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Identifying Protein Complexes from Dynamic Temporal Interval Protein-Protein Interaction Networks
Identification of protein complex is very important for revealing the underlying mechanism of biological processes. Many computational methods have been developed to identify protein complexes from static protein-protein interaction (PPI) networks. Recently, researchers are considering the dynamics...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6720829/ https://www.ncbi.nlm.nih.gov/pubmed/31531351 http://dx.doi.org/10.1155/2019/3726721 |
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author | Zhang, Jinxiong Zhong, Cheng Lin, Hai Xiang Wang, Mian |
author_facet | Zhang, Jinxiong Zhong, Cheng Lin, Hai Xiang Wang, Mian |
author_sort | Zhang, Jinxiong |
collection | PubMed |
description | Identification of protein complex is very important for revealing the underlying mechanism of biological processes. Many computational methods have been developed to identify protein complexes from static protein-protein interaction (PPI) networks. Recently, researchers are considering the dynamics of protein-protein interactions. Dynamic PPI networks are closer to reality in the cell system. It is expected that more protein complexes can be accurately identified from dynamic PPI networks. In this paper, we use the undulating degree above the base level of gene expression instead of the gene expression level to construct dynamic temporal PPI networks. Further we convert dynamic temporal PPI networks into dynamic Temporal Interval Protein Interaction Networks (TI-PINs) and propose a novel method to accurately identify more protein complexes from the constructed TI-PINs. Owing to preserving continuous interactions within temporal interval, the constructed TI-PINs contain more dynamical information for accurately identifying more protein complexes. Our proposed identification method uses multisource biological data to judge whether the joint colocalization condition, the joint coexpression condition, and the expanding cluster condition are satisfied; this is to ensure that the identified protein complexes have the features of colocalization, coexpression, and functional homogeneity. The experimental results on yeast data sets demonstrated that using the constructed TI-PINs can obtain better identification of protein complexes than five existing dynamic PPI networks, and our proposed identification method can find more protein complexes accurately than four other methods. |
format | Online Article Text |
id | pubmed-6720829 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Hindawi |
record_format | MEDLINE/PubMed |
spelling | pubmed-67208292019-09-17 Identifying Protein Complexes from Dynamic Temporal Interval Protein-Protein Interaction Networks Zhang, Jinxiong Zhong, Cheng Lin, Hai Xiang Wang, Mian Biomed Res Int Research Article Identification of protein complex is very important for revealing the underlying mechanism of biological processes. Many computational methods have been developed to identify protein complexes from static protein-protein interaction (PPI) networks. Recently, researchers are considering the dynamics of protein-protein interactions. Dynamic PPI networks are closer to reality in the cell system. It is expected that more protein complexes can be accurately identified from dynamic PPI networks. In this paper, we use the undulating degree above the base level of gene expression instead of the gene expression level to construct dynamic temporal PPI networks. Further we convert dynamic temporal PPI networks into dynamic Temporal Interval Protein Interaction Networks (TI-PINs) and propose a novel method to accurately identify more protein complexes from the constructed TI-PINs. Owing to preserving continuous interactions within temporal interval, the constructed TI-PINs contain more dynamical information for accurately identifying more protein complexes. Our proposed identification method uses multisource biological data to judge whether the joint colocalization condition, the joint coexpression condition, and the expanding cluster condition are satisfied; this is to ensure that the identified protein complexes have the features of colocalization, coexpression, and functional homogeneity. The experimental results on yeast data sets demonstrated that using the constructed TI-PINs can obtain better identification of protein complexes than five existing dynamic PPI networks, and our proposed identification method can find more protein complexes accurately than four other methods. Hindawi 2019-08-21 /pmc/articles/PMC6720829/ /pubmed/31531351 http://dx.doi.org/10.1155/2019/3726721 Text en Copyright © 2019 Jinxiong Zhang et al. https://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Zhang, Jinxiong Zhong, Cheng Lin, Hai Xiang Wang, Mian Identifying Protein Complexes from Dynamic Temporal Interval Protein-Protein Interaction Networks |
title | Identifying Protein Complexes from Dynamic Temporal Interval Protein-Protein Interaction Networks |
title_full | Identifying Protein Complexes from Dynamic Temporal Interval Protein-Protein Interaction Networks |
title_fullStr | Identifying Protein Complexes from Dynamic Temporal Interval Protein-Protein Interaction Networks |
title_full_unstemmed | Identifying Protein Complexes from Dynamic Temporal Interval Protein-Protein Interaction Networks |
title_short | Identifying Protein Complexes from Dynamic Temporal Interval Protein-Protein Interaction Networks |
title_sort | identifying protein complexes from dynamic temporal interval protein-protein interaction networks |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6720829/ https://www.ncbi.nlm.nih.gov/pubmed/31531351 http://dx.doi.org/10.1155/2019/3726721 |
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