Evidence map›Paper›PMID 27806097›Full record

ArticlePloS one2016

In Search of Functional Advantages of Knots in Proteins.

Pawel Dabrowski-Tumanski, Andrzej Stasiak, Joanna I Sulkowska

Abstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed.

  1. Novel Knotted Solenoid fold with order-shifted coil arrangement leads to nontrivial 3Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Biomolecular NMR assignments · 2026
    Article
  3. Article
  4. Theta-curves in proteins.Protein science : a publication of the Protein Society · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Homology of homologous knotted proteins.Journal of the Royal Society, Interface · 2023
    Article
  11. Are there double knots in proteins? Prediction andFrontiers in molecular biosciences · 2023
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. A ravel alliance.Nature chemistry · 2021
    Article
  18. Open questions in functional molecular topology.Communications chemistry · 2020
    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

3 authors.

Pawel Dabrowski-TumanskiCentre of New Technologies, Banacha 2c, 02-097, Warsaw, Poland.
Andrzej StasiakCenter for Integrative Genomics, University of Lausanne, 1015-Lausanne, Switzerland.ORCID http://orcid.org/0000-0002-0398-1989
Joanna I SulkowskaCentre of New Technologies, Banacha 2c, 02-097, Warsaw, Poland.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We analysed the structure of deeply knotted proteins representing three unrelated families of knotted proteins. We looked at the correlation between positions of knotted cores in these proteins and such local structural characteristics as the number of intra-chain contacts, structural stability and solvent accessibility. We observed that the knotted cores and especially their borders showed strong enrichment in the number of contacts. These regions showed also increased thermal stability, whereas their solvent accessibility was decreased. Interestingly, the active sites within these knotted proteins preferentially located in the regions with increased number of contacts that also have increased thermal stability and decreased solvent accessibility. Our results suggest that knotting of polypeptide chains provides a favourable environment for the active sites observed in knotted proteins. Some knotted proteins have homologues without a knot. Interestingly, these unknotted homologues form local entanglements that retain structural characteristics of the knotted cores.

Indexed as

Catalytic DomainModels, MolecularProtein FoldingProteinsProtein StabilityProtein Structure, SecondarySolventsProteinsSolvents

Identifiers

PMID27806097
PMCPMC5091781

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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.