Evidence map›Paper›PMID 20686683›Full record

ArticlePLoS computational biology2010

Knotted vs. unknotted proteins: evidence of knot-promoting loops.

Raffaello Potestio, Cristian Micheletti, Henri Orland

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 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing 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

35 citing papers in PubMed.

  1. Review
  2. 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
  3. Article
  4. Article
  5. Homology of homologous knotted proteins.Journal of the Royal Society, Interface · 2023
    Article
  6. Are there double knots in proteins? Prediction andFrontiers in molecular biosciences · 2023
    Article
  7. AlphaFold predicts the most complex protein knot and composite protein knots.Protein science : a publication of the Protein Society · 2022
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Molecular Knots.Angewandte Chemie (International ed. in English) · 2017
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Absence of knots in known RNA structures.Proceedings of the National Academy of Sciences of the United States of America · 2015
    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.

Raffaello PotestioSISSA - Scuola Internazionale Superiore di Studi Avanzati, Trieste, Italy.
Cristian Micheletti
Henri Orland

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Knotted proteins, because of their ability to fold reversibly in the same topologically entangled conformation, are the object of an increasing number of experimental and theoretical studies. The aim of the present investigation is to assess, on the basis of presently available structural data, the extent to which knotted proteins are isolated instances in sequence or structure space, and to use comparative schemes to understand whether specific protein segments can be associated to the occurrence of a knot in the native state. A significant sequence homology is found among a sizeable group of knotted and unknotted proteins. In this family, knotted members occupy a primary sub-branch of the phylogenetic tree and differ from unknotted ones only by additional loop segments. These "knot-promoting" loops, whose virtual bridging eliminates the knot, are found in various types of knotted proteins. Valuable insight into how knots form, or are encoded, in proteins could be obtained by targeting these regions in future computational studies or excision experiments.

Indexed as

Protein ConformationAnimalsCarbonic Anhydrase IIComputational BiologyDatabases, ProteinHumansIsomerismModels, MolecularNuclear ProteinsPhylogenyProteinsProtein Structure, TertiaryRNA-Binding ProteinsSequence AlignmentSequence Analysis, ProteinTrans-Activation Responsive RNA-Binding ProteinCarbonic Anhydrase IINuclear ProteinsProteinsRNA-Binding ProteinsTARBP1 protein, humanTrans-Activation Responsive RNA-Binding Protein

Identifiers

PMID20686683
PMCPMC2912335

What OpenQuestion holds

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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.