ArticleProceedings of the National Academy of Sciences of the United States of America2011
Site-specific and redox-controlled S-nitrosation of thioredoxin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 66 citations in OpenAlex.
- Involvement of the thioredoxin system in multiple diseases: A focus on mechanisms of action in autophagy and ferroptosis (Review).Molecular medicine reports · 2026Review
- Thioredoxin (Trx): A redox target and modulator of cellular senescence and aging-related diseases.Redox biology · 2024Review
- Insights into the Multifaceted Roles of Thioredoxin-1 System: Exploring Knockout Murine Models.Biology · 2024Review
- The C-terminal selenenylsulfide of extracellular/non-reduced thioredoxin reductase endows this protein with selectivity to small-molecule electrophilic reagents under oxidative conditions.Frontiers in molecular biosciences · 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
- Deciphering the Path ofAntioxidants (Basel, Switzerland) · 2022Article
- Organic mercury solid phase chemoselective capture for proteomic identification of S-nitrosated proteins and peptides.Nitric oxide : biology and chemistry · 2021Article
- 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
- Thioredoxins: Emerging Players in the Regulation of Protein S-Nitrosation in Plants.Plants (Basel, Switzerland) · 2020Review
- ADAM17 cytoplasmic domain modulates Thioredoxin-1 conformation and activity.Redox biology · 2020Article
- Shank3 mutation in a mouse model of autism leads to changes in the S-nitroso-proteome and affects key proteins involved in vesicle release and synaptic function.Molecular psychiatry · 2020Article
- Redox homeostasis, oxidative stress and mitophagy.Mitochondrion · 2020Review
- Endothelial nitric oxide synthase-derived nitric oxide in the regulation of metabolism.F1000Research · 2020Review
- Thioredoxin shapes theeLife · 2018Article
- Chemoproteomics Reveals Chemical Diversity and Dynamics of 4-Oxo-2-nonenal Modifications in Cells.Molecular & cellular proteomics : MCP · 2017Article
- Modulation of signaling mechanisms in the heart by thioredoxin 1.Free radical biology & medicine · 2017Review
- Biomarkers of oxidative and nitro-oxidative stress: conventional and novel approaches.British journal of pharmacology · 2017Review
- Nuclear Factor (Erythroid-Derived 2)-Like 2 and Thioredoxin-1 in Atherosclerosis and Ischemia/Reperfusion Injury in the Heart.Antioxidants & redox signaling · 2017Review
- Improved tag-switch method reveals that thioredoxin acts as depersulfidase and controls the intracellular levels of protein persulfidation.Chemical science · 2016Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Protein S-nitrosation on cysteine residues has emerged as an important posttranslational modification in mammalian cells. Previous studies have suggested a primary role for thioredoxin (Trx) in controlling protein S-nitrosation reactions. Human Trx contains five conserved Cys, including two redox-active catalytic Cys (Cys32 and Cys35) and three non-active-site Cys (Cys62, Cys69, and Cys73), all of which have been reported as targets of S-nitrosation. Prior reports have studied thermodynamic end points of nitrosation reactions; however, the kinetics of Trx nitrosation has not previously been investigated. Using the transnitrosation agent, S-nitrosoglutathione, a kinetic analysis of the selectivity and redox dependence of Trx nitrosation at physiologically relevant concentrations and times was performed, utilizing a mass spectrometry-based method for the direct analysis of the nitrosated Trx. Reduced Trx (rTrx) was nitrosated 2.7-times faster than oxidized Trx (oTrx), and rTrx was nitrosated selectively on Cys62, whereas oTrx was nitrosated only on Cys73. These sites of nitrosation were confirmed at the peptide level using a novel modification of the biotin-switch technique called the reductive switch. These results suggest separate signaling pathways for Trx-SNO under different cellular redox states.
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