The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
The redox switch: dynamic regulation of protein function by cysteine modifications
Open accessAbstract
Reactive oxygen intermediates (ROIs) and reactive nitrogen intermediates (RNIs) have now become well established as important signalling molecules in physiological settings within microorganisms, mammals and plants. These intermediates are routinely synthesised in a highly controlled and transient fashion by NADPH‐dependent enzymes, which constitute key regulators of redox signalling. Mild oxidants such as hydrogen peroxide (H 2 O 2) and especially nitric oxide (NO) signal through chemical reactions with specific atoms of target proteins that result in covalent protein modifications. Specifically, highly reactive cysteine (Cys) residues of low pK a are a major site of action for these intermediates. The oxidation of target Cys residues can result in a number of distinct redox‐based, post‐translational modifications including S‐nitrosylation, S‐glutathionylation; and sulphenic acid, sulphinic acid and disulphide formation. Importantly, such modifications precisely regulate protein structure and function. Cys‐based redox switches are now increasingly being found to underpin many different signalling systems and regulate physiological outputs across kingdoms.
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Cites
Free Radicals in Biology and Medicine
Halliwell, B., & Gutteridge, J. M. C. (2015) · doi:10.1093/acprof:oso/9780198717478.001.0001 · Cited by 8,990
Nitric oxide synthases: structure, function and inhibition
ALDERTON, W. K., COOPER, C. E., & KNOWLES, R. G. (2001) · Biochemical Journal · doi:10.1042/bj3570593 · Cited by 4,110
ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis
D'Autréaux, B., & Toledano, M. B. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2256 · Cited by 3,642
Stamler (2001) · doi:10.1016/s0092-8674(01)00495-0 · Cited by 1,261
Identification of a Plant Nitric Oxide Synthase Gene Involved in Hormonal Signaling
Guo, F.-Q., Okamoto, M., & Crawford, N. M. (2003) · Science · doi:10.1126/science.1086770 · Cited by 889
Liu, X., Miller, M. J. S., Joshi, M. S., Thomas, D. D., & Lancaster, J. R. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.5.2175 · Cited by 602
Export by red blood cells of nitric oxide bioactivity
Pawloski, J. R., Hess, D. T., & Stamler, J. S. (2001) · Nature · doi:10.1038/35054560 · Cited by 579
Bosworth, C. A., Toledo, J. C., Zmijewski, J. W., Li, Q., & Lancaster, J. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0710416106 · Cited by 220
Cited by
Nitric oxide function in plant abiotic stress
Fancy, N. N., Bahlmann, A., & Loake, G. J. (2017) · Plant, Cell & Environment · doi:10.1111/pce.12707 · Cited by 481
Self-citationNitric oxide function in plant biology: a redox cue in deconvolution
Yu, M., Lamattina, L., Spoel, S. H., & Loake, G. J. (2014) · New Phytologist · doi:10.1111/nph.12739 · Cited by 468
Self-citationCadmium stress tolerance in crop plants: Probing the role of sulfur
Gill, S. S., & Tuteja, N. (2011) · Plant Signaling & Behavior · doi:10.4161/psb.6.2.14880 · Cited by 379
Salicylic acid signaling in disease resistance
Kumar, D. (2014) · Plant Science · doi:10.1016/j.plantsci.2014.04.014 · Cited by 310
Frungillo, L., Skelly, M. J., Loake, G. J., Spoel, S. H., & Salgado, I. (2014) · Nature Communications · doi:10.1038/ncomms6401 · Cited by 256
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Metadata
- Authors
- Spadaro, D., Yun, B., Spoel, S. H., Chu, C., Wang, Y., & Loake, G. J.
- Venue
- Physiologia Plantarum
- Publisher
- Wiley
- Published
- 2010-03-15
- Volume
- 138
- Issue
- 4
- Pages
- 360-371
- ISSN
- 0031-9317 (ISSN-L)
- 1399-3054
- OpenAlex
- W2073419452
- Cited by
- 205
- References
- 8
- FWCI
- 5.88
- Type
- journal article
- Language
- en
- Open access
- bronze
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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