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Faculty

Wei Zhiyi


Associate Professor

Department of Biology

0755-88018411

weizy@sustc.edu.cn

Self-introduction:

Dr. Zhiyi Wei was attracted by the uniqueness of structural biology in understanding biology during his Ph.D. study. After his postdoctoral training at University of Washington, he joined the Hong Kong UST as a Research Assistant Professor. Now, he is an Associate Professor at South University of Science and Technology of China. His current research focus on understanding the protein-mediated interaction and molecular machinery assembly in biological processes, especially in neuronal development and related diseases. From 2009, he has published more than 20 high impact research papers in international journals, including NatureScience, Cell, Molecular Cell, and PNAS.

 

Professional Experience:

◆ 2013 – present, Associate Professor, Department of Biology, South University of Science and Technology of China

◆ 2009 – 2013, Research Associate Professor, Division of Life Science, Hong Kong University of Science and Technology

◆ 2007 – 2009, Research Fellow, School of Medicine, University of Washington

 

Educational Background:

◆ 2007, Ph.D., Biochemistry & Molecular Biology, University of Science and Technology of China

◆ 2002, B.S., Biology, University of Science and Technology of China

 

Honors & Awards:

◆ National 1000 Talent Program for Young Outstanding Scientists, 2015

◆ Oversea High-Caliber Personnel (Level B), Shenzhen Government, 2014

◆ Tin Ka Ping Fellow, Hong Kong University of Science and Technology, 2011-2013

◆ Outstanding Graduate, University of Science and Technology of China, 2007

 

Selected Publication:

(*Co-first Author,#Corresponding Author, for complete publication list, please see http://scholar.google.com/citations?user=Qdh0rU0AAAAJ)

◆Zhao HT, Sheng G, Wang J, Wang M, Bunkoczi G, Gong WM, Wei ZY#, Wang YL#. Crystal structure of the RNA-guided immune surveillance Cascade complex in Escherichia coli. Nature. 515:147-150 (2014)

◆Li YJ*, Wei ZY*, Yan Y, Wan Q, Du QS, Zhang MJ. Structure of Crumbs tail in complex with the PALS1 PDZ-SH3-GK tandem reveals a highly specific assembly mechanism for the apical Crumbs complex. Proc Natl Acad Sci USA. 111:17444-17449. (2014)

◆Wang C*, Wei ZY*, Chen KY, Ye F, Yu C, Bennett V, Zhang MJ. Structural basis of diverse membrane target recognitions by ankyrins. Elife. 3. (2014)

◆Wei ZY#, Liu XT, Yu C, Zhang MJ#. Structural basis of cargo recognitions for class V myosins. Proc Natl Acad Sci USA.110: 11314-11319. (2013)

◆Wang C, Yu C, Ye F, Wei ZY#, Zhang MJ#. Structure of the ZU5-ZU5-UPA-DD tandem of ankyrin-B reveals interaction surfaces necessary for ankyrin function. Proc Natl Acad Sci USA. 109:4822-4827 (2012)

◆Wei ZY, Zheng SL, Spangler SA, Yu C, Hoogenraad C, Zhang MJ. Liprin-mediated large signaling complex organization revealed by the liprin-α/CASK and liprin-α/liprin-β complex structures. Mol Cell. 43:586-598 (2011)

◆Wei ZY, Yan J, Lu Q, Pan LF, Zhang MJ. Cargo Recognition Mechanism of Myosin X Revealed by the Structure of its Tail MyTH4-FERM Tandem in Complex with the DCC P3 Domain. Proc Natl Acad Sci USA. 108:3572-3577 (2011)

◆Wu L, Pan LF, Wei ZY, Zhang MJ. Structure of MyTH4-FERM domains in myosin VIIa tail bound to cargo. Science. 331:757-60 (2011)

◆Liu W, Wen WY, Wei ZY, Yu J, Ye F, Liu CH, Hardie RC, Zhang MJ. The INAD scaffold is a dynamic, redox-regulated modulator of signaling in the Drosophila eye. Cell. 145:1088-1101 (2011)

◆Cheng ZH, Biechele T, Wei ZY, Morrone S, Moon RT, Wang LG, Xu WQ. Crystal structures of the extracellular domain of LRP6 and its complex with DKK1. Nat Struct Mol Biol. 18:1204-1210 (2011)

◆Wang R*, Wei ZY*, Jin H, Wu H, Yu C, Wen W, Chan LN, Wen ZL, Zhang MJ. Autoinhibition of UNC5b revealed by the cytoplasmic domain structure of the receptor. Mol Cell. 27: 692-703 (2009)

◆Yu C, Feng W, Wei ZY, Miyanoiri Y, Zhao YX, Zhang MJ. Myosin VI Undergoes Cargo-Mediated Dimerization. Cell. 138: 537-548 (2009)

 

Other Info:

◆ Research assistant and postdoctoral positions are open for application

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