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@ARTICLE{Liao:858912,
author = {Liao, Qinghua and Owen, Michael C. and Bali, Sofia and
Barz, Bogdan and Strodel, Birgit},
title = {{A}β under stress: the effects of acidosis, {C}u 2+
-binding, and oxidation on amyloid β-peptide dimers},
journal = {Chemical communications},
volume = {54},
number = {56},
issn = {1364-548X},
address = {Cambridge},
publisher = {Soc.},
reportid = {FZJ-2018-07748},
pages = {7766 - 7769},
year = {2018},
abstract = {In light of the high affinity of Cu2+ for Alzheimer's
Aβ1–42 and its ability to subsequently catalyze the
formation of radicals, we examine the effects of Cu2+
binding, Aβ oxidation, and an acidic environment on the
conformational dynamics of the smallest Aβ1–42 oligomer,
the Aβ1–42 dimer. Transition networks calculated from
Hamiltonian replica exchange molecular dynamics (H-REMD)
simulations reveal that the decreased pH considerably
increased the β-sheet content, whereas Cu2+ binding
increased the exposed hydrophobic surface area, both of
which can contribute to an increased oligomerization
propensity and toxicity.},
cin = {ICS-6},
ddc = {540},
cid = {I:(DE-Juel1)ICS-6-20110106},
pnm = {551 - Functional Macromolecules and Complexes (POF3-551)},
pid = {G:(DE-HGF)POF3-551},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:29947363},
UT = {WOS:000438237700008},
doi = {10.1039/C8CC02263A},
url = {https://juser.fz-juelich.de/record/858912},
}