Unique features of hepatitis C virus capsid formation revealed by de novo cell-free assembly.
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Hepatitis C virus proteinsIdentification of Residues in the Hepatitis C Virus Core Protein That Are Critical for Capsid Assembly in a Cell-Free SystemComplete translation of the hepatitis C virus genome in vitro: membranes play a critical role in the maturation of all virus proteins except for NS3.Hepatitis C virus core protein is a dimeric alpha-helical protein exhibiting membrane protein features.Analysis of hepatitis C virus RNA dimerization and core-RNA interactionsDifferential Biophysical Properties of Infectious Intracellular and Secreted Hepatitis C Virus ParticlesAlanine Scanning of the Hepatitis C Virus Core Protein Reveals Numerous Residues Essential for Production of Infectious VirusCore protein domains involved in hepatitis C virus-like particle assembly and budding at the endoplasmic reticulum membraneRNA chaperoning and intrinsic disorder in the core proteins of FlaviviridaeCharacterization of Hepatitis C Virus Core Protein Multimerization and Membrane Envelopment: Revelation of a Cascade of Core-Membrane InteractionsCoordination of Hepatitis C Virus Assembly by Distinct Regulatory Regions in Nonstructural Protein 5ABiochemical and biophysical characterization of cell-free synthesized Rift Valley fever virus nucleoprotein capsids enables in vitro screening to identify novel antivirals.Identification of basic amino acids at the N-terminal end of the core protein that are crucial for hepatitis C virus infectivity.hepatitis c Virus p7 is critical for capsid assembly and envelopmentMorphogenesis of infectious hepatitis C virus particlesRole of cleavage at the core-E1 junction of hepatitis C virus polyprotein in viral morphogenesisInteraction between the human immunodeficiency virus type 1 Gag matrix domain and phosphatidylinositol-(4,5)-bisphosphate is essential for efficient gag membrane binding.Host-rabies virus protein-protein interactions as druggable antiviral targetsDesign of virus-based nanomaterials for medicine, biotechnology, and energy.Virion assembly and release.Identification of novel RNA secondary structures within the hepatitis C virus genome reveals a cooperative involvement in genome packagingDimerization-driven interaction of hepatitis C virus core protein with NS3 helicase.Core as a novel viral target for hepatitis C drugs.Hepatitis C Virus Replication.Immune modulation by the hepatitis C virus core protein.Evidence for cellular uptake of recombinant hepatitis C virus non-enveloped capsid-like particles.Assembly of immature HIV-1 capsids using a cell-free system.Signal peptide peptidase-catalyzed cleavage of hepatitis C virus core protein is dispensable for virus budding but destabilizes the viral capsid.C-terminal domain of hepatitis C virus core protein is essential for secretionInterfering with hepatitis C virus assembly in vitro using affinity peptides directed towards core protein.
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P2860
Unique features of hepatitis C virus capsid formation revealed by de novo cell-free assembly.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年學術文章
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name
Unique features of hepatitis C ...... by de novo cell-free assembly.
@en
Unique features of hepatitis C ...... by de novo cell-free assembly.
@nl
type
label
Unique features of hepatitis C ...... by de novo cell-free assembly.
@en
Unique features of hepatitis C ...... by de novo cell-free assembly.
@nl
prefLabel
Unique features of hepatitis C ...... by de novo cell-free assembly.
@en
Unique features of hepatitis C ...... by de novo cell-free assembly.
@nl
P2093
P2860
P1433
P1476
Unique features of hepatitis C ...... by de novo cell-free assembly.
@en
P2093
Jaisri R Lingappa
Kevin C Klein
Stephen J Polyak
P2860
P304
P356
10.1128/JVI.78.17.9257-9269.2004
P407
P577
2004-09-01T00:00:00Z