Modulation of cellular processes by histone and non-histone protein acetylation
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Molecular Biology
Link
https://www.nature.com/articles/s41580-021-00441-y.pdf
Reference362 articles.
1. Hansen, B. K. et al. Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation. Nat. Commun. 10, 1055 (2019).
2. Zhao, Y. & Garcia, B. A. Comprehensive catalog of currently documented histone modifications. Cold Spring Harb. Perspect. Biol. 7, a025064 (2015).
3. Zhou, T., Chung, Y.-H., Chen, J. & Chen, Y. Site-specific identification of lysine acetylation stoichiometries in mammalian cells. J. Proteome Res. 15, 1103–1113 (2016).
4. Weinert, B. T. et al. Time-resolved analysis reveals rapid dynamics and broad scope of the CBP/p300 acetylome. Cell 174, 231–244.e12 (2018).
5. Weinert, B. T. et al. Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation. Sci. Signal. 4, ra48 (2011).
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