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Structure and intermolecular dynamics of aggregates populated during amyloid fibril formation studied by hydrogen/deuterium exchange.

Abstract:

The aggregation of proteins into amyloid fibrils is a complex and fascinating process associated with debilitating clinical disorders such as Alzheimer's and Parkinson's diseases. The process of aggregation involves a series of steps during which many intermediate aggregation states are populated. Recent evidence points to these intermediate states as the toxic moieties primarily responsible for cell damage or cell death, which are critical steps in the origin and progression of these disorde...

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Publication status:
Published

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Publisher copy:
10.1021/ar9002784

Authors


Carulla, N More by this author
Robinson, CV More by this author
Dobson, CM More by this author
Journal:
Accounts of chemical research
Volume:
43
Issue:
8
Pages:
1072-1079
Publication date:
2010-08-05
DOI:
EISSN:
1520-4898
ISSN:
0001-4842
URN:
uuid:d15b11af-20e1-40ef-827e-7d867c3b180e
Source identifiers:
71227
Local pid:
pubs:71227

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