Differential assembly of Hepatitis B Virus core protein on single- and double-stranded nucleic acid suggest the dsDNA-filled core is spring-loaded.
about
Virus strategies for passing the nuclear envelope barrierPreparation by alkaline treatment and detailed characterisation of empty hepatitis B virus core particles for vaccine and gene therapy applications.The hepatitis B virus core protein intradimer interface modulates capsid assembly and stability.Structural organization of pregenomic RNA and the carboxy-terminal domain of the capsid protein of hepatitis B virus.Replication-competent infectious hepatitis B virus vectors carrying substantially sized transgenes by redesigned viral polymerase translation.Functional characterization of the putative hepatitis B virus core protein late domain using retrovirus chimeras.An Aptamer against the Matrix Binding Domain on the Hepatitis B Virus Capsid Impairs Virion FormationAlteration of Mature Nucleocapsid and Enhancement of Covalently Closed Circular DNA Formation by Hepatitis B Virus Core Mutants Defective in Complete-Virion Formation.Hepatitis B Virus Core Protein Phosphorylation Sites Affect Capsid Stability and Transient Exposure of the C-terminal Domain.Hepatitis B Virus Capsids Have Diverse Structural Responses to Small-Molecule Ligands Bound to the Heteroaryldihydropyrimidine PocketTo build a virus on a nucleic acid substrate.Viral genome structures are optimal for capsid assemblyMaturation-associated destabilization of hepatitis B virus nucleocapsid.Core protein: A pleiotropic keystone in the HBV lifecycle.Assembly and Release of Hepatitis B Virus.Genetically altering the thermodynamics and kinetics of hepatitis B virus capsid assembly has profound effects on virus replication in cell culture.HBV core protein allosteric modulators differentially alter cccDNA biosynthesis from de novo infection and intracellular amplification pathways.The Structural Biology of Hepatitis B Virus: Form and Function.A molecular thermodynamic model for the stability of hepatitis B capsids.Scaffold properties are a key determinant of the size and shape of self-assembled virus-derived particlesHepatitis virus capsid polymorph stability depends on encapsulated cargo size.All-atom molecular dynamics of the HBV capsid reveals insights into biological function and cryo-EM resolution limits.Common and Distinct Capsid and Surface Protein Requirements for Secretion of Complete and Genome-free Hepatitis B Virions.Asymmetric Modification of Hepatitis B Virus (HBV) Genomes by an Endogenous Cytidine Deaminase inside HBV Cores Informs a Model of Reverse Transcription.Virus-like particles: Next-generation nanoparticles for targeted therapeutic delivery.
P2860
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P2860
Differential assembly of Hepatitis B Virus core protein on single- and double-stranded nucleic acid suggest the dsDNA-filled core is spring-loaded.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
2012年學術文章
@zh-hant
name
Differential assembly of Hepat ...... -filled core is spring-loaded.
@en
Differential assembly of Hepat ...... -filled core is spring-loaded.
@nl
type
label
Differential assembly of Hepat ...... -filled core is spring-loaded.
@en
Differential assembly of Hepat ...... -filled core is spring-loaded.
@nl
prefLabel
Differential assembly of Hepat ...... -filled core is spring-loaded.
@en
Differential assembly of Hepat ...... -filled core is spring-loaded.
@nl
P2860
P50
P1433
P1476
Differential assembly of Hepat ...... A-filled core is spring-loaded
@en
P2093
Mary S Dhason
P2860
P356
10.1016/J.VIROL.2012.04.012
P407
P577
2012-05-16T00:00:00Z