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相分离与相变分子机制研究组

 

曹  骎

博士,长聘教轨副教授课题组长博士生导师

学    士 (2004-2008) 上海交通大学

博    士 (2008-2013) 北京大学

博士后  (2013-2019) 加州大学洛杉矶分校

助理研究员(2019-2021)加州大学洛杉矶分校

Email: caoqin@sjtu.edu.cn

 

个人介绍:

本人致力于使用冷冻电镜技术解析淀粉样蛋白纤维(一种与疾病相关的蛋白聚集形式)的分子结构,并基于结构设计可抑制纤维化的抑制剂。近五年来以(共)第一作者发表在Nature Structural & Molecular Biology,Nature Chemistry等国际知名期刊发表多篇学术论文,并为Nature Communications及Cellular & Molecular Immunology等多篇知名期刊的论文审稿。于2021年入选上海市海外高层次人才引进计划。

   

研究方向:

  1. 基于冷冻电镜的淀粉样蛋白纤维结构解析
  2. 基于结构的抑制剂设计

 

代表性论文:

  1. Cao, Q., Anderson, D.H., Liang, W., Chou, J., and Saelices, L., “The inhibition of cellular toxicity of amyloid-beta by dissociated transthyretin.” The Journal of Biological Chemistry, 295, 14015-14024 (2020)
  2. Lu, J., Cao, Q., Hughes, M.P., Sawaya, M.R., Boyer, D.R., Cascio, D., and Eisenberg., D.S., “The cryo-EM structure of the fibril-forming low-complexity domain of hnRNPA2 reveals distinct differences from pathogenic amyloid and shows how mutation converts it to the pathogenic form.” Nature Communication, 11:4090 (2020)
  3. Cao, Q., Boyer, D. R., Sawaya, M. R., Ge, P., and Eisenberg, D.S., “Cryo-EM structure and inhibitor design of human IAPP (amylin) fibrils.” Nature Structural & Molecular Biology, 27:653-659 (2020)
  4. Shin, W.S., Di, J., Cao, Q., Li, B., Seidler, P.M., Murray, K.M., Bitan, G., and Jiang, L., “Amyloid β-protein oligomers promote the uptake of tau fibril seeds potentiating intracellular tau aggregation.” Alzheimer's Research & Therapy, 11: 1-13 (2019)
  5. Cao, Q., Boyer, D. R., Sawaya, M. R., Ge, P., and Eisenberg, D.S., “Cryo-EM structures of four polymorphic TDP-43 amyloid cores.” Nature Structural & Molecular Biology, 26: 619-627 (2019)
  6. Lu J., Cao, Q., Wang, C., Zheng, J., Luo, F., Xie, J., Li, Y., Ma, X., He, L., Eisenberg, D. S., Nowick, J., Jiang, L., and Li, D., “Structure-based peptide inhibitor design of amyloid-aggregation.” Frontiers in Molecular Neuroscience, 12: 54 (2019)
  7. Cao, Q., Shin, W. S., Chan, H., Vuong, C. K., Dubois, B., Li, B., Murray, K. A., Sawaya, M. R., Feigon, J., Black, D. L., Eisenberg, D. S., and Jiang, L., “Inhibiting amyloid-β cytotoxicity through its interaction with the cell surface receptor LilrB2 by structure-based design.” Nature Chemistry, 10: 1213–1221 (2018)
  8. Guenther, E. L., Cao, Q. (co-first), Trinh, H., Lu, J., Sawaya, M. R., Cascio, D., Boyer, D. R., Rodriguez, J. A., Hughes, M. P., and Eisenberg, D. S., “Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation.” Nature Structural & Molecular Biology, 25: 463-471 (2018)
  9. Wang, X.-J., Cao, Q., Zhang, Y., and Su, X.-D., “Activation and Regulation of Caspase-6 and Its Role in Neurodegenerative Diseases.” Annual Review of Pharmacology and Toxicology, 55: 553–572 (2015)
  10. Cao, Q., Wang, X.-J., Li, L.-F., and Su, X.-D., “The regulatory mechanism of the caspase 6 pro-domain revealed by crystal structure and biochemical assays.” Acta Crystallographica Section D Biological Crystallography, 70: 58–67 (2014)
  11. Cao, Q., Wang, X.-J., Liu, C.-W., Liu, D.-F., Li, L.-F., Gao, Y.-Q., and Su, X.-D., “Inhibitory mechanism of caspase-6 phosphorylation revealed by crystal structures, molecular dynamics simulations, and biochemical assays.” The Journal of Biological Chemistry, 287: 15371–9 (2012)
  12. Wang, X.-J., Cao, Q., Liu, X., Wang, K.-T., Mi, W., Zhang, Y, Li, L.-F., LeBlanc A. C., and Su, X.-D., “Crystal structures of human caspase 6 reveal a new mechanism for intramolecular cleavage self-activation.” EMBO Reports, 11: 841–847 (2010)

 

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