Explore experimentally verified cysteine-centered post-translational modifications with integrated structural and regulatory network annotations in dbSNO 3.0.
dbSNO 3.0 is an integrated knowledgebase for experimentally verified cysteine-centered post-translational modifications, enabling data-driven exploration of regulatory mechanisms, structural determinants, and functional consequences.
Integrated framework of dbSNO 3.0 for cysteine PTM annotation, regulatory networks, structural analysis, and functional prediction.
60,000+ experimentally verified cysteine modification events curated from literature and public databases.
Protein–protein interaction and pathway networks revealing cysteine-centered functional modules.
Structural mapping of modification sites to capture spatial and physicochemical context.
Sequence-based prediction and functional inference of cysteine PTMs using large language models.
Representative experimental and computational studies that advanced our understanding of cysteine-centered post-translational modifications, spanning S-nitrosylation, S-glutathionylation, and other redox-regulated cysteine modifications, and provided the conceptual and methodological foundations for dbSNO.
The first label-free, large-scale profiling of S-nitrosylated proteins in individualized colorectal cancer tissues, revealing disease-associated regulatory patterns.
A comprehensive methodological overview of experimental approaches for detecting and characterizing protein S-nitrosylation.
An early computational framework using maximal dependence decomposition to predict cysteine S-nitrosylation sites with substrate specificity.
Introduction of an S-alkylating labeling strategy enabling confident, site-specific identification of S-nitrosylated cysteine residues.
An iteratively statistical framework for predicting cysteine S-glutathionylation sites, extending cysteine-centered PTM analysis beyond S-nitrosylation.
