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@ARTICLE{Resenberger:136455,
author = {Resenberger, Ulrike K and Winklhofer, Konstanze F and
Tatzelt, Jörg},
title = {{N}europrotective and neurotoxic signaling by the prion
protein.},
journal = {Topics in current chemistry},
volume = {305},
issn = {0340-1022},
address = {Heidelberg},
publisher = {Springer},
reportid = {DZNE-2020-02777},
isbn = {978-3-642-24066-9 (print)},
series = {Topics in Current Chemistry},
pages = {101-119},
year = {2011},
comment = {Prion Proteins / Tatzelt, Jörg (Editor) ; Berlin,
Heidelberg : Springer Berlin Heidelberg, 2012, Chapter 160 ;
ISSN: 0340-1022=1436-5049 ; ISBN:
978-3-642-24066-9=978-3-642-24067-6 ;
doi:10.1007/978-3-642-24067-6},
booktitle = {Prion Proteins / Tatzelt, Jörg
(Editor) ; Berlin, Heidelberg :
Springer Berlin Heidelberg, 2012,
Chapter 160 ; ISSN: 0340-1022=1436-5049
; ISBN:
978-3-642-24066-9=978-3-642-24067-6 ;
doi:10.1007/978-3-642-24067-6},
abstract = {Prion diseases in humans and animals are characterized by
progressive neurodegeneration and the formation of
infectious particles called prions. Both features are
intimately linked to a conformational transition of the
cellular prion protein (PrP(C)) into aberrantly folded
conformers with neurotoxic and self-replicating activities.
Interestingly, there is increasing evidence that the
infectious and neurotoxic properties of PrP conformers are
not necessarily coupled. Transgenic mouse models revealed
that some PrP mutants interfere with neuronal function in
the absence of infectious prions. Vice versa, propagation of
prions can occur without causing neurotoxicity.
Consequently, it appears plausible that two partially
independent pathways exist, one pathway leading to the
propagation of infectious prions and another one that
mediates neurotoxic signaling. In this review we will
summarize current knowledge of neurotoxic PrP conformers and
discuss the role of PrP(C) as a mediator of both
stress-protective and neurotoxic signaling cascades.},
subtyp = {Review Article},
keywords = {Animals / Humans / Mice / Models, Biological / Mutation /
Neurodegenerative Diseases: metabolism / Neurons: metabolism
/ Neurons: pathology / Neurotoxicity Syndromes: metabolism /
Prion Diseases: metabolism / Prion Diseases: pathology /
Prions: metabolism / Protein Conformation / Protein
Denaturation / Protein Folding / Protein Structure, Tertiary
/ Signal Transduction / Prions (NLM Chemicals)},
cin = {AG Winklhofer / Ext AG Tatzelt},
ddc = {540},
cid = {I:(DE-2719)5000047 / I:(DE-2719)5000053},
pnm = {341 - Molecular Signaling (POF3-341) / 342 - Disease
Mechanisms and Model Systems (POF3-342)},
pid = {G:(DE-HGF)POF3-341 / G:(DE-HGF)POF3-342},
typ = {PUB:(DE-HGF)3 / PUB:(DE-HGF)16},
pubmed = {pmid:21598098},
doi = {10.1007/128_2011_160},
url = {https://pub.dzne.de/record/136455},
}