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- W2070476076 endingPage "442" @default.
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- W2070476076 abstract "Cells are constantly exposed to various oxidants, either generated endogenously due to metabolic activity or exogenously. One way that cells respond to oxidants is through the action of redox-regulated proteins. These proteins also play important roles in oxidant signaling and protein biogenesis events. The key sensors built into redox-regulated proteins are cysteines, which undergo reversible thiol oxidation in response to changes in the oxidation status of the cellular environment. In this review, we discuss three examples of redox-regulated proteins found in bacteria, mitochondria, and chloroplasts. These proteins use oxidation of their redox-sensitive cysteines to reversibly convert large structural domains into more disordered regions or vice versa. These massive structural rearrangements are directly implicated in the functions of these proteins." @default.
- W2070476076 created "2016-06-24" @default.
- W2070476076 creator A5017297567 @default.
- W2070476076 creator A5046177432 @default.
- W2070476076 date "2013-06-01" @default.
- W2070476076 modified "2023-10-02" @default.
- W2070476076 title "The roles of conditional disorder in redox proteins" @default.
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- W2070476076 doi "https://doi.org/10.1016/j.sbi.2013.02.006" @default.
- W2070476076 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3686898" @default.
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