ArticlehLife2024
Insights into varicella-zoster virus assembly from the B- and C-capsid at near-atomic resolution structures.
Article in hLife, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
16 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Varicella-zoster is a highly communicable virus that can be transmitted through the airborne route. About one quarter of people are infected with this virus. Previous studies have described the structure of A-capsid and a blurred reconstruction of the C-capsid with icosahedral symmetry. In this study, we have determined the more precise detailed structures of the varicella-zoster virus (VZV) B- and C-capsid in icosahedral symmetry using a combination of block-based reconstruction and symmetry relaxation strategies. In addition, we are reporting structural details of the portal vertex reconstructions in five-fold symmetry and portal reconstructions in twelve-fold symmetry. The structures unveil the basis for the high thermal stability of the VZV capsid. The conformational flexibility of structural elements of the capsid plays a role in the assembly of the capsid and drives processes critical for the viral life cycle. The results of the study open up new avenues for the development of drugs against a highly prevalent and contagious pathogen.
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.