scholarly journals Protection against β-amyloid-induced synaptic and memory impairments via altering β-amyloid assembly by bis(heptyl)-cognitin

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Lan Chang ◽  
Wei Cui ◽  
Yong Yang ◽  
Shujun Xu ◽  
Wenhua Zhou ◽  
...  
2017 ◽  
Vol 65 (20) ◽  
pp. 4092-4102 ◽  
Author(s):  
Siying Xiang ◽  
Fufeng Liu ◽  
Jiajia Lin ◽  
Huixin Chen ◽  
Chunhui Huang ◽  
...  

2008 ◽  
Vol 175 (1-3) ◽  
pp. 142-149 ◽  
Author(s):  
Margarita C. Dinamarca ◽  
Macarena Arrázola ◽  
Enrique Toledo ◽  
Waldo F. Cerpa ◽  
Juan Hancke ◽  
...  

2017 ◽  
Vol 23 (9) ◽  
pp. 679-684 ◽  
Author(s):  
Hanyi Xie ◽  
Jiaxi Peng ◽  
Changliang Liu ◽  
Xiaocui Fang ◽  
Hongyang Duan ◽  
...  

2017 ◽  
Vol 17 (2) ◽  
pp. 69-75
Author(s):  
Fatemeh Mehdipour ◽  
Nader Shahrokhi ◽  
Khadijeh Esmaeilpou ◽  
Taj Pari Kalantarip ◽  
Hakime Oloumi ◽  
...  

2019 ◽  
Vol 295 (2) ◽  
pp. 458-467 ◽  
Author(s):  
Yiling Xiao ◽  
Isamu Matsuda ◽  
Masafumi Inoue ◽  
Tomoya Sasahara ◽  
Minako Hoshi ◽  
...  

Increasing evidence highlights the central role of neurotoxic oligomers of the 42-residue-long β-amyloid (Aβ42) in Alzheimer's disease (AD). However, very limited information is available on the structural transition from oligomer to fibril, particularly for pathologically relevant amyloids. To the best of our knowledge, we present here the first site-specific structural characterization of Aβ42 misfolding, from toxic oligomeric assembly yielding a similar conformation to an AD-associated Aβ42 oligomer, into a fibril. Transmission EM (TEM) analysis revealed that a spherical amyloid assembly (SPA) of Aβ42 with a 15.6 ± 2.1-nm diameter forms in a ∼30-μm Aβ42 solution after a ∼10-h incubation at 4 °C, followed by a slow conversion into fibril at ∼180 h. Immunological analysis suggested that the SPA has a surface structure similar to that of amylospheroid (ASPD), a patient-derived toxic Aβ oligomer, which had a diameter of 10–15 nm in negative-stain TEM. Solid-state NMR analyses indicated that the SPA structure involves a β-loop-β motif, which significantly differed from the triple-β motif observed for the Aβ42 fibril. The comparison of the 13C chemical shifts of SPA with those of the fibril prepared in the above conditions and interstrand distance measurements suggested a large conformational change involving rearrangements of intermolecular β-sheet into in-register parallel β-sheet during the misfolding. A comparison of the SPA and ASPD 13C chemical shifts indicated that SPA is structurally similar to the ASPD relevant to AD. These observations provide insights into the architecture and key structural transitions of amyloid oligomers relevant for AD pathology.


2006 ◽  
Vol 11 (11) ◽  
pp. 1032-1048 ◽  
Author(s):  
M C Dinamarca ◽  
W Cerpa ◽  
J Garrido ◽  
J L Hancke ◽  
N C Inestrosa

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