Sensitivity of hepatitis C virus to cyclosporine A depends on nonstructural proteins NS5A and NS5B.
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Cyclosporin A associated helicase-like protein facilitates the association of hepatitis C virus RNA polymerase with its cellular cyclophilin BHepatitis C virus NS5B and host cyclophilin A share a common binding site on NS5AA single-amino-acid mutation in hepatitis C virus NS5A disrupting FKBP8 interaction impairs viral replicationChaperones in hepatitis C virus infectionCyclophilin A Is an Essential Cofactor for Hepatitis C Virus Infection and the Principal Mediator of Cyclosporine Resistance In VitroCombinations of Cyclophilin Inhibitor NIM811 with Hepatitis C Virus NS3-4A Protease or NS5B Polymerase Inhibitors Enhance Antiviral Activity and Suppress the Emergence of ResistanceCyclophilin B stimulates RNA synthesis by the HCV RNA dependent RNA polymeraseHepatitis C Virus NS5A Protein Is a Substrate for the Peptidyl-prolyl cis/trans Isomerase Activity of Cyclophilins A and BCritical Role of Cyclophilin A and Its Prolyl-Peptidyl Isomerase Activity in the Structure and Function of the Hepatitis C Virus Replication ComplexEssential Role of Cyclophilin A for Hepatitis C Virus Replication and Virus Production and Possible Link to Polyprotein Cleavage KineticsThe Isomerase Active Site of Cyclophilin A Is Critical for Hepatitis C Virus ReplicationMutations in the hepatitis C virus polymerase that increase RNA binding can confer resistance to cyclosporine AA Conserved Proline between Domains II and III of Hepatitis C Virus NS5A Influences both RNA Replication and Virus AssemblyCyclosporine Inhibits a Direct Interaction between Cyclophilins and Hepatitis C NS5AMy Cousin, My Enemy: quasispecies suppression of drug resistanceA cell-based assay for RNA synthesis by the HCV polymerase reveals new insights on mechanism of polymerase inhibitors and modulation by NS5ADEB025 (Alisporivir) inhibits hepatitis C virus replication by preventing a cyclophilin A induced cis-trans isomerisation in domain II of NS5AA major determinant of cyclophilin dependence and cyclosporine susceptibility of hepatitis C virus identified by a genetic approachIncreasing rate of cleavage at boundary between non-structural proteins 4B and 5A inhibits replication of hepatitis C virus.Ethanol and reactive species increase basal sequence heterogeneity of hepatitis C virus and produce variants with reduced susceptibility to antivirals.Evidence for separation of HCV subtype 1a into two distinct clades.Therapeutic implications of hepatitis C virus resistance to antiviral drugs.Targeting the non-structural proteins of hepatitis C virus: beyond hepatitis C virus protease and polymerase.Management of hepatitis C in patients with chronic kidney disease.Domain 3 of NS5A protein from the hepatitis C virus has intrinsic alpha-helical propensity and is a substrate of cyclophilin A.Choice of Biologic Therapy for Patients with Rheumatoid Arthritis: The Infection Perspective.Inhibitors of peptidyl proline isomerases as antivirals in hepatitis C and other viruses.Association of IL28B SNPs rs12979860 and rs8099917 on Hepatitis C Virus-RNA Status in Donors/Recipients of Living Donor Liver Transplantation.Expression of cyclophilin B is associated with malignant progression and regulation of genes implicated in the pathogenesis of breast cancer.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 CarcinomaCyclophilin inhibitors: a novel class of promising host-targeting anti-HCV agents.Cyclophilin inhibitors: an emerging class of therapeutics for the treatment of chronic hepatitis C infectionCyclophilins 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.Cyclophilin inhibitors as a novel HCV therapy.Increased replicative fitness can lead to decreased drug sensitivity of hepatitis C virus.Subtype specific differences in NS5A domain II reveals involvement of proline at position 310 in cyclosporine susceptibility of hepatitis C virus
P2860
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P2860
Sensitivity of hepatitis C virus to cyclosporine A depends on nonstructural proteins NS5A and NS5B.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
@zh
2007年學術文章
@zh-hant
name
Sensitivity of hepatitis C vir ...... ctural proteins NS5A and NS5B.
@en
type
label
Sensitivity of hepatitis C vir ...... ctural proteins NS5A and NS5B.
@en
prefLabel
Sensitivity of hepatitis C vir ...... ctural proteins NS5A and NS5B.
@en
P2093
P356
P1433
P1476
Sensitivity of hepatitis C vir ...... ctural proteins NS5A and NS5B.
@en
P2093
Adin-Cristian Andrei
Daniel S Poole
Fiona Fernandes
Justin Gerstner
Rannveig Middleton
Rob Striker
Spencer Hoover
P304
P356
10.1002/HEP.21809
P407
P577
2007-10-01T00:00:00Z