Hyperphosphorylation of the hepatitis C virus NS5A protein requires an active NS3 protease, NS4A, NS4B, and NS5A encoded on the same polyprotein
about
The lipid kinase phosphatidylinositol-4 kinase III alpha regulates the phosphorylation status of hepatitis C virus NS5ANonstructural protein 5A of hepatitis C virus inhibits the function of karyopherin beta3Hepatitis C virus RNA replication is regulated by FKBP8 and Hsp90Role for TBC1D20 and Rab1 in hepatitis C virus replication via interaction with lipid droplet-bound nonstructural protein 5APolo-like kinase 1 is involved in hepatitis C virus replication by hyperphosphorylating NS5AHuman VAP-B is involved in hepatitis C virus replication through interaction with NS5A and NS5BPhosphorylation of hepatitis C virus nonstructural protein 5A modulates its protein interactions and viral RNA replicationComplete translation of the hepatitis C virus genome in vitro: membranes play a critical role in the maturation of all virus proteins except for NS3.Characterization of cell lines carrying self-replicating hepatitis C virus RNAs.Genetic analysis of the pestivirus nonstructural coding region: defects in the NS5A unit can be complemented in trans.In Vitro Selection and Characterization of Hepatitis C Virus Serine Protease Variants Resistant to an Active-Site Peptide InhibitorProtein-Protein Interactions between Hepatitis C Virus Nonstructural ProteinsTopology of the Membrane-Associated Hepatitis C Virus Protein NS4BThe Isoform of Protein Kinase CKI Is Responsible for Hepatitis C Virus NS5A HyperphosphorylationAllelic Variation in the Hepatitis C Virus NS4B Protein Dramatically Influences RNA ReplicationCell Culture Adaptation of Hepatitis C Virus and In Vivo Viability of an Adapted VariantCharacterization of hepatitis C RNA-containing particles from human liver by density and sizeThe Hepatitis C Virus NS4B Protein Can trans-Complement Viral RNA Replication and Modulates Production of Infectious VirusIdentification of Hepatitis C Virus NS5A InhibitorsHepatitis C virus RNA replication depends on specific cis- and trans-acting activities of viral nonstructural proteinsIdentification of PTC725, an orally bioavailable small molecule that selectively targets the hepatitis C Virus NS4B proteinCloning and identification of NS5ATP2 gene and its spliced variant transactivated by hepatitis C virus non-structural protein 5A.Distinct functions of NS5A in hepatitis C virus RNA replication uncovered by studies with the NS5A inhibitor BMS-790052Insights into the complexity and functionality of hepatitis C virus NS5A phosphorylation.Hepatitis C virus NS2 protein serves as a scaffold for virus assembly by interacting with both structural and nonstructural proteinsAn overview of HCV molecular biology, replication and immune responses.Genetic complementation of hepatitis C virus nonstructural protein functions associated with replication exhibits requirements that differ from those for virion assembly.Identification of AP80978, a novel small-molecule inhibitor of hepatitis C virus replication that targets NS4B.A conserved NS3 surface patch orchestrates NS2 protease stimulation, NS5A hyperphosphorylation and HCV genome replication.The interaction between the hepatitis C proteins NS4B and NS5A is involved in viral replicationEffect on hepatitis C virus replication of combinations of direct-acting antivirals, including NS5A inhibitor daclatasvirHepatitis C Virus Genotype 1 to 6 Protease Inhibitor Escape Variants: In Vitro Selection, Fitness, and Resistance Patterns in the Context of the Infectious Viral Life Cycle.Modulation of hepatitis C virus genome encapsidation by nonstructural protein 4BHigh-throughput screening of the yeast kinome: identification of human serine/threonine protein kinases that phosphorylate the hepatitis C virus NS5A protein.Interaction between Nonstructural Proteins NS4B and NS5A Is Essential for Proper NS5A Localization and Hepatitis C Virus RNA Replication.Serine 235 Is the Primary NS5A Hyperphosphorylation Site Responsible for Hepatitis C Virus Replication.Protease Inhibitors Block Multiple Functions of the NS3/4A Protease-Helicase during the Hepatitis C Virus Life Cycle.NS5A inhibitors impair NS5A-phosphatidylinositol 4-kinase IIIα complex formation and cause a decrease of phosphatidylinositol 4-phosphate and cholesterol levels in hepatitis C virus-associated membranes.Mapping of functional domains of the lipid kinase phosphatidylinositol 4-kinase type III alpha involved in enzymatic activity and hepatitis C virus replication.Intragenic complementation of hepatitis C virus NS5A RNA replication-defective alleles.
P2860
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P2860
Hyperphosphorylation of the hepatitis C virus NS5A protein requires an active NS3 protease, NS4A, NS4B, and NS5A encoded on the same polyprotein
description
1999 nî lūn-bûn
@nan
1999 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Hyperphosphorylation of the he ...... ncoded on the same polyprotein
@ast
Hyperphosphorylation of the he ...... ncoded on the same polyprotein
@en
Hyperphosphorylation of the he ...... ncoded on the same polyprotein
@nl
type
label
Hyperphosphorylation of the he ...... ncoded on the same polyprotein
@ast
Hyperphosphorylation of the he ...... ncoded on the same polyprotein
@en
Hyperphosphorylation of the he ...... ncoded on the same polyprotein
@nl
prefLabel
Hyperphosphorylation of the he ...... ncoded on the same polyprotein
@ast
Hyperphosphorylation of the he ...... ncoded on the same polyprotein
@en
Hyperphosphorylation of the he ...... ncoded on the same polyprotein
@nl
P2093
P2860
P1433
P1476
Hyperphosphorylation of the he ...... ncoded on the same polyprotein
@en
P2093
A Clementi
P Neddermann
R De Francesco
P2860
P304
P577
1999-12-01T00:00:00Z