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Dynamic identifying protein functional modules based on adaptive density modularity in protein-protein interaction networks

BACKGROUND: The identification of protein functional modules would be a great aid in furthering our knowledge of the principles of cellular organization. Most existing algorithms for identifying protein functional modules have a common defect -- once a protein node is assigned to a functional module...

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Detalles Bibliográficos
Autores principales: Shen, Xianjun, Yi, Li, Yi, Yang, Yang, Jincai, He, Tingting, Hu, Xiaohua
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4705501/
https://www.ncbi.nlm.nih.gov/pubmed/26330105
http://dx.doi.org/10.1186/1471-2105-16-S12-S5
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author Shen, Xianjun
Yi, Li
Yi, Yang
Yang, Jincai
He, Tingting
Hu, Xiaohua
author_facet Shen, Xianjun
Yi, Li
Yi, Yang
Yang, Jincai
He, Tingting
Hu, Xiaohua
author_sort Shen, Xianjun
collection PubMed
description BACKGROUND: The identification of protein functional modules would be a great aid in furthering our knowledge of the principles of cellular organization. Most existing algorithms for identifying protein functional modules have a common defect -- once a protein node is assigned to a functional module, there is no chance to move the protein to the other functional modules during the follow-up processes, which lead the erroneous partitioning occurred at previous step to accumulate till to the end. RESULTS: In this paper, we design a new algorithm ADM (Adaptive Density Modularity) to detect protein functional modules based on adaptive density modularity. In ADM algorithm, according to the comparison between external closely associated degree and internal closely associated degree, the partitioning of a protein-protein interaction network into functional modules always evolves quickly to increase the density modularity of the network. The integration of density modularity into the new algorithm not only overcomes the drawback mentioned above, but also contributes to identifying protein functional modules more effectively. CONCLUSIONS: The experimental result reveals that the performance of ADM algorithm is superior to many state-of-the-art protein functional modules detection techniques in aspect of the accuracy of prediction. Moreover, the identified protein functional modules are statistically significant in terms of "Biological Process" annotated in Gene Ontology, which provides substantial support for revealing the principles of cellular organization.
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spelling pubmed-47055012016-01-20 Dynamic identifying protein functional modules based on adaptive density modularity in protein-protein interaction networks Shen, Xianjun Yi, Li Yi, Yang Yang, Jincai He, Tingting Hu, Xiaohua BMC Bioinformatics Research BACKGROUND: The identification of protein functional modules would be a great aid in furthering our knowledge of the principles of cellular organization. Most existing algorithms for identifying protein functional modules have a common defect -- once a protein node is assigned to a functional module, there is no chance to move the protein to the other functional modules during the follow-up processes, which lead the erroneous partitioning occurred at previous step to accumulate till to the end. RESULTS: In this paper, we design a new algorithm ADM (Adaptive Density Modularity) to detect protein functional modules based on adaptive density modularity. In ADM algorithm, according to the comparison between external closely associated degree and internal closely associated degree, the partitioning of a protein-protein interaction network into functional modules always evolves quickly to increase the density modularity of the network. The integration of density modularity into the new algorithm not only overcomes the drawback mentioned above, but also contributes to identifying protein functional modules more effectively. CONCLUSIONS: The experimental result reveals that the performance of ADM algorithm is superior to many state-of-the-art protein functional modules detection techniques in aspect of the accuracy of prediction. Moreover, the identified protein functional modules are statistically significant in terms of "Biological Process" annotated in Gene Ontology, which provides substantial support for revealing the principles of cellular organization. BioMed Central 2015-08-25 /pmc/articles/PMC4705501/ /pubmed/26330105 http://dx.doi.org/10.1186/1471-2105-16-S12-S5 Text en Copyright © 2015 Shen et al.; http://creativecommons.org/licenses/by/4.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Research
Shen, Xianjun
Yi, Li
Yi, Yang
Yang, Jincai
He, Tingting
Hu, Xiaohua
Dynamic identifying protein functional modules based on adaptive density modularity in protein-protein interaction networks
title Dynamic identifying protein functional modules based on adaptive density modularity in protein-protein interaction networks
title_full Dynamic identifying protein functional modules based on adaptive density modularity in protein-protein interaction networks
title_fullStr Dynamic identifying protein functional modules based on adaptive density modularity in protein-protein interaction networks
title_full_unstemmed Dynamic identifying protein functional modules based on adaptive density modularity in protein-protein interaction networks
title_short Dynamic identifying protein functional modules based on adaptive density modularity in protein-protein interaction networks
title_sort dynamic identifying protein functional modules based on adaptive density modularity in protein-protein interaction networks
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4705501/
https://www.ncbi.nlm.nih.gov/pubmed/26330105
http://dx.doi.org/10.1186/1471-2105-16-S12-S5
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