Evidence map›Paper›PMID 25361973›Full record

ArticleNucleic acids research2015

KnotProt: a database of proteins with knots and slipknots.

Michal Jamroz, Wanda Niemyska, Eric J Rawdon, Andrzej Stasiak, Kenneth C Millett, Piotr Sułkowski, Joanna I Sulkowska

Abstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing 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

86 citing papers in PubMed.

  1. Article
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  4. Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026
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  12. Article
  13. Knot data analysis using multiscale Gauss link integral.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  14. Is There a Functional Role for the Knotted Topology in Protein UCH-L1?Journal of chemical information and modeling · 2024
    Article
  15. Theta-curves in proteins.Protein science : a publication of the Protein Society · 2024
    Article
  16. Article
  17. Knotted artifacts in predicted 3D RNA structures.PLoS computational biology · 2024
    Article
  18. Article
  19. Evolutionary Khovanov homology.AIMS mathematics · 2024
    Article
  20. Article

26 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.

Michal JamrozFaculty of Chemistry, University of Warsaw, Pasteura 1, 02-093 Warsaw, Poland.
Wanda NiemyskaInstitute of Mathematics, University of Silesia, Bankowa 14, 40-007 Katowice, Poland.
Eric J RawdonDepartment of Mathematics, University of St. Thomas, Saint Paul, MN 55105, USA.
Andrzej StasiakCenter for Integrative Genomics, University of Lausanne, 1015-Lausanne, Switzerland jsulkowska@chem.uw.edu.pl.
Kenneth C MillettDepartment of Mathematics, University of California, Santa Barbara, CA 93106, USA.
Piotr SułkowskiFaculty of Physics, University of Warsaw, Pasteura 5, 02-093 Warsaw, Poland California Institute of Technology, Pasadena, CA 91125, USA jsulkowska@chem.uw.edu.pl.
Joanna I SulkowskaFaculty of Chemistry, University of Warsaw, Pasteura 1, 02-093 Warsaw, Poland Centre of New Technologies, University of Warsaw, Banacha 2c, 02-097, Warsaw, Poland jsulkowska@chem.uw.edu.pl.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The protein topology database KnotProt, http://knotprot.cent.uw.edu.pl/, collects information about protein structures with open polypeptide chains forming knots or slipknots. The knotting complexity of the cataloged proteins is presented in the form of a matrix diagram that shows users the knot type of the entire polypeptide chain and of each of its subchains. The pattern visible in the matrix gives the knotting fingerprint of a given protein and permits users to determine, for example, the minimal length of the knotted regions (knot's core size) or the depth of a knot, i.e. how many amino acids can be removed from either end of the cataloged protein structure before converting it from a knot to a different type of knot. In addition, the database presents extensive information about the biological functions, families and fold types of proteins with non-trivial knotting. As an additional feature, the KnotProt database enables users to submit protein or polymer chains and generate their knotting fingerprints.

Indexed as

Databases, ProteinProtein ConformationPeptidesPeptides

Identifiers

PMID25361973
PMCPMC4383900

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.