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@ARTICLE{Losasso:201198,
      author       = {Losasso, Valeria and Pietropaolo, Adriana and Zannoni,
                      Claudio and Gustincich, Stefano and Carloni, Paolo},
      title        = {{S}tructural {R}ole of {C}ompensatory {A}mino {A}cid
                      {R}eplacements in the α-{S}ynuclein {P}rotein},
      journal      = {Biochemistry},
      volume       = {50},
      number       = {32},
      issn         = {1520-4995},
      address      = {Columbus, Ohio},
      publisher    = {American Chemical Society},
      reportid     = {FZJ-2015-03503},
      pages        = {6994 - 7001},
      year         = {2011},
      abstract     = {A subset of familial Parkinson’s disease (PD) cases is
                      associated with the presence of disease-causing point
                      mutations in human α-synuclein [huAS(wt)], including A53T.
                      Surprisingly, the human neurotoxic amino acid 53T is present
                      in non-primate, wild-type sequences of α-synucleins,
                      including that expressed by mice [mAS(wt)]. Because
                      huAS(A53T) causes neurodegeneration when expressed in
                      rodents, the amino acid changes between the wild-type human
                      protein [huAS(wt)] and mAS(wt) might act as intramolecular
                      suppressors of A53T toxicity in the mouse protein, restoring
                      its physiological structure and function. The lack of
                      structural information for mAS(wt) in aqueous solution has
                      prompted us to conduct a comparative molecular dynamics
                      study of huAS(wt), huAS(A53T), and mAS(wt) in water at 300
                      K. The calculations are based on an ensemble of nuclear
                      magnetic resonance-derived huAS(wt) structures. huAS(A53T)
                      turns out to be more flexible and less compact than
                      huAS(wt). Its central (NAC) region, involved in fibril
                      formation by the protein, is more solvent-exposed than that
                      of the wild-type protein, in agreement with nuclear magnetic
                      resonance data. The compactness of mAS(wt) is similar to
                      that of the human protein. In addition, its NAC region is
                      less solvent-exposed and more rigid than that of huAS(A53T).
                      All of these features may be caused by an increase in the
                      level of intramolecular interactions on passing from
                      huAS(A53T) to mAS(wt). We conclude that the presence of
                      “compensatory replacements” in the mouse protein causes
                      a significant change in the protein relative to huAS(A53T),
                      restoring features not too dissimilar to those of the human
                      protein.},
      cin          = {GRS / IAS-5},
      ddc          = {570},
      cid          = {I:(DE-Juel1)GRS-20100316 / I:(DE-Juel1)IAS-5-20120330},
      pnm          = {899 - ohne Topic (POF2-899)},
      pid          = {G:(DE-HGF)POF2-899},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000293665500027},
      doi          = {10.1021/bi2007564},
      url          = {https://juser.fz-juelich.de/record/201198},
}