Evidence map›Paper›PMID 31009453›Full record

ArticlePLoS computational biology2019

Analyzing the symmetrical arrangement of structural repeats in proteins with CE-Symm.

Spencer E Bliven, Aleix Lafita, Peter W Rose, Guido Capitani, Andreas Prlić, Philip E Bourne

Abstract read
In one paragraph

Article in PLoS computational biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Structured Tandem Repeats in Protein Interactions.International journal of molecular sciences · 2024
    Article
  9. Review
  10. Antibiotics (Basel, Switzerland) · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. Frequency distribution of space groups in soluble and membrane proteins and their complexes.Acta crystallographica. Section F, Structural biology communications · 2021
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Development and applications of artificial symmetrical proteins.Computational and structural biotechnology journal · 2020
    Review
  20. Review
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

6 authors.

Spencer E BlivenLaboratory of Biomolecular Research, Paul Scherrer Institute, Villigen, Switzerland.ORCID 0000-0002-1200-1698
Aleix LafitaLaboratory of Biomolecular Research, Paul Scherrer Institute, Villigen, Switzerland.ORCID 0000-0003-1549-3162
Peter W RoseRCSB Protein Data Bank, San Diego Supercomputing Center, University of California San Diego, La Jolla, California, United States of America.ORCID 0000-0001-9981-9750
Guido CapitaniLaboratory of Biomolecular Research, Paul Scherrer Institute, Villigen, Switzerland.
Andreas PrlićRCSB Protein Data Bank, San Diego Supercomputing Center, University of California San Diego, La Jolla, California, United States of America.ORCID 0000-0001-6346-6391
Philip E BourneNational Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, Maryland, United States of America.ORCID 0000-0002-7618-7292

Funding

PDB MANAGEMENT BY THE RESEARCH COLLABORATORY FOR STRUCTURAL BIOINFORMATICSR01GM133198 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI BURLEY, STEPHEN K · 2019 to 2023
$19.3M
NIGMS NIH HHS R01 GM133198
6 · The paper itself

Abstract

Many proteins fold into highly regular and repetitive three dimensional structures. The analysis of structural patterns and repeated elements is fundamental to understand protein function and evolution. We present recent improvements to the CE-Symm tool for systematically detecting and analyzing the internal symmetry and structural repeats in proteins. In addition to the accurate detection of internal symmetry, the tool is now capable of i) reporting the type of symmetry, ii) identifying the smallest repeating unit, iii) describing the arrangement of repeats with transformation operations and symmetry axes, and iv) comparing the similarity of all the internal repeats at the residue level. CE-Symm 2.0 helps the user investigate proteins with a robust and intuitive sequence-to-structure analysis, with many applications in protein classification, functional annotation and evolutionary studies. We describe the algorithmic extensions of the method and demonstrate its applications to the study of interesting cases of protein evolution.

Indexed as

AlgorithmsSoftwareAmino Acid SequenceComputational BiologyDatabases, ProteinModels, MolecularProteinsSequence Analysis, ProteinProteins

Identifiers

PMID31009453
PMCPMC6504099

What OpenQuestion holds

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LicenceCC0
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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.