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@ARTICLE{Nguyen:902429,
      author       = {Nguyen, Phuong H. and Ramamoorthy, Ayyalusamy and Sahoo,
                      Bikash R. and Zheng, Jie and Faller, Peter and Straub, John
                      E. and Dominguez, Laura and Shea, Joan-Emma and Dokholyan,
                      Nikolay V. and De Simone, Alfonso and Ma, Buyong and
                      Nussinov, Ruth and Najafi, Saeed and Ngo, Son Tung and
                      Loquet, Antoine and Chiricotto, Mara and Ganguly, Pritam and
                      McCarty, James and Li, Mai Suan and Hall, Carol and Wang,
                      Yiming and Miller, Yifat and Melchionna, Simone and
                      Habenstein, Birgit and Timr, Stepan and Chen, Jiaxing and
                      Hnath, Brianna and Strodel, Birgit and Kayed, Rakez and
                      Lesné, Sylvain and Wei, Guanghong and Sterpone, Fabio and
                      Doig, Andrew J. and Derreumaux, Philippe},
      title        = {{A}myloid {O}ligomers: {A} {J}oint
                      {E}xperimental/{C}omputational {P}erspective on
                      {A}lzheimer’s {D}isease, {P}arkinson’s {D}isease, {T}ype
                      {II} {D}iabetes, and {A}myotrophic {L}ateral {S}clerosis},
      journal      = {Chemical reviews},
      volume       = {121},
      number       = {4},
      issn         = {0009-2665},
      address      = {Washington, DC},
      publisher    = {ACS Publ.},
      reportid     = {FZJ-2021-04251},
      pages        = {2545 - 2647},
      year         = {2021},
      abstract     = {Protein misfolding and aggregation is observed in many
                      amyloidogenic diseases affecting either the central nervous
                      system or a variety of peripheral tissues. Structural and
                      dynamic characterization of all species along the pathways
                      from monomers to fibrils is challenging by experimental and
                      computational means because they involve intrinsically
                      disordered proteins in most diseases. Yet understanding how
                      amyloid species become toxic is the challenge in developing
                      a treatment for these diseases. Here we review what
                      computer, in vitro, in vivo, and pharmacological experiments
                      tell us about the accumulation and deposition of the
                      oligomers of the (Aβ, tau), α-synuclein, IAPP, and
                      superoxide dismutase 1 proteins, which have been the
                      mainstream concept underlying Alzheimer’s disease (AD),
                      Parkinson’s disease (PD), type II diabetes (T2D), and
                      amyotrophic lateral sclerosis (ALS) research, respectively,
                      for many years.},
      cin          = {IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5244 - Information Processing in Neuronal Networks
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5244},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:33543942},
      UT           = {WOS:000623229200012},
      doi          = {10.1021/acs.chemrev.0c01122},
      url          = {https://juser.fz-juelich.de/record/902429},
}