Journal
METHODS
Volume 53, Issue 3, Pages 246-254Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ymeth.2011.01.001
Keywords
Kinetics; Thioflavin T; Seeding; Amyloid; Oligomer; Fluorescence
Funding
- NIH [R01 AG019322, R21 AG033757]
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The aggregation of polyglutamine containing protein sequences is implicated in a family of familial neurodegenerative diseases, the expanded CAG repeat diseases. While the cellular aggregation process undoubtedly depends on the flux and local environment of these proteins, their intrinsic physical properties and folding/aggregation propensities must also contribute to their cellular behavior. Here we describe a series of methods for determining mechanistic details of the spontaneous aggregation of polyQ-containing sequences, including the identification and structural examination of aggregation intermediates. (C) 2011 Elsevier Inc. All rights reserved.
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