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@PHDTHESIS{Samantray:836336,
      author       = {Samantray, Suman},
      othercontributors = {Lüchow, Arne and Strodel, Birgit},
      title        = {{E}ssays on the interplay between glycosaminoglycans and
                      amyloid-β peptides},
      school       = {RWTH Aachen University},
      type         = {Dissertation},
      address      = {Aachen},
      publisher    = {RWTH Aachen University},
      reportid     = {RWTH-2021-11244},
      pages        = {1 Online-Ressource : Illustrationen, Diagramme},
      year         = {2021},
      note         = {Veröffentlicht auf dem Publikationsserver der RWTH Aachen
                      University 2022; Dissertation, RWTH Aachen University, 2021},
      abstract     = {Intrinsically disordered proteins (IDPs), which represent
                      $~40\%$ of the human proteome, play crucial roles in a
                      variety of biological pathways and biomolecular assemblies.
                      Monomeric IDPs such as amyloid-β (Aβ), can aggregate into
                      insoluble, relatively inert, rigid structures called
                      fibrils, but also much more toxic, soluble struc- tures of
                      intermediate size and varying shapes, which are called
                      oligomers. The toxic aggregates of Aβ peptide are
                      implicated in the pathogenesis of Alzheimer’s disease
                      (AD). In this thesis, we use in-silico approaches to model
                      Aβ under different physiological and pathological
                      conditions to unravel their effects on the structures and
                      kinetics of the amyloid oligomers. We first highlight the
                      ramifications of molecular mechanics parameters on the
                      structural heterogeneity of Aβ and the aggregation process
                      of various Aβ fragments. Next, we demonstrate how Aβ
                      fragments aggregate in the presence of glycosaminoglycans.
                      To this end, the conformational dynamics of different
                      glycosaminoglycans was first elucidated to understand their
                      behavior in the absence Aβ fragments. The conclusions from
                      these investigations enabled us to identify force fields
                      which predict Aβ structures and dynamics in agreement with
                      experimental observations. From transition networks applied
                      to the aggregation data we deduced the structural
                      transitions during the early and intermediate stages of
                      oligomer formation. Furthermore, we elucidated the
                      intermolecular interactions between Aβ and
                      glycosaminoglycans that transpire towards enhancing,
                      stabilizing, or inhibition of Aβ aggregation behavior.},
      cin          = {153420 / 150000 / 080003},
      ddc          = {540},
      cid          = {$I:(DE-82)153420_20140620$ / $I:(DE-82)150000_20140620$ /
                      $I:(DE-82)080003_20140620$},
      typ          = {PUB:(DE-HGF)11},
      doi          = {10.18154/RWTH-2021-11244},
      url          = {https://publications.rwth-aachen.de/record/836336},
}