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Deglutathionylation of Protein-SSG As mentioned above, S-glutathionylation of proteins is dynamic and reversible, so the steady-state level of protein-SSG under various conditions depends on the relative rates of glutathionylation (formation) and deglutathionylation (breakdown) (Figure 3), providing another level of regulation for cellular processes [53]

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The trial was conducted in accordance with the Declaration of Helsinki (1996 revision) and under the principals of good clinical practice, as laid out in the International Conference on Harmonization document Good Clinical Practice Consolidated Guideline