A recombinant hepatitis B core antigen polypeptide with the protamine-like domain deleted self-assembles into capsid particles but fails to bind nucleic acids.
about
Hepatitis B virus morphogenesisPreparation by alkaline treatment and detailed characterisation of empty hepatitis B virus core particles for vaccine and gene therapy applications.Chimeric hepatitis B virus core particles with parts or copies of the hepatitis C virus core protein3.5Å cryoEM Structure of Hepatitis B Virus Core Assembled from Full-Length Core ProteinHepatitis B virus nucleocapsid assembly: primary structure requirements in the core protein.Nucleic acid chaperone activity associated with the arginine-rich domain of human hepatitis B virus core protein.A structural model for maturation of the hepatitis B virus coreRab33B Controls Hepatitis B Virus Assembly by Regulating Core Membrane Association and Nucleocapsid Processing.Testing the balanced electrostatic interaction hypothesis of hepatitis B virus DNA synthesis by using an in vivo charge rebalance approachFunctional characterization of naturally occurring variants of human hepatitis B virus containing the core internal deletion mutation.Phosphorylation of the core protein of hepatitis B virus by a 46-kilodalton serine kinase.Interaction between hepatitis B virus core protein and reverse transcriptase.Hepatitis B virus core antigen determines viral persistence in a C57BL/6 mouse model.Cys residues of the hepatitis B virus capsid protein are not essential for the assembly of viral core particles but can influence their stability.Morphogenesis of hepatitis B virus and its subviral envelope particlesSecretion of genome-free hepatitis B virus--single strand blocking model for virion morphogenesis of para-retrovirus.Phosphoacceptors 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 kinase chaperones hepatitis B virus capsid assembly and captures capsid dynamics in vitro.The morphogenic linker peptide of HBV capsid protein forms a mobile array on the interior surfaceThe hepatitis B virus core protein intradimer interface modulates capsid assembly and stability.C-terminal substitution of HBV core proteins with those from DHBV reveals that arginine-rich 167RRRSQSPRR175 domain is critical for HBV replication.Hepatitis B viral core protein disrupts human host gene expression by binding to promoter regions.A VLP library of C-terminally truncated Hepatitis B core proteins: correlation of RNA encapsidation with a Th1/Th2 switch in the immune responses of mice.HBV life cycle: entry and morphogenesis.A theoretical model for the dynamic structure of hepatitis B nucleocapsidAn Aptamer against the Matrix Binding Domain on the Hepatitis B Virus Capsid Impairs Virion FormationPhosphorylation and nuclear localization of the hepatitis B virus core protein: significance of serine in the three repeated SPRRR motifs.Detection of an RNase H activity associated with hepadnaviruses.The hepatitis B virus (HBV) precore protein inhibits HBV replication in transgenic mice.A hydrophobic heptad repeat of the core protein of woodchuck hepatitis virus is required for capsid assembly.Posttranscriptional regulation of hepatitis B virus replication by the precore protein.A Thermodynamic Model for Genome Packaging in Hepatitis B Virus.Phosphorylation-dependent binding of hepatitis B virus core particles to the nuclear pore complex.Capsid assembly and involved function analysis of twelve core protein mutants of duck hepatitis B virusA protease-sensitive hinge linking the two domains of the hepatitis B virus core protein is exposed on the viral capsid surface.A micromolar pool of antigenically distinct precursors is required to initiate cooperative assembly of hepatitis B virus capsids in Xenopus oocytes.The position of heterologous epitopes inserted in hepatitis B virus core particles determines their immunogenicity.Hepatitis B virus core antigen has two nuclear localization sequences in the arginine-rich carboxyl terminusCharacterization of hepatitis B virus capsid particle assembly in Xenopus oocytes.Differential formation of disulfide linkages in the core antigen of extracellular and intracellular hepatitis B virus core particles.
P2860
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P2860
A recombinant hepatitis B core antigen polypeptide with the protamine-like domain deleted self-assembles into capsid particles but fails to bind nucleic acids.
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
1989年论文
@zh
1989年论文
@zh-cn
name
A recombinant hepatitis B core ...... t fails to bind nucleic acids.
@ast
A recombinant hepatitis B core ...... t fails to bind nucleic acids.
@en
type
label
A recombinant hepatitis B core ...... t fails to bind nucleic acids.
@ast
A recombinant hepatitis B core ...... t fails to bind nucleic acids.
@en
prefLabel
A recombinant hepatitis B core ...... t fails to bind nucleic acids.
@ast
A recombinant hepatitis B core ...... t fails to bind nucleic acids.
@en
P2093
P2860
P1433
P1476
A recombinant hepatitis B core ...... t fails to bind nucleic acids.
@en
P2093
P2860
P304
P407
P577
1989-11-01T00:00:00Z