How many amyloid-β peptides can a neuron bind before it dies?

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Abstract

This Editorial highlights a study by Jana and coworkers published in the current issue of Journal of Neurochemistry, in which the authors performed a detailed, quantitative analysis to identify the Aβ oligomer causing neuronal cell death. While most studies so far aimed to determine the Aβ oligomer with highest toxicity using preformed and characterized Aβ oligomers added to cell cultures, this study established an approach to analyze Aβ oligomers bound to primary neurons. This may shed new light on how oligomeric status changes at the cell surface and if minor oligomeric species may account for measured effects. The authors' procedure allows to monitor the effects of different Aβ oligomers in parallel, constituting an important advancement in the research field.

Read the highlighted article ‘Membrane bound tetramer and trimer Aβ oligomeric species correlate with toxicity towards cultured neurons’ on page 594.

This Editorial highlights a study by Jana and coworkers published in the current issue of Journal of Neurochemistry, in which the authors performed a detailed, quantitative analysis to identify the Aβ oligomer causing neuronal cell death. While most studies so far aimed to determine the Aβ oligomer with highest toxicity using preformed and characterized Aβ oligomers added to cell cultures, this study established an approach to analyze Aβ oligomers bound to primary neurons. This may shed new light on how oligomeric status changes at the cell surface and if minor oligomeric species may account for measured effects. The authors' procedure allows to monitor the effects of different Aβ oligomers in parallel, constituting an important advancement in the research field.

Read the highlighted article ‘Membrane bound tetramer and trimer Aβ oligomeric species correlate with toxicity towards cultured neurons’ on page 594.

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