Protein tyrosine nitration in higher plants grown under natural and stress conditions
Open accessAbstract
Protein tyrosine nitration is a post-translational modification (PTM) mediated by reactive nitrogen species (RNS) that is linked to nitro-oxidative damages in plant cells. During the last decade, the identification of proteins undergoing this PTM under adverse environmental conditions has increased. However, there is also a basal endogenous nitration which seems to have a regulatory function. The technological advances in proteome analysis have allowed identifying these modified proteins and have shown that the number and identity of the nitrated proteins change among plant species, analysed organs and growing/culture conditions. In this work, the current knowledge of protein tyrosine nitration in higher plants under different situations is reviewed.
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3-NT has been primarily used for determination of protein nitration and nitrosative stress in clinical settings.
“3-NT, the stable endproduct of peroxynitrite-mediated oxidation formed via nitration of free or protein-bound tyrosine, has been primarily used for the determination of protein nitration and nitrosative stress in clinical settings [186,187].”
From Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases (2021) · cites this paper as [186]
The section on in vivo detection reports using antibodies against 3-nitrotyrosine to detect protein nitration in plants. The Introduction also describes nitrotyrosine as a footprint of peroxynitrite. The paper does not establish that 3-NT has been used primarily in clinical settings; its examples concern plants. (LLM, conf=0.82)
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Cited by
Sorted by citations
Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases
Kehm, R., Baldensperger, T., Raupbach, J., & Höhn, A. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101901 · Cited by 348 · see citing works
“3-NT, the stable endproduct of peroxynitrite-mediated oxidation formed via nitration of free or protein-bound tyrosine, has been primarily used for the determination of protein nitration and nitrosative stress in clinical settings [186,187].”
MethodNitro-oxidative stress vs oxidative or nitrosative stress in higher plants
Corpas, F. J., & Barroso, J. B. (2013) · New Phytologist · doi:10.1111/nph.12380 · Cited by 193 · see citing works
Self-citation
- Authors
- Corpas, F. J., Palma, J. M., del Río, L. A., & Barroso, J. B.
- Affiliations
- Consejo Superior de Investigaciones Científicas (ES)
- Universidad de Jaén (ES)
- Corresponding author
- Corpas, Francisco J.
- Venue
- Frontiers in Plant Science
- Publisher
- Frontiers Media SA
- Published
- 2013
- Volume
- 4
- Pages
- 29-29
- ISSN
- 1664-462X (ISSN-L)
- PMC
- PMC3580390
- OpenAlex
- W2007821357
- Cited by
- 128
- References
- 0
- Citations by year
- 2026: 6 · 2025: 2 · 2024: 1 · 2023: 6 · 2022: 10 · 2021: 12 · 2020: 10 · 2019: 14 · 2018: 8 · 2017: 14 · 2016: 12 · 2015: 14 · 2014: 10 · 2013: 8
- FWCI
- 17.71
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Frontiers in Plant Science (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Ministerio de Ciencia e Innovación (ACI2009-0860, BIO2009-12003-C02-01, BIO2009-12003-C02-02, AGL2011-26044, BIO192)
- Junta de Andalucía (BIO 192, BIO-286)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Stress Responses and Tolerance
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Keywords
- tyrosine nitration, higher plants, reactive nitrogen species, post-translational modification, abiotic stress, nitrated proteins, plant proteome
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