ArticleThe Journal of biological chemistry2015
Assembly Pathway of Hepatitis B Core Virus-like Particles from Genetically Fused Dimers.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
11 citing papers in PubMed, 26 citations in OpenAlex.
- Size-selective downstream processing of virus particles and non-enveloped virus-like particles.Frontiers in bioengineering and biotechnology · 2023Review
- Hierarchical Coarse-Grained Strategy for Macromolecular Self-Assembly: Application to Hepatitis B Virus-Like Particles.International journal of molecular sciences · 2022Article
- Packing and trimer-to-dimer protein reconstruction in icosahedral viral shells with a single type of symmetrical structural unit.Nanoscale advances · 2022Article
- Article
- Asymmetrizing an icosahedral virus capsid by hierarchical assembly of subunits with designed asymmetry.Nature communications · 2021Article
- Expression of quasi-equivalence and capsid dimorphism in the Hepadnaviridae.PLoS computational biology · 2020Article
- Impact of the Interaction of Hepatitis B Virus with Mitochondria and Associated Proteins.Viruses · 2020Review
- Multiple Pathways in Capsid Assembly.Journal of the American Chemical Society · 2018Article
- Hepatitis B Virus Capsid Completion Occurs through Error Correction.Journal of the American Chemical Society · 2017Article
- Production and purification of chimeric HBc virus-like particles carrying influenza virus LAH domain as vaccine candidates.BMC biotechnology · 2017Article
- HBV RNA pre-genome encodes specific motifs that mediate interactions with the viral core protein that promote nucleocapsid assembly.Nature microbiology · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Macromolecular complexes are responsible for many key biological processes. However, in most cases details of the assembly/disassembly of such complexes are unknown at the molecular level, as the low abundance and transient nature of assembly intermediates make analysis challenging. The assembly of virus capsids is an example of such a process. The hepatitis B virus capsid (core) can be composed of either 90 or 120 dimers of coat protein. Previous studies have proposed a trimer of dimers as an important intermediate species in assembly, acting to nucleate further assembly by dimer addition. Using novel genetically-fused coat protein dimers, we have been able to trap higher-order assembly intermediates and to demonstrate for the first time that both dimeric and trimeric complexes are on pathway to virus-like particle (capsid) formation.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.