Evidence map›Paper›PMID 37122282›Full record

ArticleJournal of the Royal Society, Interface2023

Homology of homologous knotted proteins.

Katherine Benjamin, Lamisah Mukta, Gabriel Moryoussef, Christopher Uren, Heather A Harrington, Ulrike Tillmann, Agnese Barbensi

Abstract read
In one paragraph

Article in Journal of the Royal Society, Interface, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Article
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  8. Homology of homologous knotted proteins.Journal of the Royal Society, Interface · 2023
    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

7 authors.

Katherine BenjaminMathematical Institute, University of Oxford, Oxford OX2 6GG, UK.
Lamisah MuktaMathematical Institute, University of Oxford, Oxford OX2 6GG, UK.
Gabriel MoryoussefMathematical Institute, University of Oxford, Oxford OX2 6GG, UK.
Christopher UrenMathematical Institute, University of Oxford, Oxford OX2 6GG, UK.
Heather A HarringtonMathematical Institute, University of Oxford, Oxford OX2 6GG, UK.ORCID 0000-0002-1705-7869
Ulrike TillmannMathematical Institute, University of Oxford, Oxford OX2 6GG, UK.
Agnese BarbensiMathematical Institute, University of Oxford, Oxford OX2 6GG, UK.ORCID 0000-0001-9348-4478

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Quantification and classification of protein structures, such as knotted proteins, often requires noise-free and complete data. Here, we develop a mathematical pipeline that systematically analyses protein structures. We showcase this geometric framework on proteins forming open-ended trefoil knots, and we demonstrate that the mathematical tool, persistent homology, faithfully represents their structural homology. This topological pipeline identifies important geometric features of protein entanglement and clusters the space of trefoil proteins according to their depth. Persistence landscapes quantify the topological difference between a family of knotted and unknotted proteins in the same structural homology class. This difference is localized and interpreted geometrically with recent advancements in systematic computation of homology generators. The topological and geometric quantification we find is robust to noisy input data, which demonstrates the potential of this approach in contexts where standard knot theoretic tools fail.

Indexed as

Protein ConformationProteinsProteinsgeneratorsknotted proteinspersistent homologytopological statistical analysis

Identifiers

PMID37122282
PMCPMC10130707

What OpenQuestion holds

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LicenceCC BY
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.