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@ARTICLE{Owen:858916,
      author       = {Owen, Michael C. and Kulig, Waldemar and Poojari, Chetan
                      and Rog, Tomasz and Strodel, Birgit},
      title        = {{P}hysiologically-relevant levels of sphingomyelin, but not
                      {GM}1, induces a β-sheet-rich structure in the
                      amyloid-β(1-42) monomer},
      journal      = {Biochimica et biophysica acta / Biomembranes Biomembranes
                      [...]},
      volume       = {1860},
      number       = {9},
      issn         = {0005-2736},
      address      = {Amsterdam},
      publisher    = {Elsevier},
      reportid     = {FZJ-2018-07752},
      pages        = {1709 - 1720},
      year         = {2018},
      abstract     = {To resolve the contribution of ceramide-containing lipids
                      to the aggregation of the amyloid-β protein into β-sheet
                      rich toxic oligomers, we employed molecular dynamics
                      simulations to study the effect of cholesterol-containing
                      bilayers comprised of POPC $(70\%$ POPC, and $30\%$
                      cholesterol) and physiologically relevant concentrations of
                      sphingomyelin (SM) $(30\%$ SM, $40\%$ POPC, and $30\%$
                      cholesterol), and the GM1 ganglioside $(5\%$ GM1, $70\%$
                      POPC, and $25\%$ cholesterol). The increased bilayer
                      rigidity provided by SM (and to a lesser degree, GM1)
                      reduced the interactions between the SM-enriched bilayer and
                      the N-terminus of Aβ42 (and also residues Ser26, Asn27, and
                      Lys28), which facilitated the formation of a β-sheet in the
                      normally disordered N-terminal region. Aβ42 remained
                      anchored to the SM-enriched bilayer through hydrogen bonds
                      with the side chain of Arg5. With β-sheets in the at the N
                      and C termini, the structure of Aβ42 in the
                      sphingomyelin-enriched bilayer most resembles β-sheet-rich
                      structures found in higher-ordered Aβ fibrils. Conversely,
                      when bound to a bilayer comprised of $5\%$ GM1, the
                      conformation remained similar to that observed in the
                      absence of GM1, with Aβ42 only making contact with one or
                      two GM1 molecules. This article is part of a Special Issue
                      entitled: Protein Aggregation and Misfolding at the Cell
                      Membrane Interface edited by Ayyalusamy Ramamoorthy.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29626441},
      UT           = {WOS:000442333600013},
      doi          = {10.1016/j.bbamem.2018.03.026},
      url          = {https://juser.fz-juelich.de/record/858916},
}