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@ARTICLE{Willbold:902420,
      author       = {Willbold, Dieter and Strodel, Birgit and Schröder, Gunnar
                      F. and Hoyer, Wolfgang and Heise, Henrike},
      title        = {{A}myloid-type {P}rotein {A}ggregation and {P}rion-like
                      {P}roperties of {A}myloids},
      journal      = {Chemical reviews},
      volume       = {121},
      number       = {13},
      issn         = {0009-2665},
      address      = {Washington, DC},
      publisher    = {ACS Publ.},
      reportid     = {FZJ-2021-04242},
      pages        = {8285 - 8307},
      year         = {2021},
      abstract     = {This review will focus on the process of amyloid-type
                      protein aggregation. Amyloid fibrils are an important
                      hallmark of protein misfolding diseases and therefore have
                      been investigated for decades. Only recently, however,
                      atomic or near-atomic resolution structures have been
                      elucidated from various in vitro and ex vivo obtained
                      fibrils. In parallel, the process of fibril formation has
                      been studied in vitro under highly artificial but
                      comparatively reproducible conditions. The review starts
                      with a summary of what is known and speculated from
                      artificial in vitro amyloid-type protein aggregation
                      experiments. A partially hypothetic fibril selection model
                      will be described that may be suitable to explain why
                      amyloid fibrils look the way they do, in particular, why at
                      least all so far reported high resolution cryo-electron
                      microscopy obtained fibril structures are in register,
                      parallel, cross-β-sheet fibrils that mostly consist of two
                      protofilaments twisted around each other. An intrinsic
                      feature of the model is the prion-like nature of all amyloid
                      assemblies. Transferring the model from the in vitro point
                      of view to the in vivo situation is not straightforward,
                      highly hypothetic, and leaves many open questions that need
                      to be addressed in the future.},
      cin          = {IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551) /
                      5244 - Information Processing in Neuronal Networks
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF3-551 / G:(DE-HGF)POF4-5244},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:34137605},
      UT           = {WOS:000674316500013},
      doi          = {10.1021/acs.chemrev.1c00196},
      url          = {https://juser.fz-juelich.de/record/902420},
}