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@ARTICLE{Barz:841567,
      author       = {Barz, Bogdan and Liao, Qinghua and Strodel, Birgit},
      title        = {{P}athways of amyloid-β aggregation depend on oligomer
                      shape},
      journal      = {Journal of the American Chemical Society},
      volume       = {140},
      number       = {1},
      issn         = {0002-7863},
      address      = {Washington, DC},
      publisher    = {American Chemical Society},
      reportid     = {FZJ-2017-08605},
      pages        = {319–327},
      year         = {2018},
      abstract     = {One of the the main research topics related to
                      Alzheimer’s disease is the aggregation of the amyloid-β
                      peptide, which was shown to follow different pathways for
                      the two major alloforms of the peptide, Aβ40 and the more
                      toxic Aβ42. Experimental studies emphasized that oligomers
                      of specific sizes appear in the early aggregation process in
                      different quantities and might be the key toxic agents for
                      each of the two alloforms. We use transition networks
                      derived from all-atom molecular dynamics simulations to show
                      that the oligomers leading to the type of oligomer
                      distributions observed in experiments originate from compact
                      conformations. Extended oligomers, on the other hand,
                      contribute more to the production of larger aggregates thus
                      driving the aggregation pro cess. We further demonstrate
                      that differences in the aggregation pathways of the two Aβ
                      alloforms occur as early as during the dimer stage. The
                      higher solvent-exposure of hydrophobic residues in Aβ42
                      oligomers contributes to the different aggregation pathways
                      of both alloforms and also to the increased cytotoxicity of
                      Aβ42.},
      cin          = {ICS-6},
      ddc          = {540},
      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},
      pubmed       = {pmid:29235346},
      UT           = {WOS:000422813300060},
      doi          = {10.1021/jacs.7b10343},
      url          = {https://juser.fz-juelich.de/record/841567},
}