ArticleJournal of molecular biology2010
Structural analysis of cysteine S-nitrosylation: a modified acid-based motif and the emerging role of trans-nitrosylation.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers.
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Who cites it
103 citing papers in PubMed, 209 citations in OpenAlex.
- Using a bioluminescence resonance energy transfer caspase biosensor to study caspase-3 cleavage site specificity.Bioscience reports · 2026Article
- Aberrant S-nitrosylation in the TCA cycle contributes to mitochondrial dysfunction, energy compromise, and synapse loss in neurodegenerative diseases.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025Review
- Nitric Oxide Regulates Multiple Signal Pathways in Plants via ProteinCurrent issues in molecular biology · 2025Review
- The evolution of S-nitrosylation detection methodology and the role of protein S-nitrosylation in various cancers.Cancer cell international · 2024Review
- Redox regulation, protein S-nitrosylation, and synapse loss in Alzheimer's and related dementias.Neuron · 2024Review
- Identification of Protein Targets ofACS chemical biology · 2024Article
- TRAP1 S-nitrosylation as a model of population-shift mechanism to study the effects of nitric oxide on redox-sensitive oncoproteins.Cell death & disease · 2023Article
- pLMSNOSite: an ensemble-based approach for predicting protein S-nitrosylation sites by integrating supervised word embedding and embedding from pre-trained protein language model.BMC bioinformatics · 2023Article
- NO and Heme Proteins: Cross-Talk between Heme and Cysteine Residues.Antioxidants (Basel, Switzerland) · 2023Review
- Reappraisal of oxidized HMGB1 as a mediator and biomarker.Future science OA · 2022Review
- Hidden networks of aberrant protein transnitrosylation contribute to synapse loss in Alzheimer's disease.Free radical biology & medicine · 2022Review
- Impact of Reactive Species on Amino Acids-Biological Relevance in Proteins and Induced Pathologies.International journal of molecular sciences · 2022Review
- A multienzyme S-nitrosylation cascade regulates cholesterol homeostasis.Cell reports · 2022Article
- Structural snapshots of nitrosoglutathione binding and reactivity underlying S-nitrosylation of photosynthetic GAPDH.Redox biology · 2022Article
- Protein Transnitrosylation Signaling Networks Contribute to Inflammaging and Neurodegenerative Disorders.Antioxidants & redox signaling · 2021Review
- Protein S-nitrosylation and oxidation contribute to protein misfolding in neurodegeneration.Free radical biology & medicine · 2021Review
- A global map of associations between types of protein posttranslational modifications and human genetic diseases.iScience · 2021Article
- S-nitrosylation-mediated coupling of G-protein alpha-2 with CXCR5 induces Hippo/YAP-dependent diabetes-accelerated atherosclerosis.Nature communications · 2021Article
- Biological Mechanisms ofAntioxidants (Basel, Switzerland) · 2021Review
- Noncanonical transnitrosylation network contributes to synapse loss in Alzheimer's disease.Science (New York, N.Y.) · 2021Article
43 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
S-Nitrosylation, the selective and reversible addition of nitric oxide (NO) moiety to cysteine (Cys) sulfur in proteins, regulates numerous cellular processes. In recent years, proteomic approaches that are capable of identifying nitrosylated Cys residues have been developed. However, the features underlying the specificity of Cys modification with NO remain poorly defined. Previous studies suggested that S-nitrosylated Cys may be flanked by an acid-base motif or hydrophobic areas and show high reactivity, low pK(a), and high sulfur atom exposure. In the current study, we prepared an extensive, manually curated data set of proteins with S-nitrosothiols, accounting for a variety of biochemical functions, organisms of origin, and physiological responses to NO. Analysis of this generic NO-Cys data set revealed that proximal acid-base motif, Cys pK(a), sulfur atom exposure, and Cys conservation or hydrophobicity in the vicinity of the modified Cys do not define the specificity of S-nitrosylation. Instead, this analysis revealed a revised acid-base motif, which is located more distantly to the Cys and has its charged groups exposed. We hypothesize that, rather than being strictly used for direct activation of Cys, the modified acid-base motif is engaged in protein-protein interactions thereby contributing to trans-nitrosylation as an important and widespread mechanism for reversible modification of Cys with NO moiety. For proteins lacking the revised motif, we discuss alternative mechanisms including a potential role of nitrosoglutathione as a trans-acting agent.
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