001     313
005     20200402205333.0
024 7 _ |2 pmid
|a pmid:18585368
024 7 _ |2 DOI
|a 10.1016/j.bbrc.2008.06.059
024 7 _ |2 WOS
|a WOS:000258208500008
037 _ _ |a PreJuSER-313
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
084 _ _ |2 WoS
|a Biophysics
100 1 _ |a Panza, G.
|b 0
|0 P:(DE-HGF)0
245 _ _ |a Spontaneous and BSE-prion-seeded amyloid formation of full length recombinant bovine prion protein
260 _ _ |a Orlando, Fla.
|b Academic Press
|c 2008
300 _ _ |a 493 - 497
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
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336 7 _ |a Journal Article
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336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |a Biochemical and Biophysical Research Communications
|x 0006-291X
|0 787
|y 4
|v 373
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a The conversion of the cellular isoform of the prion protein into the pathogenic isoform PrP(Sc) is the key event in prion diseases. The disease can occur spontaneously genetically or by infection. In earlier studies we presented an in vitro conversion system which simulates the structural transition in recPrP by varying low concentrations of SDS at constant NaCl. In the present study we adopted the conversion system from experimental Scrapie in hamster to bovine recPrP and generated amyloid fibrils. The intermediate state which is optimal for fibril formation is a soluble, beta-rich state. The system was extended using BSE-prions as seeds and led to an acceleration of fibril formation by orders of magnitude. This seeded amyloid formation assay avoids any PK-treatment, is therefore able to detect even PK-sensitive PrP(Sc) and does not require cellular components.
536 _ _ |a Funktion und Dysfunktion des Nervensystems
|c P33
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK409
|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Amyloid: biosynthesis
650 _ 2 |2 MeSH
|a Amyloid: chemistry
650 _ 2 |2 MeSH
|a Animals
650 _ 2 |2 MeSH
|a Cattle
650 _ 2 |2 MeSH
|a Cricetinae
650 _ 2 |2 MeSH
|a Encephalopathy, Bovine Spongiform: metabolism
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a PrPSc Proteins: chemistry
650 _ 2 |2 MeSH
|a PrPSc Proteins: metabolism
650 _ 2 |2 MeSH
|a Protein Conformation
650 _ 2 |2 MeSH
|a Recombinant Proteins: chemistry
650 _ 2 |2 MeSH
|a Recombinant Proteins: metabolism
650 _ 7 |0 0
|2 NLM Chemicals
|a Amyloid
650 _ 7 |0 0
|2 NLM Chemicals
|a PrPSc Proteins
650 _ 7 |0 0
|2 NLM Chemicals
|a Recombinant Proteins
650 _ 7 |a J
|2 WoSType
653 2 0 |2 Author
|a BSE-prions
653 2 0 |2 Author
|a seeded vs. spontaneous conversion
653 2 0 |2 Author
|a amyloid fibrils
653 2 0 |2 Author
|a pre-amyloid state
700 1 _ |a Stöhr, J.
|b 1
|0 P:(DE-HGF)0
700 1 _ |a Dumpitak, C.
|b 2
|0 P:(DE-HGF)0
700 1 _ |a Papathanassiou, D.
|b 3
|0 P:(DE-HGF)0
700 1 _ |a Weiss, J.
|b 4
|0 P:(DE-HGF)0
700 1 _ |a Riesner, D.
|b 5
|0 P:(DE-HGF)0
700 1 _ |a Willbold, D.
|b 6
|u FZJ
|0 P:(DE-Juel1)132029
700 1 _ |a Birkmann, E.
|b 7
|u FZJ
|0 P:(DE-Juel1)VDB65870
773 _ _ |a 10.1016/j.bbrc.2008.06.059
|g Vol. 373, p. 493 - 497
|p 493 - 497
|q 373<493 - 497
|0 PERI:(DE-600)1461396-7
|t Biochemical and biophysical research communications
|v 373
|y 2008
|x 0006-291X
856 7 _ |u http://dx.doi.org/10.1016/j.bbrc.2008.06.059
909 C O |o oai:juser.fz-juelich.de:313
|p VDB
913 1 _ |k P33
|v Funktion und Dysfunktion des Nervensystems
|l Funktion und Dysfunktion des Nervensystems
|b Gesundheit
|0 G:(DE-Juel1)FUEK409
|x 0
914 1 _ |y 2008
915 _ _ |0 StatID:(DE-HGF)0010
|a JCR/ISI refereed
920 1 _ |k INB-2
|l Molekulare Biophysik
|d 31.12.2008
|g INB
|0 I:(DE-Juel1)VDB805
|x 0
920 1 _ |k JARA-SIM
|l Jülich-Aachen Research Alliance - Simulation Sciences
|g JARA
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980 _ _ |a UNRESTRICTED
980 _ _ |a I:(DE-Juel1)ICS-6-20110106
981 _ _ |a I:(DE-Juel1)IBI-7-20200312
981 _ _ |a I:(DE-Juel1)ISB-2-20090406
981 _ _ |a I:(DE-Juel1)VDB1045
981 _ _ |a I:(DE-Juel1)ICS-6-20110106


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