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Journal article

Aβ40 and Aβ42 amyloid fibrils exhibit distinct molecular recycling properties.

Abstract:

A critical aspect to understanding the molecular basis of Alzheimer's disease (AD) is the characterization of the kinetics of interconversion between the different species present during amyloid-β protein (Aβ) aggregation. By monitoring hydrogen/deuterium exchange in Aβ fibrils using electrospray ionization mass spectrometry, we demonstrate that the Aβ molecules comprising the fibril continuously dissociate and reassociate, resulting in molecular recycling within the fibril population. Invest...

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Publication status:
Published

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Publisher copy:
10.1021/ja1117123

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Journal:
Journal of the American Chemical Society
Volume:
133
Issue:
17
Pages:
6505-6508
Publication date:
2011-05-01
DOI:
EISSN:
1520-5126
ISSN:
0002-7863
Source identifiers:
323811
Language:
English
Keywords:
Pubs id:
pubs:323811
UUID:
uuid:f50b5367-11cc-46cc-a4a7-3bf6495551f9
Local pid:
pubs:323811
Deposit date:
2012-12-19

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