Molecular basis of telaprevir resistance due to V36 and T54 mutations in the NS3-4A protease of the hepatitis C virus - Wikidata - wikimedia - TriplyDB

Molecular basis of telaprevir resistance due to V36 and T54 mutations in the NS3-4A protease of the hepatitis C virus

Molecular basis of telaprevir resistance due to V36 and T54 mutations in the NS3-4A protease of the hepatitis C virus

http://www.wikidata.org/entity/Q27486122

about

Development of a rapid phenotypic test for HCV protease inhibitors with potential use in clinical decisions HCV genotypes, characterization of mutations conferring drug resistance to protease inhibitors, and risk factors among blood donors in São Paulo, Brazil Topological analysis and interactive visualization of biological networks and protein structures.Global prevalence of pre-existing HCV variants resistant to direct-acting antiviral agents (DAAs): mining the GenBank HCV genome data Telaprevir: an NS3/4A protease inhibitor for the treatment of chronic hepatitis C.Therapeutic implications of hepatitis C virus resistance to antiviral drugs.Computational study on the molecular mechanisms of drug resistance of Narlaprevir due to V36M, R155K, V36M+R155K, T54A, and A156T mutations of HCV NS3/4A protease.Review article: adherence to medication for chronic hepatitis C - building on the model of human immunodeficiency virus antiretroviral adherence research Compensatory mutations restore the replication defects caused by cytotoxic T lymphocyte escape mutations in hepatitis C virus polymerase.Peptidomimetic escape mechanisms arise via genetic diversity in the ligand-binding site of the hepatitis C virus NS3/4A serine protease.Novel human anti-claudin 1 mAbs inhibit hepatitis C virus infection and may synergize with anti-SRB1 mAb.One-Step Recovery of scFv Clones from High-Throughput Sequencing-Based Screening of Phage Display Libraries Challenged to Cells Expressing Native Claudin-1.Ketoamide resistance and hepatitis C virus fitness in val55 variants of the NS3 serine protease.Biomedical Mutation Analysis (BMA): A software tool for analyzing mutations associated with antiviral resistance Resistance mechanisms in HCV: from evolution to intervention.A 3D structural model and dynamics of hepatitis C virus NS3/4A protease (genotype 4a, strain ED43) suggest conformational instability of the catalytic triad: implications in catalysis and drug resistivity.The efficacy and safety of telaprevir - a new protease inhibitor against hepatitis C virus.Overview of the PROVE studies evaluating the use of telaprevir in chronic hepatitis C genotype 1 patients.A new standard of care for the treatment of chronic HCV infection.Resistance-associated variants in chronic hepatitis C patients treated with protease inhibitors.UK consensus guidelines for the use of the protease inhibitors boceprevir and telaprevir in genotype 1 chronic hepatitis C infected patients.Telaprevir: a review of its use in the management of genotype 1 chronic hepatitis C.Treatment decisions and contemporary versus pending treatments for hepatitis C.Comparative study of the genetic barriers and pathways towards resistance of selective inhibitors of hepatitis C virus replication.Response of hepatitis C virus to long-term passage in the presence of alpha interferon: multiple mutations and a common phenotype.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.Genotype differences in susceptibility and resistance development of hepatitis C virus to protease inhibitors telaprevir (VX-950) and danoprevir (ITMN-191).Hepatitis C variability, patterns of resistance, and impact on therapy Single Active Site Mutation Causes Serious Resistance of HIV Reverse Transcriptase to Lamivudine: Insight from Multiple Molecular Dynamics Simulations.Computational study on the drug resistance mechanism of HCV NS3 protease to BMS-605339.Viral Surveillance in Serum Samples From Patients With Acute Liver Failure By Metagenomic Next-Generation Sequencing.Protease inhibitor resistance mutations in untreated Brazilian patients infected with HCV: novel insights about targeted genotyping approaches.HCV enters the twenty-first century.The presence of resistance mutations to protease and polymerase inhibitors in Hepatitis C virus sequences from the Los Alamos databank.Characterization of resistance to the protease inhibitor boceprevir in hepatitis C virus-infected patients.Fractionation and identification of metalloproteins from a marine cyanobacterium.Characterization of naturally occurring protease inhibitor-resistance mutations in genotype 1b hepatitis C virus patients.

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Molecular basis of telaprevir resistance due to V36 and T54 mutations in the NS3-4A protease of the hepatitis C virus

http://www.wikidata.org/entity/Q27486122

description

2008 nî lūn-bûn

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2008 թուականի Յունուարին հրատարակուած գիտական յօդուած

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Molecular basis of telaprevir ...... tease of the hepatitis C virus

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P2860

The RCSB PDB information portal for structural genomics.

The Universal Protein Resource (UniProt): an expanding universe of protein information.

Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

MUSCLE: multiple sequence alignment with high accuracy and high throughput

Enhancement of hepatitis C virus RNA replication by cell culture-adaptive mutations.

SCH 503034, a mechanism-based inhibitor of hepatitis C virus NS3 protease, suppresses polyprotein maturation and enhances the antiviral activity of alpha interferon in replicon cells.

Complex of NS3 protease and NS4A peptide of BK strain hepatitis C virus: A 2.2 Å resolution structure in a hexagonal crystal form

The solution structure of the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein provides new insights into its activation and catalytic mechanism

Inhibition of the hepatitis C virus NS3/4A protease. The crystal structures of two protease-inhibitor complexes

Pyrrolidine-5,5-trans-lactams. 4. Incorporation of a P3/P4 urea leads to potent intracellular inhibitors of hepatitis C virus NS3/4A protease

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