Evidence map›Paper›PMID 28281548›Full record

ArticleNature communications2017

Structure and assembly of scalable porous protein cages.

Eita Sasaki, Daniel Böhringer, Michiel van de Waterbeemd, Marc Leibundgut, Reinhard Zschoche, Albert J R Heck, Nenad Ban, Donald Hilvert

Abstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing 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

43 citing papers in PubMed.

  1. Article
  2. Article
  3. Chemical reviews · 2026
    Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. 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
  9. Article
  10. Article
  11. Article
  12. An interaction network approach predicts protein cage architectures in bionanotechnology.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Artificial Organelles: Towards Adding or Restoring Intracellular Activity.Chembiochem : a European journal of chemical biology · 2021
    Review
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.

Eita SasakiDepartment of Chemistry and Applied Biosciences, Laboratory of Organic Chemistry, ETH Zürich, Zürich 8093, Switzerland.ORCID 0000-0002-8202-4465
Daniel BöhringerDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zürich, Zürich 8093, Switzerland.
Michiel van de WaterbeemdBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, CH Utrecht 3584, The Netherlands.
Marc LeibundgutDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zürich, Zürich 8093, Switzerland.
Reinhard ZschocheDepartment of Chemistry and Applied Biosciences, Laboratory of Organic Chemistry, ETH Zürich, Zürich 8093, Switzerland.
Albert J R HeckBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, CH Utrecht 3584, The Netherlands.
Nenad BanDepartment of Biology, Institute of Molecular Biology and Biophysics, ETH Zürich, Zürich 8093, Switzerland.
Donald HilvertDepartment of Chemistry and Applied Biosciences, Laboratory of Organic Chemistry, ETH Zürich, Zürich 8093, Switzerland.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins that self-assemble into regular shell-like polyhedra are useful, both in nature and in the laboratory, as molecular containers. Here we describe cryo-electron microscopy (EM) structures of two versatile encapsulation systems that exploit engineered electrostatic interactions for cargo loading. We show that increasing the number of negative charges on the lumenal surface of lumazine synthase, a protein that naturally assembles into a ∼1-MDa dodecahedron composed of 12 pentamers, induces stepwise expansion of the native protein shell, giving rise to thermostable ∼3-MDa and ∼6-MDa assemblies containing 180 and 360 subunits, respectively. Remarkably, these expanded particles assume unprecedented tetrahedrally and icosahedrally symmetric structures constructed entirely from pentameric units. Large keyhole-shaped pores in the shell, not present in the wild-type capsid, enable diffusion-limited encapsulation of complementarily charged guests. The structures of these supercharged assemblies demonstrate how programmed electrostatic effects can be effectively harnessed to tailor the architecture and properties of protein cages.

Indexed as

BacteriaBacterial ProteinsCloning, MolecularCryoelectron MicroscopyDrug CarriersEscherichia coliGene ExpressionMultienzyme ComplexesPorosityProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein EngineeringProtein Interaction Domains and MotifsProtein MultimerizationProtein SubunitsRecombinant Proteins6,7-dimethyl-8-ribityllumazine synthaseBacterial ProteinsDrug CarriersMultienzyme ComplexesProtein SubunitsRecombinant Proteins

Identifiers

PMID28281548
PMCPMC5354205

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.