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Protein S-glutathionylation: a regulatory device from bacteria to humans
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Redox-based regulation of signal transduction: principles, pitfalls, and promises
Janssen-Heininger, Y. M. W., Mossman, B. T., Heintz, N. H., Forman, H. J., Kalyanaraman, B., Finkel, T., Stamler, J. S., Rhee, S. G., & van der Vliet, A. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.011 · Cited by 784
Protein kinase C signaling and oxidative stress
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Kennedy, D. O., & Wightman, E. L. (2011) · Advances in Nutrition · doi:10.3945/an.110.000117 · Cited by 684
The redox stress hypothesis of aging
Sohal, R. S., & Orr, W. C. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.10.445 · Cited by 473
Mammalian Mitochondrial Complex I: Biogenesis, Regulation, and Reactive Oxygen Species Generation
Koopman, W. J. H., Nijtmans, L. G. J., Dieteren, C. E. J., Roestenberg, P., Valsecchi, F., Smeitink, J. A. M., & Willems, P. H. G. M. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2743 · Cited by 411
Janaszak-Jasiecka, A., Płoska, A., Wierońska, J. M., Dobrucki, L. W., & Kalinowski, L. (2023) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-023-00423-2 · Cited by 358
Redox regulation of protein kinases
Corcoran, A., & Cotter, T. G. (2013) · The FEBS Journal · doi:10.1111/febs.12224 · Cited by 306
Glutathione activates virulence gene expression of an intracellular pathogen
Reniere, M. L., Whiteley, A. T., Hamilton, K. L., John, S. M., Lauer, P., Brennan, R. G., & Portnoy, D. A. (2015) · Nature · doi:10.1038/nature14029 · Cited by 277
Ansong, C., Wu, S., Meng, D., Liu, X., Brewer, H. M., Deatherage Kaiser, B. L., Nakayasu, E. S., Cort, J. R., Pevzner, P., Smith, R. D., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1221210110 · Cited by 157
Merry, T. L., Steinberg, G. R., Lynch, G. S., & McConell, G. K. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00239.2009 · Cited by 122
The Role of Bacillithiol in Gram-Positive Firmicutes
Chandrangsu, P., Loi, V. V., Antelmann, H., & Helmann, J. D. (2018) · Antioxidants & Redox Signaling · doi:10.1089/ars.2017.7057 · Cited by 120
Thiol regulation by Mn porphyrins, commonly known as SOD mimics
Batinic-Haberle, I., & Tome, M. E. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101139 · Cited by 88
Crabtree, M. J., Brixey, R., Batchelor, H., Hale, A. B., & Channon, K. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.415992 · Cited by 83
S-Glutathionylation at Cys328 and Cys542 impairs STAT3 phosphorylation
Butturini, E., Darra, E., Chiavegato, G., Cellini, B., Cozzolino, F., Monti, M., Pucci, P., Dell’Orco, D., & Mariotto, S. (2014) · ACS Chemical Biology · doi:10.1021/cb500407d · Cited by 82
Chemistry and Redox Biology of Mycothiol
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Oxidation-driven protein import into mitochondria: Insights and blind spots
Riemer, J., Fischer, M., & Herrmann, J. M. (2011) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2010.06.003 · Cited by 58
Circadian Redox and Metabolic Oscillations in Mammalian Systems
O'Neill, J. S., & Feeney, K. A. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5582 · Cited by 51
Downstream mechanisms of nitric oxide-mediated skeletal muscle glucose uptake during contraction
Merry, T. L., Lynch, G. S., & McConell, G. K. (2010) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00433.2010 · Cited by 47
Age-Related Changes in Antioxidant Enzymes Related to Hydrogen Peroxide Metabolism in Rat Inner Ear
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Protective role of bacillithiol in superoxide stress and Fe–S metabolism in Bacillus subtilis
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Zgheib, C., Kurdi, M., Zouein, F. A., Gunter, B. W., Stanley, B. A., Zgheib, J., Romero, D. G., King, S. B., Paolocci, N., & Booz, G. W. (2012) · PLoS ONE · doi:10.1371/journal.pone.0043313 · Cited by 34
McCool, E. N., Lodge, J. M., Basharat, A. R., Liu, X., Coon, J. J., & Sun, L. (2019) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-019-02206-6 · Cited by 28
Metadata
- Authors
- Dalle-Donne, I., Rossi, R., Colombo, G., Giustarini, D., & Milzani, A.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2009-02
- Volume
- 34
- Issue
- 2
- Pages
- 85-96
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W2041162400
- Cited by
- 628
- References
- 4
- FWCI
- 2.96
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
