Cyclophilin A interacts with domain II of hepatitis C virus NS5A and stimulates RNA binding in an isomerase-dependent manner.
about
Chaperones in hepatitis C virus infectionStructures of hepatitis C virus nonstructural proteins required for replicase assembly and functionSeed Sequence-Matched Controls Reveal Limitations of Small Interfering RNA Knockdown in Functional and Structural Studies of Hepatitis C Virus NS5A-MOBKL1B InteractionHCV core residues critical for infectivity are also involved in core-NS5A complex formationHepatitis C virus RNA replication depends on specific cis- and trans-acting activities of viral nonstructural proteinsHepatitis C virus NS5A is able to competitively displace c-Myc from the Bin1 SH3 domain in vitro.The combination of alisporivir plus an NS5A inhibitor provides additive to synergistic anti-hepatitis C virus activity without detectable cross-resistance.Profile of alisporivir and its potential in the treatment of hepatitis C.Cyclophilin and NS5A inhibitors, but not other anti-hepatitis C virus (HCV) agents, preclude HCV-mediated formation of double-membrane-vesicle viral factoriesFast hepatitis C virus RNA elimination and NS5A redistribution by NS5A inhibitors studied by a multiplex assay approachTreating hepatitis C infection by targeting the host.Cyclophilins facilitate dissociation of the human papillomavirus type 16 capsid protein L1 from the L2/DNA complex following virus entry.Hepatitis C virus-host interactions, replication, and viral assemblyHepatitis C virus: virology and life cycleIs there a role for cyclophilin inhibitors in the management of primary biliary cirrhosis?Role of miR-122 and lipid metabolism in HCV infection.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.ISG12a Restricts Hepatitis C Virus Infection through the Ubiquitination-Dependent Degradation Pathway.Phenotypic analysis of NS5A variant from liver transplant patient with increased cyclosporine susceptibilityAnti-HCV drugs in the pipeline.Cyclophilin A as a New Therapeutic Target for Hepatitis C Virus-induced Hepatocellular CarcinomaProteomic identification of cyclophilin A as a potential biomarker and therapeutic target in oral submucous fibrosis.Cyclophilin inhibitors: a novel class of promising host-targeting anti-HCV agents.Cyclophilin involvement in the replication of hepatitis C virus and other viruses.Cyclophilin inhibitors: an emerging class of therapeutics for the treatment of chronic hepatitis C infectionReview of direct-acting antiviral agents for the treatment of chronic hepatitis C.Cyclophilins as modulators of viral replication.The role of immunophilins in viral infection.Suppression of viral RNA binding and the assembly of infectious hepatitis C virus particles in vitro by cyclophilin inhibitors.Entangled in a membranous web: ER and lipid droplet reorganization during hepatitis C virus infection.Peptidylprolyl isomerase A governs TARDBP function and assembly in heterogeneous nuclear ribonucleoprotein complexes.Subtype specific differences in NS5A domain II reveals involvement of proline at position 310 in cyclosporine susceptibility of hepatitis C virusCyclophilin inhibitors block arterivirus replication by interfering with viral RNA synthesis.Multiple mutations in hepatitis C virus NS5A domain II are required to confer a significant level of resistance to alisporivirA conserved tandem cyclophilin-binding site in hepatitis C virus nonstructural protein 5A regulates Alisporivir susceptibility.NMR reveals the intrinsically disordered domain 2 of NS5A protein as an allosteric regulator of the hepatitis C virus RNA polymerase NS5B.Isolation and characterization of hepatitis C virus resistant to a novel phenanthridinone derivative.The cyclophilin inhibitor SCY-635 disrupts hepatitis C virus NS5A-cyclophilin A complexes.Correlation between NS5A dimerization and hepatitis C virus replication.HCV NS5A and IRF9 compete for CypA binding.
P2860
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P2860
Cyclophilin A interacts with domain II of hepatitis C virus NS5A and stimulates RNA binding in an isomerase-dependent manner.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Cyclophilin A interacts with d ...... an isomerase-dependent manner.
@en
Cyclophilin A interacts with d ...... an isomerase-dependent manner.
@en-gb
Cyclophilin A interacts with d ...... an isomerase-dependent manner.
@nl
type
label
Cyclophilin A interacts with d ...... an isomerase-dependent manner.
@en
Cyclophilin A interacts with d ...... an isomerase-dependent manner.
@en-gb
Cyclophilin A interacts with d ...... an isomerase-dependent manner.
@nl
prefLabel
Cyclophilin A interacts with d ...... an isomerase-dependent manner.
@en
Cyclophilin A interacts with d ...... an isomerase-dependent manner.
@en-gb
Cyclophilin A interacts with d ...... an isomerase-dependent manner.
@nl
P2860
P50
P356
P1433
P1476
Cyclophilin A interacts with d ...... an isomerase-dependent manner.
@en
P2093
Philippe Gallay
P2860
P304
P356
10.1128/JVI.00393-11
P407
P577
2011-05-18T00:00:00Z