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@ARTICLE{Owen:872767,
      author       = {Owen, Michael C. and Gnutt, David and Gao, Mimi and
                      Wärmländer, Sebastian K. T. S. and Jarvet, Jüri and
                      Gräslund, Astrid and Winter, Roland and Ebbinghaus, Simon
                      and Strodel, Birgit},
      title        = {{E}ffects of in vivo conditions on amyloid aggregation},
      journal      = {Chemical Society reviews},
      volume       = {48},
      number       = {14},
      issn         = {1460-4744},
      address      = {London},
      publisher    = {Soc.},
      reportid     = {FZJ-2020-00245},
      pages        = {3946 - 3996},
      year         = {2019},
      abstract     = {One of the grand challenges of biophysical chemistry is to
                      understand the principles that govern protein misfolding and
                      aggregation, which is a highly complex process that is
                      sensitive to initial conditions, operates on a huge range of
                      length- and timescales, and has products that range from
                      protein dimers to macroscopic amyloid fibrils. Aberrant
                      aggregation is associated with more than 25 diseases, which
                      include Alzheimer's, Parkinson's, Huntington's, and type II
                      diabetes. Amyloid aggregation has been extensively studied
                      in the test tube, therefore under conditions that are far
                      from physiological relevance. Hence, there is dire need to
                      extend these investigations to in vivo conditions where
                      amyloid formation is affected by a myriad of biochemical
                      interactions. As a hallmark of neurodegenerative diseases,
                      these interactions need to be understood in detail to
                      develop novel therapeutic interventions, as millions of
                      people globally suffer from neurodegenerative disorders and
                      type II diabetes. The aim of this review is to document the
                      progress in the research on amyloid formation from a
                      physicochemical perspective with a special focus on the
                      physiological factors influencing the aggregation of the
                      amyloid-β peptide, the islet amyloid polypeptide,
                      α-synuclein, and the hungingtin protein.},
      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:31192324},
      UT           = {WOS:000475647600006},
      doi          = {10.1039/C8CS00034D},
      url          = {https://juser.fz-juelich.de/record/872767},
}