首页 全所PI名录
  • 丁建平
  • 研究员,研究组长,博士生导师
  • E-mail: jpding@@sibcb.ac.cn
  • 实验室主页: 
    个人简介:
  •   1982年1月南京大学获理学学士学位;1984年10月中山大学获理学硕士学位;1987年10月复旦大学获理学博士学位。1987年11月至1989年6月,中国科学院上海硅酸盐研究所博士后。1989年7月至1991年8月,联邦德国柏林自由大学结晶学研究所洪堡基金会奖研金学者。1991年9月至2000年10月,美国新泽西州罗格斯大学,先后任化学与化学生物学系研究助理、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与细胞所、中科院分子细胞科学卓越创新中心研究员、博士生导师。获得中科院“百人计划”(2000年)和国家杰出青年基金(2001年)资助,2006年入选国家人事部“新世纪百千万人才工程”国家级人选。目前主要学术任职包括:“国际生化与分子生物学联盟”(IUBMB)“学术大会和专题会议委员会”委员(2019年-今);“中国生物化学与分子生物学会”常务理事、副秘书长(2018年-今);“中国生物物理学会”监事长(2017年-今);“上海市生物物理学会”常务理事、理事长(2014年-今);“亚洲晶体学会”理事(2006年-今);“中国晶体学会”理事(2003年-今)、“生物大分子专业委员会” 副主任委员(2012年-今) 等。《IUBMB Life》副主编(2020年-今)、《Acta Biochimica et Biophysica Sinica》主编(2020年-今);《生物化学与生物物理进展》编委(2005年-今);《生命的化学》编委(2006年-今)等。

    社会任职:
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    研究方向:
  • 真核基因表达调控的结构生物学
    研究工作:
  •   真核生物的基因表达是一个非常复杂的过程,在基因转录、mRNA加工和运输、蛋白质翻译等层次上受到多种方式的调控,表达调控的异常会导致细胞的非正常生长、发育和分化,产生多种疾病包括肿瘤。我们研究组主要针对参与染色质修饰、mTOR信号转导通路和生物代谢通路调控的重要蛋白质和蛋白质复合物,运用结构生物学、分子生物学、生物化学、细胞生物学等方法,开展蛋白质的结构、功能和分子机制的研究。这些研究工作不仅能促进人们对参与真核基因表达调控的一些重要蛋白质的生物功能、分子机理、结构和功能关系的认识,同时也能为探索与这些蛋白质的功能失调相关疾病的发病机理、寻找疾病诊断的新靶标和新方法、设计和研发治疗疾病的药物等奠定分子基础。近年来主持、参与并完成国家、科学院和地方政府的多项重大研究项目。在国际重要学术刊物上发表研究论文190多篇、近五年来发表研究论文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。

    承担科研项目情况:
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    代表论著:
  • 2016年至今发表的代表性研究论文(*通讯作者):

    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 XueGuo-Dong ChenFuhua HaoHui ChenZhaoyuan FangFang-Fang ChenBo PangQing-Lin YangXinben WeiQiang-Qiang FanChangpeng XinJiaohong ZhaoXuan DengBang-An WangXiao-Jie ZhangYueying ChuHui TangHuiyong YinWeimin MaLuonan ChenJianping DingElmar WeinholdRahul M KohliWen LiuZheng-Jiang ZhuKaiyao HuangHuiru TangGuo-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). ($Contributed equally)
    14. Shicheng Zhang, Linlin Wang, Ye Tao, Tuya Bai, Rong Lu, Tianlong Zhang, Jiangye Chen, and Jianping Ding*Structural basis for the functional role of the Shu complex in homologous recombination”, Nucleic Acids Res., 45:13068-13079, doi:10.1093/nar/gkx992 (2017).
    15. Tianlong Zhang$, 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).
    获奖及荣誉:
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    研究组成员:
  • 合影