ArticleIntervirology2014
Non-axial view of the varicella-zoster virus portal protein reveals conserved crown, wing and clip architecture.
Article in Intervirology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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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
5 citing papers in PubMed.
- Cryogenic electron tomography reveals herpesvirus capsid assembly intermediates inside the cell nucleus.Nature communications · 2026Article
- Small Molecule Compounds Inhibit Varicella-Zoster Virus Replication by Targeting the Portal Protein-Capsid Interface.Viruses · 2025Article
- Mutagenesis and functional analysis of the varicella-zoster virus portal protein.Journal of virology · 2024Article
- Review
- The varicella-zoster virus portal protein is essential for cleavage and packaging of viral DNA.Journal of virology · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
backgroundHerpesviridae encode a family of protein homologues that function as the 'port of entry' for insertion of the viral DNA into preformed capsids during encapsidation.
methodsTransmission electron microscopy (TEM) of recombinant varicella-zoster virus pORF54 was performed.
resultsResults suggest that pORF54 forms higher-order structures with itself. Enriched fractions analyzed by TEM revealed non-axial oriented portals with defined central channels and distinguishable crown, wing and clip regions.
conclusionThese morphological features are consistent with those previously reported for other herpesvirus and bacteriophage portal proteins.
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