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@ARTICLE{Wrdehoff:858404,
author = {Wördehoff, Michael and Hoyer, Wolfgang},
title = {α-{S}ynuclein {A}ggregation {M}onitored by {T}hioflavin
{T} {F}luorescence {A}ssay},
journal = {Bio-protocol},
volume = {8},
number = {14},
issn = {2331-8325},
address = {Sunnyvale, CA},
publisher = {bio-protocol.org},
reportid = {FZJ-2018-07290},
pages = {PMC6066150},
year = {2018},
abstract = {Studying the aggregation of amyloid proteins like
α-synuclein in vitro is a convenient and popular tool to
gain kinetic insights into aggregation as well as to study
factors (e.g., aggregation inhibitors) that influence it.
These aggregation assays typically make use of the
fluorescence dye Thioflavin T as a sensitive fluorescence
reporter of amyloid fibril formation and are conducted in a
plate-reader-based format, permitting the simultaneous
screening of multiple samples and conditions. However,
aggregation assays are generally prone to poor
reproducibility due to the stochastic nature of fibril
nucleation and the multiplicity of modulating factors. Here
we present a simple and reproducible protocol to study the
aggregation of α-synuclein in a plate-reader based assay.},
cin = {ICS-6},
ddc = {570},
cid = {I:(DE-Juel1)ICS-6-20110106},
pnm = {553 - Physical Basis of Diseases (POF3-553)},
pid = {G:(DE-HGF)POF3-553},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:30069495},
UT = {WOS:000457966200014},
doi = {10.21769/BioProtoc.2941},
url = {https://juser.fz-juelich.de/record/858404},
}