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曹骎
caoqin@sjtu.edu.cn
英语, 中文
上海
上海交通大学
Bio-X Research Institute
  • 2004-2008 学士: 上海交通大学
  • 2008-2013 博士: 北京大学
  • 入选上海市海外高层次人才引进计划
  • 国家级海外青年人才项目
  • 科技创新2030重大项目青年首席科学家
  • 2013-2019 - 加州大学洛杉矶分校 - 博士后
  • 2019-2021 - 加州大学洛杉矶分校 - 助理研究员
基于冷冻电镜的病理性或功能性蛋白纤维结构解析
基于结构的抑制剂设计
阿尔兹海默症早期诊断方案开发
  • Molecular architecture of the assembly of Bacillus spore coat protein GerQ revealed by cryo-EM, Cheng, Y., Kreutzberger, M., Han, J., Egelman, E., and Cao, Q., 2024
  • Serine peptidase Vpr forms enzymatically active fibrils outside Bacillus bacteria revealed by cryo-EM, Cheng, Y., Han, J., Song, M., Zhang S., Cao, Q., 2023
  • Amyloid fibrils in disease FTLD-TDP are composed of TMEM106B not TDP-43, Jiang, Y. X., Cao, Q., Sawaya, M. R., Abskharon, R., Ge, P., DeTure, M., Dickson, D. W., Fu, J. Y., Loo, R. R. O., Loo, J. A., and Eisenberg, D. S., 2022
  • Cryo-EM structures of hIAPP fibrils seeded by patient-extracted fibrils reveal new polymorphs and conserved fibril cores, Cao, Q., Boyer, D. R., Sawaya, M. R., Abskharon, R., Saelices, L., Nguyen, B.A., Lu J., Murry, K.A., Kandeel, F., and Eisenberg, D.S., 2021
  • The inhibition of cellular toxicity of amyloid-beta by dissociated transthyretin., Cao, Q., Anderson, D.H., Liang, W., Chou, J., and Saelices, L., 2020
  • Cryo-EM structure and inhibitor design of human IAPP (amylin) fibrils., Cao, Q., Boyer, D. R., Sawaya, M. R., Ge, P., and Eisenberg, D.S., 2020
  • Cryo-EM structures of four polymorphic TDP-43 amyloid cores., Cao, Q., Boyer, D. R., Sawaya, M. R., Ge, P., and Eisenberg, D.S., 2019
  • Inhibiting amyloid-β cytotoxicity through its interaction with the cell surface receptor LilrB2 by structure-based design., 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., 2018
  • Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation., Guenther, E. L., Cao, Q., Trinh, H., Lu, J., Sawaya, M. R., Cascio, D., Boyer, D. R., Rodriguez, J. A., Hughes, M. P., and Eisenberg, D. S., 2018
  • The regulatory mechanism of the caspase 6 pro-domain revealed by crystal structure and biochemical assays., Cao, Q., Wang, X.-J., Li, L.-F., and Su, X.-D., 2014
  • Inhibitory mechanism of caspase-6 phosphorylation revealed by crystal structures, molecular dynamics simulations, and biochemical assays., Cao, Q., Wang, X.-J., Liu, C.-W., Liu, D.-F., Li, L.-F., Gao, Y.-Q., and Su, X.-D., 2012
  • Molecular structure of an amyloid fibril formed by FUS low-complexity domain, Sun, Y., Zhang, S., Hu, J., Tao, Y., Xia, W., Gu, J., Li, Y., Cao, Q., Li, D., and Liu, C., 2022
  • The hereditary mutation G51D unlocks a distinct fibril strain transmissible to wild-type α-synuclein, Sun, Y., Long, H., Xia, W., Wang, K., Zhang, X., Sun, B., Cao, Q., Zhang, Y., Dai, B., Li, D., and Liu, C., 2021
  • 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., Lu, J., Cao, Q., Hughes, M.P., Sawaya, M.R., Boyer, D.R., Cascio, D., and Eisenberg., D.S., 2020
  • Amyloid β-protein oligomers promote the uptake of tau fibril seeds potentiating intracellular tau aggregation., Shin, W.S., Di, J., Cao, Q., Li, B., Seidler, P.M., Murray, K.M., Bitan, G., and Jiang, L., 2019
  • Structure-based peptide inhibitor design of amyloid-aggregation., 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., 2019
  • Activation and Regulation of Caspase-6 and Its Role in Neurodegenerative Diseases., Wang, X.-J., Cao, Q., Zhang, Y., and Su, X.-D., 2015
  • Crystal structures of human caspase 6 reveal a new mechanism for intramolecular cleavage self-activation., Wang, X.-J., Cao, Q., Liu, X., Wang, K.-T., Mi, W., Zhang, Y, Li, L.-F., LeBlanc A. C., and Su, X.-D., 2010
冷冻电镜 蛋白纤维 病理性 功能性 结构解析 抑制剂设计 阿尔兹海默症 诊断 生物化学 分子生物学

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