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- W1978425204 abstract "Protein phosphorylation catalysed by kinases plays crucial regulatory roles in intracellular signal transduction. With the increasing number of kinase-specific phosphorylation sites and disease-related phosphorylation substrates that have been identified, the desire to explore the regulatory relationship between protein kinases and disease-related phosphorylation substrates is motivated. In this work, we analysed the kinases' characteristic of all disease-related phosphorylation substrates by using our developed Phosphorylation Set Enrichment Analysis (PSEA) method. We evaluated the efficiency of our method with independent test and concluded that our approach is reliable for identifying kinases responsible for phosphorylated substrates. In addition, we found that Mitogen-activated protein kinase (MAPK) and Glycogen synthase kinase (GSK) families are more associated with abnormal phosphorylation. It can be anticipated that our method might be helpful to identify the mechanism of phosphorylation and the relationship between kinase and phosphorylation related diseases. A user-friendly web interface is now freely available at http://bioinfo.ncu.edu.cn/PKPred_Home.aspx." @default.
- W1978425204 created "2016-06-24" @default.
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- W1978425204 date "2014-03-31" @default.
- W1978425204 modified "2023-10-14" @default.
- W1978425204 title "PSEA: Kinase-specific prediction and analysis of human phosphorylation substrates" @default.
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- W1978425204 doi "https://doi.org/10.1038/srep04524" @default.
- W1978425204 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3970127" @default.
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- W1978425204 hasPublicationYear "2014" @default.
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