Hepatitis B virus capsid assembly is enhanced by naturally occurring mutation F97L.
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Precore/core region mutations of hepatitis B virus related to clinical severityConformational Changes in the Hepatitis B Virus Core Protein Are Consistent with a Role for Allostery in Virus AssemblyThermodynamic origins of protein folding, allostery, and capsid formation in the human hepatitis B virus core proteinPhosphorylation of hepatitis B virus Cp at Ser87 facilitates core assemblyCore-controlled polymorphism in virus-like particlesThe thermodynamics of virus capsid assembly.Understanding the concentration dependence of viral capsid assembly kinetics--the origin of the lag time and identifying the critical nucleus size.A heteroaryldihydropyrimidine activates and can misdirect hepatitis B virus capsid assemblyAssessment of differences in the conformational flexibility of hepatitis B virus core-antigen and e-antigen by hydrogen deuterium exchange-mass spectrometry.The hepatitis B virus core protein intradimer interface modulates capsid assembly and stability.Trapping of hepatitis B virus capsid assembly intermediates by phenylpropenamide assembly accelerators.Naturally occurring precore/core region mutations of hepatitis B virus genotype C related to hepatocellular carcinomaIn vitro screening for molecules that affect virus capsid assembly (and other protein association reactions)Conformational equilibria and rates of localized motion within hepatitis B virus capsidsPhase diagrams map the properties of antiviral agents directed against hepatitis B virus core assemblyA theory for viral capsid assembly around electrostatic cores.Allosteric Control of Icosahedral Capsid Assembly.Core protein: A pleiotropic keystone in the HBV lifecycle.Genetically altering the thermodynamics and kinetics of hepatitis B virus capsid assembly has profound effects on virus replication in cell culture.Hepatitis B virus core antigen mutations predict post-operative prognosis of patients with primary hepatocellular carcinoma.Discovery and Mechanistic Study of Benzamide Derivatives That Modulate Hepatitis B Virus Capsid Assembly.Distinguishing reversible from irreversible virus capsid assembly.A mutant hepatitis B virus core protein mimics inhibitors of icosahedral capsid self-assemblyStructurally 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.One protein, at least three structures, and many functions.A molecular thermodynamic model for the stability of hepatitis B capsids.An in vitro fluorescence screen to identify antivirals that disrupt hepatitis B virus capsid assembly.Hepatitis B virus core protein allosteric modulators can distort and disrupt intact capsids.Structures of Hepatitis B Virus Core- and e-Antigen Immune Complexes Suggest Multi-point Inhibition
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P2860
Hepatitis B virus capsid assembly is enhanced by naturally occurring mutation F97L.
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年学术文章
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2004年學術文章
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name
Hepatitis B virus capsid assembly is enhanced by naturally occurring mutation F97L.
@en
Hepatitis B virus capsid assembly is enhanced by naturally occurring mutation F97L.
@nl
type
label
Hepatitis B virus capsid assembly is enhanced by naturally occurring mutation F97L.
@en
Hepatitis B virus capsid assembly is enhanced by naturally occurring mutation F97L.
@nl
prefLabel
Hepatitis B virus capsid assembly is enhanced by naturally occurring mutation F97L.
@en
Hepatitis B virus capsid assembly is enhanced by naturally occurring mutation F97L.
@nl
P2860
P1433
P1476
Hepatitis B virus capsid assembly is enhanced by naturally occurring mutation F97L.
@en
P2093
Pablo Ceres
Stephen J Stray
P2860
P304
P356
10.1128/JVI.78.17.9538-9543.2004
P407
P577
2004-09-01T00:00:00Z