Evidence map›Paper›PMID 20369018›Full record

ArticlePLoS computational biology2010

A Stevedore's protein knot.

Daniel Bölinger, Joanna I Sułkowska, Hsiao-Ping Hsu, Leonid A Mirny, Mehran Kardar, José N Onuchic, Peter Virnau

Abstract read
In one paragraph

Article in PLoS computational biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing 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

79 citing papers in PubMed.

  1. Review
  2. Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026
    Review
  3. 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
  4. Article
  5. Is There a Functional Role for the Knotted Topology in Protein UCH-L1?Journal of chemical information and modeling · 2024
    Article
  6. Theta-curves in proteins.Protein science : a publication of the Protein Society · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Folding kinetics of an entangled protein.PLoS computational biology · 2023
    Article
  11. Entangled Motifs in Membrane Protein Structures.International journal of molecular sciences · 2023
    Article
  12. AlphaFold predicts novel human proteins with knots.Protein science : a publication of the Protein Society · 2023
    Article
  13. Article
  14. Article
  15. Are there double knots in proteins? Prediction andFrontiers in molecular biosciences · 2023
    Article
  16. Article
  17. AlphaFold predicts the most complex protein knot and composite protein knots.Protein science : a publication of the Protein Society · 2022
    Article
  18. Article
  19. Article
  20. Article

19 more citing papers are in PubMed but not listed here.

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

7 authors.

Daniel BölingerDepartment of Physics, Johannes Gutenberg-Universität Mainz, Mainz, Germany.
Joanna I Sułkowska
Hsiao-Ping Hsu
Leonid A Mirny
Mehran Kardar
José N Onuchic
Peter Virnau

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein knots, mostly regarded as intriguing oddities, are gradually being recognized as significant structural motifs. Seven distinctly knotted folds have already been identified. It is by and large unclear how these exceptional structures actually fold, and only recently, experiments and simulations have begun to shed some light on this issue. In checking the new protein structures submitted to the Protein Data Bank, we encountered the most complex and the smallest knots to date: A recently uncovered alpha-haloacid dehalogenase structure contains a knot with six crossings, a so-called Stevedore knot, in a projection onto a plane. The smallest protein knot is present in an as yet unclassified protein fragment that consists of only 92 amino acids. The topological complexity of the Stevedore knot presents a puzzle as to how it could possibly fold. To unravel this enigma, we performed folding simulations with a structure-based coarse-grained model and uncovered a possible mechanism by which the knot forms in a single loop flip.

Indexed as

Molecular Dynamics SimulationProtein FoldingDatabases, ProteinHydrolasesProtein Conformation2-haloacid dehalogenaseHydrolases

Identifiers

PMID20369018
PMCPMC2848546

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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.