Evidence map›Paper›PMID 17434527›Full record

ArticleJournal of molecular biology2007

A simple, RNA-mediated allosteric switch controls the pathway to formation of a T=3 viral capsid.

Peter G Stockley, Ottar Rolfsson, Gary S Thompson, Gabriella Basnak, Simona Francese, Nicola J Stonehouse, Steven W Homans, Alison E Ashcroft

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
10.8field-weighted citation impact, top 1% 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

85 citing papers in PubMed, 152 citations in OpenAlex.

  1. Review
  2. Article
  3. Pleomorphism in Wild-Type and Engineered PP7 Virus-Like Particles.Small (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  4. Measuring the selective packaging of RNA molecules by viral coat proteins in cells.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Hierarchical assembly is more robust than egalitarian assembly in synthetic capsids.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

25 more citing papers are in PubMed but not listed here.

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

8 authors at 1 institution in 1 country.

Peter G StockleyAstbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, UK. stockley@bmb.leeds.ac.uk
Ottar Rolfsson
Gary S Thompson
Gabriella Basnak
Simona Francese
Nicola J Stonehouse
Steven W Homans
Alison E Ashcroft
University of Leeds · GB

Funding

Biotechnology and Biological Sciences Research Council BB/D01025X/1Wellcome Trust 062164
6 · The paper itself

Abstract

Using mass spectrometry we have detected both assembly intermediates and the final product, the T=3 viral capsid, during reassembly of the RNA bacteriophage MS2. Assembly is only efficient when both types of quasiequivalent coat protein dimer seen in the final capsid are present in solution. NMR experiments confirm that interconversion of these conformers is allosterically regulated by sequence-specific binding of a short RNA stem-loop. Isotope pulse-chase experiments confirm that all intermediates observed are competent for further coat protein addition, i.e., they are all on the pathway to capsid formation, and that the unit of capsid growth is a coat protein dimer. The major intermediate species are dominated by stoichiometries derived from formation of the particle threefold axis, implying that there is a defined pathway toward the T=3 shell. These results provide the first experimental evidence for a detailed mechanistic explanation of the regulation of quasiequivalent capsid assembly. They suggest a direct role for the encapsidated RNA in assembly in vivo, which is consistent with the structure of the genomic RNA within wild-type phage.

Indexed as

Allosteric RegulationCapsidLevivirusModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularNucleic Acid ConformationProtein ConformationRNASpectrometry, Mass, Electrospray IonizationRNA

Identifiers

PMID17434527
PMCPMC7612263
OpenAlexW1963600084

What OpenQuestion holds

Textmetadata
LicenceTDM
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.