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@ARTICLE{Palomino:878039,
      author       = {Palomino, Oscar and Buratti, Fiamma A. and Sacco, Pamela S.
                      and Rossetti, Giulia and Carloni, Paolo and Fernandez,
                      Claudio O.},
      title        = {{R}ole of {T}yr-39 for the {S}tructural {F}eatures of
                      α-{S}ynuclein and for the {I}nteraction with a {S}trong
                      {M}odulator of {I}ts {A}myloid {A}ssembly},
      journal      = {International journal of molecular sciences},
      volume       = {21},
      number       = {14},
      issn         = {1422-0067},
      address      = {Basel},
      publisher    = {Molecular Diversity Preservation International},
      reportid     = {FZJ-2020-02595},
      pages        = {5061 -},
      year         = {2020},
      abstract     = {Recent studies suggest that Tyr-39 might play a critical
                      role for both the normal function and the pathological
                      dysfunction of α-synuclein (αS), an intrinsically
                      disordered protein involved in Parkinson’s disease. We
                      perform here a comparative analysis between the structural
                      features of human αS and its Y39A, Y39F, and Y39L variants.
                      By the combined application of site-directed mutagenesis,
                      biophysical techniques, and enhanced sampling molecular
                      simulations, we show that removing aromatic functionality at
                      position 39 of monomeric αS leads to protein variants
                      populating more compact conformations, conserving its
                      disordered nature and secondary structure propensities.
                      Contrasting with the subtle changes induced by mutations on
                      the protein structure, removing aromaticity at position 39
                      impacts strongly on the interaction of αS with the potent
                      amyloid inhibitor phthalocyanine tetrasulfonate (PcTS). Our
                      findings further support the role of Tyr-39 in forming
                      essential inter and intramolecular contacts that might have
                      important repercussions for the function and the dysfunction
                      of αS.},
      cin          = {INM-11 / JSC / INM-9 / IAS-5 / JARA-HPC},
      ddc          = {540},
      cid          = {I:(DE-Juel1)INM-11-20170113 / I:(DE-Juel1)JSC-20090406 /
                      I:(DE-Juel1)INM-9-20140121 / I:(DE-Juel1)IAS-5-20120330 /
                      $I:(DE-82)080012_20140620$},
      pnm          = {511 - Computational Science and Mathematical Methods
                      (POF3-511) / Exploring the conformational properties of
                      alpha-synuclein variants: an enhanced sampling study
                      $(jara0209_20200501)$},
      pid          = {G:(DE-HGF)POF3-511 / $G:(DE-Juel1)jara0209_20200501$},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32709107},
      UT           = {WOS:000554212600001},
      doi          = {10.3390/ijms21145061},
      url          = {https://juser.fz-juelich.de/record/878039},
}