Proteome-wide detection of S-nitrosylation targets and motifs using bioorthogonal cleavable-linker-based enrichment and switch technique
Reversible cysteine modifications play important roles in cellular redox signaling. Here, the authors develop a chemical proteomics strategy that enables the quantitative analysis of endogenous cysteine nitrosylation sites and their dynamic regulation under nitrosative stress conditions.
Main Authors: | Ruzanna Mnatsakanyan, Stavroula Markoutsa, Kim Walbrunn, Andreas Roos, Steven H. L. Verhelst, René P. Zahedi |
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Format: | Article |
Language: | English |
Published: |
Nature Publishing Group
2019-05-01
|
Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-019-10182-4 |
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