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@ARTICLE{deBruyn:1032184,
      author       = {de Bruyn, Emile and Dorn, Anton Emil and Rossetti, Giulia
                      and Fernandez, Claudio and Outeiro, Tiago F. and Schulz,
                      Jörg B. and Carloni, Paolo},
      title        = {{I}mpact of {P}hosphorylation on the {P}hysiological {F}orm
                      of {H}uman alpha-{S}ynuclein in {A}queous {S}olution},
      journal      = {Journal of chemical information and modeling},
      volume       = {64},
      number       = {21},
      issn         = {1549-9596},
      address      = {Washington, DC},
      publisher    = {American Chemical Society},
      reportid     = {FZJ-2024-06053},
      pages        = {8215–8226},
      year         = {2024},
      abstract     = {Serine 129 can be phosphorylated in pathological inclusions
                      formed by the intrinsically disordered protein human
                      α-synuclein (AS), a key player in Parkinson’s disease and
                      other synucleinopathies. Here, molecular simulations provide
                      insight into the structural ensemble of phosphorylated AS.
                      The simulations allow us to suggest that phosphorylation
                      significantly impacts the structural content of the
                      physiological AS conformational ensemble in aqueous
                      solution, as the phosphate group is mostly solvated. The
                      hydrophobic region of AS contains β-hairpin structures,
                      which may increase the propensity of the protein to undergo
                      amyloid formation, as seen in the nonphysiological
                      (nonacetylated) form of the protein in a recent molecular
                      simulation study. Our findings are consistent with existing
                      experimental data with the caveat of the observed
                      limitations of the force field for the phosphorylated
                      moiety.},
      cin          = {INM-9 / JSC / INM-11},
      ddc          = {540},
      cid          = {I:(DE-Juel1)INM-9-20140121 / I:(DE-Juel1)JSC-20090406 /
                      I:(DE-Juel1)INM-11-20170113},
      pnm          = {5111 - Domain-Specific Simulation $\&$ Data Life Cycle Labs
                      (SDLs) and Research Groups (POF4-511) / 5112 - Cross-Domain
                      Algorithms, Tools, Methods Labs (ATMLs) and Research Groups
                      (POF4-511) / HDS LEE - Helmholtz School for Data Science in
                      Life, Earth and Energy (HDS LEE) (HDS-LEE-20190612) / SFB
                      1286 B08 - Definition von Kaskaden molekularer
                      Veränderungen bei Synucleinopathien während der
                      Neurodegeneration (B08) (386961151) / DFG project
                      G:(GEPRIS)390729940 - EXC 2067: Multiscale Bioimaging: Von
                      molekularen Maschinen zu Netzwerken erregbarer Zellen
                      (390729940) / DFG project G:(GEPRIS)491111487 -
                      Open-Access-Publikationskosten / 2025 - 2027 /
                      Forschungszentrum Jülich (OAPKFZJ) (491111487)},
      pid          = {G:(DE-HGF)POF4-5111 / G:(DE-HGF)POF4-5112 /
                      G:(DE-Juel1)HDS-LEE-20190612 / G:(GEPRIS)386961151 /
                      G:(GEPRIS)390729940 / G:(GEPRIS)491111487},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {39462994},
      UT           = {WOS:001344038800001},
      doi          = {10.1021/acs.jcim.4c01172},
      url          = {https://juser.fz-juelich.de/record/1032184},
}