Junyi Jiang
Beijing Normal University
8 Papers
Junyi Jiang is an academic researcher from Beijing Normal University. The author has contributed to research in topics: Medicine & Biology. The author has an hindex of 3, co-authored 3 publications.
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Papers
Polycomb-like proteins link the PRC2 complex to CpG islands
Haojie Li,Robert Liefke,Junyi Jiang,Jesse V. Kurland,Wei Tian,Pujuan Deng,Weidi Zhang,Qian He,Dinshaw J. Patel,Martha L. Bulyk,Yang Shi,Yang Shi,Zhanxin Wang +12 more
TL;DR: This research provides the first, to the authors' knowledge, direct evidence to demonstrate that PCL proteins are crucial for PRC2 recruitment to CpG islands, and further clarifies the roles of these proteins in transcriptional regulation in vivo.
The SAM domain-containing protein 1 (SAMD1) acts as a repressive chromatin regulator at unmethylated CpG islands.
Bastian Stielow,Yuqiao Zhou,Yinghua Cao,Clara Simon,Hans-Martin Pogoda,Junyi Jiang,Yanpeng Ren,Sabrina K. Phanor,Iris Rohner,Andrea Nist,Thorsten Stiewe,Matthias Hammerschmidt,Yang Shi,Yang Shi,Martha L. Bulyk,Zhanxin Wang,Robert Liefke +16 more
TL;DR: In this article, the authors identify and characterize SAMD1 (SAM domain-containing protein 1) as an unmethylated CpG-binding protein, which has an atypical winged-helix domain that directly recognizes unmethylation CpGs-containing DNA via simultaneous interactions with both the major and minor groove.
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Application of an iPSC‐Derived Organoid Model for Localized Scleroderma Therapy
Jie Ma,Wei Li,Ruiyuan Cao,Dunqin Gao,Qiyu Zhang,Xiao Li,Biyou Li,Luye Lv,Mansheng Li,Junyi Jiang,Yujie Wang,Jun Liu,Zhihong Wu,Yu-Ning Zhu,Wu Zhong,Shuang Zhang,Ling Leng +16 more
TL;DR: According to the findings, the application of EM organoids on scleroderma skin can significantly reduce the degree of skin fibrosis and can provide a new therapeutic alternative for patients suffering from disfigurement and skin function defects caused by LoS.
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Structural Insights into the Distortion of the Ribosomal Small Subunit at Different Magnesium Concentrations
TL;DR: In this article , the structural heterogeneity of E. coli 30S subunits under various Mg2+ concentrations and analyzed their structural distortion by cryo-electron microscopy.
Structural basis of the human negative elongation factor NELF-B/C/E ternary complex.
Yinghua Cao,Yan-Wen Qin,Weidi Zhang,Wei Tian,Yi Ren,Jiahao Ren,Junmeng Wang,Meng Wang,Junyi Jiang,Zhanxin Wang +9 more
TL;DR: This work presents a precise model of the NELF complex, which will facilitate the understanding of its in vivo function, and observed detailed interactions between subunits and identified residues important for the association between NELF-B and Nelf-E.
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