Qin Cao

Hunan University of Traditional Chinese Medicine

Also affiliated with Shanghai Jiao Tong University, Anhui University of Science and Technology, Renji Hospital, Chinese PLA General Hospital, Nanjing University of Science and Technology, Beijing Municipal Commission of Urban Planning, Anhui Science and Technology University, Ministry of Education, Chinese Research Academy of Environmental Sciences, Huazhong University of Science and Technology, Zhejiang University, Hebei Normal University

MedicineBiochemistry, Genetics and Molecular BiologyEngineeringMaterials Science

Pilot corpus only

This score is computed over theSindex pilot corpus and does not cover the full scientific literature. Scores are relative to papers we have ingested — papers, authors, and institutions outside the pilot are not represented. Methodology.

Top 100%percentile

0Author DataRank

Indexed papers

0in pilot corpus

datarank_citation_only_1hop_v6· scope data_onlyMethodology

Papers

Driven by 14 papers. Top paper: “Cryo-EM structure and inhibitor design of human IAPP (amylin) fibrils”.

Cryo-EM structure and inhibitor design of human IAPP (amylin) fibrils

Nature Structural & Molecular Biology(2020)10.1038/s41594-020-0435-3

N/A

0.752DataRank · unranked

149 citations

David R. Boyer, M.R. Sawaya, P. Ge, David Eisenberg, Qin Cao

Molecular architecture of the assembly of Bacillus spore coat protein GerQ revealed by cryo-EM

Nature Communications(2024)10.1038/s41467-024-52422-2

N/A

0.297DataRank · unranked

5 citations

Mark A. B. Kreutzberger, Jianting Han, Edward H. Egelman, Qin Cao, Yijia Cheng

Structural and molecular homogeneity of ATTRv-T60A amyloid fibrils across patients and organs

Structure(2025)10.1016/j.str.2025.09.008

N/A

0.165DataRank · unranked

2 citations

Binh A. Nguyen, Shumaila Afrin, Virender Singh, Bret M. Evers, John M. Shelton +15 more

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 pathogenic form

bioRxiv (Cold Spring Harbor Laboratory)(2020)10.1101/2020.05.24.113621

N/A

0DataRank · unranked

1 citations

Qin Cao, Michael P. Hughes, M.R. Sawaya, David R. Boyer, Duilio Cascio +2 more

Cryo-EM structures of hIAPP fibrils seeded by patient-extracted fibrils reveal new polymorphs and conserved fibril cores

Nature Structural & Molecular Biology(2021)10.1038/s41594-021-00646-x

N/A

0DataRank · unranked

90 citations

David R. Boyer, M.R. Sawaya, Romany Abskharon, Lorena Saelices, Binh A. Nguyen +5 more

Amyloid fibrils in FTLD-TDP are composed of TMEM106B and not TDP-43

Nature(2022)10.1038/s41586-022-04670-9

N/A

0DataRank · unranked

180 citations

Qin Cao, M.R. Sawaya, Romany Abskharon, P. Ge, Michael DeTure +6 more

Cryo-EM structure of RNA-induced tau fibrils reveals a small C-terminal core that may nucleate fibril formation

Proceedings of the National Academy of Sciences(2022)10.1073/pnas.2119952119

N/A

0DataRank · unranked

98 citations

M.R. Sawaya, David R. Boyer, Qin Cao, Binh A. Nguyen, Duilio Cascio +2 more

Cryo-EM structure of RNA-induced tau fibrils reveals a small C-terminal core that may nucleate fibril formation

bioRxiv (Cold Spring Harbor Laboratory)(2022)10.1101/2022.01.28.478258

N/A

0DataRank · unranked

11 citations

M.R. Sawaya, David R. Boyer, Qin Cao, Binh A. Nguyen, Duilio Cascio +2 more

Structural polymorphism of amyloid fibrils in cardiac transthyretin amyloidosis revealed by cryo-electron microscopy

bioRxiv (Cold Spring Harbor Laboratory)(2022)10.1101/2022.06.21.496949

N/A

0DataRank · unranked

8 citations

Shumaila Afrin, Virender Singh, Yasmin Ahmed, Rose Pedretti, María del Carmen Fernández‐Ramírez +12 more

Amyloid fibrils in frontotemporal lobar degeneration with TDP-43 inclusions are composed of TMEM106B, rather than TDP-43

bioRxiv (Cold Spring Harbor Laboratory)(2022)10.1101/2022.01.31.478523

N/A

0DataRank · unranked

1 citations

Qin Cao, M.R. Sawaya, Romany Abskharon, P. Ge, Michael DeTure +6 more

Cryo-EM structures of the D290V mutant of the hnRNPA2 low-complexity domain suggests how D290V affects phase separation and aggregation

Journal of Biological Chemistry(2023)10.1016/j.jbc.2023.105531

N/A

0DataRank · unranked

5 citations

P. Ge, M.R. Sawaya, Michael P. Hughes, David R. Boyer, Qin Cao +5 more

Cryo-EM structure and inhibitor design of human IAPP (amylin) fibrils

bioRxiv (Cold Spring Harbor Laboratory)(2020)10.1101/2020.05.25.114967

N/A

0DataRank · unranked

3 citations

David R. Boyer, M.R. Sawaya, P. Ge, David Eisenberg, Qin Cao

Commonly used software tools produce conflicting and overly-optimistic AUPRC values

bioRxiv (Cold Spring Harbor Laboratory)(2024)10.1101/2024.02.02.578654

N/A

0DataRank · unranked

1 citations

Miao Chen, Zhenghao Zhang, Cathy Sin‐Hang Fung, Ran Wang, Yizhen Chen +6 more

CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid

Nature Communications(2020)10.1038/s41467-020-17905-y

N/A

0DataRank · unranked

116 citations

Qin Cao, Michael P. Hughes, M.R. Sawaya, David R. Boyer, Duilio Cascio +2 more