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DC Field | Value | Language |
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dc.citation.endPage | 1127 | - |
dc.citation.number | 8 | - |
dc.citation.startPage | 1116 | - |
dc.citation.title | METALLOMICS | - |
dc.citation.volume | 10 | - |
dc.contributor.author | Lee, Hyuck Jin | - |
dc.contributor.author | Savelieff, Masha G. | - |
dc.contributor.author | Kang, Juhye | - |
dc.contributor.author | Brophy, Megan Brunjes | - |
dc.contributor.author | Nakashige, Toshiki G. | - |
dc.contributor.author | Lee, Shin Jung C. | - |
dc.contributor.author | Nolan, Elizabeth M. | - |
dc.contributor.author | Lim, Mi Hee | - |
dc.date.accessioned | 2023-12-21T20:18:27Z | - |
dc.date.available | 2023-12-21T20:18:27Z | - |
dc.date.created | 2018-09-19 | - |
dc.date.issued | 2018-08 | - |
dc.description.abstract | Proteins from the S100 family perform numerous functions and may contribute to Alzheimer's disease (AD). Herein, we report the effects of S100A8/S100A9 heterooligomer calprotectin (CP) and the S100B homodimer on metal-free and metal-bound amyloid- (A; A(40) and A(42)) aggregation in vitro. Studies performed with CP-Ser [S100A8(C42S)/S100A9(C3S) oligomer] indicate that the protein influences the aggregation profile for A(40) in both the absence and presence of metal ions [i.e., Zn(ii) and Cu(ii)]. Moreover, the detection of A(40)-CP-Ser complexes by mass spectrometry suggests a direct interaction as a possible mechanism for the involvement of CP in A(40) aggregation. Although the interaction of CP-Ser with A(40) impacts A(40) aggregation in vitro, the protein does not attenuate A-induced toxicity in SH-SY5Y cells. In contrast, S100B has a slight effect on the aggregation of A. Overall, this work supports a potential association of CP with A in the absence and presence of metal ions in AD. | - |
dc.identifier.bibliographicCitation | METALLOMICS, v.10, no.8, pp.1116 - 1127 | - |
dc.identifier.doi | 10.1039/c8mt00091c | - |
dc.identifier.issn | 1756-5901 | - |
dc.identifier.scopusid | 2-s2.0-85051490052 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/24920 | - |
dc.identifier.url | http://pubs.rsc.org/en/Content/ArticleLanding/2018/MT/C8MT00091C#!divAbstract | - |
dc.identifier.wosid | 000442510900008 | - |
dc.language | 영어 | - |
dc.publisher | ROYAL SOC CHEMISTRY | - |
dc.title | Calprotectin influences the aggregation of metal-free and metal-bound amyloid- beta by direct interaction | - |
dc.type | Article | - |
dc.description.isOpenAccess | FALSE | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordPlus | HUMAN SERUM-ALBUMIN | - |
dc.subject.keywordPlus | ALZHEIMERS-DISEASE | - |
dc.subject.keywordPlus | A-BETA | - |
dc.subject.keywordPlus | S100 PROTEINS | - |
dc.subject.keywordPlus | INFLAMMATORY S100A9 | - |
dc.subject.keywordPlus | FIBRIL FORMATION | - |
dc.subject.keywordPlus | ZINC-BINDING | - |
dc.subject.keywordPlus | MOUSE MODEL | - |
dc.subject.keywordPlus | IN-VITRO | - |
dc.subject.keywordPlus | PEPTIDE | - |
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