All three domains of the hepatitis C virus nonstructural NS5A protein contribute to RNA binding.
about
Rab18 binds to hepatitis C virus NS5A and promotes interaction between sites of viral replication and lipid dropletsStructures of hepatitis C virus nonstructural proteins required for replicase assembly and functionDaclatasvir: potential role in hepatitis CThe crystal structure of NS5A domain 1 from genotype 1a reveals new clues to the mechanism of action for dimeric HCV inhibitorsA quantitative high-resolution genetic profile rapidly identifies sequence determinants of hepatitis C viral fitness and drug sensitivityCoordination of Hepatitis C Virus Assembly by Distinct Regulatory Regions in Nonstructural Protein 5ADEB025 (Alisporivir) inhibits hepatitis C virus replication by preventing a cyclophilin A induced cis-trans isomerisation in domain II of NS5AHepatitis C virus NS5A protein blocks epidermal growth factor receptor degradation via a proline motif- dependent interactionApplications of computer-aided approaches in the development of hepatitis C antiviral agents.Hepatitis C virus nonstructural protein 5A: biochemical characterization of a novel structural class of RNA-binding proteinsThe combination of alisporivir plus an NS5A inhibitor provides additive to synergistic anti-hepatitis C virus activity without detectable cross-resistance.Small molecules targeting hepatitis C virus-encoded NS5A cause subcellular redistribution of their target: insights into compound modes of action.Hepatitis C virus NS5A hijacks ARFGAP1 to maintain a phosphatidylinositol 4-phosphate-enriched microenvironmentModeling shows that the NS5A inhibitor daclatasvir has two modes of action and yields a shorter estimate of the hepatitis C virus half-lifeHepatitis C NS5A protein: two drug targets within the same protein with different mechanisms of resistance.Potent hepatitis C inhibitors bind directly to NS5A and reduce its affinity for RNA.Domain 3 of NS5A protein from the hepatitis C virus has intrinsic alpha-helical propensity and is a substrate of cyclophilin A.Genetic complementation of hepatitis C virus nonstructural protein functions associated with replication exhibits requirements that differ from those for virion assembly.Nonstructural protein 5A (NS5A) and human replication protein A increase the processivity of hepatitis C virus NS5B polymerase activity in vitro.Cyclophilin and NS5A inhibitors, but not other anti-hepatitis C virus (HCV) agents, preclude HCV-mediated formation of double-membrane-vesicle viral factoriesDirect binding of ledipasvir to HCV NS5A: mechanism of resistance to an HCV antiviral agent.The C terminus of NS5A domain II is a key determinant of hepatitis C virus genome replication, but is not required for virion assembly and release.Over-expression and characterization of NS3 and NS5A of Hepatitis C virus genotype 3a.Approaches to hepatitis C treatment and cure using NS5A inhibitorsHepatitis C viral protein translation: mechanisms and implications in developing antivirals.Identification of novel RNA secondary structures within the hepatitis C virus genome reveals a cooperative involvement in genome packagingFunctional characterization of bovine viral diarrhea virus nonstructural protein 5A by reverse genetic analysis and live cell imaging.Suppression of viral RNA binding and the assembly of infectious hepatitis C virus particles in vitro by cyclophilin inhibitors.Inhibition of HCV translation by disrupting the structure and interactions of the viral CRE and 3' X-tail.NS5A inhibitors for the treatment of hepatitis C infection.Intragenic complementation of hepatitis C virus NS5A RNA replication-defective alleles.A conserved tandem cyclophilin-binding site in hepatitis C virus nonstructural protein 5A regulates Alisporivir susceptibility.Polyprotein-Driven Formation of Two Interdependent Sets of Complexes Supporting Hepatitis C Virus Genome Replication.NMR reveals the intrinsically disordered domain 2 of NS5A protein as an allosteric regulator of the hepatitis C virus RNA polymerase NS5B.Correlation between NS5A dimerization and hepatitis C virus replication.A cell-permeable hairpin peptide inhibits hepatitis C viral nonstructural protein 5A-mediated translation and virus productionThe intrinsic disorder status of the human hepatitis C virus proteome.End-to-end crosstalk within the hepatitis C virus genome mediates the conformational switch of the 3'X-tail region.Cyclophilin A interacts with domain II of hepatitis C virus NS5A and stimulates RNA binding in an isomerase-dependent manner.Human single chain-transbodies that bound to domain-I of non-structural protein 5A (NS5A) of hepatitis C virus.
P2860
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P2860
All three domains of the hepatitis C virus nonstructural NS5A protein contribute to RNA binding.
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
All three domains of the hepat ...... ein contribute to RNA binding.
@ast
All three domains of the hepat ...... ein contribute to RNA binding.
@en
All three domains of the hepat ...... ein contribute to RNA binding.
@en-gb
All three domains of the hepat ...... ein contribute to RNA binding.
@nl
type
label
All three domains of the hepat ...... ein contribute to RNA binding.
@ast
All three domains of the hepat ...... ein contribute to RNA binding.
@en
All three domains of the hepat ...... ein contribute to RNA binding.
@en-gb
All three domains of the hepat ...... ein contribute to RNA binding.
@nl
prefLabel
All three domains of the hepat ...... ein contribute to RNA binding.
@ast
All three domains of the hepat ...... ein contribute to RNA binding.
@en
All three domains of the hepat ...... ein contribute to RNA binding.
@en-gb
All three domains of the hepat ...... ein contribute to RNA binding.
@nl
P2860
P50
P356
P1433
P1476
All three domains of the hepat ...... ein contribute to RNA binding.
@en
P2093
Tamara Belyaeva
P2860
P304
P356
10.1128/JVI.00616-10
P407
P577
2010-06-30T00:00:00Z