Q
Qinyue Zhao
Researcher at Peking University
Publications - 7
Citations - 33
Qinyue Zhao is an academic researcher from Peking University. The author has contributed to research in topics: Medicine & Chemistry. The author has co-authored 1 publications.
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Heparin induces α-synuclein to form new fibril polymorphs with attenuated neuropathology
Youqi Tao,Yunpeng Sun,Shi-Jie Lv,Wencheng Xia,Kun Zhao,Qianhui Xu,Qinyue Zhao,Lin He,Weidong Le,Yong Wang,Cong Liu,Dan Li +11 more
TL;DR: In this article , the structure of α-syn fibrils in complex with heparin, a representative glycosaminoglycan (GAG), determined by cryo-electron microscopy (cryo-EM).
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Generic amyloid fibrillation of TMEM106B in patient with Parkinson’s disease dementia and normal elders
Yun Fan,Qinyue Zhao,Wencheng Xia,Youqi Tao,Wenbo Yu,Mingjia Chen,Yiqi Liu,Jue Zhao,Yan Shen,Yunpeng Sun,Chenfang Si,Shenqing Zhang,Yaoyang Zhang,Wensheng Li,Cong Liu,Jian Wang,Dan Li +16 more
TL;DR: Structural characterization of α-syn amyloid brils formed in different diseases could provide mechanistic under- standing of heterogeneous α -syn pathologies.
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Conformational change of α-synuclein fibrils in cerebrospinal fluid from different clinical phases of Parkinson's disease.
Yun Fan,Yunpeng Sun,Wenbo Yu,Youqi Tao,Wencheng Xia,Yiqi Liu,Qinyue Zhao,Yi-Lin Tang,Yi-Min Sun,Feng-Tao Liu,Qin Cao,Jianjun Wu,Cong Liu,Jian Wang,Dan Li +14 more
TL;DR: In this article , the authors demonstrated structural and pathological differences between α-syn fibrils derived from patients with Parkinson's disease at a spectrum of clinical stages, which suggests potential conformational transition of α-Synuclein (α-syn) during the progression of PD.
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Identification of the insertion site of transgenic DNA based on cyclization of the target gene with the flanking sequence and nested inverse PCR
TL;DR: The established method provides a practical tool to determine the insertion site of tDNA with a sensitivity of 103 copies in 1.0 μg of gDNA and high specificity and may be further extended for gene doping detection and assessment of the safety of gene therapy and genetically modified organisms.
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Structural insights of Fe3+ induced α-synuclein fibrillation in Parkinson's disease.
TL;DR: In this article , the structural basis of the interaction of Fe3+ and α-syn in both monomeric and fibrillar forms, and sheds light on understanding the pathological role of Fe-3+ in αsyn aggregation in Parkinson's disease.