A Topology Potential-Based Method for Identifying Essential Proteins from PPI Networks

被引:95
作者
Li, Min [1 ]
Lu, Yu [1 ]
Wang, Jianxin [1 ]
Wu, Fang-Xiang [2 ,3 ]
Pan, Yi [4 ]
机构
[1] Cent S Univ, Sch Informat Sci & Engn, Changsha 410083, Hunan, Peoples R China
[2] Univ Saskatchewan, Dept Mech Engn, Saskatoon, SK S7N 5A9, Canada
[3] Univ Saskatchewan, Div Biomed Engn, Saskatoon, SK S7N 5A9, Canada
[4] Georgia State Univ, Dept Comp Sci, Atlanta, GA 30302 USA
基金
中国国家自然科学基金;
关键词
Essential proteins; protein-protein interaction network; topology potential; centrality measures; PREDICTING ESSENTIAL PROTEINS; FUNCTIONAL MODULES; ESSENTIAL GENES; FLUCTUATION DYNAMICS; SYSTEMS BIOLOGY; COMPLEXES; CENTRALITY; DISCOVERY; DATABASE; EVOLUTIONARY;
D O I
10.1109/TCBB.2014.2361350
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Essential proteins are indispensable for cellular life. It is of great significance to identify essential proteins that can help us understand the minimal requirements for cellular life and is also very important for drug design. However, identification of essential proteins based on experimental approaches are typically time-consuming and expensive. With the development of high-throughput technology in the post-genomic era, more and more protein-protein interaction data can be obtained, which make it possible to study essential proteins from the network level. There have been a series of computational approaches proposed for predicting essential proteins based on network topologies. Most of these topology based essential protein discovery methods were to use network centralities. In this paper, we investigate the essential proteins' topological characters from a completely new perspective. To our knowledge it is the first time that topology potential is used to identify essential proteins from a protein-protein interaction (PPI) network. The basic idea is that each protein in the network can be viewed as a material particle which creates a potential field around itself and the interaction of all proteins forms a topological field over the network. By defining and computing the value of each protein's topology potential, we can obtain a more precise ranking which reflects the importance of proteins from the PPI network. The experimental results show that topology potential-based methods TP and TP-NC outperform traditional topology measures: degree centrality (DC), betweenness centrality (BC), closeness centrality (CC), subgraph centrality (SC), eigenvector centrality (EC), information centrality (IC), and network centrality (NC) for predicting essential proteins. In addition, these centrality measures are improved on their performance for identifying essential proteins in biological network when controlled by topology potential.
引用
收藏
页码:372 / 383
页数:12
相关论文
共 76 条
  • [1] Structural systems biology: modelling protein interactions
    Aloy, P
    Russell, RB
    [J]. NATURE REVIEWS MOLECULAR CELL BIOLOGY, 2006, 7 (03) : 188 - 197
  • [2] InterPreTS: protein Interaction Prediction through Tertiary Structure
    Aloy, P
    Russell, RB
    [J]. BIOINFORMATICS, 2003, 19 (01) : 161 - 162
  • [3] The third dimension for protein interactions and complexes
    Aloy, P
    Russell, RB
    [J]. TRENDS IN BIOCHEMICAL SCIENCES, 2002, 27 (12) : 633 - 638
  • [4] [Anonymous], 1997, P 10 RES COMPUTATION
  • [5] [Anonymous], BMC GENOMICS
  • [6] Iterative cluster analysis of protein interaction data
    Arnau, V
    Mars, S
    Marín, I
    [J]. BIOINFORMATICS, 2005, 21 (03) : 364 - 378
  • [7] Anisotropy of fluctuation dynamics of proteins with an elastic network model
    Atilgan, AR
    Durell, SR
    Jernigan, RL
    Demirel, MC
    Keskin, O
    Bahar, I
    [J]. BIOPHYSICAL JOURNAL, 2001, 80 (01) : 505 - 515
  • [8] Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential
    Bahar, I
    Atilgan, AR
    Erman, B
    [J]. FOLDING & DESIGN, 1997, 2 (03): : 173 - 181
  • [9] Evolutionary and physiological importance of hub proteins
    Batada, Nizar N.
    Hurst, Laurence D.
    Tyers, Mike
    [J]. PLOS COMPUTATIONAL BIOLOGY, 2006, 2 (07) : 748 - 756
  • [10] The role of dynamic conformational ensembles in biomolecular recognition
    Boehr, David D.
    Nussinov, Ruth
    Wright, Peter E.
    [J]. NATURE CHEMICAL BIOLOGY, 2009, 5 (11) : 789 - 796