{"title":"用蛋白表达数据构建人组织特异性磷酸化网络","authors":"Yin-Ying Wang, Chenglei Sun, Luonan Chen, Xingming Zhao","doi":"10.1109/ISB.2013.6623807","DOIUrl":null,"url":null,"abstract":"Phosphorylation is a post-translational modification process mediated by kinases through the addition of a covalently bound phosphate group, which plays important roles in a wide range of cellular progresses, such as signaling cascades and development. Over the past years, despite many phosphorylation sites have been determined with mass spectrometry techniques, it is not clear which kinase phosphorylates which proteins. Under the circumstance, we propose a new probabilistic model to identify the substrates phosphorylated by certain kinases. Furthermore, we construct three tissue-specific phosphorylation networks based on protein expression data. Investigating the constructed tissue-specific networks, we find they are functionally consistent with the corresponding tissues, implying the effectiveness and biological significance of our proposed approach.","PeriodicalId":151775,"journal":{"name":"2013 7th International Conference on Systems Biology (ISB)","volume":"1 1","pages":"0"},"PeriodicalIF":0.0000,"publicationDate":"2013-10-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Construction of human tissue-specific phosphorylation networks with protein expression data\",\"authors\":\"Yin-Ying Wang, Chenglei Sun, Luonan Chen, Xingming Zhao\",\"doi\":\"10.1109/ISB.2013.6623807\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Phosphorylation is a post-translational modification process mediated by kinases through the addition of a covalently bound phosphate group, which plays important roles in a wide range of cellular progresses, such as signaling cascades and development. Over the past years, despite many phosphorylation sites have been determined with mass spectrometry techniques, it is not clear which kinase phosphorylates which proteins. Under the circumstance, we propose a new probabilistic model to identify the substrates phosphorylated by certain kinases. Furthermore, we construct three tissue-specific phosphorylation networks based on protein expression data. Investigating the constructed tissue-specific networks, we find they are functionally consistent with the corresponding tissues, implying the effectiveness and biological significance of our proposed approach.\",\"PeriodicalId\":151775,\"journal\":{\"name\":\"2013 7th International Conference on Systems Biology (ISB)\",\"volume\":\"1 1\",\"pages\":\"0\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2013-10-10\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"2013 7th International Conference on Systems Biology (ISB)\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1109/ISB.2013.6623807\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"2013 7th International Conference on Systems Biology (ISB)","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1109/ISB.2013.6623807","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Construction of human tissue-specific phosphorylation networks with protein expression data
Phosphorylation is a post-translational modification process mediated by kinases through the addition of a covalently bound phosphate group, which plays important roles in a wide range of cellular progresses, such as signaling cascades and development. Over the past years, despite many phosphorylation sites have been determined with mass spectrometry techniques, it is not clear which kinase phosphorylates which proteins. Under the circumstance, we propose a new probabilistic model to identify the substrates phosphorylated by certain kinases. Furthermore, we construct three tissue-specific phosphorylation networks based on protein expression data. Investigating the constructed tissue-specific networks, we find they are functionally consistent with the corresponding tissues, implying the effectiveness and biological significance of our proposed approach.