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Detection of Protein Complexes Based on Penalized Matrix Decomposition in a Sparse Protein–Protein Interaction Network.

Authors :
Cao, Buwen
Deng, Shuguang
Qin, Hua
Ding, Pingjian
Chen, Shaopeng
Li, Guanghui
Zeng, Xiangxiang
Rodríguez-Patón, Alfonso
Zou, Quan
Source :
Molecules; Jun2018, Vol. 23 Issue 6, p1460, 1p, 1 Diagram, 4 Charts, 2 Graphs
Publication Year :
2018

Abstract

High-throughput technology has generated large-scale protein interaction data, which is crucial in our understanding of biological organisms. Many complex identification algorithms have been developed to determine protein complexes. However, these methods are only suitable for dense protein interaction networks, because their capabilities decrease rapidly when applied to sparse protein–protein interaction (PPI) networks. In this study, based on penalized matrix decomposition (<italic>PMD</italic>), a novel method of penalized matrix decomposition for the identification of protein complexes (i.e., PMD<subscript>pc</subscript>) was developed to detect protein complexes in the human protein interaction network. This method mainly consists of three steps. First, the adjacent matrix of the protein interaction network is normalized. Second, the normalized matrix is decomposed into three factor matrices. The PMD<subscript>pc</subscript> method can detect protein complexes in sparse PPI networks by imposing appropriate constraints on factor matrices. Finally, the results of our method are compared with those of other methods in human PPI network. Experimental results show that our method can not only outperform classical algorithms, such as CFinder, ClusterONE, RRW, HC-PIN, and PCE-FR, but can also achieve an ideal overall performance in terms of a composite score consisting of F-measure, accuracy (ACC), and the maximum matching ratio (MMR). [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
14203049
Volume :
23
Issue :
6
Database :
Complementary Index
Journal :
Molecules
Publication Type :
Academic Journal
Accession number :
130283594
Full Text :
https://doi.org/10.3390/molecules23061460