes play a critical role in the maturation of all virus proteins except for NS3.Genetic heterogeneity of hypervariable region 1 of the hepatitis C virus (HCV) genome and sensitivity of HCV to alpha interferon therapy.Characterization of cell lines carrying self-replicating hepatitis C virus RNAs.Isolation and characterization of noncytopathic pestivirus mutants reveals a role for nonstructural protein NS4B in viral cytopathogenicity.Genetic analysis of the pestivirus nonstructural coding region: defects in the NS5A unit can be complemented in trans.Quantitative Analysis of the Hepatitis C Virus Replication ComplexPersistent and transient replication of full-length hepatitis C virus genomes in cell cultureConstruction and characterization of infectious intragenotypic and intergenotypic hepatitis C virus chimerasViral and Cellular Determinants of Hepatitis C Virus RNA Replication in Cell CultureProtein-Protein Interactions between Hepatitis C Virus Nonstructural ProteinsTopology of the Membrane-Associated Hepatitis C Virus Protein NS4BAmphipathic Helix-Dependent Localization of NS5A Mediates Hepatitis C Virus RNA ReplicationThe Isoform of Protein Kinase CKI Is Responsible for Hepatitis C Virus NS5A HyperphosphorylationConserved Determinants for Membrane Association of Nonstructural Protein 5A from Hepatitis C Virus and Related VirusesAllelic Variation in the Hepatitis C Virus NS4B Protein Dramatically Influences RNA ReplicationThe C Terminus of Hepatitis C Virus NS4A Encodes an Electrostatic Switch That Regulates NS5A Hyperphosphorylation and Viral ReplicationCell Culture Adaptation of Hepatitis C Virus and In Vivo Viability of an Adapted VariantA Genetic Interaction between Hepatitis C Virus NS4B and NS3 Is Important for RNA ReplicationThe Hepatitis C Virus NS4B Protein Can trans-Complement Viral RNA Replication and Modulates Production of Infectious VirusProduction of Infectious Genotype 1b Virus Particles in Cell Culture and Impairment by Replication Enhancing MutationsHepatitis C virus NS4B carboxy terminal domain is a membrane binding domainFormation and function of hepatitis C virus replication complexes require residues in the carboxy-terminal domain of NS4B proteinStructural and Functional Studies of Nonstructural Protein 2 of the Hepatitis C Virus Reveal Its Key Role as Organizer of Virion AssemblyHepatitis C virus RNA replication depends on specific cis- and trans-acting activities of viral nonstructural proteinsCoordination of Hepatitis C Virus Assembly by Distinct Regulatory Regions in Nonstructural Protein 5AVinexin β Interacts with Hepatitis C Virus NS5A, Modulating Its Hyperphosphorylation To Regulate Viral Propagation.Kissing-loop interaction in the 3' end of the hepatitis C virus genome essential for RNA replicationIdentification of PTC725, an orally bioavailable small molecule that selectively targets the hepatitis C Virus NS4B proteinHuman hepatitis C virus NS5A protein alters intracellular calcium levels, induces oxidative stress, and activates STAT-3 and NF-kappa B.Distinct functions of NS5A in hepatitis C virus RNA replication uncovered by studies with the NS5A inhibitor BMS-790052Hepatitis C virus NS2 protein serves as a scaffold for virus assembly by interacting with both structural and nonstructural proteinsGenetic complementation of hepatitis C virus nonstructural protein functions associated with replication exhibits requirements that differ from those for virion assembly.
P2860
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P2860
Modulation of hepatitis C virus NS5A hyperphosphorylation by nonstructural proteins NS3, NS4A, and NS4B
description
1999 nî lūn-bûn
@nan
1999 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Modulation of hepatitis C viru ...... l proteins NS3, NS4A, and NS4B
@ast
Modulation of hepatitis C viru ...... l proteins NS3, NS4A, and NS4B
@en
Modulation of hepatitis C viru ...... l proteins NS3, NS4A, and NS4B
@nl
type
label
Modulation of hepatitis C viru ...... l proteins NS3, NS4A, and NS4B
@ast
Modulation of hepatitis C viru ...... l proteins NS3, NS4A, and NS4B
@en
Modulation of hepatitis C viru ...... l proteins NS3, NS4A, and NS4B
@nl
prefLabel
Modulation of hepatitis C viru ...... l proteins NS3, NS4A, and NS4B
@ast
Modulation of hepatitis C viru ...... l proteins NS3, NS4A, and NS4B
@en
Modulation of hepatitis C viru ...... l proteins NS3, NS4A, and NS4B
@nl
P2860
P1433
P1476
Modulation of hepatitis C viru ...... l proteins NS3, NS4A, and NS4B
@en
P2093
Bartenschlager R
P2860
P304
P577
1999-09-01T00:00:00Z