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@ARTICLE{CarballoPacheco:823868,
author = {Carballo-Pacheco, Martín and Strodel, Birgit},
title = {{A}dvances in the {S}imulation of {P}rotein {A}ggregation
at the {A}tomistic {S}cale},
journal = {The journal of physical chemistry / B},
volume = {120},
number = {12},
issn = {1520-5207},
address = {Washington, DC},
publisher = {Soc.},
reportid = {FZJ-2016-06508},
pages = {2991 - 2999},
year = {2016},
abstract = {Protein aggregation into highly structured amyloid fibrils
is associated with various diseases including Alzheimer’s
disease, Parkinson’s disease, and type II diabetes.
Amyloids can also have normal biological functions and, in
the future, could be used as the basis for novel nanoscale
materials. However, a full understanding of the
physicochemical forces that drive protein aggregation is
still lacking. Such understanding is crucial for the
development of drugs that can effectively inhibit aberrant
amyloid aggregation and for the directed design of
functional amyloids. Atomistic simulations can help
understand protein aggregation. In particular, atomistic
simulations can be used to study the initial formation of
toxic oligomers which are hard to characterize
experimentally and to understand the difference in
aggregation behavior between different amyloidogenic
peptides. Here, we review the latest atomistic simulations
of protein aggregation, concentrating on amyloidogenic
protein fragments, and provide an outlook for the future in
this field.},
cin = {ICS-6},
ddc = {530},
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},
UT = {WOS:000373416700001},
pubmed = {pmid:26965454},
doi = {10.1021/acs.jpcb.6b00059},
url = {https://juser.fz-juelich.de/record/823868},
}