Identification of a Novel Determinant for Membrane Association in Hepatitis C Virus Nonstructural Protein 4B
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Flaviviral NS4b, chameleon and jack-in-the-box roles in viral replication and pathogenesis, and a molecular target for antiviral interventionHepatitis C virus relies on lipoproteins for its life cycleArchitecture and biogenesis of plus-strand RNA virus replication factoriesStructures of hepatitis C virus nonstructural proteins required for replicase assembly and functionFormation and function of hepatitis C virus replication complexes require residues in the carboxy-terminal domain of NS4B proteinAn Amphipathic -Helix at the C Terminus of Hepatitis C Virus Nonstructural Protein 4B Mediates Membrane AssociationMutations in Classical Swine Fever Virus NS4B Affect Virulence in SwineNS2 Proteins of GB Virus B and Hepatitis C Virus Share Common Protease Activities and Membrane TopologiesRecombinant production of the amino terminal cytoplasmic region of dengue virus non-structural protein 4A for structural studiesThe N-terminal region of severe acute respiratory syndrome coronavirus protein 6 induces membrane rearrangement and enhances virus replication.Influenza virus m2 ion channel protein is necessary for filamentous virion formation.Determinants for membrane association of the hepatitis C virus NS2 protease domain.Membrane interacting regions of Dengue virus NS2A protein.Amphipathic alpha-helix AH2 is a major determinant for the oligomerization of hepatitis C virus nonstructural protein 4BAminoterminal amphipathic α-helix AH1 of hepatitis C virus nonstructural protein 4B possesses a dual role in RNA replication and virus production.Equilibrium and folding simulations of NS4B H2 in pure water and water/2,2,2-trifluoroethanol mixed solvent: examination of solvation models.Influenza virus assembly and budding.Genetic complementation of hepatitis C virus nonstructural protein functions associated with replication exhibits requirements that differ from those for virion assembly.Conserved GXXXG- and S/T-like motifs in the transmembrane domains of NS4B protein are required for hepatitis C virus replicationNS4B self-interaction through conserved C-terminal elements is required for the establishment of functional hepatitis C virus replication complexes.Charged residues in hepatitis C virus NS4B are critical for multiple NS4B functions in RNA replication.Rab5 and class III phosphoinositide 3-kinase Vps34 are involved in hepatitis C virus NS4B-induced autophagy.Encoded library technology screening of hepatitis C virus NS4B yields a small-molecule compound series with in vitro replicon activity.Lipid Binding of the Amphipathic Helix Serving as Membrane Anchor of Pestivirus Glycoprotein ErnsHighly efficient full-length hepatitis C virus genotype 1 (strain TN) infectious culture system.Hepatitis C virus NS4B targets lipid droplets through hydrophobic residues in the amphipathic helicesCoevolution analysis of Hepatitis C virus genome to identify the structural and functional dependency network of viral proteins.Modulation of hepatitis C virus genome encapsidation by nonstructural protein 4BPost-translational modifications of hepatitis C viral proteins and their biological significance.The Future of HCV Therapy: NS4B as an Antiviral Target.Interaction networks of hepatitis C virus NS4B: implications for antiviral therapy.The molecular and structural basis of advanced antiviral therapy for hepatitis C virus infection.Interaction between the NS4B amphipathic helix, AH2, and charged lipid headgroups alters membrane morphology and AH2 oligomeric state--Implications for the Hepatitis C virus life cycle.NS5A Domain 1 and Polyprotein Cleavage Kinetics Are Critical for Induction of Double-Membrane Vesicles Associated with Hepatitis C Virus Replication.Modulation of replication efficacy of the hepatitis C virus replicon Con1 by site-directed mutagenesis of an NS4B aminoterminal basic leucine zipper.A hepatitis C virus NS4B inhibitor suppresses viral genome replication by disrupting NS4B's dimerization/multimerization as well as its interaction with NS5A.Identification of a class of HCV inhibitors directed against the nonstructural protein NS4B.PTC725, an NS4B-Targeting Compound, Inhibits a Hepatitis C Virus Genotype 3 Replicon, as Predicted by Genome Sequence Analysis and Determined ExperimentallyCell-free expression, purification, and membrane reconstitution for NMR studies of the nonstructural protein 4B from hepatitis C virus.Morphological and biochemical characterization of the membranous hepatitis C virus replication compartment.
P2860
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P2860
Identification of a Novel Determinant for Membrane Association in Hepatitis C Virus Nonstructural Protein 4B
description
2009 nî lūn-bûn
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2009 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2009年の論文
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2009年学术文章
@wuu
2009年学术文章
@zh-cn
2009年学术文章
@zh-hans
2009年学术文章
@zh-my
2009年学术文章
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2009年學術文章
@yue
name
Identification of a Novel Dete ...... Virus Nonstructural Protein 4B
@ast
Identification of a Novel Dete ...... Virus Nonstructural Protein 4B
@en
Identification of a Novel Dete ...... Virus Nonstructural Protein 4B
@nl
type
label
Identification of a Novel Dete ...... Virus Nonstructural Protein 4B
@ast
Identification of a Novel Dete ...... Virus Nonstructural Protein 4B
@en
Identification of a Novel Dete ...... Virus Nonstructural Protein 4B
@nl
prefLabel
Identification of a Novel Dete ...... Virus Nonstructural Protein 4B
@ast
Identification of a Novel Dete ...... Virus Nonstructural Protein 4B
@en
Identification of a Novel Dete ...... Virus Nonstructural Protein 4B
@nl
P2093
P2860
P50
P3181
P356
P1433
P1476
Identification of a Novel Dete ...... Virus Nonstructural Protein 4B
@en
P2093
Eric Diesis
Hubert E Blum
Jean-Marie Ruysschaert
Naveen Arora
Valérie Castet
Vincent Raussens
P2860
P304
P3181
P356
10.1128/JVI.02663-08
P577
2009-06-01T00:00:00Z