Evidence map›Paper›PMID 25288768›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Computational design of a self-assembling symmetrical β-propeller protein.

Arnout R D Voet, Hiroki Noguchi, Christine Addy, David Simoncini, Daiki Terada, Satoru Unzai, Sam-Yong Park, Kam Y J Zhang, Jeremy R H Tame

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
6.4field-weighted citation impact, top 2% 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

57 citing papers in PubMed, 130 citations in OpenAlex.

  1. Article
  2. Review
  3. Stability and cooperativity in chimeric de novo TIM barrels via quarter swapping.Protein science : a publication of the Protein Society · 2026
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  5. Parametrically guided design of beta barrels and transmembrane nanopores using deep learning.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Peptide-RNA Coacervates as a Cradle for the Evolution of Folded Domains.Journal of the American Chemical Society · 2022
    Article
  12. Article
  13. Article
  14. Review
  15. De novo metalloprotein design.Nature reviews. Chemistry · 2022
    Article
  16. Article
  17. Protein Assembly by Design.Chemical reviews · 2021
    Review
  18. Article
  19. Article
  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

9 authors at 1 institution in 1 country.

Arnout R D VoetStructural Bioinformatics Team, Division of Structural and Synthetic Biology, Center for Life Science Technologies, RIKEN, 1-7-22 Suehiro, Yokohama, Kanagawa 230-0045, Japan; and Drug Design Laboratory, Graduate School of Medical Life Science, Yokohama City University, 1-7-29 Suehiro, Yokohama, Kanagawa 230-0045, Japan.
Hiroki NoguchiDrug Design Laboratory, Graduate School of Medical Life Science, Yokohama City University, 1-7-29 Suehiro, Yokohama, Kanagawa 230-0045, Japan.
Christine AddyDrug Design Laboratory, Graduate School of Medical Life Science, Yokohama City University, 1-7-29 Suehiro, Yokohama, Kanagawa 230-0045, Japan.
David SimonciniStructural Bioinformatics Team, Division of Structural and Synthetic Biology, Center for Life Science Technologies, RIKEN, 1-7-22 Suehiro, Yokohama, Kanagawa 230-0045, Japan; and.
Daiki TeradaDrug Design Laboratory, Graduate School of Medical Life Science, Yokohama City University, 1-7-29 Suehiro, Yokohama, Kanagawa 230-0045, Japan.
Satoru UnzaiDrug Design Laboratory, Graduate School of Medical Life Science, Yokohama City University, 1-7-29 Suehiro, Yokohama, Kanagawa 230-0045, Japan.
Sam-Yong ParkDrug Design Laboratory, Graduate School of Medical Life Science, Yokohama City University, 1-7-29 Suehiro, Yokohama, Kanagawa 230-0045, Japan.
Kam Y J ZhangStructural Bioinformatics Team, Division of Structural and Synthetic Biology, Center for Life Science Technologies, RIKEN, 1-7-22 Suehiro, Yokohama, Kanagawa 230-0045, Japan; and kamzhang@riken.jp jtame@tsurumi.yokohama-cu.ac.jp.
Jeremy R H TameDrug Design Laboratory, Graduate School of Medical Life Science, Yokohama City University, 1-7-29 Suehiro, Yokohama, Kanagawa 230-0045, Japan kamzhang@riken.jp jtame@tsurumi.yokohama-cu.ac.jp.
Yokohama City University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The modular structure of many protein families, such as β-propeller proteins, strongly implies that duplication played an important role in their evolution, leading to highly symmetrical intermediate forms. Previous attempts to create perfectly symmetrical propeller proteins have failed, however. We have therefore developed a new and rapid computational approach to design such proteins. As a test case, we have created a sixfold symmetrical β-propeller protein and experimentally validated the structure using X-ray crystallography. Each blade consists of 42 residues. Proteins carrying 2-10 identical blades were also expressed and purified. Two or three tandem blades assemble to recreate the highly stable sixfold symmetrical architecture, consistent with the duplication and fusion theory. The other proteins produce different monodisperse complexes, up to 42 blades (180 kDa) in size, which self-assemble according to simple symmetry rules. Our procedure is suitable for creating nano-building blocks from different protein templates of desired symmetry.

Indexed as

Protein EngineeringProtein Structure, SecondaryAmino Acid SequenceBiophysicsCircular DichroismCrystallography, X-RayLightModels, MolecularModels, TheoreticalMolecular Sequence DataMycobacterium tuberculosisNanotechnologyProteinsScattering, RadiationSequence Homology, Amino AcidSoftwareProteinscomputational protein designprotein crystallographyprotein evolutionself-assemblyβ-propeller

Identifiers

PMID25288768
PMCPMC4210308
OpenAlexW2048351668

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.