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Biochem Biophys Res Commun ; 409(3): 477-82, 2011 Jun 10.
Article in English | MEDLINE | ID: mdl-21600886

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.


Subject(s)
Amyloid beta-Peptides/chemistry , Amyloid beta-Peptides/toxicity , Neurons/drug effects , Peptide Fragments/chemistry , Peptide Fragments/toxicity , Recombinant Fusion Proteins/chemistry , Recombinant Fusion Proteins/toxicity , Amyloid beta-Peptides/genetics , Animals , Apoptosis , Cerebral Cortex/cytology , Maltose-Binding Proteins/chemistry , Maltose-Binding Proteins/genetics , Maltose-Binding Proteins/toxicity , Mice , Peptide Fragments/genetics , Protein Multimerization , Recombinant Fusion Proteins/genetics , Saccharomyces cerevisiae/drug effects , Solubility
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