The DOI matches its Crossref record; 22 of the 22 references it cites were found in a registry or an index.
Nanotransducers in cellular redox signaling: modification of thiols by reactive oxygen and nitrogen species
Abstract
The control of signal transduction involves post-translational modification of proteins at key amino acids. Cysteine residues are important in the control of 'redox' cell-signaling pathways, as thiol chemistry offers the possibility of modification by structurally diverse species, including those derived from oxidized lipids, peroxides or nitric oxide. An important and provocative study of the modification of thiols in the transcription factor OxyR recently extended this hypothesis. The findings offer the enticing possibility that the cell can distinguish between different degrees of oxidant and nitrosative exposure by modification at a single site on a signaling molecule.
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“Mitochondrial proteins are also subject to attack by ROS (88, 121, 157, 257, 318).”
From Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function (2009) · cites this paper as [88]
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Cites
Free Radicals in the Physiological Control of Cell Function
Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855
Schafer, F. Q., & Buettner, G. R. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00480-4 · Cited by 4,587
Lipton, S. A., Choi, Y.-B., Pan, Z.-H., Lei, S. Z., Chen, H.-S. V., Sucher, N. J., Loscalzo, J., Singel, D. J., & Stamler, J. S. (1993) · Nature · doi:10.1038/364626a0 · Cited by 2,433
Activation of the OxyR Transcription Factor by Reversible Disulfide Bond Formation
Zheng, M., Åslund, F., & Storz, G. (1998) · Science · doi:10.1126/science.279.5357.1718 · Cited by 1,197
Stone, J. R., & Marletta, M. A. (1994) · Biochemistry · doi:10.1021/bi00184a036 · Cited by 647
Structural Basis of the Redox Switch in the OxyR Transcription Factor
Choi, H., Kim, S.-J., Mukhopadhyay, P., Cho, S., Woo, J.-R., Storz, G., & Ryu, S.-E. (2001) · Cell · doi:10.1016/s0092-8674(01)00300-2 · Cited by 568
Nitric oxide and iron proteins
Cooper, C. E. (1999) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(99)00021-3 · Cited by 510
Self-citationA Molecular Redox Switch on p21
Lander, H. M., Hajjar, D. P., Hempstead, B. L., Mirza, U. A., Chait, B. T., Campbell, S. L., & Quilliam, L. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.7.4323 · Cited by 488
Kim, S. O., Merchant, K., Nudelman, R., Beyer, W. F., Keng, T., DeAngelo, J. D., Hausladen, A., & Stamler, J. S. (2002) · Cell · doi:10.1016/s0092-8674(02)00723-7 · Cited by 484
Redox-operated genetic switches: the SoxR and OxyR transcription factors
Pomposiello, P. J., & Demple, B. (2001) · Trends in biotechnology · doi:10.1016/s0167-7799(00)01542-0 · Cited by 403
Research works printed but not linked: 1
- Zheng, 1998, Activation of the OxyR transcription factor by reversible disulfide bond formation, Science, 279, 1655, 10.1126/science.279.5357.1718 · DOI
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Autophagy, mitochondria and oxidative stress: cross-talk and redox signalling.
Lee, J., Giordano, S., & Zhang, J. (2012) · Biochemical Journal · doi:10.1042/bj20111451 · Cited by 1,438
Bacterial mercury resistance from atoms to ecosystems
Barkay, T., Miller, S. M., & Summers, A. O. (2003) · FEMS Microbiology Reviews · doi:10.1016/s0168-6445(03)00046-9 · Cited by 1,054
Nitric oxide signalling in plants
Neill, S. J., Desikan, R., & Hancock, J. T. (2003) · New Phytologist · doi:10.1046/j.1469-8137.2003.00804.x · Cited by 872
Protein Sulfenic Acids in Redox Signaling
Poole, L. B., Karplus, P. A., & Claiborne, A. (2004) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.44.101802.121735 · Cited by 604
Nitric oxide, cell bioenergetics and neurodegeneration
Moncada, S., & Bolaños, J. P. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03988.x · Cited by 555
Metadata
- Authors
- Cooper, C. E., Patel, R. P., Brookes, P. S., & Darley-Usmar, V. M.
- Affiliations
- University of Essex (GB)
- University of Alabama at Birmingham (US)
- Corresponding author
- Darley-Usmar, Victor M.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2002-10
- Volume
- 27
- Issue
- 10
- Pages
- 489-492
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W1999952146
- Cited by
- 180
- References
- 22
- Citations by year
- 2024: 3 · 2023: 2 · 2022: 4 · 2021: 1 · 2020: 4 · 2019: 5 · 2018: 3 · 2017: 5 · 2016: 8 · 2015: 5 · 2014: 9 · 2013: 6 · 2012: 11
- FWCI
- 5.06
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Trends in Biochemical Sciences (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Keywords
- redox signaling, nanotransducers, thiol modification, cysteine residues, reactive oxygen species, reactive nitrogen species, nitrosative stress, OxyR, post-translational modification, protein oxidation, nitrosylation, oxidized lipids, peroxides, nitric oxide
- MeSH terms
- Animals, Cysteine, Escherichia coli, Oxidation-Reduction, Protein Processing, Post-Translational, Proteins, Sulfhydryl Compounds, Signal Transduction, Reactive Oxygen Species, Reactive Nitrogen Species
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