Hepatitis C virus NS2 coordinates virus particle assembly through physical interactions with the E1-E2 glycoprotein and NS3-NS4A enzyme complexes.
about
Identification and targeting of an interaction between a tyrosine motif within hepatitis C virus core protein and AP2M1 essential for viral assemblyApolipoprotein E likely contributes to a maturation step of infectious hepatitis C virus particles and interacts with viral envelope glycoproteinsInhibition of cyclophilins alters lipid trafficking and blocks hepatitis C virus secretionA host YB-1 ribonucleoprotein complex is hijacked by hepatitis C virus for the control of NS3-dependent particle productionSignal peptidase complex subunit 1 participates in the assembly of hepatitis C virus through an interaction with E2 and NS2Simultaneously Targeting the NS3 Protease and Helicase Activities for More Effective Hepatitis C Virus TherapyStructural and Functional Properties of the Hepatitis C Virus p7 ViroporinHepatitis C virus molecular evolution: transmission, disease progression and antiviral therapyThe p7 protein of hepatitis C virus forms structurally plastic, minimalist ion channelsMolecular determinants and dynamics of hepatitis C virus secretionTrafficking of hepatitis C virus core protein during virus particle assemblyProduction of infectious HCV genotype 1b virus in cell culture using a novel Set of adaptive mutationsCell-death-inducing DFFA-like Effector B Contributes to the Assembly of Hepatitis C Virus (HCV) Particles and Interacts with HCV NS5AStructure-guided design affirms inhibitors of hepatitis C virus p7 as a viable class of antivirals targeting virion releaseNS2 Proteins of GB Virus B and Hepatitis C Virus Share Common Protease Activities and Membrane TopologiesComparative Proteomics Reveals Important Viral-Host Interactions in HCV-Infected Human Liver CellsHCV core residues critical for infectivity are also involved in core-NS5A complex formationA comprehensive functional map of the hepatitis C virus genome provides a resource for probing viral proteins.Hepatitis C Virus Is Released via a Noncanonical Secretory Route.Determinants for membrane association of the hepatitis C virus NS2 protease domain.A concerted action of hepatitis C virus p7 and nonstructural protein 2 regulates core localization at the endoplasmic reticulum and virus assembly.Analysis of functional differences between hepatitis C virus NS5A of genotypes 1-7 in infectious cell culture systems.NS2 is dispensable for efficient assembly of hepatitis C virus-like particles in a bipartite trans-encapsidation system.The intraviral protein interaction network of hepatitis C virus.hepatitis c Virus p7 is critical for capsid assembly and envelopmentHepatitis C virus life cycle and lipid metabolismPhosphatidylserine-specific phospholipase A1 involved in hepatitis C virus assembly through NS2 complex formationA basic cluster in the N terminus of yellow fever virus NS2A contributes to infectious particle production.A conserved NS3 surface patch orchestrates NS2 protease stimulation, NS5A hyperphosphorylation and HCV genome replication.Detergent-resistant membrane association of NS2 and E2 during hepatitis C virus replicationEmerging role of lipid droplets in host/pathogen interactions.Morphogenesis of infectious hepatitis C virus particlesThe N-terminal Helical Region of the Hepatitis C Virus p7 Ion Channel Protein Is Critical for Infectious Virus Production.Hepatitis C virus nonstructural protein 5B is involved in virus morphogenesis.Hepatitis C Virus Envelope Glycoprotein E1 Forms Trimers at the Surface of the Virion.Cell culture-adaptive mutations promote viral protein-protein interactions and morphogenesis of infectious hepatitis C virusGenetic and functional characterization of the N-terminal region of the hepatitis C virus NS2 proteinEfficiency of E2-p7 processing modulates production of infectious hepatitis C virusHuman Cathelicidin Compensates for the Role of Apolipoproteins in Hepatitis C Virus Infectious Particle FormationAdapted J6/JFH1-based Hepatitis C virus recombinants with genotype-specific NS4A show similar efficacies against lead protease inhibitors, alpha interferon, and a putative NS4A inhibitor.
P2860
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P2860
Hepatitis C virus NS2 coordinates virus particle assembly through physical interactions with the E1-E2 glycoprotein and NS3-NS4A enzyme complexes.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
Hepatitis C virus NS2 coordina ...... and NS3-NS4A enzyme complexes.
@en
Hepatitis C virus NS2 coordina ...... and NS3-NS4A enzyme complexes.
@nl
type
label
Hepatitis C virus NS2 coordina ...... and NS3-NS4A enzyme complexes.
@en
Hepatitis C virus NS2 coordina ...... and NS3-NS4A enzyme complexes.
@nl
prefLabel
Hepatitis C virus NS2 coordina ...... and NS3-NS4A enzyme complexes.
@en
Hepatitis C virus NS2 coordina ...... and NS3-NS4A enzyme complexes.
@nl
P2860
P356
P1433
P1476
Hepatitis C virus NS2 coordina ...... and NS3-NS4A enzyme complexes.
@en
P2093
Brett D Lindenbach
P2860
P304
P356
10.1128/JVI.02268-10
P407
P577
2010-12-08T00:00:00Z