Hidden information revealed by optimal community structure from a protein-complex bipartite network improves protein function prediction.

The task of extracting the maximal amount of information from a biological network has drawn much attention from researchers, for example, predicting the function of a protein from a protein-protein interaction (PPI) network. It is well known that biological networks consist of modules/communities,...

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Main Authors: Juyong Lee, Jooyoung Lee
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2013-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3618231?pdf=render
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author Juyong Lee
Jooyoung Lee
author_facet Juyong Lee
Jooyoung Lee
author_sort Juyong Lee
collection DOAJ
description The task of extracting the maximal amount of information from a biological network has drawn much attention from researchers, for example, predicting the function of a protein from a protein-protein interaction (PPI) network. It is well known that biological networks consist of modules/communities, a set of nodes that are more densely inter-connected among themselves than with the rest of the network. However, practical applications of utilizing the community information have been rather limited. For protein function prediction on a network, it has been shown that none of the existing community-based protein function prediction methods outperform a simple neighbor-based method. Recently, we have shown that proper utilization of a highly optimal modularity community structure for protein function prediction can outperform neighbor-assisted methods. In this study, we propose two function prediction approaches on bipartite networks that consider the community structure information as well as the neighbor information from the network: 1) a simple screening method and 2) a random forest based method. We demonstrate that our community-assisted methods outperform neighbor-assisted methods and the random forest method yields the best performance. In addition, we show that using the optimal community structure information is essential for more accurate function prediction for the protein-complex bipartite network of Saccharomyces cerevisiae. Community detection can be carried out either using a modified modularity for dealing with the original bipartite network or first projecting the network into a single-mode network (i.e., PPI network) and then applying community detection to the reduced network. We find that the projection leads to the loss of information in a significant way. Since our prediction methods rely only on the network topology, they can be applied to various fields where an efficient network-based analysis is required.
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spelling doaj.art-96dd88b9ee77489989245e23b2e783a12022-12-22T01:21:02ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0184e6037210.1371/journal.pone.0060372Hidden information revealed by optimal community structure from a protein-complex bipartite network improves protein function prediction.Juyong LeeJooyoung LeeThe task of extracting the maximal amount of information from a biological network has drawn much attention from researchers, for example, predicting the function of a protein from a protein-protein interaction (PPI) network. It is well known that biological networks consist of modules/communities, a set of nodes that are more densely inter-connected among themselves than with the rest of the network. However, practical applications of utilizing the community information have been rather limited. For protein function prediction on a network, it has been shown that none of the existing community-based protein function prediction methods outperform a simple neighbor-based method. Recently, we have shown that proper utilization of a highly optimal modularity community structure for protein function prediction can outperform neighbor-assisted methods. In this study, we propose two function prediction approaches on bipartite networks that consider the community structure information as well as the neighbor information from the network: 1) a simple screening method and 2) a random forest based method. We demonstrate that our community-assisted methods outperform neighbor-assisted methods and the random forest method yields the best performance. In addition, we show that using the optimal community structure information is essential for more accurate function prediction for the protein-complex bipartite network of Saccharomyces cerevisiae. Community detection can be carried out either using a modified modularity for dealing with the original bipartite network or first projecting the network into a single-mode network (i.e., PPI network) and then applying community detection to the reduced network. We find that the projection leads to the loss of information in a significant way. Since our prediction methods rely only on the network topology, they can be applied to various fields where an efficient network-based analysis is required.http://europepmc.org/articles/PMC3618231?pdf=render
spellingShingle Juyong Lee
Jooyoung Lee
Hidden information revealed by optimal community structure from a protein-complex bipartite network improves protein function prediction.
PLoS ONE
title Hidden information revealed by optimal community structure from a protein-complex bipartite network improves protein function prediction.
title_full Hidden information revealed by optimal community structure from a protein-complex bipartite network improves protein function prediction.
title_fullStr Hidden information revealed by optimal community structure from a protein-complex bipartite network improves protein function prediction.
title_full_unstemmed Hidden information revealed by optimal community structure from a protein-complex bipartite network improves protein function prediction.
title_short Hidden information revealed by optimal community structure from a protein-complex bipartite network improves protein function prediction.
title_sort hidden information revealed by optimal community structure from a protein complex bipartite network improves protein function prediction
url http://europepmc.org/articles/PMC3618231?pdf=render
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