Acetylation of histone H4 by Esa1 is required for DNA double-strand break repair
By A. Bird, David Y. Yu, Marilyn G. Pray-Grant, Qifeng Qiu, Kirsty E. Harmon, P. Megee, P. Grant, M. Smith, M. Christman. Nature, 2002
613 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/1064384f45e0c172f009d1dfbf9247e1d0ed678b
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Citations in the corpus
- RNA meets chromatin. (2005, background): “2000), and Esa1, a major essential histone H4 acetyltransferase in Saccharomyces cerevisiae with known functions in transcriptional control as well as DNA repair (Bird et al. 2002).”
- Surviving the breakup: the DNA damage checkpoint. (2006, background): “A major role for γ-H2AX is the recruitment of chromatin remodelers, including the Ino80, Rvb1, NuA4, and Swr1 complexes to the DSB (12, 17, 35, 97, 110, 147).”
- Structural and Functional Conservation of the NuA4 Histone Acetyltransferase Complex from Yeast to Humans (2004, methodology): “for nucleosomal HAT activity, full-length Tip60, Tip60b, ING3, ING3(1-300),”
- Histone acetylation and deacetylation in yeast (2003, neutral): “and causes marked sensitivity to double-strand breaks (DSBs), but not to other forms of DNA damag”
- A Protein Complex Containing the Conserved Swi2/Snf2-Related ATPase Swr1p Deposits Histone Variant H2A.Z into Euchromatin (2004, background): “While NuA4’s involvement in DNA damage survival was known (Bird et al. 2002; Choy and Kron 2002; Boudreault et al. 2003), the data presented here extended this view, suggesting that it might be more broadly required in the maintenance of genomic integrity in concert with SWR1Com.”
- Histone acetyltransferase complexes: one size doesn't fit all (2007, background): “Originally, Esa1, the catalytic subunit of NuA4, was shown to be required for DSB repai”
- Chromatin challenges during DNA replication and repair. (2007, neutral): “…INO80 and SWR1 chromatin-remodeling complexes, likely in conjunction with the NuA4 HAT, all of which are recruited to the break partly through their binding to g -H2AX itself (Bird et al., 2002; Downs et al., 2004; Morrison et al., 2004; Papamichos-Chronakis et al., 2006; van Attikum et al., 2004).”