C
Cong Liu
Researcher at Chinese Academy of Sciences
Publications - 149
Citations - 6079
Cong Liu is an academic researcher from Chinese Academy of Sciences. The author has contributed to research in topics: Medicine & Fibril. The author has an hindex of 33, co-authored 106 publications receiving 3960 citations. Previous affiliations of Cong Liu include Beijing Institute of Genomics & Howard Hughes Medical Institute.
Papers
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Journal ArticleDOI
Atomic view of a toxic amyloid small oligomer.
Arthur Laganowsky,Cong Liu,Michael R. Sawaya,Julian P. Whitelegge,Jiyong Park,Minglei Zhao,Anna Pensalfini,A.B. Soriaga,Meytal Landau,Poh K. Teng,Duilio Cascio,Charles G. Glabe,David Eisenberg +12 more
TL;DR: A segment of the fibril-forming protein αB crystalline, which forms an oligomeric complex exhibiting properties of other amyloid oligomers: β-sheet–rich structure, cytotoxicity, and recognition by an oligomers-specific antibody is identified.
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Amyloid fibril structure of α-synuclein determined by cryo-electron microscopy.
Yaowang Li,Chunyu Zhao,Feng Luo,Zhenying Liu,Xinrui Gui,Zhipu Luo,Xiang Zhang,Dan Li,Cong Liu,Xueming Li +9 more
TL;DR: This study provides molecular insight into the fibrillar assembly of α-syn at the atomic level and sheds light on the molecular pathogenesis caused by familial PD mutations ofα-syn.
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Toxic fibrillar oligomers of amyloid-β have cross-β structure
TL;DR: It is established that the preparation of toxic amyloid-β1–42 (Abeta42) fibrillar oligomers (TABFOs) shares with matureAmyloid fibrils the cross-β structure, in which adjacent β-sheets adhere by interpenetration of protein side chains.
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Selective Surface Enhanced Raman Scattering for Quantitative Detection of Lung Cancer Biomarkers in Superparticle@MOF Structure.
TL;DR: Gaseous aldehydes that are released as a result of tumor-specific tissue composition and metabolism, thereby acting as indicators of lung cancer, are guided onto SERS-active GSPs substrates through a ZIF-8 channel, demonstrating tremendous prospects for in vitro diagnoses of early stage lung cancer.
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Amyloid β-sheet mimics that antagonize protein aggregation and reduce amyloid toxicity
TL;DR: A family of robust β-sheet macrocycles that can display a variety of heptapeptide sequences from different amyloid proteins is introduced, tailored to antagonize aggregation of the proteins, thereby reducing the toxicity associated with diseases such as Alzheimer's.