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...
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American Society for Biochemistry and Molecular Biology
2019
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ftpubmed:oai:pubmedcentral.nih.gov:6364781 2023-05-15T14:56:59+02:00 Capturing Aβ42 aggregation in the cell Bemporad, Francesco Cecchi, Cristina Chiti, Fabrizio 2019-02-01 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 en eng American Society for Biochemistry and Molecular Biology http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6364781/ http://www.ncbi.nlm.nih.gov/pubmed/30710006 http://dx.doi.org/10.1074/jbc.H119.007392 © 2019 Bemporad et al. Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc. Editors' Picks Highlights Text 2019 ftpubmed https://doi.org/10.1074/jbc.H119.007392 2019-02-10T01:44:55Z 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. Text Arctic PubMed Central (PMC) Arctic Journal of Biological Chemistry 294 5 1488 1489 |
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Editors' Picks Highlights |
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Editors' Picks Highlights Bemporad, Francesco Cecchi, Cristina Chiti, Fabrizio Capturing Aβ42 aggregation in the cell |
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Editors' Picks Highlights |
description |
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. |
format |
Text |
author |
Bemporad, Francesco Cecchi, Cristina Chiti, Fabrizio |
author_facet |
Bemporad, Francesco Cecchi, Cristina Chiti, Fabrizio |
author_sort |
Bemporad, Francesco |
title |
Capturing Aβ42 aggregation in the cell |
title_short |
Capturing Aβ42 aggregation in the cell |
title_full |
Capturing Aβ42 aggregation in the cell |
title_fullStr |
Capturing Aβ42 aggregation in the cell |
title_full_unstemmed |
Capturing Aβ42 aggregation in the cell |
title_sort |
capturing aβ42 aggregation in the cell |
publisher |
American Society for Biochemistry and Molecular Biology |
publishDate |
2019 |
url |
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 |
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Arctic |
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Arctic |
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Arctic |
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Arctic |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6364781/ http://www.ncbi.nlm.nih.gov/pubmed/30710006 http://dx.doi.org/10.1074/jbc.H119.007392 |
op_rights |
© 2019 Bemporad et al. Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc. |
op_doi |
https://doi.org/10.1074/jbc.H119.007392 |
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Journal of Biological Chemistry |
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294 |
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5 |
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1488 |
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1489 |
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1766329050647756800 |