Effect of interaction between hepatitis C virus NS5A and NS5B on hepatitis C virus RNA replication with the hepatitis C virus replicon.
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Hepatitis C virus NS5B and host cyclophilin A share a common binding site on NS5ARab18 binds to hepatitis C virus NS5A and promotes interaction between sites of viral replication and lipid dropletsIsoform-specific interaction of pyruvate kinase with hepatitis C virus NS5BHuman VAP-B is involved in hepatitis C virus replication through interaction with NS5A and NS5BHepatitis C virus proteinsStructures of hepatitis C virus nonstructural proteins required for replicase assembly and functionEffect of hepatitis C virus (HCV) NS5B-nucleolin interaction on HCV replication with HCV subgenomic replicon.The C-Terminal Hydrophobic Domain of Hepatitis C Virus RNA Polymerase NS5B Can Be Replaced with a Heterologous Domain of Poliovirus Protein 3ASynergy of Small Molecular Inhibitors of Hepatitis C Virus Replication Directed at Multiple Viral TargetsIdentification of Determinants Involved in Initiation of Hepatitis C Virus RNA Synthesis by Using Intergenotypic Replicase ChimerasThe NS3 Helicase and NS5B-to-3'X Regions Are Important for Efficient Hepatitis C Virus Strain JFH-1 Replication in Huh7 CellsThe Hepatitis C Virus NS5A Stimulates NS5B During In Vitro RNA Synthesis in a Template Specific MannerA cell-based assay for RNA synthesis by the HCV polymerase reveals new insights on mechanism of polymerase inhibitors and modulation by NS5Ac-Src is required for complex formation between the hepatitis C virus-encoded proteins NS5A and NS5B: a prerequisite for replication.Ribavirin resistance in hepatitis C virus replicon-containing cell lines conferred by changes in the cell line or mutations in the replicon RNA.Small molecules targeting hepatitis C virus-encoded NS5A cause subcellular redistribution of their target: insights into compound modes of action.Hepatitis C virus non-structural protein 3 (HCV NS3): a multifunctional antiviral targetPersistent expression of hepatitis C virus non-structural proteins leads to increased autophagy and mitochondrial injury in human hepatoma cells.Heat shock protein 72 is associated with the hepatitis C virus replicase complex and enhances viral RNA replication.Distinct functions of NS5A in hepatitis C virus RNA replication uncovered by studies with the NS5A inhibitor BMS-790052The intraviral protein interaction network of hepatitis C virus.Should NS5A inhibitors serve as the scaffold for all-oral anti-HCV combination therapies?Nonstructural 5A Protein of Hepatitis C Virus Regulates Soluble Resistance-Related Calcium-Binding Protein Activity for Viral Propagation.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.Hepatitis C virus (HCV) employs multiple strategies to subvert the host innate antiviral response.Effects of Resistance-Associated NS5A Mutations in Hepatitis C Virus on Viral Production and Susceptibility to Antiviral Reagents.Dynamics of defective hepatitis C virus clones in reinfected liver grafts in liver transplant recipients: ultradeep sequencing analysis.Cellular and molecular biology of HCV infection and hepatitis.Hepatitis C virus nonstructural protein 5A (NS5A) is an RNA-binding protein.Hepatitis C virus and host cell nuclear transport machinery: a clandestine affair.Serine 235 Is the Primary NS5A Hyperphosphorylation Site Responsible for Hepatitis C Virus Replication.Inhibition of HCV translation by disrupting the structure and interactions of the viral CRE and 3' X-tail.Zinc mesoporphyrin induces rapid proteasomal degradation of hepatitis C nonstructural 5A protein in human hepatoma cells.NMR reveals the intrinsically disordered domain 2 of NS5A protein as an allosteric regulator of the hepatitis C virus RNA polymerase NS5B.Hepatitis C virus NS5A is a direct substrate of casein kinase I-alpha, a cellular kinase identified by inhibitor affinity chromatography using specific NS5A hyperphosphorylation inhibitors.The small molecules AZD0530 and dasatinib inhibit dengue virus RNA replication via Fyn kinase.Mutational analysis of hepatitis C virus nonstructural protein 5A: potential role of differential phosphorylation in RNA replication and identification of a genetically flexible domain.Interferon-beta is activated by hepatitis C virus NS5B and inhibited by NS4A, NS4B, and NS5A.Hepatitis C virus NS3 inhibitors: current and future perspectives.Mutational Analysis of Hepatitis C Virus NS5B in the Subgenomic Replicon Cell Culture.
P2860
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P2860
Effect of interaction between hepatitis C virus NS5A and NS5B on hepatitis C virus RNA replication with the hepatitis C virus replicon.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
Effect of interaction between ...... he hepatitis C virus replicon.
@en
type
label
Effect of interaction between ...... he hepatitis C virus replicon.
@en
prefLabel
Effect of interaction between ...... he hepatitis C virus replicon.
@en
P2093
P2860
P1433
P1476
Effect of interaction between ...... he hepatitis C virus replicon.
@en
P2093
Kunitada Shimotohno
Makoto Hijikata
Seishi Murakami
Shuichi Kaneko
Tetsuro Shimakami
Yuan Yuan Ma
P2860
P304
P356
10.1128/JVI.78.6.2738-2748.2004
P407
P577
2004-03-01T00:00:00Z