A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/nature03714.pdf
Reference21 articles.
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2. Kuo, M. H. et al. Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines. Nature 383, 269–272 (1996)
3. Sklenar, A. R. & Parthun, M. R. Characterization of yeast histone H3-specific type B histone acetyltransferases identifies an ADA2-independent Gcn5p activity. BMC Biochem. 5, 1–12 (2004)
4. Ye, J. et al. Histone H4 lysine 91 acetylation: A core domain modification associated with chromatin assembly. Mol. Cell 18, 123–130 (2005)
5. Verreault, A., Kaufman, P. D., Kobayashi, R. & Stillman, B. Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4. Cell 87, 95–104 (1996)
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