Topological structure analysis of the protein-protein interaction network in budding yeast
Topological structure analysis of the protein-protein interaction network in budding yeast
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DOI：
10.1093/nar/gkg340
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发表时间：
2003-05-01
影响因子：
14.9
通讯作者：
Chen, RS
中科院分区：
文献类型：
--
作者：
Bu, DB;Zhao, Y;Chen, RS
相互作用检测方法导致蛋白质之间发现了数千种相互作用，并且在大规模数据集中辨别相关性对于当今的生物学很重要。在这里，引入了一种从图理论中得出的光谱方法，以发现复杂蛋白质 - 蛋白质相互作用网络的隐藏拓扑结构（即准c和quasi-tipites）。我们的分析表明，这些隐藏的拓扑结构由生物学相关的官能团组成。该结果激发了一种新方法，可以根据拓扑结构中已知蛋白的分类来预测未表征的蛋白质的功能。使用这种频谱分析方法，从涉及11 855种相互作用的网络中分离出48个准晶体和6个准三位矿，在萌芽的酵母中2617个蛋白质之间的11 855相互作用，分配了76个未表征的蛋白质。
Interaction detection methods have led to the discovery of thousands of interactions between proteins, and discerning relevance within large-scale data sets is important to present-day biology. Here, a spectral method derived from graph theory was introduced to uncover hidden topological structures (i.e. quasi-cliques and quasi-bipartites) of complicated protein-protein interaction networks. Our analyses suggest that these hidden topological structures consist of biologically relevant functional groups. This result motivates a new method to predict the function of uncharacterized proteins based on the classification of known proteins within topological structures. Using this spectral analysis method, 48 quasi-cliques and six quasi-bipartites were isolated from a network involving 11 855 interactions among 2617 proteins in budding yeast, and 76 uncharacterized proteins were assigned functions.