ArticleFree radical biology & medicine2007
Quantification of oxidative posttranslational modifications of cysteine thiols of p21ras associated with redox modulation of activity using isotope-coded affinity tags and mass spectrometry.
Article in Free radical biology & medicine, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 66 citations in OpenAlex.
- Histone oxidation as a new mechanism of metabolic control over gene expression.Trends in genetics : TIG · 2024Review
- A How-To Guide for Mode of Action Analysis of Antimicrobial Peptides.Frontiers in cellular and infection microbiology · 2020Review
- Redox Signaling by Reactive Electrophiles and Oxidants.Chemical reviews · 2018Review
- The cysteine proteome.Free radical biology & medicine · 2015Review
- Chemical approaches to discovery and study of sources and targets of hydrogen peroxide redox signaling through NADPH oxidase proteins.Annual review of biochemistry · 2015Review
- Article
- Profiling thiol metabolites and quantification of cellular glutathione using FT-ICR-MS spectrometry.Analytical and bioanalytical chemistry · 2014Article
- Monitoring in vivo reversible cysteine oxidation in proteins using ICAT and mass spectrometry.Nature protocols · 2014Article
- Biophysical and proteomic characterization strategies for cysteine modifications in Ras GTPases.Methods in molecular biology (Clifton, N.J.) · 2014Article
- Protein glutathionylation in cardiovascular diseases.International journal of molecular sciences · 2013Review
- Proteome-wide detection and quantitative analysis of irreversible cysteine oxidation using long column UPLC-pSRM.Journal of proteome research · 2013Article
- S-glutathionylation in monocyte and macrophage (dys)function.International journal of molecular sciences · 2013Review
- Cysteine-mediated redox signaling: chemistry, biology, and tools for discovery.Chemical reviews · 2013Review
- Glutathiolated Ras: characterization and implications for Ras activation.Free radical biology & medicine · 2013Article
- Chasing cysteine oxidative modifications: proteomic tools for characterizing cysteine redox status.Circulation. Cardiovascular genetics · 2012Article
- Identification of nitration sites by peroxynitrite on p16 protein.The protein journal · 2012Article
- Regulatory control or oxidative damage? Proteomic approaches to interrogate the role of cysteine oxidation status in biological processes.Molecular & cellular proteomics : MCP · 2012Review
- Regulation of cell physiology and pathology by protein S-glutathionylation: lessons learned from the cardiovascular system.Antioxidants & redox signaling · 2012Review
- Protein S-glutathiolation: redox-sensitive regulation of protein function.Journal of molecular and cellular cardiology · 2012Review
- Effect of single amino acid substitution on oxidative modifications of the Parkinson's disease-related protein, DJ-1.Molecular & cellular proteomics : MCP · 2012Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
p21ras GTPase is the protein product of the most commonly mutated human oncogene and has been identified as a target for reactive oxygen and nitrogen species. Posttranslational modification of reactive thiols, by reversible S-glutathiolation and S-nitrosation, and potentially also by irreversible oxidation, may have significant effects on p21ras activity. Here we used an isotope-coded affinity tag (ICAT) and mass spectrometry to quantitate the reversible and irreversible oxidative posttranslational thiol modifications of p21ras caused by peroxynitrite (ONOO(-)) or glutathione disulfide (GSSG). The activity of p21ras was significantly increased after exposure to GSSG, but not to ONOO(-). The results of LC-MS/MS analysis of tryptic peptides of p21ras treated with ONOO(-) showed that ICAT labeling of Cys(118) was decreased by 47%, whereas Cys(80) was not significantly affected and was thereby shown to be less reactive. The extent of S-glutathiolation of Cys(118) by GSSG was 53%, and that of the terminal cysteines was 85%, as estimated by the decrease in ICAT labeling. The changes in ICAT labeling caused by GSSG were reversible by chemical reduction, but those caused by peroxynitrite were irreversible. The quantitative changes in thiol modification caused by GSSG associated with increased activity demonstrate the potential importance of redox modulation of p21ras.
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