Amyloid fibril aggregation: An insight into the underwater adhesion of barnacle cement

2017 ◽  
Vol 493 (1) ◽  
pp. 654-659 ◽  
Author(s):  
Xingping Liu ◽  
Chao Liang ◽  
Xinkang Zhang ◽  
Jianyong Li ◽  
Jingyun Huang ◽  
...  
Author(s):  
Kannayiram Gomathi ◽  
Jebiti Haribabu ◽  
Sivaraj Saranya ◽  
Dasararaju Gayathri ◽  
Kumaramangalam Jeyalakshmi ◽  
...  

2010 ◽  
Vol 43 (8) ◽  
pp. 2176-2178 ◽  
Author(s):  
Caroline Henry-Vitrac ◽  
Hervé Berbille ◽  
Jean-Michel Mérillon ◽  
Xavier Vitrac

2020 ◽  
Author(s):  
Devkee M Vadukul ◽  
Céline Vrancx ◽  
Pierre Burguet ◽  
Sabrina Contino ◽  
Nuria Suelves ◽  
...  

A key hallmark of Alzheimer's disease (AD) is the extracellular deposition of amyloid plaques composed primarily of the amyloidogenic amyloid-β (Aβ) peptide. The Aβ peptide is a product of sequential cleavage of the Amyloid Precursor Protein (APP), the first step of which gives rise to a C-terminal Fragment (C99). Cleavage of C99 by γ-secretase activity releases Aβ of several lengths and the Aβ42 isoform in particular has been identified as being neurotoxic. The misfolding of Aβ leads to subsequent amyloid fibril formation by nucleated polymerisation. This requires an initial and critical nucleus for self-assembly. Here, we identify and characterise the composition and self-assembly properties of cell-derived hexameric Aβ42 and show its nucleating properties which are dependent on the Aβ monomer availability. Identification of nucleating assemblies that contribute to self-assembly in this way may serve as therapeutic targets to prevent the formation of toxic oligomers.


2011 ◽  
Vol 94 (6) ◽  
pp. 68006 ◽  
Author(s):  
Liu Hong ◽  
Xianghong Qi ◽  
Yang Zhang

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