Yanjing Li
Laboratory of Molecular Biology
6 Papers
1 Citations
Yanjing Li is an academic researcher from Laboratory of Molecular Biology. The author has contributed to research in topics: Methylation & Methyltransferase. The author has an hindex of 4, co-authored 6 publications. Previous affiliations of Yanjing Li include Chinese Academy of Sciences.
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Papers
Author Correction: CRISPR-Cas9-mediated base-editing screening in mice identifies DND1 amino acids that are critical for primordial germ cell development.
Qing Li,Yanjing Li,Suming Yang,Shuo Huang,Meng Yan,Yifu Ding,Wei Tang,Xiwen Lou,Qi Yin,Zhanfei Sun,Lei Lu,Lei Lu,Huijuan Shi,Hongyan Wang,Yong Chen,Jinsong Li,Jinsong Li +16 more
TL;DR: In Fig. 2a of this Technical Report originally published, the authors inadvertently used the same set of images for the 4B 2N1 and 4B2N3 cells when preparing the figure and the three images have now been replaced with the correct versions.
Structural basis for activity regulation of MLL family methyltransferases
Yanjing Li,J. L. Han,J. L. Han,Yuebin Zhang,Fang Cao,Zhijun Liu,Zhijun Liu,Shuai Li,Jian Wu,Jian Wu,Chunyi Hu,Chunyi Hu,Yan Wang,Yan Wang,Jin Shuai,Jin Shuai,Juan Chen,Juan Chen,Liaoran Cao,Dangsheng Li,Pan Shi,Changlin Tian,Changlin Tian,Jian Zhang,Yali Dou,Guohui Li,Yong Chen,Yong Chen,Ming Lei,Ming Lei +29 more
TL;DR: This work shows that a minimized human RBBP5–ASH2L heterodimer is the structural unit that interacts with and activates all MLL family histone methyltransferases, and suggests a universal regulation mechanism for most histonemethyltransferases.
Distinct kinetic mechanisms of H3K4 methylation catalyzed by MLL3 and MLL4 core complexes.
Yongxin Zheng,Yinping Huang,Jun Mencius,Yanjing Li,Lijie Zhao,Lijie Zhao,Wanting Luo,Wanting Luo,Wanting Luo,Yong Chen,Yong Chen,Yong Chen,Shu Quan +12 more
TL;DR: In this article, the authors characterize the kinetic mechanisms of MLL3 and MLL4 ternary complexes containing the catalytic SET domain from MLL 3 or MLL 4 (MLL3SET orMLL4SET), the SPRY domain of ASH2L (ASH2LSPRY), and a short fragment of RBBP5 (RBBP-5AS-ABM) to search for possible explanations.
The internal interaction in RBBP5 regulates assembly and activity of MLL1 methyltransferase complex.
J. L. Han,Tingting Li,Yanjing Li,Muchun Li,Xiaoman Wang,Chao Peng,Chao Peng,Chen Su,Chen Su,Na Li,Yiwen Li,Ying Xu,Yong Chen,Yong Chen +13 more
TL;DR: The structure of human R BBP5 is determined and its role in the assembly and regulation of the MLL1 complex is demonstrated and a vertebrate-specific motif in the C-terminal distal region of RBBP5 contributed to nucleosome recognition and methylation of nucleosomes by the M LL1 complex.
CRISPR-Cas9-mediated base-editing screening in mice identifies DND1 amino acids that are critical for primordial germ cell development.
Qing Li,Yanjing Li,Suming Yang,Shuo Huang,Meng Yan,Yifu Ding,Wei Tang,Xiwen Lou,Qi Yin,Zhanfei Sun,Lei Lu,Lei Lu,Huijuan Shi,Hongyan Wang,Yong Chen,Jinsong Li,Jinsong Li +16 more
TL;DR: An enhanced third-generation base-editing system with extra nuclear localization sequences that can efficiently introduce a homozygous base mutation in embryonic stem cells is reported and a CRISPR–Cas9-based screen strategy that combines base editing and haploid embryonic stem cell technologies to identify amino acids critical for protein function in mice is developed.