Qin Cao
Qin Cao
Bio-X Institutes, Key Laboratory for the Genetics of Developmental and Neuropsychiatric Disorders
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Cryo-EM structures of four polymorphic TDP-43 amyloid cores
Q Cao, DR Boyer, MR Sawaya, P Ge, DS Eisenberg
Nature Structural & Molecular Biology 26 (7), 619-627, 2019
Chiral gold nanoparticles enantioselectively rescue memory deficits in a mouse model of Alzheimer’s disease
K Hou, J Zhao, H Wang, B Li, K Li, X Shi, K Wan, J Ai, J Lv, D Wang, ...
Nature Communications 11 (1), 1-11, 2020
Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation
EL Guenther, Q Cao, H Trinh, J Lu, MR Sawaya, D Cascio, DR Boyer, ...
Nature structural & molecular biology 25 (6), 463-471, 2018
Cryo-EM structure and inhibitor design of human IAPP (amylin) fibrils
Q Cao, DR Boyer, MR Sawaya, P Ge, DS Eisenberg
Nature Structural & Molecular Biology 27 (7), 653-659, 2020
Activation and regulation of caspase-6 and its role in neurodegenerative diseases
XJ Wang, Q Cao, Y Zhang, XD Su
Annual review of pharmacology and toxicology 55, 553-572, 2015
Amyloid fibrils in FTLD-TDP are composed of TMEM106B and not TDP-43
YX Jiang, Q Cao, MR Sawaya, R Abskharon, P Ge, M DeTure, ...
Nature 605 (7909), 304-309, 2022
Crystal structures of human caspase 6 reveal a new mechanism for intramolecular cleavage self‐activation
XJ Wang, Q Cao, X Liu, KT Wang, W Mi, Y Zhang, LF Li, AC LeBlanc, ...
EMBO reports 11 (11), 841-847, 2010
Amyloid β-protein oligomers promote the uptake of tau fibril seeds potentiating intracellular tau aggregation
WS Shin, J Di, Q Cao, B Li, PM Seidler, KA Murray, G Bitan, L Jiang
Alzheimer's Research & Therapy 11 (1), 1-13, 2019
CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid
J Lu, Q Cao, MP Hughes, MR Sawaya, DR Boyer, D Cascio, ...
Nature Communications 11 (1), 1-11, 2020
Structure-based peptide inhibitor design of amyloid-β aggregation
J Lu, Q Cao, C Wang, J Zheng, F Luo, J Xie, Y Li, X Ma, L He, ...
Frontiers in molecular neuroscience 12, 54, 2019
Inhibiting amyloid-β cytotoxicity through its interaction with the cell surface receptor LilrB2 by structure-based design
Q Cao, WS Shin, H Chan, CK Vuong, B Dubois, B Li, KA Murray, ...
Nature chemistry 10 (12), 1213-1221, 2018
Cryo-EM structures of hIAPP fibrils seeded by patient-extracted fibrils reveal new polymorphs and conserved fibril cores
Q Cao, DR Boyer, MR Sawaya, R Abskharon, L Saelices, BA Nguyen, ...
Nature Structural & Molecular Biology 28 (9), 724-730, 2021
The hereditary mutation G51D unlocks a distinct fibril strain transmissible to wild-type α-synuclein
Y Sun, H Long, W Xia, K Wang, X Zhang, B Sun, Q Cao, Y Zhang, B Dai, ...
Nature communications 12 (1), 1-10, 2021
Inhibitory mechanism of caspase-6 phosphorylation revealed by crystal structures, molecular dynamics simulations, and biochemical assays
Q Cao, XJ Wang, CW Liu, DF Liu, LF Li, YQ Gao, XD Su
Journal of Biological Chemistry 287 (19), 15371-15379, 2012
Conformational change of α-synuclein fibrils in cerebrospinal fluid from different clinical phases of Parkinson’s disease
Y Fan, Y Sun, W Yu, Y Tao, W Xia, Y Liu, Q Zhao, Y Tang, Y Sun, F Liu, ...
Structure, 2022
Molecular structure of an amyloid fibril formed by FUS low-complexity domain
Y Sun, S Zhang, J Hu, Y Tao, W Xia, J Gu, Y Li, Q Cao, D Li, C Liu
Iscience 25 (1), 103701, 2022
The inhibition of cellular toxicity of amyloid-β by dissociated transthyretin
Q Cao, DH Anderson, WY Liang, J Chou, L Saelices
Journal of Biological Chemistry 295 (41), 14015-14024, 2020
The regulatory mechanism of the caspase 6 pro-domain revealed by crystal structure and biochemical assays
Q Cao, XJ Wang, LF Li, XD Su
Acta Crystallographica Section D: Biological Crystallography 70 (1), 58-67, 2014
Cryo-EM structures of the D290V mutant of the hnRNPA2 low-complexity domain suggests how D290V affects phase separation and aggregation
J Lu, P Ge, MR Sawaya, MP Hughes, DR Boyer, Q Cao, R Abskharon, ...
Journal of Biological Chemistry, 105531, 2023
The cryoEM structure of the fibril-forming low-complexity domain of hnRNPA2 reveals distinct differences from pathogenic amyloid and shows how mutation converts it to the …
J Lu, Q Cao, MP Hughes, MR Sawaya, DR Boyer, D Cascio, ...
bioRxiv, 2020
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