A conserved tandem cyclophilin-binding site in hepatitis C virus nonstructural protein 5A regulates Alisporivir susceptibility.
about
Hepatitis C virus NS5B and host cyclophilin A share a common binding site on NS5AChaperones in hepatitis C virus infectionHepatitis C virus RNA replication depends on specific cis- and trans-acting activities of viral nonstructural proteinsCharacterization of the Anti-HCV Activities of the New Cyclophilin Inhibitor STG-175The 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.Hepatitis C NS5A protein: two drug targets within the same protein with different mechanisms of resistance.Intrinsic disorder mediates hepatitis C virus core-host cell protein interactions.Inhibitors of peptidyl proline isomerases as antivirals in hepatitis C and other viruses.Should NS5A inhibitors serve as the scaffold for all-oral anti-HCV combination therapies?The Novel Cyclophilin Inhibitor CPI-431-32 Concurrently Blocks HCV and HIV-1 Infections via a Similar Mechanism of Action.A Proline-Tryptophan Turn in the Intrinsically Disordered Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus RNA ReplicationHepatitis C virus-host interactions, replication, and viral assemblyPhenotypic analysis of NS5A variant from liver transplant patient with increased cyclosporine susceptibilityCyclophilins 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.Subtype specific differences in NS5A domain II reveals involvement of proline at position 310 in cyclosporine susceptibility of hepatitis C virusIntragenic complementation of hepatitis C virus NS5A RNA replication-defective alleles.Multiple mutations in hepatitis C virus NS5A domain II are required to confer a significant level of resistance to alisporivirNMR reveals the intrinsically disordered domain 2 of NS5A protein as an allosteric regulator of the hepatitis C virus RNA polymerase NS5B.
P2860
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P2860
A conserved tandem cyclophilin-binding site in hepatitis C virus nonstructural protein 5A regulates Alisporivir susceptibility.
description
2012 nî lūn-bûn
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2012年の論文
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2012年学术文章
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2012年学术文章
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2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
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2012年學術文章
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name
A conserved tandem cyclophilin ...... es Alisporivir susceptibility.
@en
A conserved tandem cyclophilin ...... es Alisporivir susceptibility.
@nl
type
label
A conserved tandem cyclophilin ...... es Alisporivir susceptibility.
@en
A conserved tandem cyclophilin ...... es Alisporivir susceptibility.
@nl
prefLabel
A conserved tandem cyclophilin ...... es Alisporivir susceptibility.
@en
A conserved tandem cyclophilin ...... es Alisporivir susceptibility.
@nl
P2093
P2860
P356
P1433
P1476
A conserved tandem cyclophilin ...... es Alisporivir susceptibility.
@en
P2093
Hengli Tang
Henry Grisé
Stephen Frausto
Timothy Logan
P2860
P304
P356
10.1128/JVI.06641-11
P407
P50
P577
2012-02-15T00:00:00Z