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Construction of dynamic probabilistic protein interaction networks for protein complex identification
BACKGROUND: Recently, high-throughput experimental techniques have generated a large amount of protein-protein interaction (PPI) data which can construct large complex PPI networks for numerous organisms. System biology attempts to understand cellular organization and function by analyzing these PPI...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4847341/ https://www.ncbi.nlm.nih.gov/pubmed/27117946 http://dx.doi.org/10.1186/s12859-016-1054-1 |
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author | Zhang, Yijia Lin, Hongfei Yang, Zhihao Wang, Jian |
author_facet | Zhang, Yijia Lin, Hongfei Yang, Zhihao Wang, Jian |
author_sort | Zhang, Yijia |
collection | PubMed |
description | BACKGROUND: Recently, high-throughput experimental techniques have generated a large amount of protein-protein interaction (PPI) data which can construct large complex PPI networks for numerous organisms. System biology attempts to understand cellular organization and function by analyzing these PPI networks. However, most studies still focus on static PPI networks which neglect the dynamic information of PPI. RESULTS: The gene expression data under different time points and conditions can reveal the dynamic information of proteins. In this study, we used an active probability-based method to distinguish the active level of proteins at different active time points. We constructed dynamic probabilistic protein networks (DPPN) to integrate dynamic information of protein into static PPI networks. Based on DPPN, we subsequently proposed a novel method to identify protein complexes, which could effectively exploit topological structure as well as dynamic information of DPPN. We used three different yeast PPI datasets and gene expression data to construct three DPPNs. When applied to three DPPNs, many well-characterized protein complexes were accurately identified by this method. CONCLUSION: The shift from static PPI networks to dynamic PPI networks is essential to accurately identify protein complex. This method not only can be applied to identify protein complex, but also establish a framework to integrate dynamic information into static networks for other applications, such as pathway analysis. |
format | Online Article Text |
id | pubmed-4847341 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-48473412016-05-04 Construction of dynamic probabilistic protein interaction networks for protein complex identification Zhang, Yijia Lin, Hongfei Yang, Zhihao Wang, Jian BMC Bioinformatics Research Article BACKGROUND: Recently, high-throughput experimental techniques have generated a large amount of protein-protein interaction (PPI) data which can construct large complex PPI networks for numerous organisms. System biology attempts to understand cellular organization and function by analyzing these PPI networks. However, most studies still focus on static PPI networks which neglect the dynamic information of PPI. RESULTS: The gene expression data under different time points and conditions can reveal the dynamic information of proteins. In this study, we used an active probability-based method to distinguish the active level of proteins at different active time points. We constructed dynamic probabilistic protein networks (DPPN) to integrate dynamic information of protein into static PPI networks. Based on DPPN, we subsequently proposed a novel method to identify protein complexes, which could effectively exploit topological structure as well as dynamic information of DPPN. We used three different yeast PPI datasets and gene expression data to construct three DPPNs. When applied to three DPPNs, many well-characterized protein complexes were accurately identified by this method. CONCLUSION: The shift from static PPI networks to dynamic PPI networks is essential to accurately identify protein complex. This method not only can be applied to identify protein complex, but also establish a framework to integrate dynamic information into static networks for other applications, such as pathway analysis. BioMed Central 2016-04-27 /pmc/articles/PMC4847341/ /pubmed/27117946 http://dx.doi.org/10.1186/s12859-016-1054-1 Text en © Zhang et al. 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. 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 Zhang, Yijia Lin, Hongfei Yang, Zhihao Wang, Jian Construction of dynamic probabilistic protein interaction networks for protein complex identification |
title | Construction of dynamic probabilistic protein interaction networks for protein complex identification |
title_full | Construction of dynamic probabilistic protein interaction networks for protein complex identification |
title_fullStr | Construction of dynamic probabilistic protein interaction networks for protein complex identification |
title_full_unstemmed | Construction of dynamic probabilistic protein interaction networks for protein complex identification |
title_short | Construction of dynamic probabilistic protein interaction networks for protein complex identification |
title_sort | construction of dynamic probabilistic protein interaction networks for protein complex identification |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4847341/ https://www.ncbi.nlm.nih.gov/pubmed/27117946 http://dx.doi.org/10.1186/s12859-016-1054-1 |
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