Chemically synthesized histone H2A Lys13 di-ubiquitination promotes binding of 53BP1 to nucleosomes.

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第一作者： Jia-Bin,Li

第一单位： Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, China.

作者： Jia-Bin,Li ^[1] ; Yun-Kun,Qi ^[2] ; Qiao-Qiao,He ^[3] ; Hua-Song,Ai ^[3] ; San-Ling,Liu ^[1] ; Jia-Xing,Wang ^[3] ; Ji-Shen,Zheng ^[1] ; Lei,Liu ^[3] ; Changlin,Tian ^[1]

作者单位： Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, China. ^[1] Tsinghua-Peking Center for Life Sciences, Department of Chemistry, Tsinghua University, Beijing 100084, China.;School of Pharmacy, Qingdao University, Qingdao, Shandong 266021, China. ^[2] Tsinghua-Peking Center for Life Sciences, Department of Chemistry, Tsinghua University, Beijing 100084, China. ^[3]

DOI 10.1038/cr.2018.6

PMID 29508853

发布时间 2020-05-11

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Cell research

2018年28卷2期

262页

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Chemically synthesized histone H2A Lys13 di-ubiquitination promotes binding of 53BP1 to nucleosomes.

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Chemically synthesized histone H2A Lys13 di-ubiquitination promotes binding of 53BP1 to nucleosomes.

Cell research

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