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 BemporadWriting – Review & Editing
;Cristina CecchiWriting – 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.File | Dimensione | Formato | |
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