Evidence map›Paper›PMID 33563988›Full record

ArticleNature communications2021

Complete and cooperative in vitro assembly of computationally designed self-assembling protein nanomaterials.

Adam J Wargacki, Tobias P Wörner, Michiel van de Waterbeemd, Daniel Ellis, Albert J R Heck, Neil P King

Abstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

39 citing papers in PubMed.

  1. Review
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  9. Improving the immunogenicity ofFrontiers in immunology · 2026
    Article
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  11. Article
  12. Review
  13. From sequence to scaffold: Computational design of protein nanoparticle vaccines from AlphaFold2-predicted building blocks.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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

6 authors.

Adam J WargackiDepartment of Biochemistry, University of Washington, Seattle, WA, USA.
Tobias P WörnerBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, The Netherlands.
Michiel van de WaterbeemdBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, The Netherlands.
Daniel EllisDepartment of Biochemistry, University of Washington, Seattle, WA, USA.
Albert J R HeckBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, The Netherlands.ORCID 0000-0002-2405-4404
Neil P KingDepartment of Biochemistry, University of Washington, Seattle, WA, USA. neil@ipd.uw.edu.ORCID 0000-0002-2978-4692

Funding

Virus TransmissionP50AI150464 · NIAID · UNIVERSITY OF UTAH · PI SUNDQUIST, WESLEY I. · 2019 to 2021
$14.9M
NIAID NIH HHS P50 AI150464
6 · The paper itself

Abstract

Recent advances in computational methods have enabled the predictive design of self-assembling protein nanomaterials with atomic-level accuracy. These design strategies focus exclusively on a single target structure, without consideration of the mechanism or dynamics of assembly. However, understanding the assembly process, and in particular its robustness to perturbation, will be critical for translating this class of materials into useful technologies. Here we investigate the assembly of two computationally designed, 120-subunit icosahedral complexes in detail using several complementary biochemical methods. We found that assembly of each material from its two constituent protein building blocks was highly cooperative and yielded exclusively complete, 120-subunit complexes except in one non-stoichiometric regime for one of the materials. Our results suggest that in vitro assembly provides a robust and controllable route for the manufacture of designed protein nanomaterials and confirm that cooperative assembly can be an intrinsic, rather than evolved, feature of hierarchically structured protein complexes.

Indexed as

Computational ChemistryModels, MolecularNanostructuresProtein ConformationProtein MultimerizationProteinsProtein StabilityProtein SubunitsProteinsProtein Subunits

Identifiers

PMID33563988
PMCPMC7873210

What OpenQuestion holds

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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.