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Detecting temporal protein complexes from dynamic protein-protein interaction networks

BACKGROUND: Proteins dynamically interact with each other to perform their biological functions. The dynamic operations of protein interaction networks (PPI) are also reflected in the dynamic formations of protein complexes. Existing protein complex detection algorithms usually overlook the inherent...

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Autores principales: Ou-Yang, Le, Dai, Dao-Qing, Li, Xiao-Li, Wu, Min, Zhang, Xiao-Fei, Yang, Peng
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4288635/
https://www.ncbi.nlm.nih.gov/pubmed/25282536
http://dx.doi.org/10.1186/1471-2105-15-335
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author Ou-Yang, Le
Dai, Dao-Qing
Li, Xiao-Li
Wu, Min
Zhang, Xiao-Fei
Yang, Peng
author_facet Ou-Yang, Le
Dai, Dao-Qing
Li, Xiao-Li
Wu, Min
Zhang, Xiao-Fei
Yang, Peng
author_sort Ou-Yang, Le
collection PubMed
description BACKGROUND: Proteins dynamically interact with each other to perform their biological functions. The dynamic operations of protein interaction networks (PPI) are also reflected in the dynamic formations of protein complexes. Existing protein complex detection algorithms usually overlook the inherent temporal nature of protein interactions within PPI networks. Systematically analyzing the temporal protein complexes can not only improve the accuracy of protein complex detection, but also strengthen our biological knowledge on the dynamic protein assembly processes for cellular organization. RESULTS: In this study, we propose a novel computational method to predict temporal protein complexes. Particularly, we first construct a series of dynamic PPI networks by joint analysis of time-course gene expression data and protein interaction data. Then a Time Smooth Overlapping Complex Detection model (TS-OCD) has been proposed to detect temporal protein complexes from these dynamic PPI networks. TS-OCD can naturally capture the smoothness of networks between consecutive time points and detect overlapping protein complexes at each time point. Finally, a nonnegative matrix factorization based algorithm is introduced to merge those very similar temporal complexes across different time points. CONCLUSIONS: Extensive experimental results demonstrate the proposed method is very effective in detecting temporal protein complexes than the state-of-the-art complex detection techniques. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/1471-2105-15-335) contains supplementary material, which is available to authorized users.
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spelling pubmed-42886352015-01-11 Detecting temporal protein complexes from dynamic protein-protein interaction networks Ou-Yang, Le Dai, Dao-Qing Li, Xiao-Li Wu, Min Zhang, Xiao-Fei Yang, Peng BMC Bioinformatics Research Article BACKGROUND: Proteins dynamically interact with each other to perform their biological functions. The dynamic operations of protein interaction networks (PPI) are also reflected in the dynamic formations of protein complexes. Existing protein complex detection algorithms usually overlook the inherent temporal nature of protein interactions within PPI networks. Systematically analyzing the temporal protein complexes can not only improve the accuracy of protein complex detection, but also strengthen our biological knowledge on the dynamic protein assembly processes for cellular organization. RESULTS: In this study, we propose a novel computational method to predict temporal protein complexes. Particularly, we first construct a series of dynamic PPI networks by joint analysis of time-course gene expression data and protein interaction data. Then a Time Smooth Overlapping Complex Detection model (TS-OCD) has been proposed to detect temporal protein complexes from these dynamic PPI networks. TS-OCD can naturally capture the smoothness of networks between consecutive time points and detect overlapping protein complexes at each time point. Finally, a nonnegative matrix factorization based algorithm is introduced to merge those very similar temporal complexes across different time points. CONCLUSIONS: Extensive experimental results demonstrate the proposed method is very effective in detecting temporal protein complexes than the state-of-the-art complex detection techniques. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/1471-2105-15-335) contains supplementary material, which is available to authorized users. BioMed Central 2014-10-04 /pmc/articles/PMC4288635/ /pubmed/25282536 http://dx.doi.org/10.1186/1471-2105-15-335 Text en © Ou-Yang et al.; licensee BioMed Central Ltd. 2014 This article is published under license to BioMed Central Ltd. 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 credited. 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 Article
Ou-Yang, Le
Dai, Dao-Qing
Li, Xiao-Li
Wu, Min
Zhang, Xiao-Fei
Yang, Peng
Detecting temporal protein complexes from dynamic protein-protein interaction networks
title Detecting temporal protein complexes from dynamic protein-protein interaction networks
title_full Detecting temporal protein complexes from dynamic protein-protein interaction networks
title_fullStr Detecting temporal protein complexes from dynamic protein-protein interaction networks
title_full_unstemmed Detecting temporal protein complexes from dynamic protein-protein interaction networks
title_short Detecting temporal protein complexes from dynamic protein-protein interaction networks
title_sort detecting temporal protein complexes from dynamic protein-protein interaction networks
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4288635/
https://www.ncbi.nlm.nih.gov/pubmed/25282536
http://dx.doi.org/10.1186/1471-2105-15-335
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