Capturing Aβ42 aggregation in the cell
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 moni...
| Published in: | Journal of Biological Chemistry |
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| Main Authors: | , , |
| Format: | Text |
| Language: | English |
| Published: |
American Society for Biochemistry and Molecular Biology
2019
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| Subjects: | |
| Online Access: | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6364781/ http://www.ncbi.nlm.nih.gov/pubmed/30710006 https://doi.org/10.1074/jbc.H119.007392 |
| Summary: | 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. |
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