J
Jinrong Min
Researcher at Structural Genomics Consortium
Publications - 166
Citations - 10796
Jinrong Min is an academic researcher from Structural Genomics Consortium. The author has contributed to research in topics: Histone methyltransferase & Tudor domain. The author has an hindex of 47, co-authored 157 publications receiving 9128 citations. Previous affiliations of Jinrong Min include Cold Spring Harbor Laboratory & University of Cambridge.
Papers
More filters
Journal ArticleDOI
Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27
Jinrong Min,Yi Zhang,Rui-Ming Xu +2 more
TL;DR: A 1.4-A-resolution structure of the chromodomain of Polycomb in complex with a hist one H3 peptide trimethylated at Lys 27 reveals a conserved mode of methyl-lysine binding and identifies Polycomb-specific interactions with histone H3, and proposes that self-association is functionally important for Polycomb.
Journal ArticleDOI
Genome-wide Regulation of 5hmC, 5mC, and Gene Expression by Tet1 Hydroxylase in Mouse Embryonic Stem Cells
Yufei Xu,Feizhen Wu,Li Tan,Lingchun Kong,Lijun Xiong,Jie Deng,Andrew J. Barbera,Lijuan Zheng,Haikuo Zhang,Stephen A. Huang,Jinrong Min,Thomas B. Nicholson,Taiping Chen,Guoliang Xu,Yang Shi,Yang Shi,Kun Zhang,Yujiang Geno Shi,Yujiang Geno Shi +18 more
TL;DR: The data suggest that Tet1 controls DNA methylation both by binding to CpG-rich regions to prevent unwanted DNA methyltransferase activity, and by converting 5mC to 5hmC through hydroxylase activity.
Journal ArticleDOI
Structural basis for selective binding of m6A RNA by the YTHDC1 YTH domain
Chao Xu,Xiao Wang,Ke Liu,Ian A Roundtree,Wolfram Tempel,Yanjun Li,Zhike Lu,Chuan He,Chuan He,Jinrong Min +9 more
TL;DR: These structural studies, together with transcriptome-wide identification of YTHDC1-binding sites and biochemical experiments, not only reveal the specific mode of m(6)A-YTH binding but also explain the preferential recognition of the GG(m( 6)A)C)C sequences by YTH DC1.
Journal ArticleDOI
Structure and function of WD40 domain proteins.
Chao Xu,Jinrong Min +1 more
TL;DR: The identification, definition and architecture of the WD40 domains are discussed, and how post-translational modifications are recognized by the large versatile family of WD40 domain proteins are discussed.
Journal ArticleDOI
Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase.
TL;DR: The structure of the catalytic domain of human Dot1, hDOT1L, in complex with S-adenosyl-L-methionine (SAM) reveals a unique organization of a mainly alpha-helical N-terminal domain and a central open alpha/beta structure, an active site consisting of a SAM binding pocket, and a potential lysine binding channel.