Abstract
Oxidative and nitrosative modifications of cysteines are very important posttranslational modifications (PTMs) that can regulate the proper folding and functions of proteins. Given the frequent correlation of oxidative and nitrosative stress with neurodegenerative diseases, it is important to accurately identify redox-sensitive cysteines and their oxidative PTMs. Oxidative PTM levels of specific cysteines are determined by the relative contributions of oxidative and reductive pathways. The actors within these pathways include both small redox molecules and oxidoreductases, such as NADPH oxidases and thioredoxins. In this chapter, we will demonstrate the use of mass spectrometry techniques to identify redox-sensitive nuclear proteins that can be selectively reduced by thioredoxin 1 (Trx1) in neuroblastoma cells. This comprehensive workflow can be applied to the identification of redox-sensitive signaling proteins involved in modulating neurodegenerative diseases.
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Acknowledgements
The chapter described is supported in part by a grant P30NS046593 from the National Institute of Neurological Disorders and Stroke. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institute of Neurological Disorders and Stroke or the National Institutes of Health. The authors report no conflict of interest.
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Jain, M.R., Wu, C., Li, Q., Cui, C., Dai, H., Li, H. (2015). Proteomics Identification of Redox-Sensitive Nuclear Protein Targets of Human Thioredoxin 1 from SHSY-5Y Neuroblastoma Cell Line. In: Grant, J., Li, H. (eds) Analysis of Post-Translational Modifications and Proteolysis in Neuroscience. Neuromethods, vol 114. Humana Press, New York, NY. https://doi.org/10.1007/7657_2015_90
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DOI: https://doi.org/10.1007/7657_2015_90
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