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- W3168604519 endingPage "1155" @default.
- W3168604519 startingPage "1134" @default.
- W3168604519 abstract "Significance: Oxidative stress is a characteristic of many systemic diseases associated with thrombosis. Thiol isomerases are a family of oxidoreductases important in protein folding and are exquisitely sensitive to the redox environment. They are essential for thrombus formation and represent a previously unrecognized layer of control of the thrombotic process. Yet, the mechanisms by which thiol isomerases function in thrombus formation are unknown. Recent Advances: The oxidoreductase activity of thiol isomerases in thrombus formation is controlled by the redox environment via oxidative changes to active site cysteines. Specific alterations can now be detected owing to advances in the chemical biology of oxidative cysteine modifications. Critical Issues: Understanding of the role of thiol isomerases in thrombus formation has focused largely on identifying single disulfide bond modifications in isolated proteins (e.g., αIIbβ3, tissue factor, vitronectin, or glycoprotein Ibα [GPIbα]). An alternative approach is to conceptualize thiol isomerases as effectors in redox signaling pathways that control thrombotic potential by modifying substrate networks. Future Directions: Cysteine-based chemical biology will be employed to study thiol-dependent dynamics mediated by the redox state of thiol isomerases at the systems level. This approach could identify thiol isomerase-dependent modifications of the disulfide landscape that are prothrombotic." @default.
- W3168604519 created "2021-06-22" @default.
- W3168604519 creator A5028221234 @default.
- W3168604519 creator A5054730000 @default.
- W3168604519 date "2021-11-01" @default.
- W3168604519 modified "2023-10-16" @default.
- W3168604519 title "Oxidative Cysteine Modification of Thiol Isomerases in Thrombotic Disease: A Hypothesis" @default.
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