移动站  | 2017年09月25日 星期一
用户登录

当前位置:首页 >> 师资队伍

基本信息:

姓名: 张兴
职务: 冷冻电镜中心主任
职称: 教授
学历: 博士
专业: 结构生物学
所属院系: 基础医学系
研究方向: 冷冻电镜、生物大分子结构
电话: 0571-88981963
信箱: xzhang1999@zju.edu.cn
个人主页:

个人简介:

 

张兴,美国普度(Purdue)大学结构生物学专业博士,长期致力于使用冷冻电镜技术研究生物大分子的结构及其组装机制,并提高单颗粒冷冻电镜的三维重构分辨率,最终在2010年间对单颗粒冷冻电镜技术的发展做出了里程碑式的贡献:首次使用单颗粒冷冻电镜技术重构出生物大分子的原子结构 (Cell, 2010, V.141, p472-482),从而确定了单颗粒冷冻电镜作为第三种可以重构生物大分子原子结构的技术,与X-射线晶体学及核磁共振技术并列。共发表SCI论文22篇,他引总数为665。其中10篇为第一作者,最高单篇他引为120 (Cell, 2010, V.141, p472-482)。发表的期刊包括《Nature》、 《Cell》、 《Nature Structural & Molecular Biology》、 《PNAS》等。其中有多篇第一作者文章被Faculty1000推荐,主要发现和结论被Nature Review Microbiology和PNAS等国际著名杂志专文评述或评为研究亮点。2016年2月回国,现任浙江大学冷冻电镜中心主任、教授和博士生导师。
 
学习和研究经历
 
19899月-19936    四川大学本科/理学学士
1993年9月-1996年6月    中科院北京电镜实验室 硕士研究生 
1999年9月-2005年6月    美国普度(Purdue)大学 博士研究生 
1996年7月-1999年7月    中科院北京电镜实验室 研究助理
2005年6月-2007年11月   美国布兰戴斯大学休斯医学研究所(HHMI) 博士后    
2007年11月-2010年9月   美国加州大学洛杉矶分校加州纳米研究所 博士后
2010年10月-2016年2月   加州大学洛杉矶分校加州纳米研究所电镜中心技术主任
2016年2月-现在          浙江大学医学院 教授、博士生导师
 
主要科研领域:
冷冻电子显微学研究生物大分子复合体的结构与功能。
 
主要研究方向如下:
1.核糖体的结构和功能
2.双链RNA病毒的感染、复制和组装机理
3.电子光学理论研究及冷冻电子显微学结构解析方法的开发
 
代表性文章:
Zhang X, Ke D, Yu X, Chang W, Sun J, Zhou H. In situ structures of the segmented genome and RNA polymerase complex inside a dsRNA virus. Nature. 2015, 527(7579): 531–534.
Zhang X, Jin, L, Fang, Q, Hui, W, Zhou, Z.H. 3.3 Å Cryo-EM Structure of a Nonenveloped Virus Reveals a Priming Mechanism for Cell Entry, Cell. 2010,141(3): 472-482. (featured on cover and PaperFlick video)
Zhang X, Patel A, Celma C, Yu X, Roy P, Zhou H. Atomic model of a nonenveloped virus reveals pH sensors for a coordinated process of cell entry. Nature Structural & molecular Biology. 2016, 23(1): 74-80.
Zhang X, Boyce M, Bhattacharya B, Zhang X, Schein S, Roy P, Zhou ZH. Bluetongue virus coat protein VP2 contains sialic acid-binding domains, and VP5 resembles enveloped virus fusion proteins. PNAS. 2010, 107(14): 6292-6297.
Zhang X, Settembre E, Xu C, Dormitzer PR, Bellamy R, Harrison SC, and Grigorieff N. Near-atomic resolution using electron cryomicroscopy and single-particle reconstruction. PNAS.2008, 105(6): 1867-1872.
 
其他发表论文:
Zhang X, Guo H, Jin L, Czornyj E, Hodes A, Hui WH, Nieh AW, Miller JF, and Zhou ZH. A new topology of the HK97-like fold revealed in Bordetella bacteriophage by cryoEM at 3.5Å resolution. eLife. 2013, 2:e01299.
Zhang X, and Zhou ZH. Limiting factors in atomic resolution cryo electron microscopy – No simple tricks. J. Struct. Biol. 2011, 175: 253-263.
Zhang X, Ji Y, Zhang L, Harrison SC, Marinescu DC, Nibert ML, Baker TS. Features of Reovirus Outer Capsid Protein m1 Revealed by Electron Cryomicroscopy and Image Reconstruction of the virion at 7.0-Å Resolution. Structure.2005, 13(10): 1545-1557.
Zhang X, Tang J, Walker SB,Hara D, Nibert ML, Duncan R, and Baker TS. Structure of Avian Orthoreovirus Virion by Electron Cryomicroscopy and Image Reconstruction. Virology. 2005, 343: 25-35.
Zhang X, Walker SB, Chipman PR, Nibert ML, Baker TS. Reovirus polymerase lambda 3 localized by cryo-electron microscopy of virions at a resolution of 7.6 Å. Nature Structural Biology. 2003, 10(12): 1011-8.
Yan X, Cardone G, Zhang X, Zhou ZH, and Baker TS. Single particle analysis integrated with microscopy: A high-throughput approach for reconstructing icosahedral particles. Journal of structural biology. 2014, 186(1): 8-18.
Mrazek J, Toso D, Ryazantsev S, Zhang X, Zhou ZH, Fernandez BC, Kickhoefer VA, and Rome LH. Polyribosomes Are Molecular 3D Nanoprinters That Orchestrate the Assembly of Vault Particles. ACS nano. 2014, 8(11): 1552-9.
Estrozi LF, Settembre EC, Goret G, McClain B, Zhang X, Chen JZ, Grigorieff N, Harrison SC. Location of the dsRNA-dependent polymerase, VP1, in rotavirus particles. J Mol Biol. 2013,425:124-132.
Zhang X, Zhang X, Zhou ZH. Low cost, high Performance hybrid GPU-CPU solution for atomic resolution CryoEM single-particle reconstruction. J.Struct. Biol. 2010, 172: 400-406.
Chen J, Settembre E, Aoki S, Zhang X, Bellamy A, Dormitzer P, Harrison S, Grigorieff N. Molecular interactions in rotavirus assembly and uncoating seen by high-resolution cryo-EM. PNAS. 2009, 106(26): 10644-10648.
Ji Y, Marinescu DC, Zhang W, Zhang X, Yan X, and Baker TS. A model-based parallel origin and orientation refinement algorithm for cryoTEM and its application to the study of virus structures. Journal of structural biology. 2006, 154(1): 1-9.
Kong Y, Zhang X, Baker TS. & Ma J. A Structural-informatics Approach for Tracing β-Sheets: Building Pseudo-Cα Traces for β-Strands in Intermediate-resolution Density Maps. Journal of molecular biology. 2004, 339: 117-130.
Odegard A, Chandran K, Zhang X, Parker JS, Baker TS, Nibert ML. Putative autocleavage of outer capsid protein m1, allowing release of myristoylated peptide m1N during particle uncoating, is critical for cell entry by reovirus. J. Virology. 2004, 78(16): 8732-45.
Bowman VD, Chase ES, Franz AW, Chipman PR, Zhang X, Perry KL, Baker TS, Smith TJ. An antibody to the putative aphid recognition site on cucumber mosaic virus recognizes pentons but not hexons, J. Virol. 2002, 76(23): 12250-8.
Kim J, Zhang X, Centonze VE, Bowman VD, Noble S, Baker TS, Nibert ML. The hydrophilic amino-terminal arm of reovirus core shell protein lambda1 is dispensable for particle assembly. J. Virol. 2002, 76(23): 12211-22.
Luongo CL, Zhang X, Walker SB, Chen Y, Broering TJ, Farsetta DL, Bowman VD, Baker TS, Nibert ML. Loss of activities for mRNA synthesis accompanies loss of lambda2 spikes from reovirus cores: an effect of lambda2 on lambda1 shell structure. Virology. 2002, 296(1): 24-38.
Chandran K, Zhang X, Olson NH, Walker SB, Chappell JD, Dermody TS, Baker TS, and Nibert ML. Complete in vitro assembly of the reovirus outer capsid produces highly infectious particles suitable for genetic studies of the receptor-binding protein. Journal of virology. 2001, 75(11): 5335-5342.