Identification of Residues Required for RNA Replication in Domains II and III of the Hepatitis C Virus NS5A Protein - Test2 - elhamkhani - TriplyDB

Identification of Residues Required for RNA Replication in Domains II and III of the Hepatitis C Virus NS5A Protein

Identification of Residues Required for RNA Replication in Domains II and III of the Hepatitis C Virus NS5A Protein

http://www.wikidata.org/entity/Q27485314

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Intrinsically unstructured domain 3 of hepatitis C Virus NS5A forms a "fuzzy complex" with VAPB-MSP domain which carries ALS-causing mutations Hepatitis C virus NS5B and host cyclophilin A share a common binding site on NS5A Role of ledipasvir/sofosbuvir combination for genotype 1 hepatitis C virus infection Chaperones in hepatitis C virus infection Regulation of Hepatitis C Virion Production via Phosphorylation of the NS5A Protein Essential Role of Domain III of Nonstructural Protein 5A for Hepatitis C Virus Infectious Particle Assembly Interaction of Hepatitis C Virus Nonstructural Protein 5A with Core Protein Is Critical for the Production of Infectious Virus Particles High-Resolution Functional Profiling of Hepatitis C Virus Genome Role of the Hepatitis C Virus Core+1 Open Reading Frame and Core cis-Acting RNA Elements in Viral RNA Translation and Replication A Cooperative Interaction between Nontranslated RNA Sequences and NS5A Protein Promotes In Vivo Fitness of a Chimeric Hepatitis C/GB Virus B Crystal Structure of a Novel Dimeric Form of NS5A Domain I Protein from Hepatitis C Virus Hepatitis C Virus NS5A Protein Is a Substrate for the Peptidyl-prolyl cis/trans Isomerase Activity of Cyclophilins A and B The Marmoset Model of GB Virus B Infections: Adaptation to Host Phenotypic Variation Production of Infectious Genotype 1b Virus Particles in Cell Culture and Impairment by Replication Enhancing Mutations Hepatitis C virus NS4B carboxy terminal domain is a membrane binding domain The Hepatitis C Virus NS5A Stimulates NS5B During In Vitro RNA Synthesis in a Template Specific Manner A Conserved Proline between Domains II and III of Hepatitis C Virus NS5A Influences both RNA Replication and Virus Assembly Architects of assembly: roles of Flaviviridae non-structural proteins in virion morphogenesis Cyclosporine Inhibits a Direct Interaction between Cyclophilins and Hepatitis C NS5A The crystal structure of NS5A domain 1 from genotype 1a reveals new clues to the mechanism of action for dimeric HCV inhibitors Seed Sequence-Matched Controls Reveal Limitations of Small Interfering RNA Knockdown in Functional and Structural Studies of Hepatitis C Virus NS5A-MOBKL1B Interaction Metabolism of phosphatidylinositol 4-kinase IIIα-dependent PI4P Is subverted by HCV and is targeted by a 4-anilino quinazoline with antiviral activity DEB025 (Alisporivir) inhibits hepatitis C virus replication by preventing a cyclophilin A induced cis-trans isomerisation in domain II of NS5A The Disordered Region of the HCV Protein NS5A: Conformational Dynamics, SH3 Binding, and Phosphorylation VAPC, an human endogenous inhibitor for hepatitis C virus (HCV) infection, is intrinsically unstructured but forms a "fuzzy complex" with HCV NS5B.A major determinant of cyclophilin dependence and cyclosporine susceptibility of hepatitis C virus identified by a genetic approach Small molecules targeting hepatitis C virus-encoded NS5A cause subcellular redistribution of their target: insights into compound modes of action.Hepatitis C virus NS5A hijacks ARFGAP1 to maintain a phosphatidylinositol 4-phosphate-enriched microenvironment Hepatitis C virus NS5A activates the mammalian target of rapamycin (mTOR) pathway, contributing to cell survival by disrupting the interaction between FK506-binding protein 38 (FKBP38) and mTOR Resistance analysis of the hepatitis C virus NS5A inhibitor BMS-790052 in an in vitro replicon system.Modeling shows that the NS5A inhibitor daclatasvir has two modes of action and yields a shorter estimate of the hepatitis C virus half-life Ethanol and reactive species increase basal sequence heterogeneity of hepatitis C virus and produce variants with reduced susceptibility to antivirals.Heat shock protein 72 is associated with the hepatitis C virus replicase complex and enhances viral RNA replication.All three domains of the hepatitis C virus nonstructural NS5A protein contribute to RNA binding.Distinct functions of NS5A in hepatitis C virus RNA replication uncovered by studies with the NS5A inhibitor BMS-790052 Cyclophilin A associates with enterovirus-71 virus capsid and plays an essential role in viral infection as an uncoating regulator Analysis of functional differences between hepatitis C virus NS5A of genotypes 1-7 in infectious cell culture systems.Hepatitis C NS5A protein: two drug targets within the same protein with different mechanisms of resistance.A cell culture adapted HCV JFH1 variant that increases viral titers and permits the production of high titer infectious chimeric reporter viruses.Comparison of the Mechanisms of Drug Resistance among HIV, Hepatitis B, and Hepatitis C.

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Identification of Residues Required for RNA Replication in Domains II and III of the Hepatitis C Virus NS5A Protein

http://www.wikidata.org/entity/Q27485314

description

2008 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

article scientifique (publié 2008-02)

@fr

articolo scientifico (pubblicato il 2008-02)

@it

artigo científico (publicado na 2008-02)

@pt

artículu científicu espublizáu en 2008

@ast

im Februar 2008 veröffentlichter wissenschaftlicher Artikel

@de

scientific article (publication date: February 2008)

@en

vedecký článok (publikovaný 2008-02)

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videnskabelig artikel (udgivet 2008-02)

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name

Identification of Residues Req ...... Hepatitis C Virus NS5A Protein

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Identification of Residues Req ...... Hepatitis C Virus NS5A Protein

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Identification of Residues Req ...... Hepatitis C Virus NS5A Protein

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Identification of Residues Req ...... Hepatitis C Virus NS5A Protein

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Identification of Residues Req ...... Hepatitis C Virus NS5A Protein

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Identification of Residues Req ...... Hepatitis C Virus NS5A Protein

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Identification of Residues Req ...... Hepatitis C Virus NS5A Protein

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Identification of Residues Req ...... Hepatitis C Virus NS5A Protein

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Identification of Residues Req ...... Hepatitis C Virus NS5A Protein

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Identification of Residues Req ...... Hepatitis C Virus NS5A Protein

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Charles M Rice

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Jason C Treadaway

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Katie L Foss

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Timothy L Tellinghuisen

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P2860

NS5A, a nonstructural protein of hepatitis C virus, binds growth factor receptor-bound protein 2 adaptor protein in a Src homology 3 domain/ligand-dependent manner and perturbs mitogenic signaling

Further studies on hepatitis C virus NS5A-SH3 domain interactions: identification of residues critical for binding and implications for viral RNA replication and modulation of cell signalling

The hepatitis C virus NS5A protein binds to members of the Src family of tyrosine kinases and regulates kinase activity

Expression of hepatitis C virus proteins induces distinct membrane alterations including a candidate viral replication complex

Mutations in Hepatitis C Virus RNAs Conferring Cell Culture Adaptation

Robust hepatitis C virus infection in vitro.

The hepatitis C viral NS3 protein is a processive DNA helicase with cofactor enhanced RNA unwinding.

Highly permissive cell lines for subgenomic and genomic hepatitis C virus RNA replication.

Production of infectious genotype 1a hepatitis C virus (Hutchinson strain) in cultured human hepatoma cells

Structure of the zinc-binding domain of an essential component of the hepatitis C virus replicase

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1073-83

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450761

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10.1128/JVI.00328-07

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3

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82

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5814115

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18032500

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Hepatitis C virus

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2224455

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