Evidence map›Paper›PMID 33239442›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

A complete rule set for designing symmetry combination materials from protein molecules.

Joshua Laniado, Todd O Yeates

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
  2. Article
  3. Chemical reviews · 2026
    Review
  4. Review
  5. Article
  6. Review
  7. Assembly and Functionality of 2D Protein Arrays.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Exploration of Structured Symmetric Cyclic Peptides as Ligands for Metal-Organic Frameworks.Chemistry of materials : a publication of the American Chemical Society · 2022
    Article
  17. Article
  18. Review
  19. Protein Assembly by Design.Chemical reviews · 2021
    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.

Joshua LaniadoMolecular Biology Institute, University of California, Los Angeles, CA 90095.ORCID 0000-0001-9441-616X
Todd O YeatesMolecular Biology Institute, University of California, Los Angeles, CA 90095; yeates@mbi.ucla.edu.ORCID 0000-0001-5709-9839

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Diverse efforts in protein engineering are beginning to produce novel kinds of symmetric self-assembling architectures, from protein cages to extended two-dimensional (2D) and three-dimensional (3D) crystalline arrays. Partial theoretical frameworks for creating symmetric protein materials have been introduced, but no complete system has been articulated. Only a minute fraction of the possible design space has been explored experimentally, in part because that space has not yet been described in theory. Here, in the form of a multiplication table, we lay out a complete rule set for materials that can be created by combining two chiral oligomeric components (e.g., proteins) in precise configurations. A unified system is described for parameterizing and searching the construction space for all such symmetry-combination materials (SCMs). In total, 124 distinct types of SCMs are identified, and then proven by computational construction. Mathematical properties, such as minimal ring or circuit size, are established for each case, enabling strategic predictions about potentially favorable design targets. The study lays out the theoretical landscape and detailed computational prescriptions for a rapidly growing area of protein-based nanotechnology, with numerous underlying connections to mathematical networks and chemical materials such as metal organic frameworks.

Indexed as

Models, ChemicalComputer SimulationMetal-Organic FrameworksNanotechnologyProtein EngineeringProteinsMetal-Organic FrameworksProteinsbiomaterialsnanotechnologyprotein designself-assemblysymmetry

Identifiers

PMID33239442
PMCPMC7749312

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.