Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/92452
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dc.contributor.authorElias, A.-
dc.contributor.authorScanlon, D.-
dc.contributor.authorMusgrave, I.-
dc.contributor.authorCarver, J.-
dc.date.issued2014-
dc.identifier.citationBBA: Proteins and Proteomics, 2014; 1844(9):1591-1598-
dc.identifier.issn1570-9639-
dc.identifier.issn1878-1454-
dc.identifier.urihttp://hdl.handle.net/2440/92452-
dc.description.abstractAbstract not available-
dc.description.statementofresponsibilityAbigail K. Elias, Denis Scanlon, Ian F. Musgrave, John A. Carver-
dc.language.isoen-
dc.publisherElsevier-
dc.rights© 2014 Published by Elsevier B.V.-
dc.source.urihttp://dx.doi.org/10.1016/j.bbapap.2014.06.006-
dc.subjectSEVI; Amyloid fibril; Cell toxicity; HIV; Protein aggregation-
dc.titleSEVI, the semen enhancer of HIV infection along with fragments from its central region, form amyloid fibrils that are toxic to neuronal cells-
dc.typeJournal article-
dc.identifier.doi10.1016/j.bbapap.2014.06.006-
pubs.publication-statusPublished-
dc.identifier.orcidMusgrave, I. [0000-0003-1016-0588]-
Appears in Collections:Aurora harvest 2
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