A novel recombinant single-chain hepatitis C virus ns3-ns4a protein with improved helicase activity
about
Comparative characterization of two DEAD-box RNA helicases in superfamily II: human translation-initiation factor 4A and hepatitis C virus non-structural protein 3 (NS3) helicaseSimultaneously Targeting the NS3 Protease and Helicase Activities for More Effective Hepatitis C Virus TherapyVirus-specific cofactor requirement and chimeric hepatitis C virus/GB virus B nonstructural protein 3Stimulation of hepatitis C virus (HCV) nonstructural protein 3 (NS3) helicase activity by the NS3 protease domain and by HCV RNA-dependent RNA polymeraseThe hepatitis C viral NS3 protein is a processive DNA helicase with cofactor enhanced RNA unwinding.Hepatitis C Virus NS3 ATPases/Helicases from Different Genotypes Exhibit Variations in Enzymatic PropertiesSingle Strand Binding Proteins Increase the Processivity of DNA Unwinding by the Hepatitis C Virus HelicaseFuel Specificity of the Hepatitis C Virus NS3 HelicaseA Method to Simultaneously Monitor Hepatitis C Virus NS3 Helicase and Protease ActivitiesNtr1 activates the Prp43 helicase to trigger release of lariat-intron from the spliceosomeMolecular determinants of TRIF proteolysis mediated by the hepatitis C virus NS3/4A proteaseThe protease domain increases the translocation stepping efficiency of the hepatitis C virus NS3-4A helicase.Hepatitis C virus NS2/3 processing is required for NS3 stability and viral RNA replication.The hepatitis C virus NS3 protein: a model RNA helicase and potential drug targetProtease inhibitor-resistant hepatitis C virus mutants with reduced fitness from impaired production of infectious virusNonstructural protein 5A (NS5A) and human replication protein A increase the processivity of hepatitis C virus NS5B polymerase activity in vitro.Establishment of a simple assay in vitro for hepatitis C virus NS3 serine protease based on recombinant substrate and single-chain proteaseThe nonstructural protein 3 protease/helicase requires an intact protease domain to unwind duplex RNA efficientlyFluorescent primuline derivatives inhibit hepatitis C virus NS3-catalyzed RNA unwinding, peptide hydrolysis and viral replicase formation.A Brownian motor mechanism of translocation and strand separation by hepatitis C virus helicase.Nucleic acid unwinding by hepatitis C virus and bacteriophage t7 helicases is sensitive to base pair stability.Emerging therapies for hepatitis C virus infection.The functional interaction of the hepatitis C virus helicase molecules is responsible for unwinding processivity.
P2860
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P2860
A novel recombinant single-chain hepatitis C virus ns3-ns4a protein with improved helicase activity
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
A novel recombinant single-cha ...... ith improved helicase activity
@ast
A novel recombinant single-cha ...... ith improved helicase activity
@en
A novel recombinant single-cha ...... ith improved helicase activity
@nl
type
label
A novel recombinant single-cha ...... ith improved helicase activity
@ast
A novel recombinant single-cha ...... ith improved helicase activity
@en
A novel recombinant single-cha ...... ith improved helicase activity
@nl
prefLabel
A novel recombinant single-cha ...... ith improved helicase activity
@ast
A novel recombinant single-cha ...... ith improved helicase activity
@en
A novel recombinant single-cha ...... ith improved helicase activity
@nl
P2093
P2860
P356
P1433
P1476
A novel recombinant single-cha ...... ith improved helicase activity
@en
P2093
S S Taremi
P2860
P304
P356
10.1110/PS.8.6.1332
P577
1999-06-01T00:00:00Z