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Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/100256
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dc.contributor.authorLiu, Y.-
dc.contributor.authorWang, T.-
dc.contributor.authorCalabrese, A.-
dc.contributor.authorCarver, J.-
dc.contributor.authorCummins, S.-
dc.contributor.authorBowie, J.-
dc.date.issued2015-
dc.identifier.citationPeptides, 2015; 73:1-6-
dc.identifier.issn0196-9781-
dc.identifier.issn1873-5169-
dc.identifier.urihttp://hdl.handle.net/2440/100256-
dc.description.abstractAbstract not available.-
dc.description.statementofresponsibilityYanqin Liu, Tianfang Wang, Antonio N. Calabrese, John A. Carver, Scott F. Cummins, John H. Bowie-
dc.language.isoen-
dc.publisherElsevier-
dc.rights© 2015 Elsevier Inc. All rights reserved.-
dc.source.urihttp://dx.doi.org/10.1016/j.peptides.2015.08.004-
dc.subjectAlzheimer’s disease; amyloid beta 1-42 (Aβ42); amyloid fibrils; caerin 1.8, an Aβ42 fibrilisation inhibitor; MALDI mass spectrometry: 1:1 adduct; [Aβ42/caerin 1.8]H+; MD simulation of 1:1 adduct in water-
dc.titleThe membrane-active amphibian peptide caerin 1.8 inhibits fibril formation of amyloid β1-42-
dc.title.alternativeThe membrane-active amphibian peptide caerin 1.8 inhibits fibril formation of amyloid beta1-42-
dc.typeJournal article-
dc.identifier.doi10.1016/j.peptides.2015.08.004-
dc.relation.grantARC-
pubs.publication-statusPublished-
Appears in Collections:Aurora harvest 3
Chemistry publications

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