Professor | Cao Qin | Asia Growth Partners

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Name	Cao Qin
Contact Information	caoqin@sjtu.edu.cn
Language ability	English, Chinese
Province	Shanghai

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Name

Cao Qin

Contact Information

caoqin@sjtu.edu.cn

Language ability

English, Chinese

Province

Shanghai

University/Lab Affiliation and Title	Shanghai Jiao Tong University
Faculty	Bio-X Research Institute
Academic Background & Achievements	2004-2008 Bachelor: Shanghai Jiao Tong University 2008-2013 Doctorate: Peking University Selected for Shanghai Overseas High-Level Talent Introduction Program National Overseas Young Talent Project Youth Chief Scientist of the Science and Technology Innovation 2030 Major Project
Work Experience	2013-2019 - University of California, Los Angeles - Postdoctoral Researcher 2019-2021 - University of California, Los Angeles - Assistant Researcher

University/Lab Affiliation and Title

Shanghai Jiao Tong University

Faculty

Bio-X Research Institute

Academic Background & Achievements

2004-2008 Bachelor: Shanghai Jiao Tong University
2008-2013 Doctorate: Peking University
Selected for Shanghai Overseas High-Level Talent Introduction Program
National Overseas Young Talent Project
Youth Chief Scientist of the Science and Technology Innovation 2030 Major Project

Work Experience

2013-2019 - University of California, Los Angeles - Postdoctoral Researcher
2019-2021 - University of California, Los Angeles - Assistant Researcher

Areas of Focus	Cryo-EM based pathological or functional protein fiber structure analysis Structure-based inhibitor design Development of early diagnosis schemes for Alzheimer's disease
Publications	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

Areas of Focus

Cryo-EM based pathological or functional protein fiber structure analysis
Structure-based inhibitor design
Development of early diagnosis schemes for Alzheimer's disease

Publications

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

Cryo-Em Protein Fibers Pathological Functional Structure Analysis Inhibitor Design Alzheimer'S Diagnosis Biochemistry Molecular Biology

Chunling Wan - Shanghai Jiao Tong University

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