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@ARTICLE{Bannach:137278,
author = {Bannach, O. and Reinartz, E. and Henke, F. and Dreßen, F.
and Oelschlegel, A. and Kaatz, M. and Groschup, M. H. and
Willbold, D. and Riesner, D. and Birkmann, E.},
title = {{A}nalysis of prion protein aggregates in blood and brain
from pre-clinical and clinical {BSE} cases},
journal = {Veterinary microbiology},
volume = {166},
number = {1-2},
issn = {0378-1135},
address = {Amsterdam [u.a.]},
publisher = {Elsevier Science},
reportid = {FZJ-2013-03735},
pages = {102 - 108},
year = {2013},
abstract = {Prion diseases are infectious neurodegenerative diseases
affecting humans and animals. The food-borne bovine
spongiform encephalopathy (BSE) had serious impact on both
economy and public health, respectively. To follow the
pathogenesis of BSE, oral challenge studies were previously
conducted, among others on the Isle of Riems, Germany
(Balkema-Buschmann et al., 2011b). In the present work brain
and plasma samples from this pathogenesis study were
subjected to surface fluorescence distribution analysis
(sFIDA). sFIDA is a diagnostic tool that exploits the
aggregated state of the disease-related prion protein (PrP)
as a biomarker for prion disorders. With the exception of
one animal, all tested brain samples from clinical cattle
exhibited a high titer of PrP particles. Moreover we could
detect PrP aggregates already 16 and 24 months after
infection. In contrast to our previous demonstration of PrP
particles in blood plasma from scrapie sheep, however, no
aggregates could be identified in plasma from pre-clinical
and clinical cattle. This is in accordance with other
studies suggesting a restriction of the BSE infection to the
central nervous system.},
cin = {ICS-6},
ddc = {630},
cid = {I:(DE-Juel1)ICS-6-20110106},
pnm = {452 - Structural Biology (POF2-452)},
pid = {G:(DE-HGF)POF2-452},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000322848100011},
pubmed = {pmid:23845735},
doi = {10.1016/j.vetmic.2013.05.021},
url = {https://juser.fz-juelich.de/record/137278},
}