The nonstructural protein 3 protease/helicase requires an intact protease domain to unwind duplex RNA efficiently
about
Hepatitis C virus proteinsFunctional cross-talk between distant domains of chikungunya virus non-structural protein 2 is decisive for its RNA-modulating activitySimultaneously Targeting the NS3 Protease and Helicase Activities for More Effective Hepatitis C Virus TherapyStructures of hepatitis C virus nonstructural proteins required for replicase assembly and functionStructure of the Dengue Virus Helicase/Nucleoside Triphosphatase Catalytic Domain at a Resolution of 2.4 AUpregulation of protein phosphatase 2Ac by hepatitis C virus modulates NS3 helicase activity through inhibition of protein arginine methyltransferase 1.Hepatitis C virus subgenomic replicon requires an active NS3 RNA helicase.Role of Divalent Metal Cations in ATP Hydrolysis Catalyzed by the Hepatitis C Virus NS3 Helicase: Magnesium Provides a Bridge for ATP to Fuel UnwindingThe C Terminus of Hepatitis C Virus NS4A Encodes an Electrostatic Switch That Regulates NS5A Hyperphosphorylation and Viral ReplicationCrystal Structure of the NS3 Protease-Helicase from Dengue VirusSingle Strand Binding Proteins Increase the Processivity of DNA Unwinding by the Hepatitis C Virus HelicaseAnalysis of the Evolutionary Forces in an Immunodominant CD8 Epitope in Hepatitis C Virus at a Population LevelEffects of Mutagenic and Chain-Terminating Nucleotide Analogs on Enzymes Isolated from Hepatitis C Virus Strains of Various GenotypesThe Two-component NS2B-NS3 Proteinase Represses DNA Unwinding Activity of the West Nile Virus NS3 HelicaseHepatitis C virus NS3 helicase forms oligomeric structures that exhibit optimal DNA unwinding activity in vitroHepatitis C Viral NS3-4A Protease Activity Is Enhanced by the NS3 HelicaseThe NS4A Protein of Hepatitis C Virus Promotes RNA-Coupled ATP Hydrolysis by the NS3 HelicaseFuel Specificity of the Hepatitis C Virus NS3 HelicaseSlow Binding Inhibition and Mechanism of Resistance of Non-nucleoside Polymerase Inhibitors of Hepatitis C VirusHelicase inhibitors as specifically targeted antiviral therapy for hepatitis CHepatitis C Virus NS2 Protein Contributes to Virus Particle Assembly via Opposing Epistatic Interactions with the E1-E2 Glycoprotein and NS3-NS4A Enzyme ComplexesThree conformational snapshots of the hepatitis C virus NS3 helicase reveal a ratchet translocation mechanism.Mechanism and Specificity of a Symmetrical Benzimidazolephenylcarboxamide Helicase InhibitorInterplay between NS3 protease and human La protein regulates translation-replication switch of Hepatitis C virusVisualizing ATP-Dependent RNA Translocation by the NS3 Helicase from HCVThe protease domain increases the translocation stepping efficiency of the hepatitis C virus NS3-4A helicase.Preparation of HCV NS3 and NS5B proteins to support small-molecule drug discovery.Novel ATP-independent RNA annealing activity of the dengue virus NS3 helicaseIdentification and analysis of hepatitis C virus NS3 helicase inhibitors using nucleic acid binding assaysThe intraviral protein interaction network of hepatitis C virus.The hepatitis C virus NS3 protein: a model RNA helicase and potential drug targetAurintricarboxylic acid modulates the affinity of hepatitis C virus NS3 helicase for both nucleic acid and ATPNonstructural protein 5A (NS5A) and human replication protein A increase the processivity of hepatitis C virus NS5B polymerase activity in vitro.Amodiaquine, an antimalarial drug, inhibits dengue virus type 2 replication and infectivity.HCV Induces Telomerase Reverse Transcriptase, Increases Its Catalytic Activity, and Promotes Caspase Degradation in Infected Human HepatocytesRNA binding by the NS3 protease of the hepatitis C virusFrom structure to function: new insights into hepatitis C virus RNA replication.Understanding helicases as a means of virus control.Identification and analysis of inhibitors targeting the hepatitis C virus NS3 helicaseFluorescent primuline derivatives inhibit hepatitis C virus NS3-catalyzed RNA unwinding, peptide hydrolysis and viral replicase formation.
P2860
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P2860
The nonstructural protein 3 protease/helicase requires an intact protease domain to unwind duplex RNA efficiently
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
The nonstructural protein 3 pr ...... unwind duplex RNA efficiently
@ast
The nonstructural protein 3 pr ...... unwind duplex RNA efficiently
@en
type
label
The nonstructural protein 3 pr ...... unwind duplex RNA efficiently
@ast
The nonstructural protein 3 pr ...... unwind duplex RNA efficiently
@en
prefLabel
The nonstructural protein 3 pr ...... unwind duplex RNA efficiently
@ast
The nonstructural protein 3 pr ...... unwind duplex RNA efficiently
@en
P2093
P2860
P356
P1476
The nonstructural protein 3 pr ...... unwind duplex RNA efficiently
@en
P2093
Angela M I Lam
Ryan S Rypma
P2860
P304
P356
10.1074/JBC.M310630200
P407
P577
2003-10-29T00:00:00Z