% IMPORTANT: The following is UTF-8 encoded. This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.
@ARTICLE{Panza:14241,
author = {Panza, G. and Luers, L. and Stöhr, J. and Nagel-Steger, L.
and Weiß, J. and Riesner, D. and Willbold, D. and Birkmann,
E.},
title = {{M}olecular interactions between prions as seeds and
recombinant prion proteins as substrates resemble the
biological interspecies barrier in vitro},
journal = {PLoS one},
volume = {5},
issn = {1932-6203},
address = {Lawrence, Kan.},
publisher = {PLoS},
reportid = {PreJuSER-14241},
pages = {e14283},
year = {2010},
note = {This authors were funded by the European Union: (Network of
Excellence "NeuroPrion", FOOD-CT-2004-506579,
http://www.neuroprion.org/en/index. html); "Presidentenfond
der Helmholtzgemeinschaft" (HGF, "Virtual Institute of
Structural Biology"), http://www.vibs-rhine-ruhr.org/; and
Food Standards Agency UK (M03R0005/004)
http://www.food.gov.uk/. Lars Luers was a fellow of the
Graduiertenkolleg 1033. Jan Stohr was supported by a
postdoctoral fellowship of the Deutsche
Forschungsgemeinschaft (DFG). The funders had no role in
study design, data collection and analysis, decision to
publish, or preparation of the manuscript.},
abstract = {Prion diseases like Creutzfeldt-Jakob disease in humans,
Scrapie in sheep or bovine spongiform encephalopathy are
fatal neurodegenerative diseases, which can be of sporadic,
genetic, or infectious origin. Prion diseases are
transmissible between different species, however, with a
variable species barrier. The key event of prion
amplification is the conversion of the cellular isoform of
the prion protein (PrP(C)) into the pathogenic isoform
(PrP(Sc)). We developed a sodiumdodecylsulfate-based PrP
conversion system that induces amyloid fibril formation from
soluble α-helical structured recombinant PrP (recPrP). This
approach was extended applying pre-purified PrP(Sc) as seeds
which accelerate fibrillization of recPrP. In the present
study we investigated the interspecies coherence of prion
disease. Therefore we used PrP(Sc) from different species
like Syrian hamster, cattle, mouse and sheep and seeded
fibrillization of recPrP from the same or other species to
mimic in vitro the natural species barrier. We could show
that the in vitro system of seeded fibrillization is in
accordance with what is known from the naturally occurring
species barriers.},
keywords = {Amyloid: chemistry / Animals / Brain: metabolism / Cattle /
Circular Dichroism / Cricetinae / Kinetics / Mesocricetus /
Mice / Neurodegenerative Diseases: metabolism / Prion
Diseases: genetics / Prion Diseases: metabolism / Prion
Diseases: transmission / Prions: chemistry / Protein
Structure, Secondary / Recombinant Proteins: chemistry /
Sheep / Sodium Dodecyl Sulfate: chemistry / Species
Specificity / Ultracentrifugation / Amyloid (NLM Chemicals)
/ Prions (NLM Chemicals) / Recombinant Proteins (NLM
Chemicals) / Sodium Dodecyl Sulfate (NLM Chemicals) / J
(WoSType)},
cin = {ISB-3 / JARA-HPC},
ddc = {500},
cid = {I:(DE-Juel1)VDB942 / $I:(DE-82)080012_20140620$},
pnm = {Funktion und Dysfunktion des Nervensystems / BioSoft:
Makromolekulare Systeme und biologische
Informationsverarbeitung},
pid = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
shelfmark = {Biology},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:21151607},
pmc = {pmc:PMC3000319},
UT = {WOS:000285135800013},
doi = {10.1371/journal.pone.0014283},
url = {https://juser.fz-juelich.de/record/14241},
}