iSuc-PseOpt: Identifying lysine succinylation sites in proteins by incorporating sequence-coupling effects into pseudo components and optimizing imbalanced training dataset
iSuc-PseOpt: Identifying lysine succinylation sites in proteins by incorporating sequence-coupling effects into pseudo components and optimizing imbalanced training dataset
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iSuc-PseOpt:通过将序列耦合效应纳入伪组件并优化不平衡训练数据集来识别蛋白质中的赖氨酸琥珀酰化位点
DOI:
10.1016/j.ab.2015.12.009
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发表时间:
2016-03-15
影响因子:
2.9
通讯作者:
Chou, Kuo-Chen
中科院分区:
文献类型:
--
作者:
Jia, Jianhua;Liu, Zi;Chou, Kuo-Chen
Succinylation is a posttranslational modification (PTM) where a succinyl group is added to a Lys (K) residue of a protein molecule. Lysine succinylation plays an important role in orchestrating various biological processes, but it is also associated with some diseases. Therefore, we are challenged by the following problem from both basic research and drug development: given an uncharacterized protein sequence containing many Lys residues, which one of them can be succinylated, and which one cannot? With the avalanche of protein sequences generated in the postgenomic age, the answer to the problem has become even more urgent. Fortunately, the statistical significance experimental data for succinylated sites in proteins have become available very recently, an indispensable prerequisite for developing a computational method to address this problem. By incorporating the sequence-coupling effects into the general pseudo amino acid composition and using KNNC (K-nearest neighbors cleaning) treatment and IHTS (inserting hypothetical training samples) treatment to optimize the training dataset, a predictor called iSuc-PseOpt has been developed. Rigorous cross-validations indicated that it remarkably outperformed the existing method. A user-friendly web-server for iSuc-PseOpt has been established at http://www.jci-bioinfo.cnfiSuc-PseOpt, where users can easily get their desired results without needing to go through the complicated mathematical equations involved. (C) 2015 Elsevier Inc. All rights reserved.