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@ARTICLE{Strodel:1046338,
author = {Strodel, Birgit},
title = {{C}hameleonic {N}ature of {A} β : {I}mplications for
{A}lzheimer's and {O}ther {A}myloid {D}iseases},
journal = {Bioessays},
volume = {47},
number = {9},
issn = {0265-9247},
address = {New York, NY},
publisher = {Wiley-Liss},
reportid = {FZJ-2025-03773},
pages = {e70039},
year = {2025},
abstract = {The amyloid-β peptide (Aβ), implicated in Alzheimer's
disease, exhibits significant polymorphism. At the monomer
level, Aβ can adopt disordered, helical, and β-hairpin
structures, influenced by environmental conditions. Both
oligomeric and fibrillar states, characterized by the
prevalence of β-sheets, are polymorphic in the arrangement
of β-strands. This chameleon-like behavior arises from
Aβ’s unique sequence and relatively flat energy
landscape, which facilitates aggregation and may contribute
to the prevalence of Alzheimer's disease, while also
enabling disaggregation, thus slowing disease progression.
In contrast, Creutzfeldt-Jakob disease, which is much rarer,
progresses far more rapidly, likely due to the steeper
energy landscape of the prion protein.},
cin = {IBI-7},
ddc = {540},
cid = {I:(DE-Juel1)IBI-7-20200312},
pnm = {5244 - Information Processing in Neuronal Networks
(POF4-524)},
pid = {G:(DE-HGF)POF4-5244},
typ = {PUB:(DE-HGF)16},
pubmed = {40641247},
UT = {WOS:001526776500001},
doi = {10.1002/bies.70039},
url = {https://juser.fz-juelich.de/record/1046338},
}