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| 001 | 173322 | ||
| 005 | 20220930130036.0 | ||
| 024 | 7 | _ | |a 10.4161/19336896.2014.983754 |2 doi |
| 024 | 7 | _ | |a 1933-6896 |2 ISSN |
| 024 | 7 | _ | |a 1933-690X |2 ISSN |
| 024 | 7 | _ | |a WOS:000348376700004 |2 WOS |
| 037 | _ | _ | |a FZJ-2014-06732 |
| 041 | _ | _ | |a English |
| 082 | _ | _ | |a 570 |
| 100 | 1 | _ | |a Müller, Henrik |0 P:(DE-Juel1)132017 |b 0 |
| 245 | _ | _ | |a Progress towards structural understanding of infectious sheep PrP-amyloid |
| 260 | _ | _ | |a Austin, Tex. |c 2014 |b Landes Bioscience |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1420465527_23891 |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 |
| 520 | _ | _ | |a The still elusive structural difference of non-infectious and infectious amyloid of the mammalian prion protein (PrP) is a major pending milestone in understanding protein-mediated infectivity in neurodegenerative diseases. Preparations of PrP-amyloid proven to be infectious have never been investigated with a high-resolution technique. All available models to date have been based on low-resolution data. Here, we establish protocols for the preparation of infectious samples of full-length recombinant (rec) PrP¡amyloid in NMR-sufficient amounts by spontaneous fibrillation and seeded fibril growth from brain extract. We link biological and structural data of infectious recPrP-amyloid, derived from bioassays, atomic force microscopy, and solid-state NMR spectroscopy. Our data indicate a semi-mobile N‑terminus, some residues with secondary chemical shifts typical of α‑helical secondary structure in the middle part between ~115 to ~155, and a distinct β‑sheet core C‑terminal of residue ~155. These findings are not in agreement with all current models for PrP-amyloid. We also provide evidence that samples seeded from brain extract may not differ in the overall arrangement of secondary structure elements, but rather in the flexibility of protein segments outside the β-core region. Taken together, our protocols provide an essential basis for the high-resolution characterization of non-infectious and infectious PrP-amyloid in the near future. |
| 536 | _ | _ | |a 452 - Structural Biology (POF2-452) |0 G:(DE-HGF)POF2-452 |c POF2-452 |f POF II |x 0 |
| 588 | _ | _ | |a Dataset connected to CrossRef, juser.fz-juelich.de |
| 700 | 1 | _ | |a Brener, Oleksandr |0 P:(DE-HGF)0 |b 1 |
| 700 | 1 | _ | |a Andreoletti, Olivier |0 P:(DE-HGF)0 |b 2 |
| 700 | 1 | _ | |a Piechatzek, Timo |0 P:(DE-Juel1)145776 |b 3 |u fzj |
| 700 | 1 | _ | |a Willbold, Dieter |0 P:(DE-Juel1)132029 |b 4 |u fzj |
| 700 | 1 | _ | |a Legname, Giuseppe |0 P:(DE-HGF)0 |b 5 |
| 700 | 1 | _ | |a Heise, Henrike |0 P:(DE-Juel1)132002 |b 6 |e Corresponding Author |u fzj |
| 773 | _ | _ | |a 10.4161/19336896.2014.983754 |g p. 00 - 00 |0 PERI:(DE-600)2267671-5 |n 5 |p 344-358 |t Prion |v 8 |y 2014 |x 1933-690X |
| 856 | 4 | _ | |u http://www.tandfonline.com/action/showCitFormats?doi=10.4161%2F19336896.2014.983754 |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/173322/files/FZJ-2014-06732.pdf |y Restricted |
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| 913 | 2 | _ | |a DE-HGF |b Key Technologies |l BioSoft – Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences |1 G:(DE-HGF)POF3-550 |0 G:(DE-HGF)POF3-551 |2 G:(DE-HGF)POF3-500 |v Functional Macromolecules and Complexes |x 0 |
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