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@ARTICLE{ColiniBaldeschi:909796,
author = {Colini Baldeschi, Arianna and Zattoni, Marco and Vanni,
Silvia and Nikolic, Lea and Ferracin, Chiara and La Sala,
Giuseppina and Summa, Maria and Bertorelli, Rosalia and
Bertozzi, Sine Mandrup and Giachin, Gabriele and Carloni,
Paolo and Bolognesi, Maria Laura and De Vivo, Marco and
Legname, Giuseppe},
title = {{I}nnovative {N}on-{P}r{P}-{T}argeted {D}rug {S}trategy
{D}esigned to {E}nhance {P}rion {C}learance},
journal = {Journal of medicinal chemistry},
volume = {65},
number = {13},
issn = {0022-2623},
address = {Washington, DC},
publisher = {ACS},
reportid = {FZJ-2022-03421},
pages = {8998 - 9010},
year = {2022},
abstract = {Prion diseases are a group of neurodegenerative disorders
characterized by the accumulation of misfolded prion protein
(called PrPSc). Although conversion of the cellular prion
protein (PrPC) to PrPSc is still not completely understood,
most of the therapies developed until now are based on
blocking this process. Here, we propose a new drug strategy
aimed at clearing prions without any direct interaction with
neither PrPC nor PrPSc. Starting from the recent discovery
of SERPINA3/SerpinA3n upregulation during prion diseases, we
have identified a small molecule, named compound 5
(ARN1468), inhibiting the function of these serpins and
effectively reducing prion load in chronically infected
cells. Although the low bioavailability of this compound
does not allow in vivo studies in prion-infected mice, our
strategy emerges as a novel and effective approach to the
treatment of prion disease.},
cin = {IAS-5 / INM-9},
ddc = {610},
cid = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121},
pnm = {5241 - Molecular Information Processing in Cellular Systems
(POF4-524)},
pid = {G:(DE-HGF)POF4-5241},
typ = {PUB:(DE-HGF)16},
pubmed = {35771181},
UT = {WOS:000836282300001},
doi = {10.1021/acs.jmedchem.2c00205},
url = {https://juser.fz-juelich.de/record/909796},
}