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@ARTICLE{TayaranianMarvian:151598,
      author       = {Tayaranian Marvian, Amir and Aliakbari, Farhang and
                      Mohammad-Beigi, Hossein and Ahmadi, Zeinab Alsadat and
                      Mehrpooyan, Sina and Lermyte, Frederik and Nasouti, Mahour
                      and Collingwood, Joanna F. and Otzen, Daniel E. and
                      Morshedi, Dina},
      title        = {{T}he status of the terminal regions of α-synuclein in
                      different forms of aggregates during fibrillization},
      journal      = {International journal of biological macromolecules},
      volume       = {155},
      issn         = {0141-8130},
      address      = {New York, NY [u.a.]},
      publisher    = {Elsevier},
      reportid     = {DZNE-2020-01182},
      pages        = {543-550},
      year         = {2020},
      abstract     = {The α-synuclein (αSN) amyloid fibrillization process is
                      known to be a crucial phenomenon associated with neuronal
                      loss in various neurodegenerative diseases, most famously
                      Parkinson's disease. The process involves different
                      aggregated species and ultimately leads to formation of
                      β-sheet rich fibrillar structures. Despite the essential
                      role of αSN aggregation in the pathoetiology of various
                      neurological disorders, the characteristics of various
                      assemblies are not fully understood. Here, we established a
                      fluorescence-based model for studying the end-parts of αSN
                      to decipher the structural aspects of aggregates during the
                      fibrillization. Our model proved highly sensitive to the
                      events at the early stage of the fibrillization process,
                      which are hardly detectable with routine techniques.
                      Combining fluorescent and PAGE analysis, we found different
                      oligomeric aggregates in the nucleation phase of
                      fibrillization with different sensitivity to SDS and
                      different structures based on αSN termini. Moreover, we
                      found that these oligomers are highly dynamic: after
                      reaching peak levels during fibrillization, they decline and
                      eventually disappear, suggesting their transformation into
                      other αSN aggregated species. These findings shed light on
                      the structural features of various αSN aggregates and their
                      dynamics in synucleinopathies.},
      keywords     = {Amyloid: chemistry / Humans / Mutant Proteins: chemistry /
                      Mutant Proteins: genetics / Mutant Proteins: metabolism /
                      Mutation / Protein Interaction Domains and Motifs / Protein
                      Multimerization / alpha-Synuclein: chemistry /
                      alpha-Synuclein: genetics / alpha-Synuclein: metabolism},
      cin          = {AG Höglinger 1 ; AG Höglinger 1},
      ddc          = {570},
      cid          = {I:(DE-2719)1110002},
      pnm          = {344 - Clinical and Health Care Research (POF3-344)},
      pid          = {G:(DE-HGF)POF3-344},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32240735},
      doi          = {10.1016/j.ijbiomac.2020.03.238},
      url          = {https://pub.dzne.de/record/151598},
}