九九九色精品,久久影院午夜高潮,国产精品一区二区三区视频网站

首頁全所PI名錄

人才隊伍

丁建平
研究員，研究組長，博士生導師
E-mail: jpding@@sibcb.ac.cn
實驗室主頁:

個人簡介：

　　1982年1月南京大學獲理學學士學位;1984年10月中山大學獲理學碩士學位;1987年10月復旦大學獲理學博士學位。1987年11月至1989年6月，中國科學院上海硅酸鹽研究所博士后。1989年7月至1991年8月，聯邦德國柏林自由大學結晶學研究所洪堡基金會獎研金學者。1991年9月至2000年10月，美國新澤西州羅格斯大學，先后任化學與化學生物學系研究助理、研究助理教授、研究副教授。2000年11月起，先后任中科院上海生科院生化與細胞所、中科院分子細胞科學卓越創(chuàng)新中心研究員、博士生導師。獲得國家杰出青年基金(2001年)資助，2006年入選國家人事部“新世紀百千萬人才工程”國家級人選。目前主要學術任職包括：“國際生化與分子生物學聯盟”(IUBMB)“學術大會和專題會議委員會”委員(2019年-今);“中國生物化學與分子生物學會”常務理事、副秘書長(2018年-今);“中國生物物理學會”監(jiān)事長(2017年-今);“上海市生物物理學會”常務理事、理事長(2014年-今);“亞洲晶體學會”理事(2006年-今);“中國晶體學會”理事(2003年-今)、“生物大分子專業(yè)委員會” 副主任委員(2012年-今) 等。《IUBMB Life》副主編(2020年-今)、《Acta Biochimica et Biophysica Sinica》主編(2020年-今);《生物化學與生物物理進展》編委(2005年-今);《生命的化學》編委(2006年-今)等。

社會任職：

研究方向：

真核基因表達調控的結構生物學

研究工作：

　　真核生物的基因表達是一個非常復雜的過程，在基因轉錄、mRNA加工和運輸、蛋白質翻譯等層次上受到多種方式的調控，表達調控的異常會導致細胞的非正常生長、發(fā)育和分化，產生多種疾病包括腫瘤。我們研究組主要針對參與染色質修飾、mTOR信號轉導通路和生物代謝通路調控的重要蛋白質和蛋白質復合物，運用結構生物學、分子生物學、生物化學、細胞生物學等方法，開展蛋白質的結構、功能和分子機制的研究。這些研究工作不僅能促進人們對參與真核基因表達調控的一些重要蛋白質的生物功能、分子機理、結構和功能關系的認識，同時也能為探索與這些蛋白質的功能失調相關疾病的發(fā)病機理、尋找疾病診斷的新靶標和新方法、設計和研發(fā)治療疾病的藥物等奠定分子基礎。近年來主持、參與并完成國家、科學院和地方政府的多項重大研究項目。在國際重要學術刊物上發(fā)表研究論文190多篇、近五年來發(fā)表研究論文30多篇，其中包括Science、Sci Advances、Nature、Nature Struct Mol Biol、Nature Med、Nature Cancer、Nature Commun、Mol Cell、Cell Res、Blood、PNAS、EMBO J、EMBO Rep、Cell Rep、Nucleic Acids Res、eLife、Cell Disc、J Biol Chem、Structure、Biochem J、JMCB等。

承擔科研項目情況：

代表論著：

2016年至今發(fā)表的代表性研究論文（*通訊作者）:
1. Wenjing Li^$, Tianlong Zhang^$, Mingliang Sun^$, Yu Shi, Xiao-Jie Zhang, Guo-Liang Xu, and Jianping Ding* “Molecular mechanism for vitamin C-derived C5-glyceryl-methylcytosine DNA modification catalyzed by algal TET homologue CMD1”, Nature Comm., 12:744, doi: 10.1038/s41467-021-21061-2 (2021). Featured article by Editors’ Highlights, Focus: Structural biology, biochemistry and biophysics, Jan 26 (2021).
2. Beibei Wang^$, Tianlong Zhang^$, You Yu, Wenhao Xu, Jianping Ding*, Dinshaw J. Patel*, and Hui Yang* “Structural basis for extended complementarity mediated inhibition in Cas13a systems”, Mol. Cell, doi: 10.1016/j.molcel.2020.12.033 (2021).
3. Jun Yang^$, Hanwen Zhu^$, Tianlong Zhang, and Jianping Ding* “Structure, substrate specificity, and catalytic mechanism of human D-2-hydroxyglutarate dehydrogenase and insights into pathogenicity of diseases associated mutations”, Cell Disc., 7:3, doi: 10.1038/s41421-020-00227-0 (2021).
4. Pengkai Sun, Yan Liu, Tengfei Ma, and Jianping Ding* “Structure and allosteric regulation of human NAD-dependent isocitrate dehydrogenase”, Cell Disc., 6:94, doi: 10.1038/s41421-020-00220-7 (2020).
5. Min Li, Xuxiao He, Weixing Guo, Hongming Yu, Shicheng Zhang, Ningning Wang, Guijun Liu, Rina Sa, Xia Shen, Yabo Jiang, Yufu Tang, Yujuan Zhuo, Chunzhao Yin, Qiaochu Tu, Nan Li, Xiaoqun Nie, Yu Li, Zhimin Hu, Hanwen Zhu, Jianping Ding, Zi Li, Te Liu, Fan Zhang, He Zhou, Shengxian Li, Jiang Yue, Zheng Yan, Shuqun Cheng, Yongzhen Tao & Huiyong Yin* “Aldolase B suppresses hepatocellular carcinogenesis by inhibiting G6PD and pentose phosphate pathways”, Nature Cancer, 1: 735-747, doi: 10.1038/s43018-020-0086-7 (2020).
6. Chunxiao Zhang, Yan Liu, Yifang Zhang, Xiangxiang Wang, Tianlong Zhang*, and Jianping Ding* “Molecular basis for the functions of dominantly active Y35N and inactive D60K Rheb mutants in mTORC1 signaling”, J. Mol. Cell Biol., 12: 741-744, doi:10.1093/jmcb/mjaa025 (2020).
7. Pengkai Sun, Tuya Bai, Tengfei Ma, and Jianping Ding* “Molecular mechanism of the dual regulatory roles of ATP on the ag heterodimer of human NAD-dependent isocitrate dehydrogenase”, Sci. Rep., 10:6225, doi:10.1038/s41598-020-63425-6 (2020).
8. Tianlong Zhang^$, Marie-Pierre Péli-Gulli^$, Zhen Zhang, Xing Tang, Jie Ye, Claudio De Virgilio*, and Jianping Ding* “Structural insights into the EGO-TC-mediated membrane tethering of the TORC1-regulatory Rag GTPases”, Sci. Adv., 8:3146, doi:10.1126/sciadv.aax8164 (2019). (^$Contributed equally)
9. Pengkai Sun, Tengfei Ma, Tianlong Zhang, Hanwen Zhu, Jianyang Zhang, and Jianping Ding* “Molecular basis for the function of the ab heterodimer of human NAD-dependent isocitrate dehydrogenase”, J. Biol. Chem., 294: 16214-16227, doi:10.1074/jbc.RA119.010099 (2019).
10. Wenjing Li, Yu Shi, Tianlong Zhang, Jie Ye, and Jianping Ding* “Structural insights into human N6amt1-Trm112 complex functioning as a protein methyltransferase”, Cell Disc., 5:51, doi:10.1038/s41421-019-0121-y (2019).
11. Hanwen Zhu, Tianlong Zhang, Fang Wang, Jun Yang, and Jianping Ding* “Structural insights into the activation of USP46 by WDR48 and WDR20”, Cell Disc., 5:34, doi:10.1038/s41421-019-0102-1 (2019).
12. Jian-Huang Xue, Guo-Dong Chen, Fuhua Hao, Hui Chen, Zhaoyuan Fang, Fang-Fang Chen, Bo Pang, Qing-Lin Yang, Xinben Wei, Qiang-Qiang Fan, Changpeng Xin, Jiaohong Zhao, Xuan Deng, Bang-An Wang, Xiao-Jie Zhang, Yueying Chu, Hui Tang, Huiyong Yin, Weimin Ma, Luonan Chen, Jianping Ding, Elmar Weinhold, Rahul M Kohli, Wen Liu, Zheng-Jiang Zhu, Kaiyao Huang, Huiru Tang, Guo-Liang Xu* “A vitamin-C-derived DNA modification catalysed by an algal TET homologue”, Nature, 569: 581-585, doi:10.1038/s41586-019-1160-0 (2019).
13. Yabing Liu^$, Lejia Hu, Tengfei Ma^$, Jun Yang, and Jianping Ding* “Insights into the inhibitory mechanisms of NADH on the ag heterodimer of human NAD-dependent isocitrate dehydrogenase”, Sci. Rep., 8:3146, doi:10.1038/s41598-018-21584-7 (2018). (^$Contributed equally)
14. Shicheng Zhang, Linlin Wang, Ye Tao, Tuya Bai, Rong Lu, Tianlong Zhang, Jiangye Chen, and Jianping Ding* “Structural basis for the functional role of the Shu complex inhomologous recombination”, Nucleic Acids Res., 45:13068-13079, doi:10.1093/nar/gkx992 (2017).
15. Tianlong Zhang^$, Rong Wang^$, Zhijing Wang, Xiangxiang Wang, Fang Wang, and Jianping Ding* “Structural basis for Ragulator functioning as a scaffold in membrane-anchoring of Rag GTPases and mTORC1”, Nature Comm., 8: 1394, doi:10.1038/s41467-017-01567-4 (2017).
16. Chen Zhong*, Jinlong Shen, Huibing Zhang, Guangyi Li, Senlin Shen, Fang Wang, Kuan Hu, Longxing Cao, Yongning He, and Jianping Ding* “Cbln1 and Cbln4 are structurally similar but differ in GluD2 binding interactions”, Cell Rep. 20: 2328-2340; doi:10.1016/j.celrep.2017.08.031 (2017).
17. Chen Zhong, Rongfen Huo, Kuan Hu, Jinlong Shen, Dangsheng Li, Ningli Li, and Jianping Ding* “Molecular basis for the recognition of CCN1 by monoclonal antibody 093G9”, J. Mol. Recognit., 30: e2645; doi:10.1002/jmr.2645, Accepted May 10, Epub Jun 13 (2017).
18. Ye Tao^$, Chen Zhong^$, Junjun Zhu, Shutong Xu, and Jianping Ding* “Structural and mechanistic insights into regulation of HBO1 histone acetyltransferase activity by BRPF2”, Nucleic Acids Res., 45: 5707-5719; doi:10.1093/nar/gkx142 (2017).
19. Tengfei Ma, Yingjie Peng, Wei Huang, Yabing Liu, and Jianping Ding* “The b and g subunits play distinct functional roles in the a₂bg heterotetramer of human NAD-dependent isocitrate dehydrogenase”, Sci. Rep., 7: 41882; doi:10.1038/srep41882 (2017).
20. Tengfei Ma, Yingjie Peng, Wei Huang, and Jianping Ding* “Molecular mechanism of the allosteric regulation of the ag heterodimer of human NAD-dependent isocitrate dehydrogenase”, Sci. Rep., 7: 40921; doi:10.1038/srep40921 (2017).
21. Wenshuai Wang^$, Xiaoyu Sun^$, Yanbing Li^$, Jinpeng Su^$, Zhiyang Ling, Tianlong Zhang, Fang Wang, Hong Zhang, Hualan Chen*, Jianping Ding*, and Bing Sun* “Human antibody 3E1 targets the HA stem region of H1N1 and H5N6 influenza A viruses”, Nature Comm., 7: 13577, doi:10.1038/ncomms13577 (2016).
22. Jing Xia^$, Rong Wang^$, Tianlong Zhang*, and Jianping Ding* “Structural insight into the arginine binding specificity of CASTOR1 in amino acid-dependent mTORC1 signaling”, Cell Disc., 2: 16035, doi:10.1038/celldisc.2016.35, Accepted Aug 31, Epub Sep 13 (2016).
23. Rong Wang, Zhijing Wang, Kaikai Wang, Tianlong Zhang*, and Jianping Ding* “Structural basis for targeting BIG1 to Golgi apparatus through interaction of its DCB domain with Arl1”, J. Mol. Cell Biol., 8: 459-461, dio:10.1093/jmcb/mjw033 (2016).

獲獎及榮譽：

研究組成員：

合影