N‐homocysteinylation of α‐synuclein promotes its aggregation and neurotoxicity-Reference-Cited by-同舟云学术

N‐homocysteinylation of α‐synuclein promotes its aggregation and neurotoxicity

Published:2022-11-27 Issue:3 Volume:22 Page:
ISSN:1474-9718
Container-title:Aging Cell
language:en
Short-container-title:Aging Cell

Author:

Zhou Lingyan¹^ORCID,Guo Tao¹,Meng Lanxia¹^ORCID,Zhang Xingyu¹^ORCID,Tian Ye¹,Dai Lijun¹,Niu Xuan¹,Li Yiming¹,Liu Congcong¹,Chen Guiqin¹²,Liu Chaoyang¹³,Ke Wei¹,Zhang Zhaohui¹,Bao Anyu⁴,Zhang Zhentao¹⁵

Affiliation:

1. Department of Neurology Renmin Hospital of Wuhan University Wuhan China

2. Department of Pathology and Laboratory Medicine Emory University School of Medicine Atlanta Georgia USA

3. Research Center for Environment and Health Zhongnan University of Economics and Law Wuhan China

4. Department of Clinical Laboratory Renmin Hospital of Wuhan University Wuhan China

5. TaiKang Center for Life and Medical Science Wuhan University Wuhan China

Funder

National Key Research and Development Program of China

National Natural Science Foundation of China

Publisher

Wiley

Subject

Cell Biology,Aging

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1111/acel.13745

Reference42 articles.

1. Parkinson’s disease is a type of amyloidosis featuring accumulation of amyloid fibrils of α-synuclein

2. Diagnosis and Treatment of Parkinson Disease

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4. α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation

5. N‐homocysteinylation of tau and MAP1 is increased in autopsy specimens of Alzheimer's disease and vascular dementia

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