Oligomerization and toxicity of Aß fusion proteins
| dc.contributor.author | Caine, J. | |
| dc.contributor.author | Bharadwaj, Prashant | |
| dc.contributor.author | Sankovich, S. | |
| dc.contributor.author | Ciccotosto, G. | |
| dc.contributor.author | Streltsov, V. | |
| dc.contributor.author | Varghese, J. | |
| dc.date.accessioned | 2017-01-30T10:47:05Z | |
| dc.date.available | 2017-01-30T10:47:05Z | |
| dc.date.created | 2015-10-29T04:08:41Z | |
| dc.date.issued | 2011 | |
| dc.identifier.citation | Caine, J. and Bharadwaj, P. and Sankovich, S. and Ciccotosto, G. and Streltsov, V. and Varghese, J. 2011. Oligomerization and toxicity of Aß fusion proteins. Biochemical and Biophysical Research Communications. 409 (3): pp. 477-482. | |
| dc.identifier.uri | http://hdl.handle.net/20.500.11937/5565 | |
| dc.identifier.doi | 10.1016/j.bbrc.2011.05.029 | |
| dc.description.abstract |
This study has found that the Maltose binding protein Aß42 fusion protein (MBP-Aß42) forms soluble oligomers while the shorter MBP-Aß16 fusion and control MBP did not. MBP-Aß42, but neither MBP-Aß16 nor control MBP, was toxic in a dose-dependent manner in both yeast and primary cortical neuronal cells. This study demonstrates the potential utility of MBP-Aß42 as a reagent for drug screening assays in yeast and neuronal cell cultures and as a candidate for further Aß42 characterization. © 2011 . | |
| dc.title | Oligomerization and toxicity of Aß fusion proteins | |
| dc.type | Journal Article | |
| dcterms.source.volume | 409 | |
| dcterms.source.number | 3 | |
| dcterms.source.startPage | 477 | |
| dcterms.source.endPage | 482 | |
| dcterms.source.issn | 0006-291X | |
| dcterms.source.title | Biochemical and Biophysical Research Communications | |
| curtin.department | School of Biomedical Sciences | |
| curtin.accessStatus | Fulltext not available |
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