HU HongYu & LIN XiaoJing State Key Laboratory of Molecular Biology,Institute of Biochemistry and Cell Biology,Shanghai Institutes for Biological Sciences,Chinese Academy of Sciences,Shanghai 200031,China
基金项目:
the National Natural Science Foundation of China (Grants Nos. 39990600 and 30570377),the Chinese Academy of Sciences (Grant Nos. STZ97-2-02 and KSCX2-SW-209),the Shanghai Commission of Science and Technology (Grant Nos. 98QA14017 and 03JC14081)
摘 要:
The abnormal aggregation of α-synuclein (α-Syn) is thought to be closely associated with Parkinson's disease, but the pathogenesis is still unclear. In this review, we survey the latest development in the molecular mechanism of abnormal α-Syn aggregation, especially in the aspects of the core sequences, aggregation inhibitors, structural transformation and filament morphologies. By exploring the mecha-nism of α-Syn aggregation, we will have a better understanding of the disease pathogenesis, and de-velop strategies for preventing and treating this severe disease.