The arginine clusters of the carboxy-terminal domain of the core protein of hepatitis B virus make pleiotropic contributions to genome replication.
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Thermodynamic origins of protein folding, allostery, and capsid formation in the human hepatitis B virus core proteinHepatitis B virus molecular biology and pathogenesisNucleic acid chaperone activity associated with the arginine-rich domain of human hepatitis B virus core protein.Rab33B Controls Hepatitis B Virus Assembly by Regulating Core Membrane Association and Nucleocapsid Processing.Allosteric conformational changes of human HBV core protein transform its assembly.Serine phosphoacceptor sites within the core protein of hepatitis B virus contribute to genome replication pleiotropically.Encapsidated hepatitis B virus reverse transcriptase is poised on an ordered RNA latticePhosphoacceptors threonine 162 and serines 170 and 178 within the carboxyl-terminal RRRS/T motif of the hepatitis B virus core protein make multiple contributions to hepatitis B virus replication.A theoretical study of SRPK interaction with the flexible domains of hepatitis B capsids.C-terminal substitution of HBV core proteins with those from DHBV reveals that arginine-rich 167RRRSQSPRR175 domain is critical for HBV replication.Structural organization of pregenomic RNA and the carboxy-terminal domain of the capsid protein of hepatitis B virus.Sulfamoylbenzamide derivatives inhibit the assembly of hepatitis B virus nucleocapsids.A theoretical model for the dynamic structure of hepatitis B nucleocapsidA novel pyridazinone derivative inhibits hepatitis B virus replication by inducing genome-free capsid formationHepatitis B Virus Core Protein Phosphorylation Sites Affect Capsid Stability and Transient Exposure of the C-terminal Domain.Hepatitis B Virus Polymerase Localizes to the Mitochondria, and Its Terminal Protein Domain Contains the Mitochondrial Targeting Signal.HBV maintains electrostatic homeostasis by modulating negative charges from phosphoserine and encapsidated nucleic acidsResidues Arg703, Asp777, and Arg781 of the RNase H domain of hepatitis B virus polymerase are critical for viral DNA synthesis.Engineering hepatitis B virus core particles for targeting HER2 receptors in vitro and in vivo.Large-scale production and structural and biophysical characterizations of the human hepatitis B virus polymerase.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.Discovery and Mechanistic Study of Benzamide Derivatives That Modulate Hepatitis B Virus Capsid Assembly.Polo-like-kinase 1 is a proviral host-factor for hepatitis B virus replication.Yield Optimisation of Hepatitis B Virus Core Particles in E. coli Expression System for Drug Delivery Applications.The interface between hepatitis B virus capsid proteins affects self-assembly, pregenomic RNA packaging, and reverse transcription.The Structural Biology of Hepatitis B Virus: Form and Function.Mutation of arginine residues to avoid non-specific cellular uptakes for hepatitis B virus core particles.Hepatitis virus capsid polymorph stability depends on encapsulated cargo size.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.Common and Distinct Capsid and Surface Protein Requirements for Secretion of Complete and Genome-free Hepatitis B Virions.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 AntiviralsPost-translational Modification Control of HBV Biological Processes
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P2860
The arginine clusters of the carboxy-terminal domain of the core protein of hepatitis B virus make pleiotropic contributions to genome replication.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
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
2010年论文
@zh
2010年论文
@zh-cn
name
The arginine clusters of the c ...... butions to genome replication.
@en
The arginine clusters of the c ...... butions to genome replication.
@nl
type
label
The arginine clusters of the c ...... butions to genome replication.
@en
The arginine clusters of the c ...... butions to genome replication.
@nl
prefLabel
The arginine clusters of the c ...... butions to genome replication.
@en
The arginine clusters of the c ...... butions to genome replication.
@nl
P2860
P356
P1433
P1476
The arginine clusters of the c ...... butions to genome replication.
@en
P2093
Daniel D Loeb
Eric B Lewellyn
P2860
P304
P356
10.1128/JVI.01957-10
P407
P577
2010-11-17T00:00:00Z