A diagnostic fragment ion in tandem mass spectrometry enables confident protein lactylation assignment and the discovery of broad lysine modification beyond histones.
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References
Ferguson, B. S. et al. Eur. J. Appl. Physiol. 118, 691–728 (2018).
Certo, M., Tsai, C. H., Pucino, V., Ho, P. C. & Mauro, C. Nat. Rev. Immunol. 21, 151–161 (2021).
Zhang, D. et al. Nature 574, 575–580 (2019).
Wan, N. et al. Nat. Methods https://doi.org/10.1038/s41592-022-01523-1 (2022).
Muroski, J. M., Fu, J. Y., Nguyen, H. H., Ogorzalek Loo, R. R. & Loo, J. A. Proteomics 21, e2000111 (2021).
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This project was funded by NIH grant 1RF1AG064250.
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Wu, X., Tao, W.A. Uncovering ubiquitous protein lactylation. Nat Methods 19, 793–794 (2022). https://doi.org/10.1038/s41592-022-01536-w
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DOI: https://doi.org/10.1038/s41592-022-01536-w