Not all scale-free networks are born equal: the role of the seed graph in PPI network evolution
- PMID: 17616981
- PMCID: PMC1913096
- DOI: 10.1371/journal.pcbi.0030118
Not all scale-free networks are born equal: the role of the seed graph in PPI network evolution
Abstract
The (asymptotic) degree distributions of the best-known "scale-free" network models are all similar and are independent of the seed graph used; hence, it has been tempting to assume that networks generated by these models are generally similar. In this paper, we observe that several key topological features of such networks depend heavily on the specific model and the seed graph used. Furthermore, we show that starting with the "right" seed graph (typically a dense subgraph of the protein-protein interaction network analyzed), the duplication model captures many topological features of publicly available protein-protein interaction networks very well.
Conflict of interest statement
Figures







References
-
- Jeong H, Mason S, Barabási AL, Oltvai ZN. Lethality and centrality in protein networks. Nature. 2001;411:41. - PubMed
-
- Wagner A. The Yeast protein interaction network evolves rapidly and contains few redundant duplicate genes. Mol Biol Evol. 2001;18:1283–1292. - PubMed
-
- Han J, Dupuy D, Bertin N, Cusick M, Vidal M. Effect of sampling on topology predictions of protein–protein interaction networks. Nature Biotech. 2005;23:839–844. - PubMed
-
- Przulj N, Corneil DG, Jurisica I. Modeling interactome: Scale-free or geometric? Bioinformatics. 2005;150:216–231. - PubMed
-
- Tanaka R, Yi TM, Doyle J. Some protein interaction data do not exhibit power law statistics. FEBS Letters. 2005;579:5140–5144. - PubMed
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases