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An additive-free model for tau self-assembly
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posted on 2023-06-10, 06:31 authored by Youssra Al-Hilaly, Karen E Marshall, Liisa Lutter, Luca Biasetti, Kurtis Mengham, Charles R Harrington, Wei-Feng Xue, Claude M Wischik, Louise C SerpellTau is a natively unfolded protein that contributes to the stability of microtubules. Under pathological conditions such as Alzheimer’s disease (AD), tau protein misfolds and self-assembles to form paired helical filaments (PHFs) and straight filaments (SFs). Full-length tau protein assembles poorly and its self-assembly is enhanced with polyanions such as heparin and RNA in vitro, but a role for heparin or other polyanions in vivo remains unclear. Recently, a truncated form of tau (297–391) has been shown to self-assemble in the absence of additives which provides an alternative in vitro PHF model system. Here we describe methods to prepare in vitro PHFs and SFs from tau (297–391) named dGAE. We also discuss the range of biophysical/biochemical techniques used to monitor tau filament assembly and structure.
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Publication status
- Published
ISSN
1064-3745Publisher
Humana, New York, NYExternal DOI
Volume
2551Page range
163-188Book title
Protein AggregationISBN
9781071625972Department affiliated with
- Biochemistry Publications
Research groups affiliated with
- Dementia Research Group Publications
Full text available
- No
Peer reviewed?
- Yes
Legacy Posted Date
2023-03-20Usage metrics
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