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Cell (2026), Nature (2022), Advanced Materials (2025), Molecular Neurodegeneration (2026), Nature Communications （2024, 2023）等国际知名期刊发表多篇学术论文，入选国家级及上海市级海外高层次人才引进计划等

1. 基于冷冻电镜的病理性或功能性蛋白纤维结构解析

2. 以纤维为靶点的诊疗药物开发

3. 阿尔兹海默症早期诊断方案开发

1.       Han, J. and Cao, Q^#., “Structural basis for human RegⅢα filament formation” Communications Chemistry, 9, 117 (2026)

2.       Li, D., Zhao, Q., Tao, Y., Lv, S., Zhao, W., Li, Y., Xiong, X., Wang, Z., Xu, W., Zhang, Y., Liu, C., Le, W., Kang, W., Li, D^#., Cao, Q^#., Dai B^#., “Tissue-Specific Extraction and Structural Elucidation of Actin‐Tropomyosin‐Myosin Complexes from Human and Rodent” Aggregate, e70265 (2026)

3.       Song, M., Zheng H., Han, J., Xu, K., Zhang, D^#., and Cao, Q^#., “The molecular fidelity of Aβ pathology in 5xFAD and App^NL−FPsen1^P117L mice revealed by cryo-EM” Molecular Neurodegeneration, 21, 10 (2026)

4.       Liu, W., Han, J., Gong, W., Zhang, F^#., and Cao, Q^#., “Structure of pancreatic hIAPP fibrils derived from patients with type 2 diabetes” Cell, 189, 1-10 (2026)

5.       Jiang, Y., Peña-Díaz, S., Zhang, Z., Daugberg, A. O. H., Hemnández, M. L., Nielsen, J., Huang. Q., Qin, S., Dueholm, M. K. D., Dong, M., Pederen, J. S., Cao, Q^#., Otzen, D^#., and Wang, H^#., “Natural design of a stabilized cross-β fold: Structure of the FuA FapC from Pseudomonas sp. UK4 reveals a critical role for stacking of imperfect repeats” Advanced Materials, 37, 250503 (2025)

6.       Han, J., Song, M., Cheng, Y., Gong, W., Zhang, F^#., and Cao, Q^#., “Structure of human glycoprotein 2 reveals mechanisms underlying filament formation and adaption to proteolytic environment in the digestive tract” PLOS Biology, 23, e3003238 (2025)

7.       Song, M., Han, J., and Cao, Q^#., “Cryo-EM structure of amyloid fibrils formed by full-length human αA-crystallin with pathogenic mutation R116C” Communications Chemistry, 8, 233 (2025)

8.       Li, S., Li, S., Cheng, Y., Fang, Y^#., Cao, Q^#., and Cao, Y^#., “Dual hydrophilic-hydrophobic core architecture in soy glycinin amyloid fibrils revealed by cryo-EM” Advanced Science, e09821 (2025)

9.       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” Nature Communications, 15, 8091 (2024).

10.   Cheng, Y., Han, J., Song, M., Zhang S., Cao, Q^#., “Serine peptidase Vpr forms enzymatically active fibrils outside Bacillus bacteria revealed by cryo-EM” Nature Communications, 14, 7503 (2023). 

11.   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 and not TDP-43” Nature, 605:304-309 (2022)

12.   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)

13.   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)

14.   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)

15.   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)

16.   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)