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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},
}