Two novel conserved motifs in the hepatitis C virus NS3 protein critical for helicase action.
about
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 GenotypesHelicase inhibitors as specifically targeted antiviral therapy for hepatitis CThree conformational snapshots of the hepatitis C virus NS3 helicase reveal a ratchet translocation mechanism.Mechanism and Specificity of a Symmetrical Benzimidazolephenylcarboxamide Helicase InhibitorInvestigation of Translocation, DNA Unwinding, and Protein Displacement by NS3h, the Helicase Domain from the Hepatitis C Virus HelicaseStructural basis for DNA duplex separation by a superfamily-2 helicaseVisualizing ATP-Dependent RNA Translocation by the NS3 Helicase from HCVStructural basis of RNA recognition and activation by innate immune receptor RIG-IThe T4 Phage SF1B Helicase Dda Is Structurally Optimized to Perform DNA Strand SeparationCrystal structure of quinone reductase 2 in complex with resveratrolX-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 GB virus C (GBV-C) NS3 serine protease inhibits HIV-1 replication in a CD4+ T lymphocyte cell line without decreasing HIV receptor expressionThe hepatitis C virus NS3 protein: a model RNA helicase and potential drug targetPrimuline derivatives that mimic RNA to stimulate hepatitis C virus NS3 helicase-catalyzed ATP hydrolysis.Significance of monoclonal antibodies against the conserved epitopes within non-structural protein 3 helicase of hepatitis C virusRobust full-length hepatitis C virus genotype 2a and 2b infectious cultures using mutations identified by a systematic approach applicable to patient strains.Bacteriophage replication modules.Understanding helicases as a means of virus control.The nonstructural protein 3 protease/helicase requires an intact protease domain to unwind duplex RNA efficientlyEnhanced nucleic acid binding to ATP-bound hepatitis C virus NS3 helicase at low pH activates RNA unwinding.Melting of Duplex DNA in the Absence of ATP by the NS3 Helicase Domain through Specific Interaction with a Single-Strand/Double-Strand JunctionElectrostatic analysis of the hepatitis C virus NS3 helicase reveals both active and allosteric site locations.Grip it and rip it: structural mechanisms of DNA helicase substrate binding and unwinding.Mutations in HCV non-structural genes do not contribute to resistance to nitazoxanide in replicon-containing cells.Structure of the DEAH/RHA ATPase Prp43p bound to RNA implicates a pair of hairpins and motif Va in translocation along RNA.Direct fluorometric measurement of hepatitis C virus helicase activity.pH-dependent conformational changes in the HCV NS3 protein modulate its ATPase and helicase activities.The interdomain interface in bifunctional enzyme protein 3/4A (NS3/4A) regulates protease and helicase activities.Structure and Mechanisms of SF1 DNA Helicases.NS3 from Hepatitis C Virus Strain JFH-1 Is an Unusually Robust Helicase That Is Primed To Bind and Unwind Viral RNA.Role of hepatitis C virus proteins (C, NS3, NS5A) in hepatic oncogenesis.Allostery in the dengue virus NS3 helicase: Insights into the NTPase cycle from molecular simulations.
P2860
Q27472781-93882EA4-03E8-4328-B820-EB5D64B9222DQ27478187-98E194D1-094B-46A1-88FD-E14BF4980B1EQ27486248-B53549B4-D1C0-4B01-861B-67D001B8092BQ27488958-FDC9DB30-00B4-4A38-B1DC-7F26E6EE3BB4Q27490905-0610CAD4-33E4-407F-8AD3-5FFD17CF051BQ27491015-49330CEE-E180-407B-A07A-182C959FB6FDQ27491347-5F4DE182-8D72-4C42-B646-A8058518EC53Q27645485-2DCEB2B7-63BC-4580-974A-CAC133782EDAQ27666298-178218FE-C673-4BB7-9D72-8AF247F16109Q27674465-C6CB330D-8775-4668-AAB7-AF1F62BF8FA3Q27679439-23001E43-FE8C-47DC-BB0D-96FBB8D5D747Q28280502-E7738987-42BF-4F6A-8A74-0B352304BF71Q30651534-94225FCC-2F1A-447B-A1AF-6E567EEFE6E3Q34003758-B4152081-D4CA-4C7D-BDAC-F48A378BC27DQ34146275-EB9C44FD-23A5-4E42-98B6-4418DFEB236BQ34607601-BCF23272-C8CF-467A-99C8-515DC02722BCQ34736874-8DA6E00B-D55B-4A09-B250-2D8D2224E9A7Q34875792-F9E2649D-92FE-40F7-A8E0-06D818B5700DQ35935502-6774E72B-6D9A-4B0F-966B-32A4980D156EQ36440552-5984BE7B-4834-495D-9A02-2DB842E207F6Q36447325-A8A6E536-0BAA-4606-AAA1-A651FCE9C001Q36607807-840DBEC2-F3B2-4113-9F3A-E323DDFF8C78Q37346577-098C4FAF-933A-4FBC-8FB3-77FFF0A79865Q37418186-EA04B548-A104-4F0E-AC49-E4D02DB8CFB8Q37592346-43EA8EF9-320A-4F8B-A3DC-DD1929D2E4CBQ38240728-30C2DFF5-475B-497F-99C5-9376A25DDD4BQ39518505-30E29C39-4657-4D61-B22F-D6B25A2F36C7Q40239505-E5929AC2-2985-4FF9-B7BC-B4DBF55580D8Q40549110-1D6C592F-0D46-4AC4-8546-971AFCBA0FCBQ41771076-E6FD286F-2F3A-42FD-B62C-DA2E2FBA844BQ41959786-1796CE54-731A-418F-947D-1779F38ED10BQ42921287-36E652A7-B67C-4CC9-A91F-C766DB9429FAQ43047125-43D75164-876B-4F20-B169-FEB7C4F01F40Q45399951-E901B2B6-A716-4F83-8219-F781354C39B9Q52586095-1AC4D0AF-1809-45B7-BA08-2165A7747768
P2860
Two novel conserved motifs in the hepatitis C virus NS3 protein critical for helicase action.
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
Two novel conserved motifs in ...... critical for helicase action.
@ast
Two novel conserved motifs in ...... critical for helicase action.
@en
type
label
Two novel conserved motifs in ...... critical for helicase action.
@ast
Two novel conserved motifs in ...... critical for helicase action.
@en
prefLabel
Two novel conserved motifs in ...... critical for helicase action.
@ast
Two novel conserved motifs in ...... critical for helicase action.
@en
P2860
P356
P1476
Two novel conserved motifs in ...... critical for helicase action.
@en
P2093
Angela M I Lam
David Keeney
P2860
P304
44514-44524
P356
10.1074/JBC.M306444200
P407
P577
2003-08-27T00:00:00Z