Hepatitis C Virus NS5A Protein Is a Substrate for the Peptidyl-prolyl cis/trans Isomerase Activity of Cyclophilins A and B
about
Cyclosporin A associated helicase-like protein facilitates the association of hepatitis C virus RNA polymerase with its cellular cyclophilin BHepatitis C virus NS5B and host cyclophilin A share a common binding site on NS5AChaperones in hepatitis C virus infectionHost-Targeting Agents to Prevent and Cure Hepatitis C Virus InfectionCuring a viral infection by targeting the host: the example of cyclophilin inhibitorsFuture classes of hepatitis C virus therapeutic agentsDirect acting antivirals for the treatment of chronic viral hepatitisCyclophilin Inhibitors Remodel the Endoplasmic Reticulum of HCV-Infected Cells in a Unique Pattern Rendering Cells Impervious to a ReinfectionEssential Role of Cyclophilin A for Hepatitis C Virus Replication and Virus Production and Possible Link to Polyprotein Cleavage KineticsA Conserved Proline between Domains II and III of Hepatitis C Virus NS5A Influences both RNA Replication and Virus AssemblyCyclosporine Inhibits a Direct Interaction between Cyclophilins and Hepatitis C NS5ASeed Sequence-Matched Controls Reveal Limitations of Small Interfering RNA Knockdown in Functional and Structural Studies of Hepatitis C Virus NS5A-MOBKL1B InteractionHepatitis C virus RNA replication depends on specific cis- and trans-acting activities of viral nonstructural proteinsCharacterization of the Anti-HCV Activities of the New Cyclophilin Inhibitor STG-175DEB025 (Alisporivir) inhibits hepatitis C virus replication by preventing a cyclophilin A induced cis-trans isomerisation in domain II of NS5ABoth Cyclophilin Inhibitors and Direct-Acting Antivirals Prevent PKR Activation in HCV-Infected Cells.A major determinant of cyclophilin dependence and cyclosporine susceptibility of hepatitis C virus identified by a genetic approachIdentification of Conus peptidylprolyl cis-trans isomerases (PPIases) and assessment of their role in the oxidative folding of conotoxins.Increasing rate of cleavage at boundary between non-structural proteins 4B and 5A inhibits replication of hepatitis C virus.All three domains of the hepatitis C virus nonstructural NS5A protein contribute to RNA binding.Cyclophilin A associates with enterovirus-71 virus capsid and plays an essential role in viral infection as an uncoating regulatorProfile of alisporivir and its potential in the treatment of hepatitis C.Genomic and proteomic analysis of Schizaphis graminum reveals cyclophilin proteins are involved in the transmission of cereal yellow dwarf virusIntrinsic disorder mediates hepatitis C virus core-host cell protein interactions.Domain 3 of NS5A protein from the hepatitis C virus has intrinsic alpha-helical propensity and is a substrate of cyclophilin A.Cyclophilin and NS5A inhibitors, but not other anti-hepatitis C virus (HCV) agents, preclude HCV-mediated formation of double-membrane-vesicle viral factoriesDiscovery of Novel Small Molecule Anti-HCV Agents via the CypA Inhibitory Mechanism Using O-Acylation-Directed Lead Optimization.A Proline-Tryptophan Turn in the Intrinsically Disordered Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus RNA ReplicationHepatitis C virus-host interactions, replication, and viral assemblyCoevolution analysis of Hepatitis C virus genome to identify the structural and functional dependency network of viral proteins.The C terminus of NS5A domain II is a key determinant of hepatitis C virus genome replication, but is not required for virion assembly and release.Phenotypic analysis of NS5A variant from liver transplant patient with increased cyclosporine susceptibilityAnti-HCV drugs in the pipeline.Cyclophilin A as a New Therapeutic Target for Hepatitis C Virus-induced Hepatocellular CarcinomaActivity of hexokinase is increased by its interaction with hepatitis C virus protein NS5A.Host-targeting agents in the treatment of hepatitis C: a beginning and an end?Cyclophilin inhibitors: a novel class of promising host-targeting anti-HCV agents.New targets for antiviral therapy of chronic hepatitis C.Cyclophilin inhibitors: an emerging class of therapeutics for the treatment of chronic hepatitis C infectionThe molecular and structural basis of advanced antiviral therapy for hepatitis C virus infection.
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P2860
Hepatitis C Virus NS5A Protein Is a Substrate for the Peptidyl-prolyl cis/trans Isomerase Activity of Cyclophilins A and B
description
2009 nî lūn-bûn
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2009 թուականի Մայիսին հրատարակուած գիտական յօդուած
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2009 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2009年の論文
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2009年学术文章
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2009年学术文章
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2009年学术文章
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2009年学术文章
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2009年学术文章
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2009年學術文章
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name
Hepatitis C Virus NS5A Protein ...... tivity of Cyclophilins A and B
@ast
Hepatitis C Virus NS5A Protein ...... tivity of Cyclophilins A and B
@en
Hepatitis C Virus NS5A Protein ...... tivity of Cyclophilins A and B
@nl
type
label
Hepatitis C Virus NS5A Protein ...... tivity of Cyclophilins A and B
@ast
Hepatitis C Virus NS5A Protein ...... tivity of Cyclophilins A and B
@en
Hepatitis C Virus NS5A Protein ...... tivity of Cyclophilins A and B
@nl
prefLabel
Hepatitis C Virus NS5A Protein ...... tivity of Cyclophilins A and B
@ast
Hepatitis C Virus NS5A Protein ...... tivity of Cyclophilins A and B
@en
Hepatitis C Virus NS5A Protein ...... tivity of Cyclophilins A and B
@nl
P2860
P50
P3181
P356
P1476
Hepatitis C Virus NS5A Protein ...... tivity of Cyclophilins A and B
@en
P2093
Aurélie Badillo
Dries Verdegem
P2860
P304
P3181
P356
10.1074/JBC.M809244200
P407
P50
P577
2009-05-15T00:00:00Z