Evidence map›Paper›PMID 21742267›Full record

ArticleStructure (London, England : 1993)2011

Insights into the evolution of a complex virus from the crystal structure of vaccinia virus D13.

Mohammad W Bahar, Stephen C Graham, David I Stuart, Jonathan M Grimes

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
3.7field-weighted citation impact, top 6% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

60 citing papers in PubMed, 94 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Maturation of Viruses.Sub-cellular biochemistry · 2024
    Review
  7. The Basic Architecture of Viruses.Sub-cellular biochemistry · 2024
    Review
  8. Assembly and Evolution of Poxviruses.Advances in experimental medicine and biology · 2024
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. In Silico Repurposed Drugs against Monkeypox Virus.Molecules (Basel, Switzerland) · 2022
    Article
  16. Longitudinal Aspects of VITT.Seminars in hematology · 2022
    Article
  17. Article
  18. Cellular homologs of the double jelly-roll major capsid proteins clarify the origins of an ancient virus kingdom.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Mohammad W BaharThe Division of Structural Biology and the Oxford Protein Production Facility, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, OX3 7BN, UK.
Stephen C Graham
David I Stuart
Jonathan M Grimes
Centre for Human Genetics · GB

Funding

Medical Research Council G1000099Medical Research Council G1100525Medical Research Council G19/3Wellcome Trust 075491/Z/04Wellcome Trust 090532
6 · The paper itself

Abstract

The morphogenesis of poxviruses such as vaccinia virus (VACV) sees the virion shape mature from spherical to brick-shaped. Trimeric capsomers of the VACV D13 protein form a transitory, stabilizing lattice on the surface of the initial spherical immature virus particle. The crystal structure of D13 reveals that this major scaffolding protein comprises a double β barrel "jelly-roll" subunit arranged as pseudo-hexagonal trimers. These structural features are characteristic of the major capsid proteins of a lineage of large icosahedral double-stranded DNA viruses including human adenovirus and the bacteriophages PRD1 and PM2. Structure-based phylogenetic analysis confirms that VACV belongs to this lineage, suggesting that (analogously to higher organism embryogenesis) early poxvirus morphogenesis reflects their evolution from a lineage of viruses sharing a common icosahedral ancestor.

Indexed as

Amino Acid SequenceBacteriophage PRD1Biological EvolutionCapsidCapsid ProteinsCloning, MolecularCorticoviridaeCrystallizationCrystallography, X-RayHumansModels, MolecularMolecular Sequence DataPhylogenyPlasmidsProtein ConformationProtein Structure, SecondaryCapsid ProteinsRecombinant Fusion Proteins

Identifiers

PMID21742267
PMCPMC3136756
OpenAlexW2122186275

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.