Conformational Changes in the Hepatitis B Virus Core Protein Are Consistent with a Role for Allostery in Virus Assembly
about
Virus assembly and maturation: auto-regulation through allosteric molecular switchesPreparation by alkaline treatment and detailed characterisation of empty hepatitis B virus core particles for vaccine and gene therapy applications.Antigenic Switching of Hepatitis B Virus by Alternative Dimerization of the Capsid ProteinThermodynamic origins of protein folding, allostery, and capsid formation in the human hepatitis B virus core proteinAssembly-Directed Antivirals Differentially Bind Quasiequivalent Pockets to Modify Hepatitis B Virus Capsid Tertiary and Quaternary StructureAllosteric conformational changes of human HBV core protein transform its assembly.Molecular basis for the high degree of antigenic cross-reactivity between hepatitis B virus capsids (HBcAg) and dimeric capsid-related protein (HBeAg): insights into the enigmatic nature of the e-antigenAssessment of differences in the conformational flexibility of hepatitis B virus core-antigen and e-antigen by hydrogen deuterium exchange-mass spectrometry.Exploring the paths of (virus) assemblyThe hepatitis B virus core protein intradimer interface modulates capsid assembly and stability.Subunit exchange rates in Hepatitis B virus capsids are geometry- and temperature-dependent.Trapping of hepatitis B virus capsid assembly intermediates by phenylpropenamide assembly accelerators.Role of the propeptide in controlling conformation and assembly state of hepatitis B virus e-antigen2-amino-N-(2,6-dichloropyridin-3-yl)acetamide derivatives as a novel class of HBV capsid assembly inhibitor.Cryo-EM study of Hepatitis B virus core antigen capsids decorated with antibodies from a human patient.High-resolution crystal structure of a hepatitis B virus replication inhibitor bound to the viral core proteinSpecificity of an anti-capsid antibody associated with Hepatitis B Virus-related acute liver failure.Hepatitis B Virus Capsids Have Diverse Structural Responses to Small-Molecule Ligands Bound to the Heteroaryldihydropyrimidine PocketChimeric derivatives of hepatitis B virus core particles carrying major epitopes of the rubella virus E1 glycoproteinAllosteric Control of Icosahedral Capsid Assembly.Virus assembly, allostery and antiviralsCore protein: A pleiotropic keystone in the HBV lifecycle.Assembly and Release of Hepatitis B Virus.Influences on viral replication and sensitivity to GLS4, a HAP compound, of naturally occurring T109/V124 mutations in hepatitis B virus core protein.Genetically altering the thermodynamics and kinetics of hepatitis B virus capsid assembly has profound effects on virus replication in cell culture.A Molecular Breadboard: Removal and Replacement of Subunits in an Hepatitis B Virus Capsid.HBV RNA pre-genome encodes specific motifs that mediate interactions with the viral core protein that promote nucleocapsid assembly.Illuminating the Reaction Pathways of Viromimetic Assembly.Heteroaryldihydropyrimidine (HAP) and Sulfamoylbenzamide (SBA) Inhibit Hepatitis B Virus Replication by Different Molecular MechanismsTabulation as a high-resolution alternative to coarse-graining protein interactions: Initial application to virus capsid subunits.Hepatitis B virus peptide inhibitors: solution structures and interactions with the viral capsid.Structurally similar woodchuck and human hepadnavirus core proteins have distinctly different temperature dependences of assembly.The interface between hepatitis B virus capsid proteins affects self-assembly, pregenomic RNA packaging, and reverse transcription.Assembly Pathway of Hepatitis B Core Virus-like Particles from Genetically Fused Dimers.Using ion mobility spectrometry-mass spectrometry to decipher the conformational and assembly characteristics of the hepatitis B capsid protein.Kinetic constraints on self-assembly into closed supramolecular structures.One protein, at least three structures, and many functions.The Structural Biology of Hepatitis B Virus: Form and Function.RNA encapsidation by SV40-derived nanoparticles follows a rapid two-state mechanism.A molecular thermodynamic model for the stability of hepatitis B capsids.
P2860
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P2860
Conformational Changes in the Hepatitis B Virus Core Protein Are Consistent with a Role for Allostery in Virus Assembly
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2010 nî lūn-bûn
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2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2010年の論文
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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
name
Conformational Changes in the ...... or Allostery in Virus Assembly
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Conformational Changes in the ...... or Allostery in Virus Assembly
@en
Conformational Changes in the ...... or Allostery in Virus Assembly
@nl
type
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Conformational Changes in the ...... or Allostery in Virus Assembly
@ast
Conformational Changes in the ...... or Allostery in Virus Assembly
@en
Conformational Changes in the ...... or Allostery in Virus Assembly
@nl
prefLabel
Conformational Changes in the ...... or Allostery in Virus Assembly
@ast
Conformational Changes in the ...... or Allostery in Virus Assembly
@en
Conformational Changes in the ...... or Allostery in Virus Assembly
@nl
P2093
P2860
P356
P1433
P1476
Conformational Changes in the ...... or Allostery in Virus Assembly
@en
P2093
Charles E Dann
Charles Packianathan
Sarah P Katen
P2860
P304
P356
10.1128/JVI.02033-09
P577
2010-02-01T00:00:00Z