The NS5A protein of hepatitis C virus is a zinc metalloprotein.
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The lipid kinase phosphatidylinositol-4 kinase III alpha regulates the phosphorylation status of hepatitis C virus NS5AHepatitis C virus RNA replication is regulated by FKBP8 and Hsp90A single-amino-acid mutation in hepatitis C virus NS5A disrupting FKBP8 interaction impairs viral replicationRole for TBC1D20 and Rab1 in hepatitis C virus replication via interaction with lipid droplet-bound nonstructural protein 5ARab18 binds to hepatitis C virus NS5A and promotes interaction between sites of viral replication and lipid dropletsHuman VAP-B is involved in hepatitis C virus replication through interaction with NS5A and NS5BHepatitis C virus NS5A protein interacts with phosphatidylinositol 4-kinase type IIIalpha and regulates viral propagationHepatitis C virus proteinsRole of ledipasvir/sofosbuvir combination for genotype 1 hepatitis C virus infectionMechanisms of Hepatitis C Viral Resistance to Direct Acting AntiviralsPathophysiologic and transcriptomic analyses of viscerotropic yellow fever in a rhesus macaque modelAsymmetric binding to NS5A by daclatasvir (BMS-790052) and analogs suggests two novel modes of HCV inhibition.Human Choline Kinase-α Promotes Hepatitis C Virus RNA Replication through Modulation of Membranous Viral Replication Complex FormationMolecular virology of hepatitis C virus (HCV): 2006 updateStructure of the zinc-binding domain of an essential component of the hepatitis C virus replicaseThe NS5A Protein of Bovine Viral Diarrhea Virus Contains an Essential Zinc-Binding Site Similar to That of the Hepatitis C Virus NS5A ProteinAn 85-aa segment of the GB virus type C NS5A phosphoprotein inhibits HIV-1 replication in CD4+ Jurkat T cellsThe Isoform of Protein Kinase CKI Is Responsible for Hepatitis C Virus NS5A HyperphosphorylationConserved Determinants for Membrane Association of Nonstructural Protein 5A from Hepatitis C Virus and Related VirusesAnalysis of Hepatitis C Virus Superinfection Exclusion by Using Novel Fluorochrome Gene-Tagged Viral GenomesPretreatment Sequence Diversity Differences in the Full-Length Hepatitis C Virus Open Reading Frame Correlate with Early Response to TherapyStudying Hepatitis C Virus: Making the Best of a Bad VirusIdentification of Residues Required for RNA Replication in Domains II and III of the Hepatitis C Virus NS5A ProteinHepatitis C virus NS5A protein binds the SH3 domain of the Fyn tyrosine kinase with high affinity: mutagenic analysis of residues within the SH3 domain that contribute to the interactionRegulation of Hepatitis C Virion Production via Phosphorylation of the NS5A ProteinEssential Role of Domain III of Nonstructural Protein 5A for Hepatitis C Virus Infectious Particle AssemblyInteraction of Hepatitis C Virus Nonstructural Protein 5A with Core Protein Is Critical for the Production of Infectious Virus ParticlesHigh-Resolution Functional Profiling of Hepatitis C Virus GenomeCrystal Structure of a Novel Dimeric Form of NS5A Domain I Protein from Hepatitis C VirusHepatitis C Virus NS5A Protein Is a Substrate for the Peptidyl-prolyl cis/trans Isomerase Activity of Cyclophilins A and BThe Hepatitis C Virus NS5A Stimulates NS5B During In Vitro RNA Synthesis in a Template Specific MannerA Conserved Proline between Domains II and III of Hepatitis C Virus NS5A Influences both RNA Replication and Virus AssemblyArchitects of assembly: roles of Flaviviridae non-structural proteins in virion morphogenesisIdentification of Hepatitis C Virus NS5A InhibitorsStructural and Functional Studies of Nonstructural Protein 2 of the Hepatitis C Virus Reveal Its Key Role as Organizer of Virion AssemblyThe crystal structure of NS5A domain 1 from genotype 1a reveals new clues to the mechanism of action for dimeric HCV inhibitorsSeed Sequence-Matched Controls Reveal Limitations of Small Interfering RNA Knockdown in Functional and Structural Studies of Hepatitis C Virus NS5A-MOBKL1B InteractionMetabolism of phosphatidylinositol 4-kinase IIIα-dependent PI4P Is subverted by HCV and is targeted by a 4-anilino quinazoline with antiviral activitySensitivity of a ribavirin resistant mutant of hepatitis C virus to other antiviral drugsCoordination of Hepatitis C Virus Assembly by Distinct Regulatory Regions in Nonstructural Protein 5A
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P2860
The NS5A protein of hepatitis C virus is a zinc metalloprotein.
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
The NS5A protein of hepatitis C virus is a zinc metalloprotein.
@en
type
label
The NS5A protein of hepatitis C virus is a zinc metalloprotein.
@en
prefLabel
The NS5A protein of hepatitis C virus is a zinc metalloprotein.
@en
P2093
P356
P1476
The NS5A protein of hepatitis C virus is a zinc metalloprotein.
@en
P2093
Charles M Rice
Joseph Marcotrigiano
Timothy L Tellinghuisen
P304
48576-48587
P356
10.1074/JBC.M407787200
P407
P577
2004-08-31T00:00:00Z