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Chemically synthesized histone H2A Lys13 di-ubiquitination promotes binding of 53BP1 to nucleosomes
by
Jia-Bin Li;Yun-Kun Qi;Qiao-Qiao He;Hua-Song Ai;San-ling Liu;Jia-Xing Wang;Ji-Shen Zheng;Lei Liu;Changlin Tian
in
H2A;化学;绑定;p53;蛋白质;约束力;DNA;管理者
/ Histone H2A
/ Nucleosomes
/ Ubiquitination
2018
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Chemically synthesized histone H2A Lys13 di-ubiquitination promotes binding of 53BP1 to nucleosomes
by
Jia-Bin Li;Yun-Kun Qi;Qiao-Qiao He;Hua-Song Ai;San-ling Liu;Jia-Xing Wang;Ji-Shen Zheng;Lei Liu;Changlin Tian
in
H2A;化学;绑定;p53;蛋白质;约束力;DNA;管理者
/ Histone H2A
/ Nucleosomes
/ Ubiquitination
2018
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Chemically synthesized histone H2A Lys13 di-ubiquitination promotes binding of 53BP1 to nucleosomes
Journal Article
Chemically synthesized histone H2A Lys13 di-ubiquitination promotes binding of 53BP1 to nucleosomes
2018
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Overview
Dear Editor,
p53-binding protein 1 (53BP1) is a critical regulator of cellular response to DNA double-strand breaks (DSBs) . To accomplish its repair function, 53BP1 must be recruited to the chromatin surrounding DSB sites that carry H4 methylation at Lys20 and H2A ubiquitination at Lys15 .
Publisher
Nature Publishing Group
Subject
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