By Toren Finkel (Editor), J. Silvio Gutkind (Editor)
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Extra resources for Signal Transduction and Human Disease, May 2003
Sample text
And Ryu, S. (2001). Structural basis of the redox switch in the OxyR transcription factor. Cell 105, 103–113. Cornwell, T. , Boerth, N. , and Lincoln, T. M. (1994). Inhibition of smooth muscle cell growth by nitric oxide and activation of cAMPdependent protein kinase by cGMP. Am J Physiol 267, C1405–C1413. D’Agostino, R. , Russell, M. , Huse, D. , Ellison, R. , Wilson, P. , and Hartz, S. C. (2000). Primary and subsequent coronary risk appraisal: new results from the Framingham study. Am Heart J 139, 272–281.
In such a scenario (see Fig. 9. A putative cycle of redox modification of target proteins. The signature of specific targets for hydrogen peroxide in cells may be the presence of a reactive cysteine residue. This amino acid can be ionized at physiological pH and is therefore a target for ROS-mediated signaling. Oxidation of the cysteine to the sulfenic form is reversible, potentially by interaction with glutathione (GSH) forming a mix-disulfide intermediate. Stronger oxidants could result in further oxidation to the sulfonic ion, which is generally not viewed as a reversible modification.
2001).