Protein S-nitrosylation: Purview and parameters
Abstract
S-nitrosylation, the covalent attachment of a nitrogen monoxide group to the thiol side chain of cysteine, has emerged as an important mechanism for dynamic, post-translational regulation of most or all main classes of protein. S-nitrosylation thereby conveys a large part of the ubiquitous influence of nitric oxide (NO) on cellular signal transduction, and provides a mechanism for redox-based physiological regulation.
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Formation of nitric oxide is catalyzed by three isoforms of nitric oxide synthase (endothelial, neuronal, inducible), all using arginine and oxygen to produce citrulline and nitric oxide.
“Formation of •NO is catalyzed by three isoforms of nitric oxide synthase (NOS) (Fig. 6): endothelial NOS, neuronal NOS or inducible NOS. All NOS isoforms use arginine and oxygen to produce citrulline and •NO [70].”
From Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases (2021) · cites this paper as [70]
NO has novel functions through cGMP-independent and protein S-nitrosylation-dependent intracellular signaling pathways.
“recent studies have indicated novel functions for NO through cGMP-independent and protein S-nitrosylation-dependent intracellular signaling pathways [9].”
From NO-Rich Diet for Lifestyle-Related Diseases (2015) · cites this paper as [9]
Nitrite-induced transnitrosylation in organs might be an alternative in vivo nitrite signaling for mammalian biology, including protection of protein thiols from irreversible oxidation, transcriptional modulation, and posttranslational regulation of proteins.
“These observations indicate that the nitrite-induced transnitrosylation in organs might be an alternative in vivo nitrite signaling for the mammalian biology including protection of protein thiols from irreversible oxidation, transcriptional modulation, and posttranslational regulation of most classes of proteins present in all cells [9]”
From NO-Rich Diet for Lifestyle-Related Diseases (2015) · cites this paper as [9]
Increased NO bioavailability can improve the intracellular redox environment by S-nitrosylation-mediated modulation of most classes of proteins present in all cells.
“increased NO bioavailability can improve the intracellular redox environment by S-nitrosylation-mediated modulation of most classes of proteins present in all cells [9,40].”
From NO-Rich Diet for Lifestyle-Related Diseases (2015) · cites this paper as [9]
NO suppresses TLR4-mediated inflammation and ROS production by inactivating IκκB/NF-κβ.
“NO suppresses the TLR4-mediated inflammation and ROS production by inactivating IkB kinase-β/nuclear factor-κB (IκκB/NF-κβ) [9,63]”
From NO-Rich Diet for Lifestyle-Related Diseases (2015) · cites this paper as [9]
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- Authors
- Hess, D. T., Matsumoto, A., Kim, S.-O., Marshall, H. E., & Stamler, J. S.
- Affiliations
- Duke University (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Stamler, Jonathan S.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2005-02-01
- Volume
- 6
- Issue
- 2
- Pages
- 150-166
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2065773243
- Cited by
- 2,153
- References
- 156
- Citations by year
- 2026: 38 · 2025: 56 · 2024: 70 · 2023: 68 · 2022: 87 · 2021: 90 · 2020: 89 · 2019: 92 · 2018: 87 · 2017: 102 · 2016: 104 · 2015: 103 · 2014: 99 · 2013: 135 · 2012: 125
- FWCI
- 9.39
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Keywords
- S-nitrosylation, nitric oxide, cysteine thiol modification, post-translational regulation, redox regulation, signal transduction
- MeSH terms
- Amino Acid Sequence, Animals, Cell Membrane, Cysteine, Humans, Models, Biological, Models, Chemical, Models, Molecular, Molecular Sequence Data, Nitric Oxide, Nitrogen, Oxidation-Reduction, Protein Processing, Post-Translational, Proteins, Sulfhydryl Compounds, Signal Transduction, GTP Phosphohydrolases
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