唐淳
近期热点
资料介绍
个人简历
唐淳于1998毕业于浙江大学生物系。1998至2003年在美国马里兰大学霍华德休斯研究员Michael Summers院士的指导下,开展了对于逆转录病毒的蛋白和RNA的溶液结构的研究,获得生物化学博士学位。2003至2008年在美国国立卫生中心(NIH)糖尿病肾病和消化病研究所(NIDDK)的物理化学实验室(LCP)的G. Marius Clore院士实验室开展了博士后研究,开展了核磁共振(NMR)的方法学研究。2008-2010年在美国密苏里大学生物化学系任助理教授。2010年回国任中科院武汉物理与数学研究所研究员,并担任中科院生物磁共振重点实验室主任。2020年加入北京大学化学学院物理化学系,并加入生命科学联合中心。\r\rPersonal Information\r2020 -- : Boya Professor, College of Chemistry and Molecular Engineering, Peking University\r2020 -- : Senior Investigator, PKU-Tsinghua Center for Life Sciences\r2010 -- : Principal Investigator, Wuhan Institute of Physics and Mathematics of the Chinese Academy of Sciences\r2008 -- 2010: Assistant Professor, Department of Biochemistry, University of Missouri, Columbia\r2003 -- 2008: Postdoc, Laboratory of Chemical Physics, National Institute of Diabetes Digestive and Kidney Diseases, National Institutes of Health\r2003: Ph.D. degree in Biochemistry, University of Maryland, Baltimore County\r1998: B.S. degree in Biology, Zhejiang University研究领域
"""""Method development of biomolecular NMR\rMethod development for integrative structure refinement近期论文
Ma YX, Li HZ, Gong Z, Yang S, Wang P and Tang C. (2022) Nucleobase Clustering Contributes to the Formation and Hollowing of Repeat-Expansion RNA Condensate. J. Am. Chem. Soc, doi.org/10.1021/jacs.1c12085\r\rDong X, Qin LY, Gong Z, Qin S, Zhou HX and Tang C. (2022) Preferential Interactions of a Crowder Protein with the Specific Binding Site of a Native Protein Complex. J Phys Chem Lett, doi.org/10.1021/acs.jpclett.1c03794\r\rCzaplewski C, Gong Z, Lubecka EA, Xue K, Tang C, Liwo A. (2021) Recent Developments in Data-Assisted Modeling of Flexible Proteins. Front. Mol. Biosci, doi.org/10.3389/fmolb.2021.765562\r\rFu WT, Zhang MK, Liao JN, Tang Q, Lei YX, Gong Z, Shan LH, Duan MJ, Chai X, Pang JP, Tang C, Wang XW, Xu XH, Li D, Sheng R, Hou TJ. (2021) Discovery of a Novel Androgen Receptor Antagonist Manifesting Evidence to Disrupt the Dimerization of the Ligand-Binding Domain via Attenuating the Hydrogen-Bonding Network Between the Two Monomers. J. Med. Chem, doi.org/10.1021/acs.jmedchem.1c01287\r\rKogut M, Gong Z, Tang C, Liwo A. (2021)Pseudopotentials for coarse-grained cross-link-assisted modeling of protein structures. J Comput Chem,42 (29) : 2054-2067\r\rQin LY, Gong Z, Liu K, Dong X and Tang C. (2021)Kinetic Constraints in the Specific Interaction between Phosphorylated Ubiquitin and Proteasomal Shuttle Factors. Biomolecules,10.3390 / biom11071008 \r\r Lerner E, Barth A, Hendrix J, Ambrose B, Birkedal V, Blanchard SC, Börner R, Chung HS, Cordes T, Craggs TD, Deniz AA, Diao JJ, Fei JY, Gonzalez RL, Gopich IV, Ha T, Hanke CA, Haran G, Hatzakis NS, Hohng SC, Hong SC, Hugel T, Ingargiola A, Joo C, Kapanidis AN, Kim HD, Laurence T, Lee NK, Lee TH, Lemke EA, Margeat E, Michaelis J, Michalet X, Myong S, Nettels D, Peulen TO, Ploetz E, Razvag Y, Robb NC, Schuler B, Soleimaninejad H, Tang C, Vafabakhsh R, Lamb DC, Seidel CA, Weiss S. (2021) FRET-based dynamic structural biology: Challenges, perspectives and an appeal for open-science practices. eLife, 2021;10:e60416\r\rGong Z, Ye SX and Tang C. (2020) Tightening the Crosslinking Distance Restraints for Better Resolution of Protein Structure and Dynamics. Structure, 28:1160-1167\r\rYang J, Gong Z, Lu YB, Xu CJ, Wei TF, Yang MS, Zhan TW, Yang YH, Lin L, Liu JF, Tang C and Zhang WP. (2020) FLIM–FRET-Based Structural Characterization of a Class-A GPCR Dimer in the Cell Membrane. J Mol Biol,432:4596-4611\r\rGong Z, Yang S, Dong X, Yang QF, Zhu YL, Xiao Y, Tang C. (2020)Hierarchical Conformational Dynamics Confers Thermal Adaptability to preQ1 RNA Riboswitches. J Mol Biol , 4 32:4523-4543 \r\rGong Z, Ye SX, Nie ZF and Tang C. (2020) The Conformational Preference of Chemical Cross-linkers Determines the Cross-linking Probability of Reactive Protein Residues. J Phy Chem B , 123:4446-4453\r\rTang C , Gong Z. (2020) Integrating Non-NMR Distance Restraints to Augment NMR Depiction of Protein Structure and Dynamics. J Mol Biol,432:2913-2929\r\rTang C and Zhang wp. (2020) How Phosphorylation by PINK1 Remodels the Ubiquitin System: A Perspective from Structure and Dynamics. Biochemistry, 59:26-33\r\rYou ZY, Jiang WX, Qin LY, Gong Z, Wan W, Li J, Wang YS, Zhang HT, Peng C, Zhou TH, Tang C and Liu W. (2019) Requirement for p62 acetylation in the aggregation of ubiquitylated proteins under nutrient stress. Nat Commun,10:5792\r\rGong Z, Yang S, Yang QF, Zhu YL, Jiang J and Tang C. (2019) Refining RNA solution structures with the integrative use of label-free paramagnetic relaxation enhancement NMR. Biophys. Rep, 5:244-253\r\rYe SX, Gong Z, Yang J, An YX, Liu Z, Zhao Q, Lescop E, Dong X, Tang C. (2019) Ubiquitin is double-phosphorylated by PINK1 for enhanced pH-sensitivity of conformational switch. Protein & Cell, 10:908-913\r\rYang QF, Tang C. (2019) On the necessity of an integrative approach to understand protein structural dynamics. J Zhejiang Univ Sci B, 20(6):496-502\r\rLiu Z, Dong X, Yi HW, Yang J, Gong Z, Wang Y, Liu K, Zhang WP, Tang C. (2019) Structural basis for the recognition of K48-linked Ub chain by proteasomal receptor Rpn13. Cell Discov, 5:19 相关热点