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@ARTICLE{Rossetti:201099,
      author       = {Rossetti, G. and Bongarzone, S. and Carloni, P.},
      title        = {{C}omputational {S}tudies on the {P}rion {P}rotein},
      journal      = {Current topics in medicinal chemistry},
      volume       = {13},
      number       = {19},
      issn         = {1568-0266},
      address      = {Spring House, Pa.},
      publisher    = {Bentham Science Publishers},
      reportid     = {FZJ-2015-03404},
      pages        = {2419 - 2431},
      year         = {2013},
      abstract     = {Prion diseases are rare neurodegenerative diseases
                      characterized by the conversion of the prion protein from
                      its native state (PrPC) towards the so-called 'scrapie
                      form', rich in β-strands. Computational approaches, here
                      briefly reviewed, are instrumental to understand the
                      intrinsic instability of PrPC fold and how the latter is
                      affected by mutations, binding of metals as well as by
                      different environmental conditions, such as pH and
                      temperature. These studies also provide a structural basis
                      for the binding of anti-prion compounds, which may block the
                      conversion to the scrapie form and, consequently, may
                      inhibit fibril formation.},
      cin          = {IAS-5 / JSC / GRS},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)JSC-20090406 /
                      I:(DE-Juel1)GRS-20100316},
      pnm          = {411 - Computational Science and Mathematical Methods
                      (POF2-411)},
      pid          = {G:(DE-HGF)POF2-411},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {24059339},
      doi          = {10.2174/15680266113136660170},
      url          = {https://juser.fz-juelich.de/record/201099},
}