ArticleACS chemical biology2010
Proteomic and mass spectroscopic quantitation of protein S-nitrosation differentiates NO-donors.
Article in ACS chemical biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers, 1 of them a synthesis that pooled it.
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Who cites it
23 citing papers in PubMed, 1 synthesis or guideline pooled it, 46 citations in OpenAlex.
- Differential alkylation-based redox proteomics--Lessons learnt.Redox biology · 2015Pooled it
- Proteome-wide profiling of S-nitrosylated proteins using the SNOTRAP probe and mass spectrometry-based detection.Nature protocols · 2026Review
- Comprehensive Redox Profiling of the Thiol Proteome ofMolecular & cellular proteomics : MCP · 2018Article
- Comparative and integrative metabolomics reveal thatThe Journal of biological chemistry · 2018Article
- Biomarkers of oxidative and nitro-oxidative stress: conventional and novel approaches.British journal of pharmacology · 2017Review
- Quantitative proteomic characterization of redox-dependent post-translational modifications on protein cysteines.Molecular bioSystems · 2017Review
- Proteomic approaches to quantify cysteine reversible modifications in aging and neurodegenerative diseases.Proteomics. Clinical applications · 2016Review
- Chemoproteomic Strategy to Quantitatively Monitor Transnitrosation Uncovers Functionally Relevant S-Nitrosation Sites on Cathepsin D and HADH2.Cell chemical biology · 2016Article
- Dual Labeling Biotin Switch Assay to Reduce Bias Derived From Different Cysteine Subpopulations: A Method to Maximize S-Nitrosylation Detection.Circulation research · 2015Article
- Monitoring in vivo reversible cysteine oxidation in proteins using ICAT and mass spectrometry.Nature protocols · 2014Article
- Proteomic profiling of nitrosative stress: protein S-oxidation accompanies S-nitrosylation.ACS chemical biology · 2014Article
- Detection of S-nitrosothiols.Biochimica et biophysica acta · 2014Review
- Oxidative stress and the HIV-infected brain proteome.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2013Review
- Cysteine-mediated redox signaling: chemistry, biology, and tools for discovery.Chemical reviews · 2013Review
- S-nitrosation of glutathione transferase p1-1 is controlled by the conformation of a dynamic active site helix.The Journal of biological chemistry · 2013Article
- Mechanism-based triarylphosphine-ester probes for capture of endogenous RSNOs.Journal of the American Chemical Society · 2013Article
- Quinone-induced activation of Keap1/Nrf2 signaling by aspirin prodrugs masquerading as nitric oxide.Chemical research in toxicology · 2012Article
- Chemical methods for the direct detection and labeling of S-nitrosothiols.Antioxidants & redox signaling · 2012Review
- Strategies and tools to explore protein S-nitrosylation.Biochimica et biophysica acta · 2012Review
- A Conspectus of Cellular Mechanisms of Nitrosothiol Formation from Nitric Oxide.Forum on immunopathological diseases and therapeutics · 2012Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Protein S-nitrosation has been argued to be the most important signaling pathway mediating the bioactivity of NO. This post-translational modification of protein thiols is the result of chemical nitrosation of cysteine residues. The term NO-donors covers very different chemical classes, from clinical therapeutics to probes of routine use in chemical biology; their different chemistry is predicted to result in distinctive biology regulated by protein S-nitrosation. To measure the extent of protein S-nitrosation by NO-donors, a proteomic mass spectrometry method was developed, which quantitates free thiol versus nitrosothiol for each modified cysteine residue, coined d-Switch. This method is adapted from the biotin switch (BST) method, used extensively to identify S-nitrosated proteins in complex biological mixtures; however, BST does not quantitate free thiol. Since glutathione-S-transferase P1-1 (GST-P1) has been proposed to be a biological "NO-carrier", GST-P1 was used as a reporter protein. The 5 different chemical classes of NO-donors compared by d-Switch demonstrated very different profiles of protein S-nitrosation and response to O(2) and cysteine, although all NO-donors were oxidants toward GST-P1. The low limits of detection and the ability to use established MS database searching allowed facile generalization of the d-Switch method. Therefore after incubation of neuronal cell cultures with nitrosothiol, it was possible to quantitate not only S-nitrosation of GST-P1 but also many other proteins, including novel targets such as ubiquitin carboxyl-terminal esterase L1 (UCHL1). Moreover, d-Switch also allowed identification of non-nitrosated proteins and quantitation of degree of nitrosation for individual protein thiols.
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Registered trials
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