3.5Å cryoEM Structure of Hepatitis B Virus Core Assembled from Full-Length Core Protein
about
Integrative Modeling of Macromolecular Assemblies from Low to Near-Atomic ResolutionRole of Marine Natural Products in the Genesis of Antiviral AgentsNucleic acid chaperone activity associated with the arginine-rich domain of human hepatitis B virus core protein.Single-step antibody-based affinity cryo-electron microscopy for imaging and structural analysis of macromolecular assemblies.The hepatitis B virus core protein intradimer interface modulates capsid assembly and stability.A theoretical study of SRPK interaction with the flexible domains of hepatitis B capsids.Distinct Viral Lineages from Fish and Amphibians Reveal the Complex Evolutionary History of Hepadnaviruses.A Thermodynamic Model for Genome Packaging in Hepatitis B Virus.Hepatitis B Virus Core Protein Phosphorylation Sites Affect Capsid Stability and Transient Exposure of the C-terminal Domain.HBV maintains electrostatic homeostasis by modulating negative charges from phosphoserine and encapsidated nucleic acidsEngineering hepatitis B virus core particles for targeting HER2 receptors in vitro and in vivo.Core protein: A pleiotropic keystone in the HBV lifecycle.Assembly and Release of Hepatitis B Virus.Deciphering the Origin and Evolution of Hepatitis B Viruses by Means of a Family of Non-enveloped Fish Viruses.HBV RNA pre-genome encodes specific motifs that mediate interactions with the viral core protein that promote nucleocapsid assembly.An N-terminal extension to the hepatitis B virus core protein forms a poorly ordered trimeric spike in assembled virus-like particles.The Structural Biology of Hepatitis B Virus: Form and Function.A molecular thermodynamic model for the stability of hepatitis B capsids.The diverse functions of the hepatitis B core/capsid protein (HBc) in the viral life cycle: Implications for the development of HBc-targeting antivirals.Enhanced stability of a chimeric hepatitis B core antigen virus-like-particle (HBcAg-VLP) by a C-terminal linker-hexahistidine-peptide.All-atom molecular dynamics of the HBV capsid reveals insights into biological function and cryo-EM resolution limits.Multiple roles of core protein linker in hepatitis B virus replication.Assembly Properties of Hepatitis B Virus Core Protein Mutants Correlate with Their Resistance to Assembly-Directed Antivirals
P2860
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P2860
3.5Å cryoEM Structure of Hepatitis B Virus Core Assembled from Full-Length Core Protein
description
2013 nî lūn-bûn
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2013 թուականին հրատարակուած գիտական յօդուած
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2013 թվականին հրատարակված գիտական հոդված
@hy
2013年の論文
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2013年論文
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2013年論文
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2013年論文
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2013年論文
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2013年論文
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2013年论文
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name
3.5Å cryoEM Structure of Hepatitis B Virus Core Assembled from Full-Length Core Protein
@ast
3.5Å cryoEM Structure of Hepatitis B Virus Core Assembled from Full-Length Core Protein
@en
3.5Å cryoEM Structure of Hepatitis B Virus Core Assembled from Full-Length Core Protein
@nl
type
label
3.5Å cryoEM Structure of Hepatitis B Virus Core Assembled from Full-Length Core Protein
@ast
3.5Å cryoEM Structure of Hepatitis B Virus Core Assembled from Full-Length Core Protein
@en
3.5Å cryoEM Structure of Hepatitis B Virus Core Assembled from Full-Length Core Protein
@nl
prefLabel
3.5Å cryoEM Structure of Hepatitis B Virus Core Assembled from Full-Length Core Protein
@ast
3.5Å cryoEM Structure of Hepatitis B Virus Core Assembled from Full-Length Core Protein
@en
3.5Å cryoEM Structure of Hepatitis B Virus Core Assembled from Full-Length Core Protein
@nl
P2093
P2860
P1433
P1476
3.5Å cryoEM Structure of Hepatitis B Virus Core Assembled from Full-Length Core Protein
@en
P2093
Chiaho Shih
Jonathan Jih
Z Hong Zhou
P2860
P304
P356
10.1371/JOURNAL.PONE.0069729
P407
P577
2013-01-01T00:00:00Z