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@ARTICLE{NagelSteger:823869,
      author       = {Nagel-Steger, Luitgard and Owen, Michael C. and Strodel,
                      Birgit},
      title        = {{A}n {A}ccount of {A}myloid {O}ligomers: {F}acts and
                      {F}igures {O}btained from {E}xperiments and {S}imulations},
      journal      = {ChemBioChem},
      volume       = {17},
      number       = {8},
      issn         = {1439-4227},
      address      = {Weinheim},
      publisher    = {Wiley-VCH},
      reportid     = {FZJ-2016-06509},
      pages        = {657 - 676},
      year         = {2016},
      abstract     = {The deposition of amyloid in brain tissue in the context of
                      neurodegenerative diseases involves the formation of
                      intermediate species—termed oligomers—of lower molecular
                      mass and with structures that deviate from those of mature
                      amyloid fibrils. Because these oligomers are thought to be
                      primarily responsible for the subsequent disease
                      pathogenesis, the elucidation of their structure is of
                      enormous interest. Nevertheless, because of the high
                      aggregation propensity and the polydispersity of oligomeric
                      species formed by the proteins or peptides in question, the
                      preparation of appropriate samples for high-resolution
                      structural methods has proven to be rather difficult. This
                      is why theoretical approaches have been of particular
                      importance in gaining insights into possible oligomeric
                      structures for some time. Only recently has it been possible
                      to achieve some progress with regard to the experimentally
                      based structural characterization of defined oligomeric
                      species. Here we discuss how theory and experiment are used
                      to determine oligomer structures and what can be done to
                      improve the integration of the two disciplines.},
      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},
      UT           = {WOS:000375124500003},
      pubmed       = {pmid:26910367},
      doi          = {10.1002/cbic.201500623},
      url          = {https://juser.fz-juelich.de/record/823869},
}