Evidence map›Paper›PMID 33744290›Full record

ReviewThe Journal of biological chemistry

Icosahedral virus structures and the protein data bank.

John E Johnson, Arthur J Olson

Open access · goldAbstract readReview
In one paragraph

Review in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
4.2field-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

20 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. The virus lesson: Teaching viral structure and quasi-symmetry in mixed reality.Protein science : a publication of the Protein Society · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Point mutation in a virus-like capsid drives symmetry reduction to form tetrahedral cages.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. X-Ray Crystallography of Viruses.Sub-cellular biochemistry · 2024
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

John E JohnsonDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, USA. Electronic address: jackj@scripps.edu.
Arthur J OlsonDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, USA.
Scripps Research Institute · US

Funding

X-ray Crystallographic Fragment Screening CoreU54AI150472 · NIAID · SEATTLE CHILDREN'S HOSPITAL · PI LYUMKIS, DMITRY · 2019 to 2021
$15.7M
Modeling and Interacting with the Visible Molecular CellR01GM120604 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI AUTIN, LUDOVIC · 2016 to 2025
$4.2M
NIAID NIH HHS U54 AI150472NIGMS NIH HHS R01 GM120604
6 · The paper itself

Abstract

The structural study of icosahedral viruses has a long and impactful history in both crystallographic methodology and molecular biology. The evolution of the Protein Data Bank has paralleled and supported these studies providing readily accessible formats dealing with novel features associated with viral particle symmetries and subunit interactions. This overview describes the growth in size and complexity of icosahedral viruses from the first early studies of small RNA plant viruses and human picornaviruses up to the larger and more complex bacterial phage, insect, and human disease viruses such as Zika, hepatitis B, Adeno and Polyoma virus. The analysis of icosahedral viral capsid protein domain folds has shown striking similarities, with the beta jelly roll motif observed across multiple evolutionarily divergent species. The icosahedral symmetry of viruses drove the development of noncrystallographic symmetry averaging as a powerful phasing method, and the constraints of maintaining this symmetry resulted in the concept of quasi-equivalence in viral structures. Symmetry also played an important early role in demonstrating the power of cryo-electron microscopy as an alternative to crystallography in generating atomic resolution structures of these viruses. The Protein Data Bank has been a critical resource for assembling and disseminating these structures to a wide community, and the virus particle explorer (VIPER) was developed to enable users to easily generate and view complete viral capsid structures from their asymmetric building blocks. Finally, we share a personal perspective on the early use of computer graphics to communicate the intricacies, interactions, and beauty of these virus structures.

Indexed as

Databases, ProteinComputer GraphicsVirionVirusesstructural modelstructure–functionvirologyvirus assemblyvirus structure

Identifiers

PMID33744290
PMCPMC8081926
OpenAlexW3136584239

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.