Hydrophobic Modification of Carboxyl-Terminated Polyamidoamine Dendrimer Surface Creates a Potent Inhibitor of Amyloid-β Fibrillation

Langmuir ◽  
2018 ◽  
Vol 34 (47) ◽  
pp. 14419-14427 ◽  
Author(s):  
Ziyuan Wang ◽  
Xiaoyan Dong ◽  
Yan Sun
Langmuir ◽  
2018 ◽  
Vol 34 (50) ◽  
pp. 15569-15577 ◽  
Author(s):  
Xi Li ◽  
Baolong Xie ◽  
Yan Sun

Biochemistry ◽  
2000 ◽  
Vol 39 (30) ◽  
pp. 8698-8704 ◽  
Author(s):  
Mark S. Shearman ◽  
Dirk Beher ◽  
Earl E. Clarke ◽  
Huw D. Lewis ◽  
Tim Harrison ◽  
...  

2012 ◽  
Vol 513 (1) ◽  
pp. 51-56 ◽  
Author(s):  
Hiroko Ushikubo ◽  
Sayaka Watanabe ◽  
Yui Tanimoto ◽  
Kazuho Abe ◽  
Aiki Hiza ◽  
...  

2014 ◽  
Vol 56 ◽  
pp. 99-110 ◽  
Author(s):  
David Allsop ◽  
Jennifer Mayes

One of the hallmarks of AD (Alzheimer's disease) is the formation of senile plaques in the brain, which contain fibrils composed of Aβ (amyloid β-peptide). According to the ‘amyloid cascade’ hypothesis, the aggregation of Aβ initiates a sequence of events leading to the formation of neurofibrillary tangles, neurodegeneration, and on to the main symptom of dementia. However, emphasis has now shifted away from fibrillar forms of Aβ and towards smaller and more soluble ‘oligomers’ as the main culprit in AD. The present chapter commences with a brief introduction to the disease and its current treatment, and then focuses on the formation of Aβ from the APP (amyloid precursor protein), the genetics of early-onset AD, which has provided strong support for the amyloid cascade hypothesis, and then on the development of new drugs aimed at reducing the load of cerebral Aβ, which is still the main hope for providing a more effective treatment for AD in the future.


2014 ◽  
Vol 56 ◽  
pp. 69-83 ◽  
Author(s):  
Ko-Fan Chen ◽  
Damian C. Crowther

The formation of amyloid aggregates is a feature of most, if not all, polypeptide chains. In vivo modelling of this process has been undertaken in the fruitfly Drosophila melanogaster with remarkable success. Models of both neurological and systemic amyloid diseases have been generated and have informed our understanding of disease pathogenesis in two main ways. First, the toxic amyloid species have been at least partially characterized, for example in the case of the Aβ (amyloid β-peptide) associated with Alzheimer's disease. Secondly, the genetic underpinning of model disease-linked phenotypes has been characterized for a number of neurodegenerative disorders. The current challenge is to integrate our understanding of disease-linked processes in the fly with our growing knowledge of human disease, for the benefit of patients.


2006 ◽  
Vol 175 (4S) ◽  
pp. 255-256
Author(s):  
Cyrill A. Rentsch ◽  
Jeroen Buijs ◽  
Geertje Van der Horst ◽  
Petra Van Overveld ◽  
Antoinette Wetterwald ◽  
...  

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