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タイトル
和文: 
英文:Highly Precise Protein-Protein Interaction Prediction Based on Consensus Between Template-Based and de Novo Docking Methods 
著者
和文: 大上 雅史, 松崎 由理, 下田 雄大, 石田 貴士, 秋山 泰.  
英文: Masahito Ohue, Yuri Matsuzaki, Takehiro Shimoda, Takashi Ishida, Yutaka Akiyama.  
言語 English 
掲載誌/書名
和文: 
英文:BMC Proceedings 
巻, 号, ページ Volume 7    Supplement 7    S6
出版年月 2013年12月20日 
出版者
和文: 
英文:BioMed Central 
会議名称
和文: 
英文: 
開催地
和文: 
英文: 
公式リンク http://www.biomedcentral.com/1753-6561/7/S7/S6
 
DOI https://doi.org/10.1186/1753-6561-7-S7-S6
アブストラクト Background Elucidation of protein-protein interaction (PPI) networks is important for understanding disease mechanisms and for drug discovery. Tertiary-structure-based in silico PPI prediction methods have been developed with two typical approaches: a method based on template matching with known protein structures and a method based on de novo protein docking. However, the template-based method has a narrow applicable range because of its use of template information, and the de novo docking based method does not have good prediction performance. In addition, both of these in silico prediction methods have insufficient precision, and require validation of the predicted PPIs by biological experiments, leading to considerable expenditure; therefore, PPI prediction methods with greater precision are needed. Results We have proposed a new structure-based PPI prediction method by combining template-based prediction and de novo docking prediction. When we applied the method to the human apoptosis signaling pathway, we obtained a precision value of 0.333, which is higher than that achieved using conventional methods (0.231 for PRISM, a template-based method, and 0.145 for MEGADOCK, a non-template-based method), while maintaining an F-measure value (0.285) comparable to that obtained using conventional methods (0.296 for PRISM, and 0.220 for MEGADOCK). Conclusions Our consensus method successfully predicted a PPI network with greater precision than conventional template/non-template methods, which may thus reduce the cost of validation by laboratory experiments for confirming novel PPIs from predicted PPIs. Therefore, our method may serve as an aid for promoting interactome analysis.

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