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An integrated resource for post-translational modifications (PTMs), providing not only a comprehensive dataset of experimentally verified PTMs that are supported by the literature but also an integrative platform for accessing all available databases and tools that are associated with PTM analysis. In addition to collecting experimental PTM data from public databases, this update manually curates more than 12 000 PTM peptides, including the emerging S-nitrosylation, S-glutathionylation and succinylation, from approximately 500 research articles which were extracted by text mining. This update develops an integrative platform for PTM analyses by integrating all available databases and tools that are associated with over 20 PTM types.
A public resource to allow efficient access to experimentally validated S-glutathionylation sites and comprehensive bioinformatics analyses, including functional annotations, structural characteristics and substrate motifs for S-glutathionylation sites. The database not only provides a benchmark dataset for the development of computational prediction tools and their comparison but also supplies the potential glutathionylated targets for verification and other biological applications.
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Provides information about protein oxidative modification verified by experimental studies. For each modified cysteine, the exact position, modification type and flanking sequence are provided. Additional information, including gene name, organism, sequence, literature references and links to UniProt and PDB, is also supplied. The database supports several functions including data search, blast and browsing. RedoxDB not only includes data from case-by-case studies but also integrates high-throughput data from proteomics studies. RedoxDB is useful for both experimental studies and computational analyses of protein oxidative modification.
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