Domain 3 of NS5A protein from the hepatitis C virus has intrinsic alpha-helical propensity and is a substrate of cyclophilin A. - sprookjes - yvandenbroek - TriplyDB

Domain 3 of NS5A protein from the hepatitis C virus has intrinsic alpha-helical propensity and is a substrate of cyclophilin A.

Domain 3 of NS5A protein from the hepatitis C virus has intrinsic alpha-helical propensity and is a substrate of cyclophilin A.

http://www.wikidata.org/entity/Q35063336

about

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 Chaperones in hepatitis C virus infection Virologic Tools for HCV Drug Resistance Testing Structures of hepatitis C virus nonstructural proteins required for replicase assembly and function Hepatitis C virus RNA replication depends on specific cis- and trans-acting activities of viral nonstructural proteins Both Cyclophilin Inhibitors and Direct-Acting Antivirals Prevent PKR Activation in HCV-Infected Cells.Hepatitis C virus NS5A inhibitors and drug resistance mutations.Potent hepatitis C inhibitors bind directly to NS5A and reduce its affinity for RNA.Structural and molecular basis of interaction of HCV non-structural protein 5A with human casein kinase 1α and PKR.Intrinsic disorder mediates hepatitis C virus core-host cell protein interactions.Nonstructural protein 5A (NS5A) and human replication protein A increase the processivity of hepatitis C virus NS5B polymerase activity in vitro.Cyclophilin and NS5A inhibitors, but not other anti-hepatitis C virus (HCV) agents, preclude HCV-mediated formation of double-membrane-vesicle viral factories Should NS5A inhibitors serve as the scaffold for all-oral anti-HCV combination therapies?A Proline-Tryptophan Turn in the Intrinsically Disordered Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus RNA Replication Cyclophilins facilitate dissociation of the human papillomavirus type 16 capsid protein L1 from the L2/DNA complex following virus entry.Hepatitis C virus-host interactions, replication, and viral assembly Coevolution analysis of Hepatitis C virus genome to identify the structural and functional dependency network of viral proteins.Phenotypic analysis of NS5A variant from liver transplant patient with increased cyclosporine susceptibility Anti-HCV drugs in the pipeline.Cyclophilin A as a New Therapeutic Target for Hepatitis C Virus-induced Hepatocellular Carcinoma Activity of hexokinase is increased by its interaction with hepatitis C virus protein NS5A.Hepatitis C virus assembly imaging Cyclophilin inhibitors: a novel class of promising host-targeting anti-HCV agents.The molecular and structural basis of advanced antiviral therapy for hepatitis C virus infection.Cyclophilins as modulators of viral replication.The role of immunophilins in viral infection.Functional characterization of bovine viral diarrhea virus nonstructural protein 5A by reverse genetic analysis and live cell imaging.Direct-acting antiviral agents for hepatitis C: structural and mechanistic insights.Fluorescence resonance energy transfer-based intracellular assay for the conformation of hepatitis C virus drug target NS5A.A conserved tandem cyclophilin-binding site in hepatitis C virus nonstructural protein 5A regulates Alisporivir susceptibility.NMR reveals the intrinsically disordered domain 2 of NS5A protein as an allosteric regulator of the hepatitis C virus RNA polymerase NS5B.The Casein Kinase 2-Dependent Phosphorylation of NS5A Domain 3 from Hepatitis C Virus Followed by Time-Resolved NMR Spectroscopy.Novel nucleoside analogues targeting HCV replication through an NS5A-dependent inhibition mechanism.New insights regarding HCV-NS5A structure/function and indication of genotypic differences.The cyclophilin inhibitor SCY-635 disrupts hepatitis C virus NS5A-cyclophilin A complexes.Correlation between NS5A dimerization and hepatitis C virus replication.HCV NS5A and IRF9 compete for CypA binding.The intrinsic disorder status of the human hepatitis C virus proteome.Intracellular hepatitis C modeling predicts infection dynamics and viral protein mechanisms.

P2860

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P2860

Domain 3 of NS5A protein from the hepatitis C virus has intrinsic alpha-helical propensity and is a substrate of cyclophilin A.

http://www.wikidata.org/entity/Q35063336

description

2011 nî lūn-bûn

@nan

2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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Domain 3 of NS5A protein from ...... a substrate of cyclophilin A.

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Domain 3 of NS5A protein from ...... a substrate of cyclophilin A.

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JBC.M110.182436

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Journal of Biological Chemistry

P1476

Domain 3 of NS5A protein from ...... a substrate of cyclophilin A.

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P2093

Arnaud Leroy

http://www.w3.org/2001/XMLSchema#string

Aurélie Badillo

http://www.w3.org/2001/XMLSchema#string

Dries Verdegem

http://www.w3.org/2001/XMLSchema#string

François Penin

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P2860

Intrinsically Disordered Proteins in Human Diseases: Introducing the D 2 Concept

Cyclophilin B is a functional regulator of hepatitis C virus RNA polymerase

Hepatitis C virus infection protein network

Multiple cyclophilins involved in different cellular pathways mediate HCV replication

Association of hepatitis C virus replication complexes with microtubules and actin filaments is dependent on the interaction of NS3 and NS5A

Debio 025, a cyclophilin binding molecule, is highly efficient in clearing hepatitis C virus (HCV) replicon-containing cells when used alone or in combination with specifically targeted antiviral therapy for HCV (STAT-C) inhibitors

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

A simple method for displaying the hydropathic character of a protein

Hepatitis C virus core protein is a dimeric alpha-helical protein exhibiting membrane protein features.

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

P304

20441-20454

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scholarly article

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10.1074/JBC.M110.182436

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23

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P478

286

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Ralf Bartenschlager

Xavier Hanoulle

Jean-Michel Wieruszeski

Isabelle Landrieu

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2011-04-13T00:00:00Z

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51048422

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21489988

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3121464

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