Gast ::
| Hauptseite > Publikationsdatenbank > Stoichiometric Zn 2+ interferes with the self-association of Aβ42: Insights from size distribution analysis > print |
| Hauptseite > Publikationsdatenbank > Stoichiometric Zn 2+ interferes with the self-association of Aβ42: Insights from size distribution analysis > print |
| 001 | 843873 | ||
| 005 | 20210129232710.0 | ||
| 024 | 7 | _ | |a 10.1016/j.ijbiomac.2018.02.123 |2 doi |
| 024 | 7 | _ | |a 0141-8130 |2 ISSN |
| 024 | 7 | _ | |a 1879-0003 |2 ISSN |
| 024 | 7 | _ | |a pmid:29476859 |2 pmid |
| 024 | 7 | _ | |a WOS:000432503100074 |2 WOS |
| 037 | _ | _ | |a FZJ-2018-01403 |
| 041 | _ | _ | |a English |
| 082 | _ | _ | |a 540 |
| 100 | 1 | _ | |a Zhang, Tao |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a Stoichiometric Zn 2+ interferes with the self-association of Aβ42: Insights from size distribution analysis |
| 260 | _ | _ | |a New York, NY [u.a.] |c 2018 |b Elsevier |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1526968818_12331 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a The abnormal aggregation of amyloid β (Aβ) peptides in the brain has been recognized as a central event in Alzheimer's disease (AD). Divalent metal ions such as Zn2+ have been shown to be closely involved in modulating Aβ self-association. Although the link between Zn2+ dyshomeostasis and brain Aβ deposition has been established, the effect of Zn2+ on the aggregation of Aβ is still incompletely clarified. By combining analytical ultracentrifugation (AUC), circular dichroism (CD) spectroscopy, thioflavin T (ThT) assay and atomic force microscopy (AFM) imaging, we analyzed the impact of stoichiometric Zn2+ on the aggregation process of Aβ42, the main toxic isoform of Aβ species in the brain. Aβ42 aggregates found in the presence of Zn2+ were smaller in size, non-fibrillary and showed less β-sheet structures than aggregates formed in absence of Zn2+. AUC showed that Zn2+ was capable of retaining monomeric Aβ42 in solution. Zn2+ chelation by EDTA totally reversed the inhibitory effect of Zn2+ on Aβ42 fibrillation. Our results provide further evidence that Zn2+ shifts the self-association of Aβ42 toward a non-fibrillary pathway by interfering with the aggregation process at multiple levels. |
| 536 | _ | _ | |a 553 - Physical Basis of Diseases (POF3-553) |0 G:(DE-HGF)POF3-553 |c POF3-553 |f POF III |x 0 |
| 588 | _ | _ | |a Dataset connected to CrossRef |
| 700 | 1 | _ | |a Pauly, Thomas |0 0000-0001-6556-7145 |b 1 |
| 700 | 1 | _ | |a Nagel-Steger, Luitgard |0 P:(DE-Juel1)162443 |b 2 |e Corresponding author |
| 773 | _ | _ | |a 10.1016/j.ijbiomac.2018.02.123 |g p. S0141813017348365 |0 PERI:(DE-600)1483284-7 |p 631-639 |t International journal of biological macromolecules |v 113 |y 2018 |x 0141-8130 |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/843873/files/Stoichiometric%20Zn%202%2B%20interferes%20with%20the%20self-association%20of%20A%CE%B242_%20Insights%20from%20size%20distribution%20analysis.pdf |y Restricted |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/843873/files/Stoichiometric%20Zn%202%2B%20interferes%20with%20the%20self-association%20of%20A%CE%B242_%20Insights%20from%20size%20distribution%20analysis.pdf?subformat=pdfa |x pdfa |y Restricted |
| 909 | C | O | |o oai:juser.fz-juelich.de:843873 |p VDB |
| 910 | 1 | _ | |a Forschungszentrum Jülich |0 I:(DE-588b)5008462-8 |k FZJ |b 0 |6 P:(DE-HGF)0 |
| 910 | 1 | _ | |a Forschungszentrum Jülich |0 I:(DE-588b)5008462-8 |k FZJ |b 2 |6 P:(DE-Juel1)162443 |
| 913 | 1 | _ | |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 |4 G:(DE-HGF)POF |3 G:(DE-HGF)POF3 |
| 914 | 1 | _ | |y 2018 |
| 915 | _ | _ | |a Nationallizenz |0 StatID:(DE-HGF)0420 |2 StatID |
| 915 | _ | _ | |a JCR |0 StatID:(DE-HGF)0100 |2 StatID |b INT J BIOL MACROMOL : 2015 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0200 |2 StatID |b SCOPUS |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0300 |2 StatID |b Medline |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0310 |2 StatID |b NCBI Molecular Biology Database |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0600 |2 StatID |b Ebsco Academic Search |
| 915 | _ | _ | |a Peer Review |0 StatID:(DE-HGF)0030 |2 StatID |b ASC |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0199 |2 StatID |b Thomson Reuters Master Journal List |
| 915 | _ | _ | |a WoS |0 StatID:(DE-HGF)0110 |2 StatID |b Science Citation Index |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0150 |2 StatID |b Web of Science Core Collection |
| 915 | _ | _ | |a WoS |0 StatID:(DE-HGF)0111 |2 StatID |b Science Citation Index Expanded |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)1030 |2 StatID |b Current Contents - Life Sciences |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)1050 |2 StatID |b BIOSIS Previews |
| 915 | _ | _ | |a IF < 5 |0 StatID:(DE-HGF)9900 |2 StatID |
| 920 | _ | _ | |l yes |
| 920 | 1 | _ | |0 I:(DE-Juel1)ICS-6-20110106 |k ICS-6 |l Strukturbiochemie |x 0 |
| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a VDB |
| 980 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
| 980 | _ | _ | |a UNRESTRICTED |
| 981 | _ | _ | |a I:(DE-Juel1)IBI-7-20200312 |
| Library | Collection | CLSMajor | CLSMinor | Language | Author |
|---|