The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Cysteine Redox Sensor in PKGIa Enables Oxidant-Induced Activation
Abstract
Changes in the concentration of oxidants in cells can regulate biochemical signaling mechanisms that control cell function. We have found that guanosine 3′,5′-monophosphate (cGMP)–dependent protein kinase (PKG) functions directly as a redox sensor. The Iα isoform, PKGIα, formed an interprotein disulfide linking its two subunits in cells exposed to exogenous hydrogen peroxide. This oxidation directly activated the kinase in vitro, and in rat cells and tissues. The affinity of the kinase for substrates it phosphorylates was enhanced by disulfide formation. This oxidation-induced activation represents an alternate mechanism for regulation along with the classical activation involving nitric oxide and cGMP. This mechanism underlies cGMP-independent vasorelaxation in response to oxidants in the cardiovascular system and provides a molecular explantion for how hydrogen peroxide can operate as an endothelium-derived hyperpolarizing factor.
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Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
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Cited by
Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling
Ray, P. D., Huang, B.-W., & Tsuji, Y. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.01.008 · Cited by 4,373
Beyond oxidative stress: an immunologist's guide to reactive oxygen species
Nathan, C., & Cunningham-Bussel, A. (2013) · Nature Reviews Immunology · doi:10.1038/nri3423 · Cited by 1,619
Thiol chemistry and specificity in redox signaling
Winterbourn, C. C., & Hampton, M. B. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.05.004 · Cited by 1,226
ATM Activation by Oxidative Stress
Guo, Z., Kozlov, S., Lavin, M. F., Person, M. D., & Paull, T. T. (2010) · Science · doi:10.1126/science.1192912 · Cited by 1,079
The basics of thiols and cysteines in redox biology and chemistry
Poole, L. B. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.11.013 · Cited by 1,031
Metadata
- Authors
- Burgoyne, J. R., Madhani, M., Cuello, F., Charles, R. L., Brennan, J. P., Schröder, E., Browning, D. D., & Eaton, P.
- Venue
- Science
- Published
- 2007-09-07
- Volume
- 317
- Issue
- 5843
- Pages
- 1393-1397
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2085253569
- Cited by
- 457
- References
- 5
- FWCI
- 10.18
- Type
- journal article
- Language
- en
- Open access
- closed
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- Burgoyne, J. R., Madhani, M., Cuello, F., Charles, R. L., Brennan, J. P., Schröder, E., Browning, D. D., & Eaton, P. (2007). Cysteine Redox Sensor in PKGIa Enables Oxidant-Induced Activation. Science. https://doi.org/10.1126/science.1144318
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