The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Antioxidant Systems are Regulated by Nitric Oxide-Mediated Post-translational Modifications (NO-PTMs)
Open accessAbstract
Nitric oxide (NO) is a biological messenger that orchestrates a plethora of plant functions, mainly through post-translational modifications (PTMs) such as S-nitrosylation or tyrosine nitration. In plants, hundreds of proteins have been identified as potential targets of these NO-PTMs under physiological and stress conditions indicating the relevance of NO in plant-signaling mechanisms. Among these NO protein targets, there are different antioxidant enzymes involved in the control of reactive oxygen species (ROS), such as H2O2, which is also a signal molecule. This highlights the close relationship between ROS/NO signaling pathways. The major plant antioxidant enzymes, including catalase, superoxide dismutases (SODs) peroxiredoxins (Prx) and all the enzymatic components of the ascorbate-glutathione (Asa-GSH) cycle, have been shown to be modulated to different degrees by NO-PTMs. This mini-review will update the recent knowledge concerning the interaction of NO with these antioxidant enzymes, with a special focus on the components of the Asa-GSH cycle and their physiological relevance.
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Zelko, I. N., Mariani, T. J., & Folz, R. J. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00905-x · Cited by 2,212
Protein S-nitrosylation: Purview and parameters
Hess, D. T., Matsumoto, A., Kim, S.-O., Marshall, H. E., & Stamler, J. S. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1569 · Cited by 2,153
A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans
Liu, L., Hausladen, A., Zeng, M., Que, L., Heitman, J., & Stamler, J. S. (2001) · Nature · doi:10.1038/35068596 · Cited by 913
Abello, N., Kerstjens, H. A. M., Postma, D. S., & Bischoff, R. (2009) · Journal of Proteome Research · doi:10.1021/pr900039c · Cited by 359
Crystal Structure of the Antioxidant Enzyme Glutathione Reductase Inactivated by Peroxynitrite
Savvides, S. N., Scheiwein, M., Böhme, C. C., Arteel, G. E., Karplus, P. A., Becker, K., & Schirmer, R. H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108190200 · Cited by 127
Cited by
The Role of the Plant Antioxidant System in Drought Tolerance
Laxa, M., Liebthal, M., Telman, W., Chibani, K., & Dietz, K.-J. (2019) · Antioxidants · doi:10.3390/antiox8040094 · Cited by 855
Metadata
- Authors
- Begara-Morales, J. C., Sánchez-Calvo, B., Chaki, M., Valderrama, R., Mata-Pérez, C., Padilla, M. N., Corpas, F. J., & Barroso, J. B.
- Venue
- Frontiers in Plant Science
- Publisher
- Frontiers Media SA
- Published
- 2016-02-16
- Volume
- 7
- Pages
- 152-152
- ISSN
- 1664-462X (ISSN-L)
- OpenAlex
- W2330657976
- Cited by
- 170
- References
- 5
- FWCI
- 21.02
- Type
- journal article
- Language
- en
- Open access
- gold
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- Begara-Morales, J. C., Sánchez-Calvo, B., Chaki, M., Valderrama, R., Mata-Pérez, C., Padilla, M. N., Corpas, F. J., & Barroso, J. B. (2016). Antioxidant Systems are Regulated by Nitric Oxide-Mediated Post-translational Modifications (NO-PTMs). Frontiers in Plant Science. https://doi.org/10.3389/fpls.2016.00152
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