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Dive into the research topics where Jiangning Song is active.

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Featured researches published by Jiangning Song.


Bioinformatics | 2014

Cascleave 2.0, a new approach for predicting caspase and granzyme cleavage targets.

Mingjun Wang; Xing-Ming Zhao; Hao Tan; Tatsuya Akutsu; James C. Whisstock; Jiangning Song

MOTIVATIONnCaspases and granzyme B (GrB) are important proteases involved in fundamental cellular processes and play essential roles in programmed cell death, necrosis and inflammation. Although a number of substrates for both types have been experimentally identified, the complete repertoire of caspases and granzyme B substrates remained to be fully characterized. Accordingly, systematic bioinformatics studies of known cleavage sites may provide important insights into their substrate specificity and facilitate the discovery of novel substrates.nnnRESULTSnWe develop a new bioinformatics tool, termed Cascleave 2.0, which builds on previous success of the Cascleave tool for predicting generic caspase cleavage sites. It can be efficiently used to predict potential caspase-specific cleavage sites for the human caspase-1, 3, 6, 7, 8 and GrB. In particular, we integrate heterogeneous sequence and protein functional information from various sources to improve the prediction accuracy of Cascleave 2.0. During classification, we use both maximum relevance minimum redundancy and forward feature selection techniques to quantify the relative contribution of each feature to prediction and thus remove redundant as well as irrelevant features. A systematic evaluation of Cascleave 2.0 using the benchmark data and comparison with other state-of-the-art tools using independent test data indicate that Cascleave 2.0 outperforms other tools on protease-specific cleavage site prediction of caspase-1, 3, 6, 7 and GrB. Cascleave 2.0 is anticipated to be used as a powerful tool for identifying novel substrates and cleavage sites of caspases and GrB and help understand the functional roles of these important proteases in human proteolytic cascades.nnnAVAILABILITY AND IMPLEMENTATIONnhttp://www.structbioinfor.org/cascleave2/.


Bioinformatics | 2017

POSSUM: a bioinformatics toolkit for generating numerical sequence feature descriptors based on PSSM profiles

Jiawei Wang; Bingjiao Yang; Jerico Revote; André Leier; Tatiana T. Marquez-Lago; Geoffrey I. Webb; Jiangning Song; Kuo-Chen Chou; Trevor Lithgow

Summary: Evolutionary information in the form of a Position‐Specific Scoring Matrix (PSSM) is a widely used and highly informative representation of protein sequences. Accordingly, PSSM‐based feature descriptors have been successfully applied to improve the performance of various predictors of protein attributes. Even though a number of algorithms have been proposed in previous studies, there is currently no universal web server or toolkit available for generating this wide variety of descriptors. Here, we present POSSUM (Position‐Specific Scoring matrix‐based feature generator for machine learning), a versatile toolkit with an online web server that can generate 21 types of PSSM‐based feature descriptors, thereby addressing a crucial need for bioinformaticians and computational biologists. We envisage that this comprehensive toolkit will be widely used as a powerful tool to facilitate feature extraction, selection, and benchmarking of machine learning‐based models, thereby contributing to a more effective analysis and modeling pipeline for bioinformatics research. Availability and implementation: http://possum.erc.monash.edu/. Contact: [email protected] or [email protected] Supplementary information: Supplementary data are available at Bioinformatics online.


Journal of Theoretical Biology | 2018

PREvaIL, an integrative approach for inferring catalytic residues using sequence, structural, and network features in a machine-learning framework

Jiangning Song; Fuyi Li; Kazuhiro Takemoto; Gholamreza Haffari; Tatsuya Akutsu; Kuo-Chen Chou; Geoffrey I. Webb

Determining the catalytic residues in an enzyme is critical to our understanding the relationship between protein sequence, structure, function, and enhancing our ability to design novel enzymes and their inhibitors. Although many enzymes have been sequenced, and their primary and tertiary structures determined, experimental methods for enzyme functional characterization lag behind. Because experimental methods used for identifying catalytic residues are resource- and labor-intensive, computational approaches have considerable value and are highly desirable for their ability to complement experimental studies in identifying catalytic residues and helping to bridge the sequence-structure-function gap. In this study, we describe a new computational method called PREvaIL for predicting enzyme catalytic residues. This method was developed by leveraging a comprehensive set of informative features extracted from multiple levels, including sequence, structure, and residue-contact network, in a random forest machine-learning framework. Extensive benchmarking experiments on eight different datasets based on 10-fold cross-validation and independent tests, as well as side-by-side performance comparisons with seven modern sequence- and structure-based methods, showed that PREvaIL achieved competitive predictive performance, with an area under the receiver operating characteristic curve and area under the precision-recall curve ranging from 0.896 to 0.973 and from 0.294 to 0.523, respectively. We demonstrated that this method was able to capture useful signals arising from different levels, leveraging such differential but useful types of features and allowing us to significantly improve the performance of catalytic residue prediction. We believe that this new method can be utilized as a valuable tool for both understanding the complex sequence-structure-function relationships of proteins and facilitating the characterization of novel enzymes lacking functional annotations.


Briefings in Bioinformatics | 2015

Towards more accurate prediction of ubiquitination sites: a comprehensive review of current methods, tools and features

Zhen Chen; Yuan Zhou; Ziding Zhang; Jiangning Song

Protein ubiquitination is one of the most important reversible post-translational modifications (PTMs). In many biochemical, pathological and pharmaceutical studies on understanding the function of proteins in biological processes, identification of ubiquitination sites is an important first step. However, experimental approaches for identifying ubiquitination sites are often expensive, labor-intensive and time-consuming, partly due to the dynamics and reversibility of ubiquitination. In silico prediction of ubiquitination sites is potentially a useful strategy for whole proteome annotation. A number of bioinformatics approaches and tools have recently been developed for predicting protein ubiquitination sites. However, these tools have different methodologies, prediction algorithms, functionality and features, which complicate their utility and application. The purpose of this review is to aid users in selecting appropriate tools for specific analyses and circumstances. We first compared five popular webservers and standalone software options, assessing their performance on four up-to-date ubiquitination benchmark datasets from Saccharomyces cerevisiae, Homo sapiens, Mus musculus and Arabidopsis thaliana. We then discussed and summarized these tools to guide users in choosing among the tools efficiently and rapidly. Finally, we assessed the importance of features of existing tools for ubiquitination site prediction, ranking them by performance. We also discussed the features that make noticeable contributions to species-specific ubiquitination site prediction.


Briefings in Bioinformatics | 2018

iProt-Sub: a comprehensive package for accurately mapping and predicting protease-specific substrates and cleavage sites

Jiangning Song; Yanan Wang; Fuyi Li; Tatsuya Akutsu; Neil D. Rawlings; Geoffrey I. Webb; Kuo-Chen Chou

Abstract Regulation of proteolysis plays a critical role in a myriad of important cellular processes. The key to better understanding the mechanisms that control this process is to identify the specific substrates that each protease targets. To address this, we have developed iProt-Sub, a powerful bioinformatics tool for the accurate prediction of protease-specific substrates and their cleavage sites. Importantly, iProt-Sub represents a significantly advanced version of its successful predecessor, PROSPER. It provides optimized cleavage site prediction models with better prediction performance and coverage for more species-specific proteases (4 major protease families and 38 different proteases). iProt-Sub integrates heterogeneous sequence and structural features and uses a two-step feature selection procedure to further remove redundant and irrelevant features in an effort to improve the cleavage site prediction accuracy. Features used by iProt-Sub are encoded by 11 different sequence encoding schemes, including local amino acid sequence profile, secondary structure, solvent accessibility and native disorder, which will allow a more accurate representation of the protease specificity of approximately 38 proteases and training of the prediction models. Benchmarking experiments using cross-validation and independent tests showed that iProt-Sub is able to achieve a better performance than several existing generic tools. We anticipate that iProt-Sub will be a powerful tool for proteome-wide prediction of protease-specific substrates and their cleavage sites, and will facilitate hypothesis-driven functional interrogation of protease-specific substrate cleavage and proteolytic events.


Bioinformatics | 2018

PROSPERous: high-throughput prediction of substrate cleavage sites for 90 proteases with improved accuracy

Jiangning Song; Fuyi Li; André Leier; Tatiana T. Marquez-Lago; Tatsuya Akutsu; Gholamreza Haffari; Kuo-Chen Chou; Geoffrey I. Webb; Robert N. Pike

SummarynProteases are enzymes that specifically cleave the peptide backbone of their target proteins. As an important type of irreversible post-translational modification, protein cleavage underlies many key physiological processes. When dysregulated, proteases actions are associated with numerous diseases. Many proteases are highly specific, cleaving only those target substrates that present certain particular amino acid sequence patterns. Therefore, tools that successfully identify potential target substrates for proteases may also identify previously unknown, physiologically relevant cleavage sites, thus providing insights into biological processes and guiding hypothesis-driven experiments aimed at verifying protease-substrate interaction. In this work, we present PROSPERous, a tool for rapid in silico prediction of protease-specific cleavage sites in substrate sequences. Our tool is based on logistic regression models and uses different scoring functions and their pairwise combinations to subsequently predict potential cleavage sites. PROSPERous represents a state-of-the-art tool that enables fast, accurate and high-throughput prediction of substrate cleavage sites for 90 proteases.nnnAvailability and implementationnhttp://prosperous.erc.monash.edu/[email protected] or [email protected] or [email protected] informationnSupplementary data are available at Bioinformatics online.


BMC Biotechnology | 2014

Cloning, expression and characterization of a pectate lyase from Paenibacillus sp. 0602 in recombinant Escherichia coli

Xiaoman Li; Huilin Wang; Cheng Zhou; Yanhe Ma; Jian Li; Jiangning Song

BackgroundBiotechnological applications of microbial pectate lyases (Pels) in plant fiber processing are considered as environmentally friendly. As such, they become promising substitutes for conventional chemical degumming process. Since applications of Pels in various fields are widening, it is necessary to explore new pectolytic microorganisms and enzymes for efficient and effective usage. Here, we describe the cloning, expression, characterization and application of the recombinant Pel protein from a pectolytic bacterium of the genus Paenibacillus in Escherichia coli.ResultsA Pel gene (pelN) was cloned using degenerate PCR and inverse PCR from the chromosomal DNA of Paenibacillus sp. 0602. The open reading frame of pelN encodes a 30 amino acid signal peptide and a 445 amino acid mature protein belonging to the polysaccharide lyase family 1. The maximum Pel activity produced by E. coli in shake flasks reached 2,467.4 U mL−1, and the purified recombinant enzyme exhibits a specific activity of 2,060 U mg−1 on polygalacturonic acid (PGA). The maximum activity was observed in a buffer with 5xa0mM Ca2+ at pHxa09.8 and 65°C. PelN displays a half-life of around 9xa0h and 42xa0h at 50°C and 45°C, respectively. The biochemical treatment achieved the maximal reduction of percentage weight (30.5%) of the ramie bast fiber.ConclusionsThis work represents the first study that describes the extracellular expression of a Pel gene from Paenibacillus species in E. coli. The high yield of the extracellular overexpression, relevant thermostability and efficient degumming using combined treatments indicate its strong potential for large-scale industrial production.


Briefings in Bioinformatics | 2016

Comprehensive assessment and performance improvement of effector protein predictors for bacterial secretion systems III, IV and VI

Yi An; Jiawei Wang; Chen Li; André Leier; Tatiana T. Marquez-Lago; Jonathan J. Wilksch; Yang Zhang; Geoffrey I. Webb; Jiangning Song; Trevor Lithgow

Bacterial effector proteins secreted by various protein secretion systems play crucial roles in host-pathogen interactions. In this context, computational tools capable of accurately predicting effector proteins of the various types of bacterial secretion systems are highly desirable. Existing computational approaches use different machine learning (ML) techniques and heterogeneous features derived from protein sequences and/or structural information. These predictors differ not only in terms of the used ML methods but also with respect to the used curated data sets, the features selection and their prediction performance. Here, we provide a comprehensive survey and benchmarking of currently available tools for the prediction of effector proteins of bacterial types III, IV and VI secretion systems (T3SS, T4SS and T6SS, respectively). We review core algorithms, feature selection techniques, tool availability and applicability and evaluate the prediction performance based on carefully curated independent test data sets. In an effort to improve predictive performance, we constructed three ensemble models based on ML algorithms by integrating the output of all individual predictors reviewed. Our benchmarks demonstrate that these ensemble models outperform all the reviewed tools for the prediction of effector proteins of T3SS and T4SS. The webserver of the proposed ensemble methods for T3SS and T4SS effector protein prediction is freely available at http://tbooster.erc.monash.edu/index.jsp. We anticipate that this survey will serve as a useful guide for interested users and that the new ensemble predictors will stimulate research into host-pathogen relationships and inspiration for the development of new bioinformatics tools for predicting effector proteins of T3SS, T4SS and T6SS.


Scientific Reports | 2017

PhosphoPredict: A bioinformatics tool for prediction of human kinase-specific phosphorylation substrates and sites by integrating heterogeneous feature selection

Jiangning Song; Huilin Wang; Jiawei Wang; André Leier; Tatiana T. Marquez-Lago; Bingjiao Yang; Ziding Zhang; Tatsuya Akutsu; Geoffrey I. Webb; Roger J. Daly

Protein phosphorylation is a major form of post-translational modification (PTM) that regulates diverse cellular processes. In silico methods for phosphorylation site prediction can provide a useful and complementary strategy for complete phosphoproteome annotation. Here, we present a novel bioinformatics tool, PhosphoPredict, that combines protein sequence and functional features to predict kinase-specific substrates and their associated phosphorylation sites for 12 human kinases and kinase families, including ATM, CDKs, GSK-3, MAPKs, PKA, PKB, PKC, and SRC. To elucidate critical determinants, we identified feature subsets that were most informative and relevant for predicting substrate specificity for each individual kinase family. Extensive benchmarking experiments based on both five-fold cross-validation and independent tests indicated that the performance of PhosphoPredict is competitive with that of several other popular prediction tools, including KinasePhos, PPSP, GPS, and Musite. We found that combining protein functional and sequence features significantly improves phosphorylation site prediction performance across all kinases. Application of PhosphoPredict to the entire human proteome identified 150 to 800 potential phosphorylation substrates for each of the 12 kinases or kinase families. PhosphoPredict significantly extends the bioinformatics portfolio for kinase function analysis and will facilitate high-throughput identification of kinase-specific phosphorylation sites, thereby contributing to both basic and translational research programs.


Scientific Reports | 2016

Crysalis: an integrated server for computational analysis and design of protein crystallization.

Huilin Wang; Liubin Feng; Ziding Zhang; Geoffrey I. Webb; Donghai Lin; Jiangning Song

The failure of multi-step experimental procedures to yield diffraction-quality crystals is a major bottleneck in protein structure determination. Accordingly, several bioinformatics methods have been successfully developed and employed to select crystallizable proteins. Unfortunately, the majority of existing in silico methods only allow the prediction of crystallization propensity, seldom enabling computational design of protein mutants that can be targeted for enhancing protein crystallizability. Here, we present Crysalis, an integrated crystallization analysis tool that builds on support-vector regression (SVR) models to facilitate computational protein crystallization prediction, analysis, and design. More specifically, the functionality of this new tool includes: (1) rapid selection of target crystallizable proteins at the proteome level, (2) identification of site non-optimality for protein crystallization and systematic analysis of all potential single-point mutations that might enhance protein crystallization propensity, and (3) annotation of target protein based on predicted structural properties. We applied the design mode of Crysalis to identify site non-optimality for protein crystallization on a proteome-scale, focusing on proteins currently classified as non-crystallizable. Our results revealed that site non-optimality is based on biases related to residues, predicted structures, physicochemical properties, and sequence loci, which provides in-depth understanding of the features influencing protein crystallization. Crysalis is freely available at http://nmrcen.xmu.edu.cn/crysalis/.

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André Leier

University of Alabama at Birmingham

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Tatiana T. Marquez-Lago

University of Alabama at Birmingham

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Kuo-Chen Chou

University of Electronic Science and Technology of China

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Jun Shen

Information Technology University

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Lei Wang

Information Technology University

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