@inbook{d5336cacf1e94534a3f98242b3a0cca4,
title = "Biotin switch processing and mass spectrometry analysis of S-nitrosated thioredoxin and its transnitrosation targets",
abstract = "S-Nitrosation is a key posttranslational modification in regulating proteins in both normal physiology and diverse human diseases. To identify novel therapies for human diseases linked to oxidative and nitrosative stress, understanding how cells control S-nitrosation specificity could be critical. Among the enzymes known to control S-nitrosation of proteins, thioredoxin 1 (Trx1), a conserved disulfide reductase, transnitrosates and denitrosates distinct sets of target proteins. To recognize the function of Trx1 in both normal and dysfunctional cells, S-nitrosation targets of Trx1 in different cells need to be identified. However, S-nitrosation is usually too labile to be detected directly by mass spectrometry (MS). Here we present two optimized MS techniques to identify S-nitrosated Trx1 and its transnitrosation targets, using both direct and indirect MS methods.",
keywords = "Mass spectrometry, S-nitrosation, Thioredoxin, Transnitrosation",
author = "Changgong Wu and Tong Liu and Yan Wang and Lin Yan and Chuanlong Cui and Annie Beuve and Hong Li",
note = "Funding Information: This chapter is produced with a grant support from the NIH-National Institute of General Medical Sciences (R01GM112415, to A.B. and H.L.), and the Orbitrap MS described here was purchased with a grant from the NIH-National Institute of Neurological Disorders and Stroke (P30NS046593). Publisher Copyright: {\textcopyright} 2018, Springer Science+Business Media, LLC, part of Springer Nature.",
year = "2018",
doi = "10.1007/978-1-4939-7695-9_20",
language = "English (US)",
series = "Methods in Molecular Biology",
publisher = "Humana Press Inc.",
pages = "253--266",
booktitle = "Methods in Molecular Biology",
}