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@ARTICLE{Strodel:889731,
author = {Strodel, Birgit},
title = {{A}myloid aggregation simulations: challenges, advances and
perspectives},
journal = {Current opinion in structural biology},
volume = {67},
issn = {0959-440X},
address = {Amsterdam [u.a.]},
publisher = {Elsevier},
reportid = {FZJ-2021-00352},
pages = {145 - 152},
year = {2021},
abstract = {In amyloid aggregation diseases soluble proteins coalesce
intoa wide array of undesirable structures, ranging
througholigomers and prefibrillar assemblies to highly
ordered amyloidfibrils and plaques. Explicit-solvent
all-atom moleculardynamics (MD) simulations of amyloid
aggregation have beenperformed for almost 20 years,
revealing valuable informationabout this phenomenon.
However, these simulations arechallenged by three main
problems. Firstly, current force fieldsmodeling amyloid
aggregation are insufficiently accurate.Secondly, the
protein concentrations in MD simulations areusually orders
of magnitude higher than those used in vitro orfound in
vivo, which has direct consequences on theaggregates that
form. Finally, the third problem is the wellknowntime-scale
limit of MD simulations. In this review Ihighlight recent
approaches to overcome these threelimitations.},
cin = {IBI-7},
ddc = {570},
cid = {I:(DE-Juel1)IBI-7-20200312},
pnm = {553 - Physical Basis of Diseases (POF3-553) / 5244 -
Information Processing in Neuronal Networks (POF4-524)},
pid = {G:(DE-HGF)POF3-553 / G:(DE-HGF)POF4-5244},
typ = {PUB:(DE-HGF)16},
pubmed = {33279865},
UT = {WOS:000647703900007},
doi = {10.1016/j.sbi.2020.10.019},
url = {https://juser.fz-juelich.de/record/889731},
}