本人致力于使用冷冻电镜技术对于天然生物样本中的蛋白质纤维进行鉴定与结构表征，并基于结构设计可抑制病理性纤维化的抑制剂。近五年来以（共）第一/通讯作者在Nature (2022), Nature Structural & Molecular Biology (2018, 2019, 2020, 2021)，Nature Chemistry (2018)，Nature Communications （2024, 2023）等国际知名期刊发表多篇学术论文，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，并担任科技创新2030重大项目青年首席科学家

1. 基于冷冻电镜的病理性或功能性蛋白纤维结构解析

2. 基于结构的抑制剂设计

3. 阿尔兹海默症早期诊断方案开发

• Cheng, Y., Kreutzberger, M., Han, J., Egelman, E#., and Cao, Q#. “Molecular architecture of the assembly of Bacillus spore coat protein GerQ revealed by cryo-EM”. Nat Commun 15, 8091 (2024).
• Cheng, Y., Han, J., Song, M., Zhang S., Cao, Q^#. “Serine peptidase Vpr forms enzymatically active fibrils outside Bacillus bacteria revealed by cryo-EM”. Nat Commun 14, 7503 (2023). 
• Jiang, Y. X., Cao, Q. (co-first), 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., “Amyloid fibrils in disease FTLD-TDP are composed of TMEM106B not TDP-43” Nature, 605:304–309 (2022)
• 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., “Cryo-EM structures of hIAPP fibrils seeded by patient-extracted fibrils reveal new polymorphs and conserved fibril cores” Nature Structural & Molecular Biology, 28:724-730 (2021)
• 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)
• 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)
• 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)
• 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)
• 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)
• 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)
• 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)
• Sun, Y., Zhang, S., Hu, J., Tao, Y., Xia, W., Gu, J., Li, Y., Cao, Q., Li, D., and Liu, C., “Molecular structure of an amyloid fibril formed by FUS low-complexity domain” iScience, 25:103701 (2022)
• Sun, Y., Long, H., Xia, W., Wang, K., Zhang, X., Sun, B., Cao, Q., Zhang, Y., Dai, B., Li, D., and Liu, C., “The hereditary mutation G51D unlocks a distinct fibril strain transmissible to wild-type α-synuclein” Nature Communication, 12:6252 (2021)
• 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)
• 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)
• 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)
• 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)
• 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）