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@ARTICLE{Barz:150941,
      author       = {Barz, Bogdan and Olubiyi, Olujide O. and Strodel, Birgit},
      title        = {{E}arly amyloid β-protein aggregation precedes
                      conformational change},
      journal      = {Chemical communications},
      volume       = {50},
      number       = {40},
      issn         = {1364-548X},
      address      = {Cambridge},
      publisher    = {Soc.},
      reportid     = {FZJ-2014-00974},
      pages        = {5373-5375},
      year         = {2014},
      abstract     = {The aggregation of amyloid-β protein (1–42) is studied
                      at experimental concentrations using all-atom molecular
                      dynamics simulations. We observe a fast aggregation into
                      oligomers without significant changes in the internal
                      structure of individual proteins. The aggregation process is
                      characterized in terms of transition networks.},
      cin          = {ICS-6},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000335011200066},
      pubmed       = {pmid:24471163},
      doi          = {10.1039/c3cc48704k},
      url          = {https://juser.fz-juelich.de/record/150941},
}