Evidence map›Paper›PMID 25168413›Full record

ReviewTrends in biotechnology2014

Superglue from bacteria: unbreakable bridges for protein nanotechnology.

Gianluca Veggiani, Bijan Zakeri, Mark Howarth

Abstract readReview
In one paragraph

Review in Trends in biotechnology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing 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

49 citing papers in PubMed.

  1. Review
  2. Article
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  5. Review
  6. De Novo Design of Proteins for Autocatalytic Isopeptide Bond Formation.Journal of the American Chemical Society · 2025
    Article
  7. Article
  8. Review
  9. Article
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  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
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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

3 authors.

Gianluca VeggianiDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Bijan ZakeriMIT Synthetic Biology Center, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.
Mark HowarthDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK. Electronic address: mark.howarth@bioch.ox.ac.uk.

Funding

European Research Council 615945
6 · The paper itself

Abstract

Biotechnology is often limited by weak interactions. We suggest that an ideal interaction between proteins would be covalent, specific, require addition of only a peptide tag to the protein of interest, and form under a wide range of conditions. Here we summarize peptide tags that are able to form spontaneous amide bonds, based on harnessing reactions of adhesion proteins from the bacterium Streptococcus pyogenes. These include the irreversible peptide-protein interaction of SpyTag with SpyCatcher, as well as irreversible peptide-peptide interactions via SpyLigase. We describe existing applications, including polymerization to enhance cancer cell capture, assembly of living biomaterial, access to diverse protein shapes, and improved enzyme resilience. We also indicate future opportunities for resisting biological force and extending the scope of protein nanotechnology.

Indexed as

Adhesins, BacterialBiotechnologyNanotechnologyProtein EngineeringRecombinant ProteinsModels, MolecularStreptococcus pyogenesAdhesins, BacterialRecombinant Proteinsbiomimeticmechanobiologynanobiotechnologyprotein engineeringsupramolecular assemblysynthetic biology

Identifiers

PMID25168413
PMCPMC4281928

What OpenQuestion holds

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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.