ArticleACS chemical biology2014
Proteomic profiling of nitrosative stress: protein S-oxidation accompanies S-nitrosylation.
Article in ACS chemical biology, 2014. 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, 34 citations in OpenAlex.
- Differential alkylation-based redox proteomics--Lessons learnt.Redox biology · 2015Pooled it
- Regulation of Ras Signaling by S-Nitrosylation.Antioxidants (Basel, Switzerland) · 2023Review
- Redox regulation of the immune response.Cellular & molecular immunology · 2022Review
- Curcumin Decreases Hippocampal Neurodegeneration and Nitro-Oxidative Damage to Plasma Proteins and Lipids Caused by Short-Term Exposure to Ozone.Molecules (Basel, Switzerland) · 2021Article
- The cell biology of Parkinson's disease.The Journal of cell biology · 2021Review
- Metabolomics Reveals Differences in Aqueous Humor Composition in Patients With and Without Pseudoexfoliation Syndrome.Frontiers in molecular biosciences · 2021Article
- The interplay between oxidative stress and bioenergetic failure in neuropsychiatric illnesses: can we explain it and can we treat it?Molecular biology reports · 2020Review
- Identification of new targets of S-nitrosylation in neural stem cells by thiol redox proteomics.Redox biology · 2020Article
- Thioredoxin shapes theeLife · 2018Article
- Proteomic analysis of S-nitrosylated nuclear proteins in rat cortical neurons.Science signaling · 2018Article
- Comparative and integrative metabolomics reveal thatThe Journal of biological chemistry · 2018Article
- Evidence against Stable Protein S-Nitrosylation as a Widespread Mechanism of Post-translational Regulation.Molecular cell · 2018Article
- The Enzymatic and Structural Basis for Inhibition of Echinococcus granulosus Thioredoxin Glutathione Reductase by Gold(I).Antioxidants & redox signaling · 2017Article
- Nitrosative Stress, Hypernitrosylation, and Autoimmune Responses to Nitrosylated Proteins: New Pathways in Neuroprogressive Disorders Including Depression and Chronic Fatigue Syndrome.Molecular neurobiology · 2017Review
- Quantitative proteomic characterization of redox-dependent post-translational modifications on protein cysteines.Molecular bioSystems · 2017Review
- Thiol-Based Redox Modulation of Soluble Guanylyl Cyclase, the Nitric Oxide Receptor.Antioxidants & redox signaling · 2017Review
- Proteomic approaches to quantify cysteine reversible modifications in aging and neurodegenerative diseases.Proteomics. Clinical applications · 2016Review
- Nitric oxide inhibits topoisomerase II activity and induces resistance to topoisomerase II-poisons in human tumor cells.Biochimica et biophysica acta · 2016Article
- Glutathione adducts induced by ischemia and deletion of glutaredoxin-1 stabilize HIF-1α and improve limb revascularization.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Identification of novel S-nitrosation sites in soluble guanylyl cyclase, the nitric oxide receptor.Journal of proteomics · 2016Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Reversible chemical modifications of protein cysteine residues by S-nitrosylation and S-oxidation are increasingly recognized as important regulatory mechanisms for many protein classes associated with cellular signaling and stress response. Both modifications may theoretically occur under cellular nitrosative or nitroxidative stress. Therefore, a proteomic isotope-coded approach to parallel, quantitative analysis of cysteome S-nitrosylation and S-oxidation was developed. Modifications of cysteine residues of (i) human glutathione-S-transferase P1-1 (GSTP1) and (ii) the schistosomiasis drug target thioredoxin glutathione reductase (TGR) were studied. Both S-nitrosylation (SNO) and S-oxidation to disulfide (SS) were observed for reactive cysteines, dependent on concentration of added S-nitrosocysteine (CysNO) and independent of oxygen. SNO and SS modifications of GSTP1 were quantified and compared for therapeutically relevant NO and HNO donors from different chemical classes, revealing oxidative modification for all donors. Observations on GSTP1 were extended to cell cultures, analyzed after lysis and in-gel digestion. Treatment of living neuronal cells with CysNO, to induce nitrosative stress, caused levels of S-nitrosylation and S-oxidation of GSTP1 comparable to those of cell-free studies. Cysteine modifications of PARK7/DJ-1, peroxiredoxin-2, and other proteins were identified, quantified, and compared to overall levels of protein S-nitrosylation. The new methodology has allowed identification and quantitation of specific cysteome modifications, demonstrating that nitroxidation to protein disulfides occurs concurrently with S-nitrosylation to protein-SNO in recombinant proteins and living cells under nitrosative stress.
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