Phenotypic Characterization of Resistant Val36 Variants of Hepatitis C Virus NS3-4A Serine Protease - Wikidata - wikimedia - TriplyDB

Phenotypic Characterization of Resistant Val36 Variants of Hepatitis C Virus NS3-4A Serine Protease

Phenotypic Characterization of Resistant Val36 Variants of Hepatitis C Virus NS3-4A Serine Protease

http://www.wikidata.org/entity/Q27485288

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Hepatitis C virus protease inhibitor-resistance mutations: our experience and review Development of a rapid phenotypic test for HCV protease inhibitors with potential use in clinical decisions Relative Replication Capacity and Selective Advantage Profiles of Protease Inhibitor-Resistant Hepatitis C Virus (HCV) NS3 Protease Mutants in the HCV Genotype 1b Replicon System Naturally occurring dominant resistance mutations to hepatitis C virus protease and polymerase inhibitors in treatment-naïve patients Drug resistance against HCV NS3/4A inhibitors is defined by the balance of substrate recognition versus inhibitor binding A multi-variant, viral dynamic model of genotype 1 HCV to assess the in vivo evolution of protease-inhibitor resistant variants Probing of exosites leads to novel inhibitor scaffolds of HCV NS3/4A proteinase Geno2pheno[HCV] - A Web-based Interpretation System to Support Hepatitis C Treatment Decisions in the Era of Direct-Acting Antiviral Agents Treatment of hepatitis C with an interferon-based lead-in phase: a perspective from mathematical modelling Modelling clinical data shows active tissue concentration of daclatasvir is 10-fold lower than its plasma concentration.Characterization of V36C, a novel amino acid substitution conferring hepatitis C virus (HCV) resistance to telaprevir, a potent peptidomimetic inhibitor of HCV protease.Preclinical characterization of the antiviral activity of SCH 900518 (narlaprevir), a novel mechanism-based inhibitor of hepatitis C virus NS3 protease.A viral dynamic model for treatment regimens with direct-acting antivirals for chronic hepatitis C infection.Therapeutic implications of hepatitis C virus resistance to antiviral drugs.Rapid emergence of protease inhibitor resistance in hepatitis C virus.Hepatitis C virus drug resistance and immune-driven adaptations: relevance to new antiviral therapy.From resistance to stimulation: the evolution of a virus in the presence of a dominant lethal inhibitory scaffolding protein.Protease inhibitor-resistant hepatitis C virus mutants with reduced fitness from impaired production of infectious virus Ribavirin Inhibits Parrot Bornavirus 4 Replication in Cell Culture Modeling quasispecies and drug resistance in hepatitis C patients treated with a protease inhibitor Naturally occurring mutations to HCV protease inhibitors in treatment-naïve patients.Virological response and safety of 24-week telaprevir alone in Japanese patients infected with hepatitis C virus subtype 1b.ve-SEQ: Robust, unbiased enrichment for streamlined detection and whole-genome sequencing of HCV and other highly diverse pathogens Evaluating the Role of Cellular Immune Responses in the Emergence of HCV NS3 Resistance Mutations During Protease Inhibitor Therapy Hepatitis C Virus Genotype 1 to 6 Protease Inhibitor Escape Variants: In Vitro Selection, Fitness, and Resistance Patterns in the Context of the Infectious Viral Life Cycle.Improving Viral Protease Inhibitors to Counter Drug Resistance.Avoiding therapeutic pitfalls: the rational use of specifically targeted agents against hepatitis C infection.Viral adaptation to an antiviral protein enhances the fitness level to above that of the uninhibited wild type The efficacy and safety of telaprevir - a new protease inhibitor against hepatitis C virus.Viral response to specifically targeted antiviral therapy for hepatitis C and the implications for treatment success.Emerging therapies for hepatitis C virus.Overview of the PROVE studies evaluating the use of telaprevir in chronic hepatitis C genotype 1 patients.Telaprevir: a novel NS3/4 protease inhibitor for the treatment of hepatitis C.Resistance-associated variants in chronic hepatitis C patients treated with protease inhibitors.Telaprevir: a review of its use in the management of genotype 1 chronic hepatitis C.Natural prevalence of hepatitis C virus (HCV) variants resistant to protease and polymerase inhibitors in patients infected with HCV genotype 1 in Tunisia.Resistance Mechanisms in Hepatitis C Virus: implications for Direct-Acting Antiviral Use.Pharmacodynamic analysis of a serine protease inhibitor, MK-4519, against hepatitis C virus using a novel in vitro pharmacodynamic system.Biochemical evaluation of HCV NS3 protease inhibitors.Hepatitis C variability, patterns of resistance, and impact on therapy

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Phenotypic Characterization of Resistant Val36 Variants of Hepatitis C Virus NS3-4A Serine Protease

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2008 nî lūn-bûn

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2008 թվականի հունվարին հրատարակված գիտական հոդված

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Ute Müh

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P2860

Mutations conferring resistance to a hepatitis C virus (HCV) RNA-dependent RNA polymerase inhibitor alone or in combination with an HCV serine protease inhibitor in vitro.

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

Preclinical profile of VX-950, a potent, selective, and orally bioavailable inhibitor of hepatitis C virus NS3-4A serine protease

VX-950, a Novel Hepatitis C Virus (HCV) NS3-4A Protease Inhibitor, Exhibits Potent Antiviral Activities in HCV Replicon Cells

Selection and Characterization of Replicon Variants Dually Resistant to Thumb- and Palm-Binding Nonnucleoside Polymerase Inhibitors of the Hepatitis C Virus

In Vitro Selection and Characterization of Hepatitis C Virus Serine Protease Variants Resistant to an Active-Site Peptide Inhibitor

Molecular Mechanism of a Thumb Domain Hepatitis C Virus Nonnucleoside RNA-Dependent RNA Polymerase Inhibitor

A central region in the hepatitis C virus NS4A protein allows formation of an active NS3-NS4A serine proteinase complex in vivo and in vitro

Expression and identification of hepatitis C virus polyprotein cleavage products

Characterization of the hepatitis C virus-encoded serine proteinase: determination of proteinase-dependent polyprotein cleavage sites

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Hepatitis C virus

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