Volume 32, No 6, Jun 2022

ISSN: 1001-0602 
EISSN: 1748-7838 2018 
impact factor 17.848* 
(Clarivate Analytics, 2019)

Volume 32 Issue 6, June 2022: 585-588   |  Open Access

LETTERS TO THE EDITOR

Generic amyloid fibrillation of TMEM106B in patient with Parkinson’s disease dementia and normal elders

Yun Fan^1,† , Qinyue Zhao^2,3,† , Wencheng Xia^4,5,† , Youqi Tao^2,3 , Wenbo Yu¹ , Mingjia Chen¹ , Yiqi Liu¹ , Jue Zhao¹ , Yan Shen¹ , Yunpeng Sun^4,5 , Chenfang Si^4,5 , Shenqing Zhang^2,3 , Yaoyang Zhang^4,5 , Wensheng Li⁶ , Cong Liu^4,5,* , Jian Wang^1,* , Dan Li^2,3,7,*

¹Department of Neurology and National Research Center for Aging and Medicine & National Center for Neurological Disorders, State Key Laboratory of Medical Neurobiology, Huashan Hospital, Fudan University, Shanghai, China
²Bio-X Institutes, Key Laboratory for the Genetics of Developmental and Neuropsychiatric Disorders (Ministry of Education), Shanghai Jiao Tong University, Shanghai, China
³BioX-Renji Hospital Research Center, Renji Hospital, School of Medicine, Shanghai Jiao Tong University, Shanghai, China
⁴Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, China
⁵University of Chinese Academy of Sciences, Beijing, China
⁶Department of Anatomy and Histoembryology, School of Basic Medical Sciences, State Key Laboratory of Medical Neurobiology and MOE Frontiers Center for Brain Science, Institutes of Brain Science, Fudan University, Shanghai, China
⁷Zhangjiang Institute for Advanced Study, Shanghai Jiao Tong University, Shanghai, China
^†These authors contributed equally: Yun Fan, Qinyue Zhao, Wencheng Xia
Correspondence: Cong Liu(liulab@sioc.ac.cn)Jian Wang(wangjian_hs@fudan.edu.cn)Dan Li(lidan2017@sjtu.edu.cn)

Dear Editor,

Protein amyloid aggregation is a histological hallmark of neurodegenerative diseases (NDs).1,2 In synucleinopathies including Parkinson’s disease (PD), Parkinson’s disease dementia (PDD), dementia with Lewy body and multiple system atrophy, α-synuclein (α-syn) is commonly characterized to form amyloid aggregates presenting distinct pathological activities in diseased brains.3,4 Structural characterization of α-syn amyloid fibrils formed in different diseases could provide mechanistic understanding of heterogeneous α-syn pathologies.5,6

https://doi.org/10.1038/s41422-022-00665-3

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