Evidence map›Paper›PMID 28097215›Full record

ArticleScience advances2017

An ambiguity principle for assigning protein structural domains.

Guillaume Postic, Yassine Ghouzam, Romain Chebrek, Jean-Christophe Gelly

Abstract read
In one paragraph

Article in Science advances, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Family-level specialization in protein domain insertion architectures.Protein science : a publication of the Protein Society · 2026
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  5. Semi-supervised segmentation of RNA 3D structures using density-based clustering.Computational and structural biotechnology journal · 2025
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  18. Approaches for the Identification of Intrinsically Disordered Protein Domains.Methods in molecular biology (Clifton, N.J.) · 2023
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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

4 authors.

Guillaume PosticINSERM U1134, Paris, France.; Université Paris Diderot, Sorbonne Paris Cité, UMR_S 1134, Paris, France.; Institut National de la Transfusion Sanguine, Paris, France.; Laboratory of Excellence GR-Ex, Paris, France.
Yassine GhouzamINSERM U1134, Paris, France.; Université Paris Diderot, Sorbonne Paris Cité, UMR_S 1134, Paris, France.; Institut National de la Transfusion Sanguine, Paris, France.; Laboratory of Excellence GR-Ex, Paris, France.
Romain ChebrekINSERM U1134, Paris, France.; Université Paris Diderot, Sorbonne Paris Cité, UMR_S 1134, Paris, France.; Institut National de la Transfusion Sanguine, Paris, France.; Laboratory of Excellence GR-Ex, Paris, France.
Jean-Christophe GellyINSERM U1134, Paris, France.; Université Paris Diderot, Sorbonne Paris Cité, UMR_S 1134, Paris, France.; Institut National de la Transfusion Sanguine, Paris, France.; Laboratory of Excellence GR-Ex, Paris, France.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ambiguity is the quality of being open to several interpretations. For an image, it arises when the contained elements can be delimited in two or more distinct ways, which may cause confusion. We postulate that it also applies to the analysis of protein three-dimensional structure, which consists in dividing the molecule into subunits called domains. Because different definitions of what constitutes a domain can be used to partition a given structure, the same protein may have different but equally valid domain annotations. However, knowledge and experience generally displace our ability to accept more than one way to decompose the structure of an object-in this case, a protein. This human bias in structure analysis is particularly harmful because it leads to ignoring potential avenues of research. We present an automated method capable of producing multiple alternative decompositions of protein structure (web server and source code available at www.dsimb.inserm.fr/sword/). Our innovative algorithm assigns structural domains through the hierarchical merging of protein units, which are evolutionarily preserved substructures that describe protein architecture at an intermediate level, between domain and secondary structure. To validate the use of these protein units for decomposing protein structures into domains, we set up an extensive benchmark made of expert annotations of structural domains and including state-of-the-art domain parsing algorithms. The relevance of our "multipartitioning" approach is shown through numerous examples of applications covering protein function, evolution, folding, and structure prediction. Finally, we introduce a measure for the structural ambiguity of protein molecules.

Indexed as

AlgorithmsDatabases, ProteinModels, MolecularProtein DomainsProteinsProtein Structure, SecondaryProteinsprotein domainsProtein structurestructural bioinformaticsstructure partitioning

Identifiers

PMID28097215
PMCPMC5235333

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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.