The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Redox compartmentalization and cellular stress
Open accessAbstract
Mammalian cells are highly organized to optimize function. For instance, oxidative energy‐producing processes in mitochondria are sequestered away from plasma membrane redox signalling complexes and also from nuclear DNA, which is subject to oxidant‐induced mutation. Proteins are unique among macromolecules in having reversible oxidizable elements, ‘sulphur switches', which support dynamic regulation of structure and function. Accumulating evidence shows that redox signalling and control systems are maintained under kinetically limited steady states, which are highly displaced from redox equilibrium and distinct among organelles. Mitochondria are most reducing and susceptible to oxidation under stressed conditions, while nuclei are also reducing but relatively resistant to oxidation. Within compartments, the glutathione and thioredoxin systems serve parallel and non‐redundant functions to maintain the dynamic redox balance of subsets of protein cysteines, which function in redox signalling and control. This organization allows cells to be poised to respond to cell stress but also creates sites of vulnerability. Importantly, disruption of redox organization is a common basis for disease. Research tools are becoming available to elucidate details of subcellular redox organization, and this development highlights an opportunity for a new generation of targeted antioxidants to enhance and restore redox signalling and control in disease prevention.
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Cites
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
NOX enzymes and the biology of reactive oxygen
Lambeth, J. D. (2004) · Nature Reviews Immunology · doi:10.1038/nri1312 · Cited by 3,125
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Jones, D. P. (2006) · Antioxidants & Redox Signaling · doi:10.1089/ars.2006.8.1865 · Cited by 1,726
Self-citationSignaling Functions of Reactive Oxygen Species
Forman, H. J., Maiorino, M., & Ursini, F. (2010) · Biochemistry · doi:10.1021/bi9020378 · Cited by 827
Rajasekaran, N. S., Connell, P., Christians, E. S., Yan, L.-J., Taylor, R. P., Orosz, A., Zhang, X. Q., Stevenson, T. J., Peshock, R. M., Leopold, J. A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.06.044 · Cited by 437
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Self-citationA key role for mitochondria in endothelial signaling by plasma cysteine/cystine redox potential
Go, Y.-M., Park, H., Koval, M., Orr, M., Reed, M., Liang, Y., Smith, D., Pohl, J., & Jones, D. P. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.10.050 · Cited by 103
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Cited by
The Role of Oxidative Stress in Parkinson's Disease
Dias, V., Junn, E., & Mouradian, M. M. (2013) · Journal of Parkinson’s Disease · doi:10.3233/jpd-130230 · Cited by 1,845
Rochette, L., Lorin, J., Zeller, M., Guilland, J.-C., Lorgis, L., Cottin, Y., & Vergely, C. (2013) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2013.07.004 · Cited by 456
Oxidative Stress and Human Hypertension: Vascular Mechanisms, Biomarkers, and Novel Therapies
Montezano, A. C., Dulak-Lis, M., Tsiropoulou, S., Harvey, A., Briones, A. M., & Touyz, R. M. (2015) · Canadian Journal of Cardiology · doi:10.1016/j.cjca.2015.02.008 · Cited by 323
Thiol/disulfide redox states in signaling and sensing
Go, Y.-M., & Jones, D. P. (2013) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.764840 · Cited by 241
Self-citationCabungcal, J.-H., Steullet, P., Kraftsik, R., Cuenod, M., & Do, K. Q. (2013) · Biological Psychiatry · doi:10.1016/j.biopsych.2012.09.020 · Cited by 232
Metadata
- Authors
- Jones, D. P., & Go, Y. ‐.
- Venue
- Diabetes, Obesity and Metabolism
- Publisher
- Wiley
- Published
- 2010-10
- Volume
- 12
- Issue
- s2
- Pages
- 116-125
- ISSN
- 1462-8902 (ISSN-L)
- 1463-1326
- OpenAlex
- W2062609826
- Cited by
- 246
- References
- 8
- FWCI
- 6.38
- 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).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
