Mingzhu Wang
Chinese Academy of Sciences
25 Papers
38 Citations
Mingzhu Wang is an academic researcher from Chinese Academy of Sciences. The author has contributed to research in topics: Nucleosome & Histone H3. The author has an hindex of 17, co-authored 21 publications.
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Papers
Cryo-em study of the chromatin fiber reveals a double helix twisted by tetranucleosomal units
Feng Song,Ping Chen,Dapeng Sun,Mingzhu Wang,Liping Dong,Dan Liang,Rui-Ming Xu,Ping Zhu,Guohong Li +8 more
TL;DR: The 11-angstrom–resolution cryogenic electron microscopy (cryo-EM) structures of 30-nanometer chromatin fibers reconstituted in the presence of linker histone H1 and with different nucleosome repeat lengths provide mechanistic insights into how nucleosomes compact into higher-order Chromatin fibers.
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Structural basis for allosteric, substrate-dependent stimulation of SIRT1 activity by resveratrol
TL;DR: The structure of SIRT1 is solved in complex with resveratrol and a 7-amino-4-methylcoumarin (AMC)-containing peptide and reveals the presence of three resver atrol molecules, two of which mediate the interaction between the AMC peptides and the NTD of Sirt1.
215
Structural insights into protein arginine symmetric dimethylation by PRMT5
TL;DR: It is discovered that a conserved phenylalanine in the active site is critical for specifying symmetric addition of methyl groups, which implies a potentially regulatable outcome of arginine dimethylation that may provide versatile control of eukaryotic gene expression.
153
Structural Basis for Hydroxymethylcytosine Recognition by the SRA Domain of UHRF2
TL;DR: The structure of UHRF2-SRA in complex with a 5hmC-containing DNA reveals that the conformation of a phenylalanine allows the formation of an optimal5hmC binding pocket, and a hydrogen bond between the hydroxyl group of 5hm C and UHRf2- SRA is critical for their preferential binding.
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Nα-acetylated Sir3 stabilizes the conformation of a nucleosome-binding loop in the BAH domain
Dongxue Yang,Qianglin Fang,Mingzhu Wang,Ren Ren,Hong Wang,Meng He,Youwei Sun,Na Yang,Rui-Ming Xu +8 more
TL;DR: X-ray crystallography is shown to show that the acetylated N terminus of Sir3 does not interact with the nucleosome directly, but instead stabilizes a nucleosomesome-binding loop in the BAH domain.
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