Please use this identifier to cite or link to this item:
https://doi.org/10.1186/1471-2105-15-335
DC Field | Value | |
---|---|---|
dc.title | Detecting temporal protein complexes from dynamic protein-protein interaction networks | |
dc.contributor.author | Ou-Yang, L | |
dc.contributor.author | Dai, D.-Q | |
dc.contributor.author | Li, X.-L | |
dc.contributor.author | Wu, M | |
dc.contributor.author | Zhang, X.-F | |
dc.contributor.author | Yang, P | |
dc.date.accessioned | 2020-10-27T11:12:03Z | |
dc.date.available | 2020-10-27T11:12:03Z | |
dc.date.issued | 2014 | |
dc.identifier.citation | Ou-Yang, L, Dai, D.-Q, Li, X.-L, Wu, M, Zhang, X.-F, Yang, P (2014). Detecting temporal protein complexes from dynamic protein-protein interaction networks. BMC Bioinformatics 15 (1) : 335. ScholarBank@NUS Repository. https://doi.org/10.1186/1471-2105-15-335 | |
dc.identifier.issn | 14712105 | |
dc.identifier.uri | https://scholarbank.nus.edu.sg/handle/10635/181524 | |
dc.description.abstract | Background: Proteins dynamically interact with each other to perform their biological functions. The dynamic operations of protein interaction networks (PPI) are also reflected in the dynamic formations of protein complexes. Existing protein complex detection algorithms usually overlook the inherent temporal nature of protein interactions within PPI networks. Systematically analyzing the temporal protein complexes can not only improve the accuracy of protein complex detection, but also strengthen our biological knowledge on the dynamic protein assembly processes for cellular organization. Results: In this study, we propose a novel computational method to predict temporal protein complexes. Particularly, we first construct a series of dynamic PPI networks by joint analysis of time-course gene expression data and protein interaction data. Then a Time Smooth Overlapping Complex Detection model (TS-OCD) has been proposed to detect temporal protein complexes from these dynamic PPI networks. TS-OCD can naturally capture the smoothness of networks between consecutive time points and detect overlapping protein complexes at each time point. Finally, a nonnegative matrix factorization based algorithm is introduced to merge those very similar temporal complexes across different time points. Conclusions: Extensive experimental results demonstrate the proposed method is very effective in detecting temporal protein complexes than the state-of-the-art complex detection techniques. © 2014 Ou-Yang et al. | |
dc.rights | Attribution 4.0 International | |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | |
dc.source | Unpaywall 20201031 | |
dc.subject | Complex networks | |
dc.subject | Complexation | |
dc.subject | Factorization | |
dc.subject | Gene expression | |
dc.subject | Matrix algebra | |
dc.subject | Time series analysis | |
dc.subject | Biological functions | |
dc.subject | Cellular organization | |
dc.subject | Dynamic proteins | |
dc.subject | Nonnegative matrix factorization | |
dc.subject | Protein complexes | |
dc.subject | Protein interaction networks | |
dc.subject | Stable interaction | |
dc.subject | Transient interactions | |
dc.subject | Proteins | |
dc.subject | experimental model | |
dc.subject | gene expression | |
dc.subject | joint | |
dc.subject | protein assembly | |
dc.subject | protein protein interaction | |
dc.subject | algorithm | |
dc.subject | article | |
dc.subject | biology | |
dc.subject | gene expression profiling | |
dc.subject | genetics | |
dc.subject | metabolism | |
dc.subject | methodology | |
dc.subject | protein analysis | |
dc.subject | time | |
dc.subject | protein | |
dc.subject | Algorithms | |
dc.subject | Computational Biology | |
dc.subject | Gene Expression Profiling | |
dc.subject | Protein Interaction Mapping | |
dc.subject | Proteins | |
dc.subject | Time Factors | |
dc.type | Article | |
dc.contributor.department | DEPARTMENT OF COMPUTER SCIENCE | |
dc.description.doi | 10.1186/1471-2105-15-335 | |
dc.description.sourcetitle | BMC Bioinformatics | |
dc.description.volume | 15 | |
dc.description.issue | 1 | |
dc.description.page | 335 | |
Appears in Collections: | Elements Staff Publications |
Show simple item record
Files in This Item:
File | Description | Size | Format | Access Settings | Version | |
---|---|---|---|---|---|---|
10_1186_1471-2105-15-335.pdf | 2.13 MB | Adobe PDF | OPEN | None | View/Download |
This item is licensed under a Creative Commons License