ArticlePloS one2015
GSHSite: exploiting an iteratively statistical method to identify s-glutathionylation sites with substrate specificity.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 37 citations in OpenAlex.
- Integrating Redox Proteomics and Computational Modeling to Decipher Thiol-Based Oxidative Post-Translational Modifications (oxiPTMs) in Plant Stress Physiology.International journal of molecular sciences · 2025Review
- Exploring the Role of Unconventional Post-Translational Modifications in Cancer Diagnostics and Therapy.Current protein & peptide science · 2024Review
- dbPTM in 2022: an updated database for exploring regulatory networks and functional associations of protein post-translational modifications.Nucleic acids research · 2022Article
- Computational repurposing of therapeutic small molecules from cancer to pulmonary hypertension.Science advances · 2021Article
- Residue-Residue Contact Can Be a Potential Feature for the Prediction of Lysine Crotonylation Sites.Frontiers in genetics · 2021Article
- A novel approach for predicting protein S-glutathionylation.BMC bioinformatics · 2020Article
- Redox Post-translational Modifications of Protein Thiols in Brain Aging and Neurodegenerative Conditions-Focus on S-Nitrosation.Frontiers in aging neuroscience · 2020Review
- Characterization and Identification of Lysine Succinylation Sites based on Deep Learning Method.Scientific reports · 2019Article
- Proteomic Identification of Protein Glutathionylation in Cardiomyocytes.Journal of proteome research · 2019Article
- Characterization and identification of lysine glutarylation based on intrinsic interdependence between positions in the substrate sites.BMC bioinformatics · 2019Article
- dbPTM in 2019: exploring disease association and cross-talk of post-translational modifications.Nucleic acids research · 2019Article
- Coenzyme A, protein CoAlation and redox regulation in mammalian cells.Biochemical Society transactions · 2018Review
- MDD-carb: a combinatorial model for the identification of protein carbonylation sites with substrate motifs.BMC systems biology · 2017Article
- Investigation and identification of protein carbonylation sites based on position-specific amino acid composition and physicochemical features.BMC bioinformatics · 2017Article
- MDD-Palm: Identification of protein S-palmitoylation sites with substrate motifs based on maximal dependence decomposition.PloS one · 2017Article
- Glutathione and Glutathione Transferase Omega 1 as Key Posttranslational Regulators in Macrophages.Microbiology spectrum · 2017Review
- Protein Thiol Redox Signaling in Monocytes and Macrophages.Antioxidants & redox signaling · 2016Review
- Protein S-glutathionlyation links energy metabolism to redox signaling in mitochondria.Redox biology · 2016Review
- UbiSite: incorporating two-layered machine learning method with substrate motifs to predict ubiquitin-conjugation site on lysines.BMC systems biology · 2016Article
- A new scheme to discover functional associations and regulatory networks of E3 ubiquitin ligases.BMC systems biology · 2016Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
S-glutathionylation, the covalent attachment of a glutathione (GSH) to the sulfur atom of cysteine, is a selective and reversible protein post-translational modification (PTM) that regulates protein activity, localization, and stability. Despite its implication in the regulation of protein functions and cell signaling, the substrate specificity of cysteine S-glutathionylation remains unknown. Based on a total of 1783 experimentally identified S-glutathionylation sites from mouse macrophages, this work presents an informatics investigation on S-glutathionylation sites including structural factors such as the flanking amino acids composition and the accessible surface area (ASA). TwoSampleLogo presents that positively charged amino acids flanking the S-glutathionylated cysteine may influence the formation of S-glutathionylation in closed three-dimensional environment. A statistical method is further applied to iteratively detect the conserved substrate motifs with statistical significance. Support vector machine (SVM) is then applied to generate predictive model considering the substrate motifs. According to five-fold cross-validation, the SVMs trained with substrate motifs could achieve an enhanced sensitivity, specificity, and accuracy, and provides a promising performance in an independent test set. The effectiveness of the proposed method is demonstrated by the correct identification of previously reported S-glutathionylation sites of mouse thioredoxin (TXN) and human protein tyrosine phosphatase 1b (PTP1B). Finally, the constructed models are adopted to implement an effective web-based tool, named GSHSite (http://csb.cse.yzu.edu.tw/GSHSite/), for identifying uncharacterized GSH substrate sites on the protein sequences.
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