BackgroundLysine succinylation is a new kind of post-translational modification which plays a key role in protein conformation regulation and cellular function control. To understand the mechanism of succinylation profoundly, it is necessary to identify succinylation sites in proteins accurately. However, traditional methods, experimental approaches, are labor-intensive and time-consuming. Computational prediction methods have been proposed recent years, and they are popular because of their convenience and high speed. In this study, we developed a new method to predict succinylation sites in protein combining multiple features, including amino acid composition, binary encoding, physicochemical property and grey pseudo amino acid composition, with a feature selection scheme (information gain). And then, it was trained using SVM (Support Vector Machine) and an ensemble learning algorithm.ResultsThe performance of this method was measured with an accuracy of 89.14% and a MCC (Matthew Correlation Coefficient) of 0.79 using 10-fold cross validation on training dataset and an accuracy of 84.5% and a MCC of 0.2 on independent dataset.ConclusionsThe conclusions made from this study can help to understand more of the succinylation mechanism. These results suggest that our method was very promising for predicting succinylation sites. The source code and data of this paper are freely available athttps://github.com/ningq669/PSuccE.Electronic supplementary materialThe online version of this article (10.1186/s12859-018-2249-4) contains supplementary material, which is available to authorized users.
Motivation: Discovering long noncoding RNA (lncRNA)–disease associations is a fundamental and critical part in understanding disease etiology and pathogenesis. However, only a few lncRNA–disease associations have been identified because of the time-consuming and expensive biological experiments. As a result, an efficient computational method is of great importance and urgently needed for identifying potential lncRNA–disease associations. With the ability of exploiting node features and relationships in network, graph-based learning models have been commonly utilized by these biomolecular association predictions. However, the capability of these methods in comprehensively fusing node features, heterogeneous topological structures and semantic information is distant from optimal or even satisfactory. Moreover, there are still limitations in modeling complex associations between lncRNAs and diseases. Results: In this paper, we develop a novel heterogeneous graph attention network framework based on meta-paths for predicting lncRNA–disease associations, denoted as HGATLDA. At first, we conduct a heterogeneous network by incorporating lncRNA and disease feature structural graphs, and lncRNA–disease topological structural graph. Then, for the heterogeneous graph, we conduct multiple metapath-based subgraphs and then utilize graph attention network to learn node embeddings from neighbors of these homogeneous and heterogeneous subgraphs. Next, we implement attention mechanism to adaptively assign weights to multiple metapath-based subgraphs and get more semantic information. In addition, we combine neural inductive matrix completion to reconstruct lncRNA–disease associations, which is applied for capturing complicated associations between lncRNAs and diseases. Moreover, we incorporate cost-sensitive neural network into the loss function to tackle the commonly imbalance problem in lncRNA–disease association prediction. Finally, extensive experimental results demonstrate the effectiveness of our proposed framework.
Protein pupylation is a type of post-translation modification, which plays a crucial role in cellular function of bacterial organisms in prokaryotes. To have a better insight of the mechanisms underlying pupylation an initial, but important, step is to identify pupylation sites. To date, several computational methods have been established for the prediction of pupylation sites which usually artificially design the negative samples using the verified pupylation proteins to train the classifiers. However, if this process is not properly done it can affect the performance of the final predictor dramatically. In this work, different from previous computational methods, we proposed an enhanced positive-unlabeled learning algorithm (EPuL) to the pupylation site prediction problem, which uses only positive and unlabeled samples. Firstly, we separate the training dataset into the positive dataset and the unlabeled dataset which contains the remaining non-annotated lysine residues. Then, the EPuL algorithm is utilized to select the reliably negative initial dataset and then iteratively pick out the non-pupylation sites. The performance of the proposed method was measured with an accuracy of 90.24%, an Area Under Curve (AUC) of 0.93 and an MCC of 0.81 by 10-fold cross-validation. A user-friendly web server for predicting pupylation sites was developed and was freely available at .
Glycation is a non-enzymatic process occurring inside or outside the host body by attaching a sugar molecule to a protein or lipid molecule. It is an important form of post-translational modification (PTM), which impairs the function and changes the characteristics of the proteins so that the identification of the glycation sites may provide some useful guidelines to understand various biological functions of proteins. In this study, we proposed an accurate prediction tool, named Glypre, for lysine glycation. Firstly, we used multiple informative features to encode the peptides. These features included the position scoring function, secondary structure, AAindex, and the composition of k-spaced amino acid pairs. Secondly, the distribution of distinctive features of the residues surrounding the glycation and non-glycation sites was statistically analysed. Thirdly, based on the distribution of these features, we developed a new predictor by using different optimal window sizes for different properties and a two-step feature selection method, which utilized the maximum relevance minimum redundancy method followed by a greedy feature selection procedure. The performance of Glypre was measured with a sensitivity of 57.47%, a specificity of 90.78%, an accuracy of 79.68%, area under the receiver-operating characteristic (ROC) curve (AUC) of 0.86, and a Matthews’s correlation coefficient (MCC) of 0.52 by 10-fold cross-validation. The detailed analysis results showed that our predictor may play a complementary role to other existing methods for identifying protein lysine glycation. The source code and datasets of the Glypre are available in the Supplementary File.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
hi@scite.ai
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.