Evidence map›Paper›PMID 29097661›Full record

ArticleScientific reports2017

GRAFENE: Graphlet-based alignment-free network approach integrates 3D structural and sequence (residue order) data to improve protein structural comparison.

Fazle E Faisal, Khalique Newaz, Julie L Chaney, Jun Li, Scott J Emrich, Patricia L Clark, Tijana Milenković

Erratum issuedAbstract readComparative Study
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
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  9. Review
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  11. Article
  12. Article
  13. Network analysis of synonymous codon usage.Bioinformatics (Oxford, England) · 2020
    Article
  14. Article
  15. Chromatin network markers of leukemia.Bioinformatics (Oxford, England) · 2020
    Article
  16. Network-based protein structural classification.Royal Society open science · 2020
    Article
  17. Article
  18. Functional geometry of protein interactomes.Bioinformatics (Oxford, England) · 2019
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Fazle E FaisalDepartment of Computer Science and Engineering, University of Notre Dame, Notre Dame, IN, 46556, USA.
Khalique NewazDepartment of Computer Science and Engineering, University of Notre Dame, Notre Dame, IN, 46556, USA.
Julie L ChaneyDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN, 46556, USA.
Jun LiDepartment of Applied and Computational Mathematics and Statistics, University of Notre Dame, Notre Dame, IN, 46556, USA.
Scott J EmrichDepartment of Computer Science and Engineering, University of Notre Dame, Notre Dame, IN, 46556, USA.
Patricia L ClarkDepartment of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN, 46556, USA.
Tijana MilenkovićDepartment of Computer Science and Engineering, University of Notre Dame, Notre Dame, IN, 46556, USA. tmilenko@nd.edu.

Funding

Influence of Translation on Protein FoldingR01GM074807 · NIGMS · UNIVERSITY OF NOTRE DAME · PI CLARK, PATRICIA LOUISE · 2005 to 2014
$2.8M
Integrative computational framework for pattern mining in big -omics data: linking synonymous codon usage to protein biogenesisR01GM120733 · NIGMS · UNIVERSITY OF NOTRE DAME · PI CLARK, PATRICIA LOUISE, EMRICH, SCOTT · 2016 to 2019
$1.1M
A network-based method for predicting gene interactions in artemisinin resistanceR21AI111286 · NIAID · UNIVERSITY OF NOTRE DAME · PI FERDIG, MICHAEL T · 2015 to 2016
$418k
NIAID NIH HHS R21 AI111286NIGMS NIH HHS R01 GM074807NIGMS NIH HHS R01 GM120733
6 · The paper itself

Abstract

Initial protein structural comparisons were sequence-based. Since amino acids that are distant in the sequence can be close in the 3-dimensional (3D) structure, 3D contact approaches can complement sequence approaches. Traditional 3D contact approaches study 3D structures directly and are alignment-based. Instead, 3D structures can be modeled as protein structure networks (PSNs). Then, network approaches can compare proteins by comparing their PSNs. These can be alignment-based or alignment-free. We focus on the latter. Existing network alignment-free approaches have drawbacks: 1) They rely on naive measures of network topology. 2) They are not robust to PSN size. They cannot integrate 3) multiple PSN measures or 4) PSN data with sequence data, although this could improve comparison because the different data types capture complementary aspects of the protein structure. We address this by: 1) exploiting well-established graphlet measures via a new network alignment-free approach, 2) introducing normalized graphlet measures to remove the bias of PSN size, 3) allowing for integrating multiple PSN measures, and 4) using ordered graphlets to combine the complementary PSN data and sequence (specifically, residue order) data. We compare synthetic networks and real-world PSNs more accurately and faster than existing network (alignment-free and alignment-based), 3D contact, or sequence approaches.

Indexed as

SoftwareAlgorithmsAmino AcidsComputer GraphicsDatabases, ProteinModels, BiologicalProtein ConformationProteinsAmino AcidsProteins

Identifiers

PMID29097661
PMCPMC5668259

What OpenQuestion holds

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LicenceCC BY
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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.