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Oligomerization and toxicity of Aβ fusion proteins.

Authors :
Caine JM
Bharadwaj PR
Sankovich SE
Ciccotosto GD
Streltsov VA
Varghese J
Source :
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2011 Jun 10; Vol. 409 (3), pp. 477-82. Date of Electronic Publication: 2011 May 12.
Publication Year :
2011

Abstract

This study has found that the Maltose binding protein Aβ42 fusion protein (MBP-Aβ42) forms soluble oligomers while the shorter MBP-Aβ16 fusion and control MBP did not. MBP-Aβ42, but neither MBP-Aβ16 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-Aβ42 as a reagent for drug screening assays in yeast and neuronal cell cultures and as a candidate for further Aβ42 characterization.<br /> (Crown Copyright © 2011. Published by Elsevier Inc. All rights reserved.)

Details

Language :
English
ISSN :
1090-2104
Volume :
409
Issue :
3
Database :
MEDLINE
Journal :
Biochemical and biophysical research communications
Publication Type :
Academic Journal
Accession number :
21600886
Full Text :
https://doi.org/10.1016/j.bbrc.2011.05.029