Enhanced nucleic acid binding to ATP-bound hepatitis C virus NS3 helicase at low pH activates RNA unwinding.
about
Functional cross-talk between distant domains of chikungunya virus non-structural protein 2 is decisive for its RNA-modulating activityUpregulation 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 UnwindingEffects of Mutagenic and Chain-Terminating Nucleotide Analogs on Enzymes Isolated from Hepatitis C Virus Strains of Various GenotypesHepatitis C Viral NS3-4A Protease Activity Is Enhanced by the NS3 HelicaseFuel Specificity of the Hepatitis C Virus NS3 HelicaseHelicase inhibitors as specifically targeted antiviral therapy for hepatitis CMechanism and Specificity of a Symmetrical Benzimidazolephenylcarboxamide Helicase InhibitorX-ray structure of the pestivirus NS3 helicase and its conformation in solution.Hepatitis C virus non-structural protein 3 (HCV NS3): a multifunctional antiviral targetThe hepatitis C virus NS3 protein: a model RNA helicase and potential drug targetBenzothiazole and Pyrrolone Flavivirus Inhibitors Targeting the Viral Helicase.Amodiaquine, an antimalarial drug, inhibits dengue virus type 2 replication and infectivity.Understanding helicases as a means of virus control.Fluorescent primuline derivatives inhibit hepatitis C virus NS3-catalyzed RNA unwinding, peptide hydrolysis and viral replicase formation.Electrostatic analysis of the hepatitis C virus NS3 helicase reveals both active and allosteric site locations.Essential role of the N-terminal domain in the regulation of RIG-I ATPase activity.pH-dependent conformational changes in the HCV NS3 protein modulate its ATPase and helicase activities.Binding by the hepatitis C virus NS3 helicase partially melts duplex DNA.The interdomain interface in bifunctional enzyme protein 3/4A (NS3/4A) regulates protease and helicase activities.
P2860
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P2860
Enhanced nucleic acid binding to ATP-bound hepatitis C virus NS3 helicase at low pH activates RNA unwinding.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on 02 August 2004
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Enhanced nucleic acid binding ...... ow pH activates RNA unwinding.
@en
Enhanced nucleic acid binding ...... ow pH activates RNA unwinding.
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type
label
Enhanced nucleic acid binding ...... ow pH activates RNA unwinding.
@en
Enhanced nucleic acid binding ...... ow pH activates RNA unwinding.
@nl
prefLabel
Enhanced nucleic acid binding ...... ow pH activates RNA unwinding.
@en
Enhanced nucleic acid binding ...... ow pH activates RNA unwinding.
@nl
P2860
P356
P1476
Enhanced nucleic acid binding ...... ow pH activates RNA unwinding.
@en
P2093
Angela M I Lam
Ryan S Rypma
P2860
P304
P356
10.1093/NAR/GKH743
P407
P577
2004-08-02T00:00:00Z