Biological selectivity and functional aspects of protein tyrosine nitration
Abstract
The formation of nitric oxide in biological systems has led to the discovery of a number of post-translational protein modifications that could regulate protein function or potentially be utilized as transducers of nitric oxide signaling. Principal among the nitric oxide-mediated protein modifications are: the nitric oxide-iron heme binding, the S-nitrosylation of reduced cysteine residues, and the C-nitration of tyrosine and tryptophan residues. With the exception of the nitric oxide binding to heme iron proteins, the other two modifications appear to require secondary reactions of nitric oxide and the formation of nitrogen oxides. The rapid development of analytical and immunological methodologies has allowed for the quantification of S-nitrosylated and C-nitrated proteins in vivo revealing an apparent selectivity and specificity of the proteins modified. This review is primarily focused upon the nitration of tyrosine residues discussing parameters that may govern the in vivo selectivity of protein nitration, and the potential biological significance and clinical relevance of this nitric oxide-mediated protein modification.
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Accumulation of 3-nitrotyrosine in proteins is indicative of ROS and RNS stress.
“Accumulation of 3-nitrotyrosine in proteins is indicative of ROS and RNS stress (188).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [188]
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- Authors
- Ischiropoulos, H.
- Affiliations
- Children's Hospital of Philadelphia (US)
- Corresponding author
- Ischiropoulos, Harry
- ORCID
- Ischiropoulos, Harry
- Venue
- Biochemical and Biophysical Research Communications
- Publisher
- Elsevier BV
- Published
- 2003-06
- Volume
- 305
- Issue
- 3
- Pages
- 776-783
- ISSN
- 0006-291X (ISSN-L)
- OpenAlex
- W2121191392
- Cited by
- 500
- References
- 71
- Citations by year
- 2026: 4 · 2025: 5 · 2024: 12 · 2023: 9 · 2022: 13 · 2021: 5 · 2020: 12 · 2019: 11 · 2018: 10 · 2017: 15 · 2016: 20 · 2015: 18 · 2014: 27 · 2013: 18 · 2012: 32
- FWCI
- 18.97
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical and Biophysical Research Communications (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (AG 13966, R01AG013966)
- National Heart, Lung, and Blood Institute (HL54926, R01HL054926)
- Topics
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Keywords
- tyrosine nitration, nitric oxide, post-translational protein modification, S-nitrosylation, nitric oxide signaling, nitrogen oxides, clinical relevance
- MeSH terms
- Amino Acid Sequence, Disease Susceptibility, Humans, Nitric Oxide, Protein Processing, Post-Translational, Proteins, Tyrosine
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Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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