Yigong Shi
Tsinghua University
268 Papers
1.5K Citations
Yigong Shi is an academic researcher from Tsinghua University. The author has contributed to research in topics: Biology & Small nuclear RNA. The author has an hindex of 106, co-authored 248 publications. Previous affiliations of Yigong Shi include Kettering University & Westlake University.
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Papers
Crystal structure of the γ-secretase component nicastrin
Tian Xie,Chuangye Yan,Rui Zhou,Yanyu Zhao,Linfeng Sun,Guanghui Yang,Peilong Lu,Dan Ma,Yigong Shi +8 more
TL;DR: The first atomic-resolution crystal structure of a eukaryotic Nicastrin which shares significant sequence homology with human nicastrin is reported, which reveals the fine details of nicASTrin and allows structure modeling of human nicastsrin and suggests a working model of nicastin function.
A structural basis for mutational inactivation of the tumour suppressor Smad4.
TL;DR: The crystal structure of the C-terminal domain (CTD) of the Smad4/DPC4 tumour suppressor is described, revealing that it forms a crystallographic trimer through a conserved protein–protein interface, to which the majority of the tumour-derived missense mutations map.
Crystal structure of a Smad MH1 domain bound to DNA: insights on DNA binding in TGF-beta signaling.
TL;DR: The Smad family of proteins, which are frequently targeted by tumorigenic mutations in cancer, mediate TGF-beta signaling from cell membrane to nucleus with a conserved 11-residue beta hairpin embedded in the major groove of DNA.
TIPE3 Is the Transfer Protein of Lipid Second Messengers that Promote Cancer
Svetlana Fayngerts,Jianping Wu,Camilla L. Oxley,Xianglan Liu,Anastassios Vourekas,Terry Cathopoulis,Zhaojun Wang,Jian Cui,Suxia Liu,Honghong Sun,Mark A. Lemmon,Lining Zhang,Yigong Shi,Youhai H. Chen +13 more
TL;DR: It is reported here that TIPE3 (TNFAIP8L3) is the transfer protein of phosphoinositide second messengers that promote cancer and its function and metabolism are controlled by a specific transfer protein during tumorigenesis.
Structure of an endogenous yeast 26S proteasome reveals two major conformational states
Bai Luan,Xiuliang Huang,Jianping Wu,Ziqing Mei,Yiwei Wang,Xiaobin Xue,Chuangye Yan,Jiawei Wang,Daniel Finley,Yigong Shi,Feng Wang +10 more
TL;DR: Cryo-EM structures of the endogenous 26S proteasome from Saccharomyces cerevisiae reveal two distinct conformational states, which appear to correspond to different states of ATP hydrolysis and substrate binding, and serve as a molecular basis for mechanistic understanding of proteAsome function.