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| Home > Publications database > Mechanisms of prion protein assembly into amyloid > print |
| 001 | 62861 | ||
| 005 | 20200402210514.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:18268326 |
| 024 | 7 | _ | |2 pmc |a pmc:PMC2268150 |
| 024 | 7 | _ | |2 DOI |a 10.1073/pnas.0712036105 |
| 024 | 7 | _ | |2 WOS |a WOS:000253469900031 |
| 024 | 7 | _ | |a altmetric:21819146 |2 altmetric |
| 037 | _ | _ | |a PreJuSER-62861 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 000 |
| 084 | _ | _ | |2 WoS |a Multidisciplinary Sciences |
| 100 | 1 | _ | |a Stöhr, J. |b 0 |0 P:(DE-HGF)0 |
| 245 | _ | _ | |a Mechanisms of prion protein assembly into amyloid |
| 260 | _ | _ | |a Washington, DC |b Academy |c 2008 |
| 300 | _ | _ | |a 2409 - 2414 |
| 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 |y 7 |v 105 |
| 500 | _ | _ | |a Record converted from VDB: 12.11.2012 |
| 520 | _ | _ | |a The conversion of the alpha-helical, cellular isoform of the prion protein (PrP(C)) to the insoluble, beta-sheet-rich, infectious, disease-causing isoform (PrP(Sc)) is the key event in prion diseases. In an earlier study, several forms of PrP were converted into a fibrillar state by using an in vitro conversion system consisting of low concentrations of SDS and 250 mM NaCl. Here, we characterize the structure of the fibril precursor state, that is, the soluble state under fibrillization conditions. CD spectroscopy, analytical ultracentrifugation, and chemical cross-linking indicate that the precursor state exists in a monomer-dimer equilibrium of partially denatured, alpha-helical PrP, with a well defined contact site of the subunits in the dimer. Using fluorescence with thioflavin T, we monitored and quantitatively described the kinetics of seeded fibril formation, including dependence of the reaction on substrate and seed concentrations. Exponential, seed-enhanced growth can be achieved in homogeneous solution, which can be enhanced by sonication. From these data, we propose a mechanistic model of fibrillization, including the presence of several intermediate structures. These studies also provide a simplified amplification system for prions. |
| 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: chemistry |
| 650 | _ | 2 | |2 MeSH |a Amyloid: metabolism |
| 650 | _ | 2 | |2 MeSH |a Amyloid: ultrastructure |
| 650 | _ | 2 | |2 MeSH |a Circular Dichroism |
| 650 | _ | 2 | |2 MeSH |a Cross-Linking Reagents: chemistry |
| 650 | _ | 2 | |2 MeSH |a Dimerization |
| 650 | _ | 2 | |2 MeSH |a Microscopy, Electron |
| 650 | _ | 2 | |2 MeSH |a Prions: chemistry |
| 650 | _ | 2 | |2 MeSH |a Prions: metabolism |
| 650 | _ | 2 | |2 MeSH |a Prions: ultrastructure |
| 650 | _ | 2 | |2 MeSH |a Ultracentrifugation |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Amyloid |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Cross-Linking Reagents |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Prions |
| 650 | _ | 7 | |a J |2 WoSType |
| 700 | 1 | _ | |a Weinmann, N. |b 1 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Wille, H. |b 2 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Kaimann, K. |b 3 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Nagel-Steger, L. |b 4 |u FZJ |0 P:(DE-Juel1)VDB72731 |
| 700 | 1 | _ | |a Birkmann, E. |b 5 |u FZJ |0 P:(DE-Juel1)VDB65870 |
| 700 | 1 | _ | |a Panza, G. |b 6 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Prusinder, S. B. |b 7 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Eigen, M. |b 8 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Riesner, D. |b 9 |0 P:(DE-HGF)0 |
| 773 | _ | _ | |a 10.1073/pnas.0712036105 |g Vol. 105, p. 2409 - 2414 |p 2409 - 2414 |q 105<2409 - 2414 |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/PMC2268150 |
| 909 | C | O | |o oai:juser.fz-juelich.de:62861 |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)99742 |
| 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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