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https://doi.org/10.3390/ijms20020302
Title: | KSIMC: Predicting kinase–Substrate interactions based on matrix completion | Authors: | Gan, J Qiu, J Deng, C Lan, W Chen, Q Hu, Y |
Keywords: | algorithm amino acid sequence Article bioinformatics computer analysis enzyme substrate complex false positive result gene expression human kinase substrate interaction measurement accuracy molecular docking protein interaction protein phosphorylation receiver operating characteristic sequence alignment signal transduction validation process antagonists and inhibitors biology biophysics chemistry enzyme specificity factual database phosphorylation protein analysis theoretical model phosphotransferase Algorithms Biophysical Phenomena Computational Biology Databases, Factual Humans Models, Theoretical Phosphorylation Phosphotransferases Protein Interaction Mapping Sequence Alignment Substrate Specificity |
Issue Date: | 2019 | Citation: | Gan, J, Qiu, J, Deng, C, Lan, W, Chen, Q, Hu, Y (2019). KSIMC: Predicting kinase–Substrate interactions based on matrix completion. International Journal of Molecular Sciences 20 (2) : 302. ScholarBank@NUS Repository. https://doi.org/10.3390/ijms20020302 | Rights: | Attribution 4.0 International | Abstract: | Protein phosphorylation is an important chemical modification catalyzed by kinases. It plays important roles in many cellular processes. Predicting kinase–substrate interactions is vital to understanding the mechanism of many diseases. Many computational methods have been proposed to identify kinase–substrate interactions. However, the prediction accuracy still needs to be improved. Therefore, it is necessary to develop an efficient computational method to predict kinase–substrate interactions. In this paper, we propose a novel computational approach, KSIMC, to identify kinase–substrate interactions based on matrix completion. Firstly, the kinase similarity and substrate similarity are calculated by aligning sequence of kinase–kinase and substrate–substrate, respectively. Then, the original association network is adjusted based on the similarities. Finally, the matrix completion is used to predict potential kinase–substrate interactions. The experiment results show that our method outperforms other state-of-the-art algorithms in performance. Furthermore, the relevant databases and scientific literature verify the effectiveness of our algorithm for new kinase–substrate interaction identification. © 2019 by the authors. Licensee MDPI, Basel, Switzerland. | Source Title: | International Journal of Molecular Sciences | URI: | https://scholarbank.nus.edu.sg/handle/10635/183294 | ISSN: | 16616596 | DOI: | 10.3390/ijms20020302 | Rights: | Attribution 4.0 International |
Appears in Collections: | Staff Publications Elements |
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