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| 001 | 12607 | ||
| 005 | 20200402205930.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:20822103 |
| 024 | 7 | _ | |2 DOI |a 10.1021/ja103725c |
| 024 | 7 | _ | |2 WOS |a WOS:000282304000055 |
| 024 | 7 | _ | |a altmetric:3315919 |2 altmetric |
| 037 | _ | _ | |a PreJuSER-12607 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 540 |
| 084 | _ | _ | |2 WoS |a Chemistry, Multidisciplinary |
| 100 | 1 | _ | |a Strodel, B. |b 0 |u FZJ |0 P:(DE-Juel1)132024 |
| 245 | _ | _ | |a Transmembrane Structures for Alzheimer’s Aß1-42 Oligomers |
| 260 | _ | _ | |a Washington, DC |b American Chemical Society |c 2010 |
| 300 | _ | _ | |a 13300 - 13312 |
| 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 the American Chemical Society |x 0002-7863 |0 23404 |y 38 |v 132 |
| 500 | _ | _ | |a B.S. gratefully acknowledges the Julich Supercomputing Centre for providing and maintaining the computing resources used in this work. C.S.W. thanks the EPSRC for financial support. |
| 520 | _ | _ | |a We model oligomers of the Alzheimer's amyloid β-peptide Aβ(1-42) in an implicit membrane to obtain insight into the mechanism of amyloid toxicity. It has been suggested that Aβ oligomers are the toxic species, causing membrane disruption in neuronal cells due to pore formation. We use basin-hopping global optimization to identify the most stable structures for the Aβ(1-42) peptide monomer and small oligomers up to the octamer inserted into a lipid bilayer. To improve the efficacy of the basin-hopping approach, we introduce a basin-hopping parallel tempering scheme and an oligomer generation procedure. The most stable membrane-spanning structure for the monomer is identified as a β-sheet, which exhibits the typical strand-turn-strand motif observed in NMR experiments. We find ordered β-sheets for the dimer to the hexamer, whereas for the octamer, we observe that the ordered structures separate into distinct tetrameric units that are rotated or shifted with respect to each other. This effect leads to an increase in favorable peptide-peptide interactions, thereby stabilizing the membrane-inserted octamer. On the basis of these results, we suggest that Aβ pores may consist of tetrameric and hexameric β-sheet subunits. These Aβ pore models are consistent with the results of biophysical and biochemical experiments. |
| 536 | _ | _ | |a Funktion und Dysfunktion des Nervensystems |c P33 |2 G:(DE-HGF) |0 G:(DE-Juel1)FUEK409 |x 0 |
| 536 | _ | _ | |a BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung |c P45 |0 G:(DE-Juel1)FUEK505 |x 1 |
| 588 | _ | _ | |a Dataset connected to Web of Science, Pubmed |
| 650 | _ | 2 | |2 MeSH |a Amyloid beta-Peptides: chemistry |
| 650 | _ | 2 | |2 MeSH |a Biopolymers: chemistry |
| 650 | _ | 2 | |2 MeSH |a Models, Molecular |
| 650 | _ | 2 | |2 MeSH |a Nuclear Magnetic Resonance, Biomolecular |
| 650 | _ | 2 | |2 MeSH |a Peptide Fragments: chemistry |
| 650 | _ | 2 | |2 MeSH |a Protein Conformation |
| 650 | _ | 2 | |2 MeSH |a Thermodynamics |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Amyloid beta-Peptides |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Biopolymers |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Peptide Fragments |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a amyloid beta-protein (1-42) |
| 650 | _ | 7 | |a J |2 WoSType |
| 700 | 1 | _ | |a Lee, J.W.L. |b 1 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Whittleston, C.S. |b 2 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Wales, D.J. |b 3 |0 P:(DE-HGF)0 |
| 773 | _ | _ | |a 10.1021/ja103725c |g Vol. 132, p. 13300 - 13312 |p 13300 - 13312 |q 132<13300 - 13312 |0 PERI:(DE-600)1472210-0 |t Journal of the American Chemical Society |v 132 |y 2010 |x 0002-7863 |
| 856 | 7 | _ | |u http://dx.doi.org/10.1021/ja103725c |
| 909 | C | O | |o oai:juser.fz-juelich.de:12607 |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 |
| 913 | 1 | _ | |k P45 |v BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung |l Biologische Informationsverarbeitung |b Schlüsseltechnologien |0 G:(DE-Juel1)FUEK505 |x 1 |
| 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)POF3-553 |2 G:(DE-HGF)POF3-500 |v Physical Basis of Diseases |x 0 |
| 914 | 1 | _ | |y 2010 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0010 |a JCR/ISI refereed |
| 920 | 1 | _ | |k ISB-3 |l Strukturbiochemie |d 31.12.2010 |g ISB |0 I:(DE-Juel1)VDB942 |x 0 |
| 970 | _ | _ | |a VDB:(DE-Juel1)124311 |
| 980 | _ | _ | |a VDB |
| 980 | _ | _ | |a ConvertedRecord |
| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
| 980 | _ | _ | |a UNRESTRICTED |
| 981 | _ | _ | |a I:(DE-Juel1)IBI-7-20200312 |
| 981 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
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