ArticleNucleic acids research2015
dbSNO 2.0: a resource for exploring structural environment, functional and disease association and regulatory network of protein S-nitrosylation.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed.
- CysDBase: a comprehensive database of cysteine post-translational modifications across protein sequence, structure, microenvironment, class, cellular localization, biological pathway, and taxonomy.Database : the journal of biological databases and curation · 2026Article
- Gas-mediated reinforcement of cancer therapies: emerging strategies and future perspectives.Chemical science · 2025Review
- S-Nitrosylation in Cardiovascular Disorders: The State of the Art.Biomolecules · 2025Review
- Identification of Protein Targets ofACS chemical biology · 2024Article
- CHHM: a Manually Curated Catalogue of Human Histone Modifications Revealing Hotspot Regions and Unique Distribution Patterns.International journal of biological sciences · 2024Article
- CysModDB: a comprehensive platform with the integration of manually curated resources and analysis tools for cysteine posttranslational modifications.Briefings in bioinformatics · 2022Article
- Thirty years of molecular dynamics simulations on posttranslational modifications of proteins.Physical chemistry chemical physics : PCCP · 2022Review
- Deciphering the Path ofAntioxidants (Basel, Switzerland) · 2022Article
- An atlas of posttranslational modifications on RNA binding proteins.Nucleic acids research · 2022Article
- Hsp70 in Redox Homeostasis.Cells · 2022Review
- Nitric oxide inhibits endothelial cell apoptosis by inhibiting cysteine-dependent SOD1 monomerization.FEBS open bio · 2022Article
- dbPTM in 2022: an updated database for exploring regulatory networks and functional associations of protein post-translational modifications.Nucleic acids research · 2022Article
- A global map of associations between types of protein posttranslational modifications and human genetic diseases.iScience · 2021Article
- Cysteine modifications (oxPTM) and protein sulphenylation-mediated sulfenome expression in plants: evolutionary conserved signaling networks?Plant signaling & behavior · 2021Article
- iNOS Associates With Poor Survival in Melanoma: A Role for Nitric Oxide in the PI3K-AKT Pathway Stimulation and PTEN S-Nitrosylation.Frontiers in oncology · 2021Article
- Recent Advances in Predicting Protein S-Nitrosylation Sites.BioMed research international · 2021Review
- Human carbonic anhydrases and post-translational modifications: a hidden world possibly affecting protein properties and functions.Journal of enzyme inhibition and medicinal chemistry · 2020Review
- Post-Translational S-Nitrosylation of Proteins in Regulating Cardiac Oxidative Stress.Antioxidants (Basel, Switzerland) · 2020Review
- RESTful API for iPTMnet: a resource for protein post-translational modification network discovery.Database : the journal of biological databases and curation · 2020Article
- Characterization and Identification of Lysine Succinylation Sites based on Deep Learning Method.Scientific reports · 2019Article
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9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Given the increasing number of proteins reported to be regulated by S-nitrosylation (SNO), it is considered to act, in a manner analogous to phosphorylation, as a pleiotropic regulator that elicits dual effects to regulate diverse pathophysiological processes by altering protein function, stability, and conformation change in various cancers and human disorders. Due to its importance in regulating protein functions and cell signaling, dbSNO (http://dbSNO.mbc.nctu.edu.tw) is extended as a resource for exploring structural environment of SNO substrate sites and regulatory networks of S-nitrosylated proteins. An increasing interest in the structural environment of PTM substrate sites motivated us to map all manually curated SNO peptides (4165 SNO sites within 2277 proteins) to PDB protein entries by sequence identity, which provides the information of spatial amino acid composition, solvent-accessible surface area, spatially neighboring amino acids, and side chain orientation for 298 substrate cysteine residues. Additionally, the annotations of protein molecular functions, biological processes, functional domains and human diseases are integrated to explore the functional and disease associations for S-nitrosoproteome. In this update, users are allowed to search a group of interested proteins/genes and the system reconstructs the SNO regulatory network based on the information of metabolic pathways and protein-protein interactions. Most importantly, an endogenous yet pathophysiological S-nitrosoproteomic dataset from colorectal cancer patients was adopted to demonstrate that dbSNO could discover potential SNO proteins involving in the regulation of NO signaling for cancer pathways.
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