Evidence map›Paper›PMID 28790186›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Beyond icosahedral symmetry in packings of proteins in spherical shells.

Majid Mosayebi, Deborah K Shoemark, Jordan M Fletcher, Richard B Sessions, Noah Linden, Derek N Woolfson, Tanniemola B Liverpool

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
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

16 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Design strategies for the self-assembly of polyhedral shells.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  6. Anticancer Activity of Reconstituted Ribonuclease S-Decorated Artificial Viral Capsid.Chembiochem : a European journal of chemical biology · 2022
    Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Connectability of protein cages.Nanoscale advances · 2020
    Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. 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

7 authors.

Majid MosayebiSchool of Mathematics, University of Bristol, Bristol BS8 1TW, United Kingdom; t.liverpool@bristol.ac.uk majid.mosayebi@bristol.ac.uk n.linden@bristol.ac.uk d.n.woolfson@bristol.ac.uk.
Deborah K ShoemarkBrisSynBio, Life Sciences Building, Bristol BS8 1TQ, United Kingdom.
Jordan M FletcherSchool of Chemistry, University of Bristol, Bristol BS8 1TS, United Kingdom.
Richard B SessionsBrisSynBio, Life Sciences Building, Bristol BS8 1TQ, United Kingdom.
Noah LindenSchool of Mathematics, University of Bristol, Bristol BS8 1TW, United Kingdom; t.liverpool@bristol.ac.uk majid.mosayebi@bristol.ac.uk n.linden@bristol.ac.uk d.n.woolfson@bristol.ac.uk.
Derek N WoolfsonBrisSynBio, Life Sciences Building, Bristol BS8 1TQ, United Kingdom; t.liverpool@bristol.ac.uk majid.mosayebi@bristol.ac.uk n.linden@bristol.ac.uk d.n.woolfson@bristol.ac.uk.
Tanniemola B LiverpoolSchool of Mathematics, University of Bristol, Bristol BS8 1TW, United Kingdom; t.liverpool@bristol.ac.uk majid.mosayebi@bristol.ac.uk n.linden@bristol.ac.uk d.n.woolfson@bristol.ac.uk.

Funding

Biotechnology and Biological Sciences Research Council BB/L01386X/1Biotechnology and Biological Sciences Research Council BB/M002969/1
6 · The paper itself

Abstract

The formation of quasi-spherical cages from protein building blocks is a remarkable self-assembly process in many natural systems, where a small number of elementary building blocks are assembled to build a highly symmetric icosahedral cage. In turn, this has inspired synthetic biologists to design de novo protein cages. We use simple models, on multiple scales, to investigate the self-assembly of a spherical cage, focusing on the regularity of the packing of protein-like objects on the surface. Using building blocks, which are able to pack with icosahedral symmetry, we examine how stable these highly symmetric structures are to perturbations that may arise from the interplay between flexibility of the interacting blocks and entropic effects. We find that, in the presence of those perturbations, icosahedral packing is not the most stable arrangement for a wide range of parameters; rather disordered structures are found to be the most stable. Our results suggest that (

Indexed as

Models, MolecularProtein ConformationProtein MultimerizationAlgorithmsKineticsProteinsThermodynamicsProteinscoarse-grained modelingicosahedral symmetryprotein cageprotein designself-assembly

Identifiers

PMID28790186
PMCPMC5576817

What OpenQuestion holds

Textmetadata
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.