Novel imaging techniques with ever-increasing resolution are invaluable tools for the study of protein deposition, as they allow the self-assembly of proteins to be directly investigated in living cells. For the first time, the acceleration in Aβ42 aggregation induced by the Arctic mutation was monitored in cells, revealing a number of distinct morphologies that form sequentially. This approach will help discriminate the impacts of mutations on amyloid protein processing, Aβ aggregation propensity, and other mechanistic outcomes.

Capturing Aβ42 aggregation in the cell / Francesco Bemporad, Cristina Cecchi, Fabrizio Chiti. - In: JOURNAL OF BIOLOGICAL CHEMISTRY. - ISSN 1083-351X. - STAMPA. - 294:(2019), pp. 1488-1489. [10.1074/jbc.H119.007392]

Capturing Aβ42 aggregation in the cell

Francesco Bemporad
Writing – Review & Editing
;
Cristina Cecchi
Writing – Review & Editing
;
Fabrizio Chiti
Writing – Review & Editing
2019

Abstract

Novel imaging techniques with ever-increasing resolution are invaluable tools for the study of protein deposition, as they allow the self-assembly of proteins to be directly investigated in living cells. For the first time, the acceleration in Aβ42 aggregation induced by the Arctic mutation was monitored in cells, revealing a number of distinct morphologies that form sequentially. This approach will help discriminate the impacts of mutations on amyloid protein processing, Aβ aggregation propensity, and other mechanistic outcomes.
2019
294
1488
1489
Francesco Bemporad, Cristina Cecchi, Fabrizio Chiti
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/1148758
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