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Identifying protein complexes based on node embeddings obtained from protein-protein interaction networks
BACKGROUND: Protein complexes are one of the keys to deciphering the behavior of a cell system. During the past decade, most computational approaches used to identify protein complexes have been based on discovering densely connected subgraphs in protein-protein interaction (PPI) networks. However,...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6150962/ https://www.ncbi.nlm.nih.gov/pubmed/30241459 http://dx.doi.org/10.1186/s12859-018-2364-2 |
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author | Liu, Xiaoxia Yang, Zhihao Sang, Shengtian Zhou, Ziwei Wang, Lei Zhang, Yin Lin, Hongfei Wang, Jian Xu, Bo |
author_facet | Liu, Xiaoxia Yang, Zhihao Sang, Shengtian Zhou, Ziwei Wang, Lei Zhang, Yin Lin, Hongfei Wang, Jian Xu, Bo |
author_sort | Liu, Xiaoxia |
collection | PubMed |
description | BACKGROUND: Protein complexes are one of the keys to deciphering the behavior of a cell system. During the past decade, most computational approaches used to identify protein complexes have been based on discovering densely connected subgraphs in protein-protein interaction (PPI) networks. However, many true complexes are not dense subgraphs and these approaches show limited performances for detecting protein complexes from PPI networks. RESULTS: To solve these problems, in this paper we propose a supervised learning method based on network node embeddings which utilizes the informative properties of known complexes to guide the search process for new protein complexes. First, node embeddings are obtained from human protein interaction network. Then the protein interactions are weighted through the similarities between node embeddings. After that, the supervised learning method is used to detect protein complexes. Then the random forest model is used to filter the candidate complexes in order to obtain the final predicted complexes. Experimental results on real human and yeast protein interaction networks show that our method effectively improves the performance for protein complex detection. CONCLUSIONS: We provided a new method for identifying protein complexes from human and yeast protein interaction networks, which has great potential to benefit the field of protein complex detection. |
format | Online Article Text |
id | pubmed-6150962 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-61509622018-09-26 Identifying protein complexes based on node embeddings obtained from protein-protein interaction networks Liu, Xiaoxia Yang, Zhihao Sang, Shengtian Zhou, Ziwei Wang, Lei Zhang, Yin Lin, Hongfei Wang, Jian Xu, Bo BMC Bioinformatics Research Article BACKGROUND: Protein complexes are one of the keys to deciphering the behavior of a cell system. During the past decade, most computational approaches used to identify protein complexes have been based on discovering densely connected subgraphs in protein-protein interaction (PPI) networks. However, many true complexes are not dense subgraphs and these approaches show limited performances for detecting protein complexes from PPI networks. RESULTS: To solve these problems, in this paper we propose a supervised learning method based on network node embeddings which utilizes the informative properties of known complexes to guide the search process for new protein complexes. First, node embeddings are obtained from human protein interaction network. Then the protein interactions are weighted through the similarities between node embeddings. After that, the supervised learning method is used to detect protein complexes. Then the random forest model is used to filter the candidate complexes in order to obtain the final predicted complexes. Experimental results on real human and yeast protein interaction networks show that our method effectively improves the performance for protein complex detection. CONCLUSIONS: We provided a new method for identifying protein complexes from human and yeast protein interaction networks, which has great potential to benefit the field of protein complex detection. BioMed Central 2018-09-21 /pmc/articles/PMC6150962/ /pubmed/30241459 http://dx.doi.org/10.1186/s12859-018-2364-2 Text en © The Author(s) 2018 Open Access This 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 Liu, Xiaoxia Yang, Zhihao Sang, Shengtian Zhou, Ziwei Wang, Lei Zhang, Yin Lin, Hongfei Wang, Jian Xu, Bo Identifying protein complexes based on node embeddings obtained from protein-protein interaction networks |
title | Identifying protein complexes based on node embeddings obtained from protein-protein interaction networks |
title_full | Identifying protein complexes based on node embeddings obtained from protein-protein interaction networks |
title_fullStr | Identifying protein complexes based on node embeddings obtained from protein-protein interaction networks |
title_full_unstemmed | Identifying protein complexes based on node embeddings obtained from protein-protein interaction networks |
title_short | Identifying protein complexes based on node embeddings obtained from protein-protein interaction networks |
title_sort | identifying protein complexes based on node embeddings obtained from protein-protein interaction networks |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6150962/ https://www.ncbi.nlm.nih.gov/pubmed/30241459 http://dx.doi.org/10.1186/s12859-018-2364-2 |
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