施一公

个人简介

       施一公教授,1967年生于河南郑州,1989年提前一年毕业于清华大学生物科学与技术系,1995年获美国约翰霍普金斯大学生物物理专业博士学位,1998年开始任教于美国普林斯顿大学分子生物学系,2003年破格晋升为终身正教授,2007年成为终身讲席教授,是该系历史上最年轻的终身教授和终身讲席教授。施一公教授从2005至2008年担任华人生物学家协会(Chinese Biological Investigators Society)主席。胸怀一颗拳拳报国心,2008年施一公教授回到清华大学开始全职工作,婉拒了霍华德休斯研究员的优厚待遇,并于同年辞去普林斯顿大学终身教职。施一公教授的研究内容主要是运用分子生物学手段研究肿瘤发生和细胞凋亡的分子机理,其研究成果所获国际专利中的一项已开始针对癌症晚期患者的临床试验。在回国短短两年半的时间里,他带领着博士研究生在国际前沿基础研究领域做出了一系列重大研究成果,以通讯作者在世界顶尖学术期刊《科学》、《自然》和《细胞》上发表了5篇论文,他领导下的清华大学结构生物学中心已经成为世界瞩目的一流研究中心。施一公教授的研究工作得到国际同行广泛认可,2003年被国际蛋白质学会授予鄂文西格青年科学家奖,成为二十年来唯一获此殊荣的华裔学者。2009年,施一公教授入选美国科协(AAAS)Fellow。2010年4月,施一公教授荣获赛克勒国际生物物理学奖。

主要论著

Programmed cell death (apoptosis):

 

1. Shiqian Qi, Yuxun Pang, Qi Hu, Qun Liu, Hua Li, Yulian Zhou, Tianxi He, Qionglin Liang, Yexing Liu,   Xiaoqiu Yuan, Guoan Luo, Huilin Li, Jiawei Wang, Nieng Yan, and Yigong Shi (2010). Crystal structure of the Caenorhabditis elegans apoptosome reveals an octameric assembly of CED-4.Cell 141, 446-457.

2. Qing Bao, Wenyun Lu, Joshua D. Rabinowitz, and Yigong Shi (2007). Calcium blocks formation of apoptosome by blocking nucleotide exchange in Apaf-1.  Mol. Cell 25, 181–191.

3. Nieng Yan, Jijie Chai, Eui Seung Lee, Lichuan Gu, Qun Liu, Jiaqing He, Jia-Wei Wu, David Kokel, Huilin Li, Quan Hao, Ding Xue, and Yigong Shi (2005). Structure of the CED-4/CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans. Nature 437, 831–837.

4. Stefan J. Riedl, Wenyu Li, Yang Chao, Robert Schwarzenbacher, and Yigong Shi (2005). Structure of the apoptotic protease activating factor 1 (Apaf-1) bound to ADP.  Nature 434, 926–933.

5. Nieng Yan, Lichuan Gu, David Kokel, Jijie Chai, Wenyu Li, Aidong Han, Lin Chen, Ding Xue, and Yigong Shi (2004). Structural, Biochemical and Functional Analyses of CED-9 Recognition by the Pro-apoptotic Proteins EGL-1 and CED-4.  Mol. Cell 15, 999–1006.

6. Nieng Yan, Jia-Wei Wu, Jun R. Huh, Jijie Chai, Wenyu Li, Bruce A. Hay, and Yigong Shi (2004). Molecular mechanisms of DrICE inhibition by DIAP1 and removal of inhibition by Reaper, Hid, and Grim. Nature-Structural & Molecular Biology 11 (5), 420–428.

7. Jijie Chai, Nieng Yan, Jun R. Huh, Jia-Wei Wu, Wenyu Li, Bruce A. Hay, and Yigong Shi (2003). Molecular mechanism of Reaper/Grim/Hid-mediated suppression of DIAP1-dependent Dronc ubiquitination. Nature-Structural Biology 10, 892-898.

8. Eric N. Shiozaki, Jijie Chai, Daniel J. Rigotti, Stefan J. Riedl, Pingwei Li, Srinivasa M. Srinivasula, Emad S. Alnemri, Robert Fairman, and Yigong  Shi (2003). Mechanism of XIAP-mediated Inhibition of Caspase-9. Mol. Cell 11, 519-527.

9. Jijie Chai Qi Wu, Eric Shiozaki, Srinivasa M. Srinivasula, Emad S. Alnemri, and Yigong  Shi (2001). Crystal Structure of a Caspase Zymogen: Mechanisms of Activation and Substrate Binding. Cell  107, 399-407.

10. Jijie Chai, Eric Shiozaki, Srinivasa M. Srinivasula, Qi Wu, Pinaki Datta, Emad S. Alnemri, and Yigong Shi (2001).  Structural Basis of Caspase-7 Inhibition by XIAP. Cell 104, 769-780.

11. Geng Wu, Jijie Chai, Tomeka Suber, Jia-Wei Wu, Chunying Du, Xiaodong Wang, and Yigong Shi (2000).  Structural Basis of IAP Recognition by Smac/DIABLO. Nature408, 1008-1012.

12. Jijie Chai, Chunying Du, Jia-Wei Wu, Saw Kyin, Xiaodong Wang, and Yigong Shi (2000).  Structural and Biochemical Basis of Apoptotic Activation by Smac/DIABLO. Nature  406, 855-862.

13. Hongxu Qin, Srinivasa M. Srinivasula, Geng Wu, Emad S. Alnemri, Yigong Shi (1999). Structural Basis of Procaspase-9 Recruitment by the Apoptotic Protease Activating Factor 1. Nature  399, 549-557.

 

SMAD proteins in TGF-bsignaling:

 

1. Yigong Shi and Joan Massagué (2003).  Mechanisms of TGF-bsignaling from Cell Membrane to the Nucleus. Cell 113, 685-700.

2. Jia-Wei Wu, Ariel R. Krawitz, Jijie Chai, Wenyu Li, Fangjiu Zhang, Kunxin Luo, and Yigong Shi (2002).  Structural Mechanism of Smad4 Recognition by the Nuclear Oncoprotein Ski: Insight on Ski-Mediated Repression of TGF-bSignaling.  Cell 111, 357-367.

3. Jia-Wei Wu, Min Hu, Jijie Chai, Morgan Huse, Carey Li, Saw Kyin, Robert Fairman, Tom Muir, Joan Massagué, and Yigong Shi (2001).  Crystal Structure of a Phosphorylated Smad2: Recognition of Phosphoserine Motif and Insights on Smad Function in TGF-bSignaling.  Mol. Cell  8, 1277-1289.

4. Geng Wu, Ye-Guang Chen, Barish Ozdamar, Cassie Gyuricza, P. Andrew Chong, Jeffrey L. Wrana, Joan Massagué, and Yigong Shi (2000).  Structural Basis of Smad2 Recruitment by the Smad Anchor for Receptor Activation (SARA).  Science  287, 92-97.

5. Yigong Shi, Yan-Fei Wang, Lata Jayaraman, Haijuan Yang, Joan Massagué, and Nikola Pavletich (1998).  Crystal Structure of A Smad MH1 Domain Bound to DNA: Insights on DNA-binding in TGF-bSignaling.  Cell, 94, 585-594.

 

Protein phosphatase 2A (PP2A):

 

1. Yigong Shi (2009). Structure and Mechanism of Protein Serine/Threonine Phosphatases. Cell 139, 468-484.

2. Yongna Xing, Zhu Li, Yu Chen, Philip D. Jeffery, and Yigong Shi (2008). Structural Mechnism of Demethylation and Inaction of Protein Phosphatase 2A.  Cell 133, 154-163.

3. Yu Chen, Yanhui Xu, Qing Bao, Yongna Xing, Zhu Li, Zheng Lin, Jeffry Stock, Philip P. Jeffrey, Yigong Shi (2007) Structural and biochemical insights into the regulation of protein phosphatase 2Aby small t antigen of SV40. Nature Struct Mol Biol. 14(6), 527-34. Epub 2007 May 27.

4. Yanhui Xu, Xing Yongna, Yu Chen, Yang Chao, Zheng Lin, Eugene Fan, Jong W. Yu, Stefan Strack, Philip D. Jeffrey, and Yigong Shi (2006). Structure of the Protein Phosphatase 2AHoloenzyme.  Cell 127, 1239–1251.

5. Xing Yongna, Yanhui Xu, Yu Chen, Philip D. Jeffrey, Yang Chao, Zheng Lin, Zhu Li, Stefan Strack, Jeffry B Stock, and Yigong Shi (2006). Structure of Protein Phosphatase 2ABound to Tumor-inducing Toxins.  Cell 127, 341-352.

6. Yang Chao, Yongna Xing, Yu Chen, Yanhui Xu, Zheng Lin, Zhu Li, Philip D. Jeffrey, Jeffry B. Stock and Yigong Shi (2006).  Structure and Mechanism of the Phosphotyrosyl Phosphatase Activator.  Mol. Cell 23, 535-546.

 

Membrane protein structure and function:

 

1. Xiang Gao, Lijun Zhou, Xuyao Jiao, Feiran Lu, Chuangye Yan, Xin Zeng, Jiawei Wang, and Yigong Shi (2010). Mechanism of substrate recognition and transport by an amino acid antiporter. Nature 463, 828-832.  Epub 2010 Jan 20.

2. Yi Wang, Yongjian Huang, Jiawei Wang, Chao Cheng, Weijiao Huang, Peilong Lu, Ya-Nan Xu, Pengye Wang, Nieng Yan, and Yigong Shi (2009). Structure of the formate transporter FocA reveals a pentameric aquaporin-like channel.  Nature 462, 467-472.

3. Xiaochun Li, Boyuan Wang, Lihui Feng, Hui Kang, Yang Qi, Jiawei Wang, and Yigong Shi (2009). Cleavage of RseA by RseP requires a carboxyl-terminal hydrophobic amino acid following DegS cleavage. Proc. Natl. Acad. Sci. USA  106, 14837-42[Epub 2009 August 18].

4. Xiang Gao, Feiran Lu, Lijun Zhou, Shangyu Dang, Linfeng Sun, Xiaochun Li, Jiawei Wang, and Yigong Shi (2009). Structure and Mechanism of an Amino Acid Antiporter.Science 324, 1565-1568. Epub 2009 May 28.

5. Liang Feng, Hanchi Yan, Zhuoru Wu, Nieng Yan, Zhe Wang, Philip D. Jeffrey, and Yigong Shi (2007). Structure of a Site-2 Protease Family Intramembrane Metalloprotease.   Science 318, 1608-1612.

6. Zhuoru Wu, Nieng Yan, Liang Feng, Adam Oberstein, Hanchi Yan, Rosanna P. Baker, Lichuan Gu, Philip D. Jeffrey, Sinisa Urban, and Yigong Shi (2006). Structural analysis of a rhomboid family intramembrane protease reveals a gating mechanism for substrate entry. Nature Structural & Molecular Biology13, 1084-1091. 2006 Nov 10; [Epub ahead of print].

 

Protein degradation and quality control:

 

1. Fan Zhang , Zhuoru Wu, Ping Zhang, Geng Tian, Daniel Finley, and Yigong Shi (2009). Mechanism of substrate unfolding and translocation by the regulatory particle of the proteasome from Methanocaldococcus jannaschii.Mol Cell 34, 485-496.

2. Fan Zhang , Min Hu, Geng Tian, Ping Zhang, Daniel Finley, Philip D. Jeffrey, and Yigong Shi (2009). Structural insights into the regulatory particle of the proteasome from Methanocaldococcus jannaschii.Mol Cell 34, 473-484.

3. Min Hu, Pingwei Li, Muyang Li, Wenyu Li, Tingting Yao, Jia-Wei Wu, Wei Gu, Robert E. Cohen, and Yigong Shi (2002). Crystal Structure of a UBP-family Deubiquitinating Enzyme in Isolation and in Complex with Ubiquitin Aldehyde. Cell 111, 1041-1054.

Copyright © 2013 Qiu Shi Science and Technologies Foundation. All rights reserved.

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