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@ARTICLE{SnchezLpez:858742,
author = {Sánchez-López, Carolina and Rossetti, Giulia and
Quintanar, Liliana and Carloni, Paolo},
title = {{S}tructural {D}eterminants of the {P}rion {P}rotein
{N}-{T}erminus and {I}ts {A}dducts with {C}opper {I}ons},
journal = {International journal of molecular sciences},
volume = {20},
number = {1},
issn = {1422-0067},
address = {Basel},
publisher = {Molecular Diversity Preservation International},
reportid = {FZJ-2018-07587},
pages = {18},
year = {2019},
abstract = {The N-terminus of the prion protein is a large
intrinsically disordered region encompassing approximately
125 amino acids. In this paper, we review its structural and
functional properties, with a particular emphasis on its
binding to copper ions. The latter is exploited by the
region’s conformational flexibility to yield a variety of
biological functions. Disease-linked mutations and
proteolytic processing of the protein can impact its
copper-binding properties, with important structural and
functional implications, both in health and disease
progression.},
cin = {IAS-5 / JSC / INM-9},
ddc = {540},
cid = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)JSC-20090406 /
I:(DE-Juel1)INM-9-20140121},
pnm = {571 - Connectivity and Activity (POF3-571) / 574 - Theory,
modelling and simulation (POF3-574) / 511 - Computational
Science and Mathematical Methods (POF3-511)},
pid = {G:(DE-HGF)POF3-571 / G:(DE-HGF)POF3-574 /
G:(DE-HGF)POF3-511},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:30577569},
UT = {WOS:000459747700018},
doi = {10.3390/ijms20010018},
url = {https://juser.fz-juelich.de/record/858742},
}