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@ARTICLE{Rossetti:201192,
      author       = {Rossetti, Giulia and Cong, Xiaojing and Caliandro, Rocco
                      and Legname, Giuseppe and Carloni, Paolo},
      title        = {{C}ommon {S}tructural {T}raits across {P}athogenic
                      {M}utants of the {H}uman {P}rion {P}rotein and {T}heir
                      {I}mplications for {F}amilial {P}rion {D}iseases},
      journal      = {Journal of molecular biology},
      volume       = {411},
      number       = {3},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2015-03497},
      pages        = {700 - 712},
      year         = {2011},
      abstract     = {Human (Hu) familial prion diseases are associated with
                      about 40 point mutations of the gene coding for the prion
                      protein (PrP). Most of the variants associated with these
                      mutations are located in the globular domain of the protein.
                      We performed 50 ns of molecular dynamics for each of these
                      mutants to investigate their structure in aqueous solution.
                      Overall, 1.6 μs of molecular dynamics data is presented.
                      The calculations are based on the AMBER(parm99) force field,
                      which has been shown to reproduce very accurately the
                      structural features of the HuPrP wild type and a few
                      variants for which experimental structural information is
                      available. The variants present structural determinants
                      different from those of wild-type HuPrP and the protective
                      mutation HuPrP(E219K-129M). These include the loss of salt
                      bridges in α2–α3 regions and the loss of π-stacking
                      interactions in the β2–α2 loop. In addition, in the
                      majority of the mutants, the α3 helix is more flexible and
                      Y169 is more solvent exposed. The presence of similar traits
                      in this large spectrum of mutations hints to a role of these
                      fingerprints in their known disease-causing properties.
                      Overall, the regions most affected by disease-linked
                      mutations in terms of structure and/or flexibility are those
                      involved in the pathogenic conversion to the scrapie form of
                      the protein and in the interaction with cellular partners.
                      These regions thus emerge as optimal targets for antibody-
                      and ligand-binding studies.},
      cin          = {German Research School for Simulation Sciences (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:000293938500014},
      doi          = {10.1016/j.jmb.2011.06.008},
      url          = {https://juser.fz-juelich.de/record/201192},
}