Regulation of de novo-initiated RNA synthesis in hepatitis C virus RNA-dependent RNA polymerase by intermolecular interactions.
about
Hepatitis C virus NS5B and host cyclophilin A share a common binding site on NS5ARNA-Dependent RNA Polymerases of Picornaviruses: From the Structure to Regulatory MechanismsCommon and unique features of viral RNA-dependent polymerasesAssembly, purification, and pre-steady-state kinetic analysis of active RNA-dependent RNA polymerase elongation complexThe Structure of the RNA-Dependent RNA Polymerase of a Permutotetravirus Suggests a Link between Primer-Dependent and Primer-Independent PolymerasesInitiation of RNA synthesis by the hepatitis C virus RNA-dependent RNA polymerase is affected by the structure of the RNA template.De novo polymerase activity and oligomerization of hepatitis C virus RNA-dependent RNA-polymerases from genotypes 1 to 5Viral double-strand RNA-binding proteins can enhance innate immune signaling by toll-like Receptor 3.Phosphorylation of hepatitis C virus RNA polymerases ser29 and ser42 by protein kinase C-related kinase 2 regulates viral RNA replication.Identification and functional characterization of the nascent RNA contacting residues of the hepatitis C virus RNA-dependent RNA polymerase.Affinity labeling of hepatitis C virus replicase with a nucleotide analogue: identification of binding site.Structural basis for RNA-genome recognition during bacteriophage Qβ replication.Residues Arg283, Arg285, and Ile287 in the nucleotide binding pocket of bovine viral diarrhea virus NS5B RNA polymerase affect catalysis and fidelity.Viruses and viral proteins.Interference of hepatitis C virus replication in cell culture by antisense peptide nucleic acids targeting the X-RNA.Norovirus RNA-dependent RNA polymerase is phosphorylated by an important survival kinase, AktThe classic swine fever virus (CSFV) core protein can enhance de novo-initiated RNA synthesis by the CSFV polymerase NS5B.Biochemical study of the comparative inhibition of hepatitis C virus RNA polymerase by VX-222 and filibuvir.NMR reveals the intrinsically disordered domain 2 of NS5A protein as an allosteric regulator of the hepatitis C virus RNA polymerase NS5B.Interstitial contacts in an RNA-dependent RNA polymerase lattice.Purification and Biochemical Characterisation of Rabbit Calicivirus RNA-Dependent RNA Polymerases and Identification of Non-Nucleoside InhibitorsStructural and regulatory elements of HCV NS5B polymerase--β-loop and C-terminal tail--are required for activity of allosteric thumb site II inhibitors.Surface for catalysis by poliovirus RNA-dependent RNA polymerase.A Crystal Structure of Classical Swine Fever Virus NS5B Reveals a Novel N-terminal Domain.
P2860
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P2860
Regulation of de novo-initiated RNA synthesis in hepatitis C virus RNA-dependent RNA polymerase by intermolecular interactions.
description
2010 nî lūn-bûn
@nan
2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年学术文章
@wuu
2010年学术文章
@zh-cn
2010年学术文章
@zh-hans
2010年学术文章
@zh-my
2010年学术文章
@zh-sg
2010年學術文章
@yue
name
Regulation of de novo-initiate ...... y intermolecular interactions.
@ast
Regulation of de novo-initiate ...... y intermolecular interactions.
@en
type
label
Regulation of de novo-initiate ...... y intermolecular interactions.
@ast
Regulation of de novo-initiate ...... y intermolecular interactions.
@en
prefLabel
Regulation of de novo-initiate ...... y intermolecular interactions.
@ast
Regulation of de novo-initiate ...... y intermolecular interactions.
@en
P2093
P2860
P356
P1433
P1476
Regulation of de novo-initiate ...... by intermolecular interactions
@en
P2093
P2860
P304
P356
10.1128/JVI.02446-09
P577
2010-04-07T00:00:00Z