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| Home > Publications database > Solid-state NMR reveals structural differences between fibrils of wild-type and disease-related A53T mutant alpha-synuclein > print |
| Home > Publications database > Solid-state NMR reveals structural differences between fibrils of wild-type and disease-related A53T mutant alpha-synuclein > print |
| 001 | 276 | ||
| 005 | 20200402205331.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:18539297 |
| 024 | 7 | _ | |2 DOI |a 10.1016/j.jmb.2008.05.026 |
| 024 | 7 | _ | |2 WOS |a WOS:000257564000002 |
| 024 | 7 | _ | |a altmetric:514845 |2 altmetric |
| 037 | _ | _ | |a PreJuSER-276 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 570 |
| 084 | _ | _ | |2 WoS |a Biochemistry & Molecular Biology |
| 100 | 1 | _ | |a Heise, H. |b 0 |u FZJ |0 P:(DE-Juel1)VDB77857 |
| 245 | _ | _ | |a Solid-state NMR reveals structural differences between fibrils of wild-type and disease-related A53T mutant alpha-synuclein |
| 260 | _ | _ | |a Amsterdam [u.a.] |b Elsevier |c 2008 |
| 300 | _ | _ | |a 444 - 450 |
| 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 Journal of Molecular Biology |x 0022-2836 |0 3552 |y 3 |v 380 |
| 500 | _ | _ | |a Record converted from VDB: 12.11.2012 |
| 520 | _ | _ | |a Fibrils from the Parkinson's-disease-related A53T mutant of alpha-synuclein were investigated by solid-state NMR spectroscopy, electron microscopy, and atomic force microscopy. Sequential solid-state NMR resonance assignments were obtained for a large fraction of the fibril core. Experiments conducted above and below the freezing point suggest that the fibrils contain regions with increased mobility and structural elements different from beta-strand character, in addition to the rigid beta-sheet-rich core region. As in earlier studies on wild-type alpha-synuclein, the C-terminus was found to be flexible and unfolded, whereas the main core region was highly rigid and rich in beta-sheets. Compared to fibrils from wild-type alpha-synuclein, the well-ordered beta-sheet region extends to at least L38 and L100. These results demonstrate that a disease-related mutant of alpha-synuclein differs in both aggregation kinetics and fibril structure. |
| 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 Amino Acid Sequence |
| 650 | _ | 2 | |2 MeSH |a Escherichia coli: genetics |
| 650 | _ | 2 | |2 MeSH |a Freezing |
| 650 | _ | 2 | |2 MeSH |a Humans |
| 650 | _ | 2 | |2 MeSH |a Microscopy, Atomic Force |
| 650 | _ | 2 | |2 MeSH |a Microscopy, Electron |
| 650 | _ | 2 | |2 MeSH |a Molecular Sequence Data |
| 650 | _ | 2 | |2 MeSH |a Mutation |
| 650 | _ | 2 | |2 MeSH |a Nuclear Magnetic Resonance, Biomolecular: methods |
| 650 | _ | 2 | |2 MeSH |a Parkinson Disease: genetics |
| 650 | _ | 2 | |2 MeSH |a Parkinson Disease: pathology |
| 650 | _ | 2 | |2 MeSH |a Protein Structure, Secondary |
| 650 | _ | 2 | |2 MeSH |a Recombinant Proteins: chemistry |
| 650 | _ | 2 | |2 MeSH |a Recombinant Proteins: metabolism |
| 650 | _ | 2 | |2 MeSH |a Recombinant Proteins: ultrastructure |
| 650 | _ | 2 | |2 MeSH |a alpha-Synuclein: chemistry |
| 650 | _ | 2 | |2 MeSH |a alpha-Synuclein: genetics |
| 650 | _ | 2 | |2 MeSH |a alpha-Synuclein: metabolism |
| 650 | _ | 2 | |2 MeSH |a alpha-Synuclein: ultrastructure |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Recombinant Proteins |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a alpha-Synuclein |
| 650 | _ | 7 | |a J |2 WoSType |
| 653 | 2 | 0 | |2 Author |a solid-state NMR |
| 653 | 2 | 0 | |2 Author |a amyloid |
| 653 | 2 | 0 | |2 Author |a Parkinson's disease |
| 653 | 2 | 0 | |2 Author |a alpha-synuclein |
| 653 | 2 | 0 | |2 Author |a AFM |
| 700 | 1 | _ | |a Celej, M.S. |b 1 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Becker, S. |b 2 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Riedel, D. |b 3 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Pelah, A. |b 4 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Kumar, A. |b 5 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Jovin, T.M. |b 6 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Baldus, M. |b 7 |0 P:(DE-HGF)0 |
| 773 | _ | _ | |a 10.1016/j.jmb.2008.05.026 |g Vol. 380, p. 444 - 450 |p 444 - 450 |q 380<444 - 450 |0 PERI:(DE-600)1355192-9 |t Journal of molecular biology |v 380 |y 2008 |x 0022-2836 |
| 856 | 7 | _ | |u http://dx.doi.org/10.1016/j.jmb.2008.05.026 |
| 909 | C | O | |o oai:juser.fz-juelich.de:276 |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)100532 |
| 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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