In vitro characterization of a purified NS2/3 protease variant of hepatitis C virus.
about
Complete translation of the hepatitis C virus genome in vitro: membranes play a critical role in the maturation of all virus proteins except for NS3.PKR-dependent mechanisms of gene expression from a subgenomic hepatitis C virus clone.Construction and characterization of infectious intragenotypic and intergenotypic hepatitis C virus chimerasProtein-Protein Interactions between Hepatitis C Virus Nonstructural ProteinsNS3 Helicase Domains Involved in Infectious Intracellular Hepatitis C Virus Particle AssemblyDevelopment of Intergenotypic Chimeric Replicons To Determine the Broad-Spectrum Antiviral Activities of Hepatitis C Virus Polymerase InhibitorsHepatitis C virus NS2 is a protease stimulated by cofactor domains in NS3Determinants of the Hepatitis C Virus Nonstructural Protein 2 Protease Domain Required for Production of Infectious VirusA comparative analysis of the fluorescence properties of the wild-type and active site mutants of the hepatitis C virus autoprotease NS2-3Hepatitis C virus NS2/3 processing is required for NS3 stability and viral RNA replication.Structure of the catalytic domain of the hepatitis C virus NS2-3 protease.Targeting the non-structural proteins of hepatitis C virus: beyond hepatitis C virus protease and polymerase.Mechanisms of drug resistance and novel approaches to therapy for chronic hepatitis C.Epoxide based inhibitors of the hepatitis C virus non-structural 2 autoproteaseRecent developments in target identification against hepatitis C virus.Hepatitis C Virus Proteins Interact with the Endosomal Sorting Complex Required for Transport (ESCRT) Machinery via Ubiquitination To Facilitate Viral Envelopment.Current drug discovery strategies for treatment of hepatitis C virus infection.The Hepatitis C Virus Nonstructural Protein 2 (NS2): An Up-and-Coming Antiviral Drug Target.Current and future therapies for hepatitis C virus infection: from viral proteins to host targets.Zinc is a negative regulator of hepatitis C virus RNA replication.Identification of residues involved in NS2 homodimerization and elucidation of their impact on the HCV life cycle.An NS3 serine protease inhibitor abrogates replication of subgenomic hepatitis C virus RNA.NS2 proteases from hepatitis C virus and related hepaciviruses share composite active sites and previously unrecognized intrinsic proteolytic activities.
P2860
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P2860
In vitro characterization of a purified NS2/3 protease variant of hepatitis C virus.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh-hant
name
In vitro characterization of a purified NS2/3 protease variant of hepatitis C virus.
@en
In vitro characterization of a purified NS2/3 protease variant of hepatitis C virus.
@nl
type
label
In vitro characterization of a purified NS2/3 protease variant of hepatitis C virus.
@en
In vitro characterization of a purified NS2/3 protease variant of hepatitis C virus.
@nl
prefLabel
In vitro characterization of a purified NS2/3 protease variant of hepatitis C virus.
@en
In vitro characterization of a purified NS2/3 protease variant of hepatitis C virus.
@nl
P2093
P2860
P356
P1476
In vitro characterization of a purified NS2/3 protease variant of hepatitis C virus.
@en
P2093
P2860
P304
46678-46684
P356
10.1074/JBC.M108266200
P407
P577
2001-10-08T00:00:00Z