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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},
}