School of Medicine, Ningbo University, Zhejiang Provincial Key Laboratory of Pathophysiology,School of Medicine, Ningbo University, Zhejiang Provincial Key Laboratory of Pathophysiology,School of Medicine, Ningbo University, Zhejiang Provincial Key Laboratory of Pathophysiology
This work was supported by grants from The National Natural Science Foundation of China (81471398), Natural Science Foundation of Zhejiang Province (LY16H090001), Ningbo Natural Science Foundation (2014A610258, 2015A610211), Ningbo Talent Project, Disciplinary Project of Ningbo University (xkl141058), K.C.Wong Magna Fund in Ningbo University
Alzheimer’s disease (AD) is a neurodegenerative disorders characterized by impaired memory and cognitive functions. The pathogenesis of AD is very complicated, it is extensively documented that the accumulation of β-amyloid peptide (Aβ) is a vital contributing factor in the pathology of AD. Aβ can be divided into different forms of species, such as monomer, oligomer, and fibril. Increasing evidence suggests that oligomeric Aβ, may be the main mediators which contribute to the cognitive deficits and neurodegeneration in AD. The oligomeric Aβ has different aggregation configuration, which play different roles in the process of AD. This review mainly illustrates the role and underlying mechanisms of differently aggregated components of oligomeric Aβ in the progress of AD.
AN Peng-Yuan, WANG Qin-Wen, XU Shu-Jun. The Role and Underlying Mechanism of Differently Aggregated Components of Oligomeric β-Amyloid Protein in The Progress of Alzheimer’s Disease[J]. Progress in Biochemistry and Biophysics,2016,43(2):109-114
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