Cyclophilin A Is an Essential Cofactor for Hepatitis C Virus Infection and the Principal Mediator of Cyclosporine Resistance In Vitro - Test2 - elhamkhani - TriplyDB

Cyclophilin A Is an Essential Cofactor for Hepatitis C Virus Infection and the Principal Mediator of Cyclosporine Resistance In Vitro

Cyclophilin A Is an Essential Cofactor for Hepatitis C Virus Infection and the Principal Mediator of Cyclosporine Resistance In Vitro

http://www.wikidata.org/entity/Q27486118

about

Cyclophilin E functions as a negative regulator to influenza virus replication by impairing the formation of the viral ribonucleoprotein complex Cyclosporin A associated helicase-like protein facilitates the association of hepatitis C virus RNA polymerase with its cellular cyclophilin B Hepatitis C virus NS5B and host cyclophilin A share a common binding site on NS5A Inhibition of cyclophilins alters lipid trafficking and blocks hepatitis C virus secretion Rab18 binds to hepatitis C virus NS5A and promotes interaction between sites of viral replication and lipid droplets Debio 025, a cyclophilin binding molecule, is highly efficient in clearing hepatitis C virus (HCV) replicon-containing cells when used alone or in combination with specifically targeted antiviral therapy for HCV (STAT-C) inhibitors Chaperones in hepatitis C virus infection Modeling Viral Infectious Diseases and Development of Antiviral Therapies Using Human Induced Pluripotent Stem Cell-Derived Systems Hepatitis C virus comes for dinner: How the hepatitis C virus interferes with autophagy Curing a viral infection by targeting the host: the example of cyclophilin inhibitors Direct acting antivirals for the treatment of chronic viral hepatitis Cyclophilin Inhibitors Remodel the Endoplasmic Reticulum of HCV-Infected Cells in a Unique Pattern Rendering Cells Impervious to a Reinfection Cyclophilin B stimulates RNA synthesis by the HCV RNA dependent RNA polymerase Hepatitis C Virus NS5A Protein Is a Substrate for the Peptidyl-prolyl cis/trans Isomerase Activity of Cyclophilins A and B Critical Role of Cyclophilin A and Its Prolyl-Peptidyl Isomerase Activity in the Structure and Function of the Hepatitis C Virus Replication Complex Hepatitis C virus replicons: dinosaurs still in business?Cyclosporine Inhibits Flavivirus Replication through Blocking the Interaction between Host Cyclophilins and Viral NS5 Protein Essential Role of Cyclophilin A for Hepatitis C Virus Replication and Virus Production and Possible Link to Polyprotein Cleavage Kinetics The Isomerase Active Site of Cyclophilin A Is Critical for Hepatitis C Virus Replication Mutations in the hepatitis C virus polymerase that increase RNA binding can confer resistance to cyclosporine A A genome-wide genetic screen for host factors required for hepatitis C virus propagation A Conserved Proline between Domains II and III of Hepatitis C Virus NS5A Influences both RNA Replication and Virus Assembly Towards a small animal model for hepatitis C SCY-635, a Novel Nonimmunosuppressive Analog of Cyclosporine That Exhibits Potent Inhibition of Hepatitis C Virus RNA Replication In Vitro A cell protection screen reveals potent inhibitors of multiple stages of the hepatitis C virus life cycle Cyclosporine Inhibits a Direct Interaction between Cyclophilins and Hepatitis C NS5A Elucidating novel hepatitis C virus-host interactions using combined mass spectrometry and functional genomics approaches A combined proteomics/genomics approach links hepatitis C virus infection with nonsense-mediated mRNA decay Characterization of the Anti-HCV Activities of the New Cyclophilin Inhibitor STG-175 DEB025 (Alisporivir) inhibits hepatitis C virus replication by preventing a cyclophilin A induced cis-trans isomerisation in domain II of NS5A A review of treatment modalities for Middle East Respiratory Syndrome.Isoform-specific inhibition of cyclophilins Novel permissive cell lines for complete propagation of hepatitis C virus.Simultaneous reduction and digestion of proteins with disulfide bonds for hydrogen/deuterium exchange monitored by mass spectrometry.A major determinant of cyclophilin dependence and cyclosporine susceptibility of hepatitis C virus identified by a genetic approach Peptidyl-prolyl isomerase Pin1 is a cellular factor required for hepatitis C virus propagation.Cyclophilin A restricts influenza A virus replication through degradation of the M1 protein.Productive hepatitis C virus infection of stem cell-derived hepatocytes reveals a critical transition to viral permissiveness during differentiation.Cyclophilin A associates with enterovirus-71 virus capsid and plays an essential role in viral infection as an uncoating regulator Barriers of hepatitis C virus interspecies transmission

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Cyclophilin A Is an Essential Cofactor for Hepatitis C Virus Infection and the Principal Mediator of Cyclosporine Resistance In Vitro

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2008 nî lūn-bûn

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2008 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2008 թվականի հունիսին հրատարակված գիտական հոդված

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2008年の論文

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Cyclophilin A Is an Essential ...... closporine Resistance In Vitro

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Andre Irsigler

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Feng Yang

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Heather B Nelson

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Jason M Robotham

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Rachael Kenworthy

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P2860

Cyclophilin A regulates HIV-1 infectivity, as demonstrated by gene targeting in human T cells

Identification of FBL2 as a geranylgeranylated cellular protein required for hepatitis C virus RNA replication

The cyclophilin multigene family of peptidyl-prolyl isomerases. Characterization of three separate human isoforms

Hepatitis C virus RNA replication is regulated by FKBP8 and Hsp90

Cyclophilin B is a functional regulator of hepatitis C virus RNA polymerase

Human VAP-B is involved in hepatitis C virus replication through interaction with NS5A and NS5B

Phosphorylation of hepatitis C virus nonstructural protein 5A modulates its protein interactions and viral RNA replication

X-ray structure of a cyclophilin B/cyclosporin complex: comparison with cyclophilin A and delineation of its calcineurin-binding domain

The hydrophobic pocket of cyclophilin is the binding site for the human immunodeficiency virus type 1 Gag polyprotein

Robust hepatitis C virus infection in vitro.

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397710

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10.1128/JVI.02614-07

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11

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82

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5467896

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18385230

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2395199

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