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001     340
005     20200402205336.0
024 7 _ |2 pmid
|a pmid:18669653
024 7 _ |2 pmc
|a pmc:PMC2504809
024 7 _ |2 DOI
|a 10.1073/pnas.0804721105
024 7 _ |2 WOS
|a WOS:000258308500036
037 _ _ |a PreJuSER-340
041 _ _ |a eng
082 _ _ |a 000
084 _ _ |2 WoS
|a Multidisciplinary Sciences
100 1 _ |a Elfrink, K.
|b 0
|0 P:(DE-HGF)0
245 _ _ |a Structural changes of membrane-anchored native PrPc
260 _ _ |a Washington, DC
|b Academy
|c 2008
300 _ _ |a 10815 - 10819
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |a Proceedings of the National Academy of Sciences of the United States of America
|x 0027-8424
|0 5100
|v 105
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a Misfolding and subsequent aggregation of endogenous proteins constitute essential steps in many human disorders, including Alzheimer and prion diseases. In most prion protein-folding studies, the posttranslational modifications, the lipid anchor in particular, were lacking. Here, we studied a fully posttranslationally modified cellular prion protein, carrying two N-glycosylations and the natural GPI anchor. We used time-resolved FTIR to study the prion protein secondary structure changes when binding to a raft-like lipid membrane via its GPI anchor. We observed that membrane anchoring above a threshold concentration induced refolding of the prion protein to intermolecular beta-sheets. Such transition is not observed in solution and is membrane specific. Excessive membrane anchoring, analyzed with molecular sensitivity, is thought to be a crucial event in the development of prion diseases.
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 Animals
650 _ 2 |2 MeSH
|a Cricetinae
650 _ 2 |2 MeSH
|a Membrane Proteins: genetics
650 _ 2 |2 MeSH
|a Mesocricetus
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a PrPC Proteins: genetics
650 _ 2 |2 MeSH
|a Protein Conformation
650 _ 2 |2 MeSH
|a Protein Folding
650 _ 2 |2 MeSH
|a Spectroscopy, Fourier Transform Infrared
650 _ 7 |0 0
|2 NLM Chemicals
|a Membrane Proteins
650 _ 7 |0 0
|2 NLM Chemicals
|a PrPC Proteins
650 _ 7 |a J
|2 WoSType
653 2 0 |2 Author
|a FTIR
653 2 0 |2 Author
|a membrane anchoring
653 2 0 |2 Author
|a prion protein
653 2 0 |2 Author
|a protein aggregation
653 2 0 |2 Author
|a secondary structure
700 1 _ |a Ollesch, J.
|b 1
|0 P:(DE-HGF)0
700 1 _ |a Stoehr, J.
|b 2
|0 P:(DE-HGF)0
700 1 _ |a Willbold, D.
|b 3
|u FZJ
|0 P:(DE-Juel1)132029
700 1 _ |a Riesner, D.
|b 4
|0 P:(DE-HGF)0
700 1 _ |a Gerwert, K.
|b 5
|0 P:(DE-HGF)0
773 _ _ |a 10.1073/pnas.0804721105
|g Vol. 105, p. 10815 - 10819
|p 10815 - 10819
|q 105<10815 - 10819
|0 PERI:(DE-600)1461794-8
|t Proceedings of the National Academy of Sciences of the United States of America
|v 105
|y 2008
|x 0027-8424
856 7 _ |2 Pubmed Central
|u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2504809
909 C O |o oai:juser.fz-juelich.de:340
|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
970 _ _ |a VDB:(DE-Juel1)100614
980 _ _ |a VDB
980 _ _ |a ConvertedRecord
980 _ _ |a journal
980 _ _ |a I:(DE-Juel1)ISB-2-20090406
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)ICS-6-20110106

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