...
首页> 外文期刊>Journal of Theoretical Biology >K-Partite cliques of protein interactions: A novel subgraph topology for functional coherence analysis on PPI networks
【24h】

K-Partite cliques of protein interactions: A novel subgraph topology for functional coherence analysis on PPI networks

机译:蛋白质相互作用的K-Partite派系:用于PPI网络功能相干分析的新型子图拓扑

获取原文
获取原文并翻译 | 示例
           

摘要

Many studies are aimed at identifying dense clusters/subgraphs from protein-protein interaction (PPI) networks for protein function prediction. However, the prediction performance based on the dense clusters is actually worse than a simple guilt-by-association method using neighbor counting ideas. This indicates that the local topological structures and properties of PPI networks are still open to new theoretical investigation and empirical exploration. We introduce a novel topological structure called k-partite cliques of protein interactions-a functionally coherent but not-necessarily dense subgraph topology in PPI networks-to study PPI networks. A k-partite protein clique is a maximal k-partite clique comprising two or more nonoverlapping protein subsets between any two of which full interactions are exhibited. In the detection of PPI's maximal k-partite cliques, we propose to transform PPI networks into induced K-partite graphs where edges exist only between the partites. Then, we present a maximal k-partite clique mining (MaCMik) algorithm to enumerate maximal k-partite cliques from K-partite graphs. Our MaCMik algorithm is then applied to a yeast PPI network. We observed interesting and unusually high functional coherence in k-partite protein cliques-the majority of the proteins in k-partite protein cliques, especially those in the same partites, share the same functions, although k-partite protein cliques are not restricted to be dense compared with dense subgraph patterns or (quasi-)cliques. The idea of k-partite protein cliques provides a novel approach of characterizing PPI networks, and so it will help function prediction for unknown proteins.
机译:许多研究旨在从蛋白质-蛋白质相互作用(PPI)网络中识别密集的簇/子图,以预测蛋白质功能。但是,基于密集聚类的预测性能实际上比使用邻居计数思想的简单的逐个内关联方法要差。这表明PPI网络的局部拓扑结构和性质仍在接受新的理论研究和经验探索。我们介绍了一种新型的拓扑结构,称为蛋白质相互作用的k-partique团-在PPI网络中功能上相干但不必要的密集子图拓扑结构,以研究PPI网络。 k部分蛋白质团是最大的k部分蛋白质团,其包含两个或多个在任何两个之间表现出完全相互作用的非重叠蛋白质子集。在检测PPI的最大k粒子群时,我们建议将PPI网络转换为诱导的K粒子图,其中边仅存在于粒子之间。然后,我们提出了一个最大的k部族挖掘(MaCMik)算法,以从K部图中枚举最大的k部族。然后将我们的MaCMik算法应用于酵母PPI网络。我们观察到k部分蛋白质组中有趣且异常高的功能相关性-尽管k部分蛋白质组不限于以下几种,但k部分蛋白质组中的大多数蛋白质(尤其是相同部分中的蛋白质)具有相同的功能。与密集的子图模式或(准)斜率相比。 k-partite蛋白质集团的想法提供了表征PPI网络的新颖方法,因此将有助于未知蛋白质的功能预测。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号