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- W2039924630 endingPage "1393" @default.
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- W2039924630 abstract "A large number of proteins contain free thiols that can be modified by the formation of internal disulphides or by mixed disulphides with low-molecular-mass thiols. The majority of these latter modifications result from the interaction of protein thiols with the endogenous glutathione pool. Protein glutathionylation and disulphide formation are of significance both for defence against oxidative damage and in redox signalling. As mitochondria are central to both oxidative damage and redox signalling within the cell, these modifications of mitochondrial proteins are of particular importance. In the present study, we review the mechanisms and physiological significance of these processes." @default.
- W2039924630 created "2016-06-24" @default.
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- W2039924630 date "2005-10-26" @default.
- W2039924630 modified "2023-10-13" @default.
- W2039924630 title "Disulphide formation on mitochondrial protein thiols" @default.
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- W2039924630 doi "https://doi.org/10.1042/bst0331390" @default.
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