title: Revisiting topological properties and models of protein-protein interaction networks from the perspective of dataset evolution.
abstract: Protein-protein interaction (PPI) networks are crucial for organisms. Many research efforts have thus been devoted to the study on the topological properties and models of PPI networks. However, existing studies did not always report consistent results on the topological properties of PPI networks. Although a number of PPI network models have been introduced, yet in the literature there is no convincing conclusion on which model is best for describing PPI networks. This situation is primarily caused by the incompleteness of current PPI datasets. To solve this problem, in this study, the authors propose to revisit the topological properties and models of PPI networks from the perspective of PPI dataset evolution. Concretely, they used 12 PPI datasets of Arabidopsis thaliana and 10 PPI datasets of Saccharomyces cerevisiae from different Biological General Repository for Interaction Datasets (BioGRID) database versions, and compared the topological properties of these datasets and the fitting capabilities of five typical PPI network models over these datasets.
authors.affiliation: Shanghai Key Lab of Intelligent Information Processing, and School of Computer Science, Fudan University, Shanghai 200433, People's Republic of China.
authors.forename: Mingyu
authors.initials: M
authors.lastname: Shao
authors.affiliation: Shanghai Key Lab of Intelligent Information Processing, and School of Computer Science, Fudan University, Shanghai 200433, People's Republic of China. sgzhou@fudan.edu.cn.
authors.forename: Shuigeng
authors.initials: S
authors.lastname: Zhou
authors.affiliation: Department of Computer Science & Technology, Tongji University, Shanghai 201804, People's Republic of China.
authors.forename: Jihong
authors.initials: J
authors.lastname: Guan
mesh_terms: D003198:Computer Simulation; D057225:Data Mining / Q000379:methods*; D030562:Databases, Protein; D008954:Models, Biological; D025941:Protein Interaction Mapping / Q000379:methods*; D020543:Proteome / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology*
chemical_list: D020543:Proteome