Structural comparisons of hepatitis B core antigen particles with different C-terminal lengths.
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Summary
Three-dimensional structures of hepatitis B virus particles reconstructed by cryo-electron microscopy showed that their capsid structures are highly similar, while the RNA content is increased upon the retention of more amino acid residues at the C-terminus of core protein, suggesting the crucial role of the basic C- terminal tail on determining the genome size.
- Type
- article
- Published
- 2010-05-01
- Cited by
- 14
- References
- 25
- OpenAlex
- https://openalex.org/W20144668
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:31235043
Keywords
Computer science
References
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Cited by
- An Investigation into the Use of a Plant-Expressed Virus-Like Particle as an Oral Vaccine Candidate
- A Thermodynamic Model for Genome Packaging in Hepatitis B Virus.
- Density functional theory for encapsidated polyelectrolytes: a comparison with Monte Carlo simulation.
- 3.5Å cryoEM Structure of Hepatitis B Virus Core Assembled from Full-Length Core Protein
- Naturally occurring core immune-escape and carboxy-terminal mutations in patients with e antigen negative chronic hepatitis B
- Secretion of Genome-Free Hepatitis B Virus – Single Strand Blocking Model for Virion Morphogenesis of Para-retrovirus
- The true story and advantages of the famous Hepatitis B virus core particles: Outlook 2016
- Discovery and Mechanistic Study of Benzamide Derivatives That Modulate Hepatitis B Virus Capsid Assembly
- Cumulative Author Index for 2010
- Effects of Different Lengths of a Nucleic Acid Binding Region and Bound Nucleic Acids on the Phase Behavior and Purification Process of HBcAg Virus-Like Particles
- Human adenovirus type 7 virus-like particle vaccine induces Dendritic cell maturation through the TLR4/NF-κB pathway and is highly immunogenic.
- Effective removal of host cell-derived nucleic acids bound to hepatitis B core antigen virus-like particles by heparin chromatography
- Molecular Models for Hepatitis B Virus Capsid Formation, Maturation, and Envelopment
- core assembled from full-length core protein.
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