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Amyloids and protein aggregation
A general discovery in protein science in the past few decades has been the finding that a number of unrelated proteins and peptides all have a marked propensity to form amyloid fibrils in vivo and in vitro. These structures have become known as the pathological hallmark of some of the most prevalen...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society of Chemistry
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10284024/ https://www.ncbi.nlm.nih.gov/pubmed/37350828 http://dx.doi.org/10.1039/d2sc90225g |
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author | Linse, Sara Knowles, Tuomas |
author_facet | Linse, Sara Knowles, Tuomas |
author_sort | Linse, Sara |
collection | PubMed |
description | A general discovery in protein science in the past few decades has been the finding that a number of unrelated proteins and peptides all have a marked propensity to form amyloid fibrils in vivo and in vitro. These structures have become known as the pathological hallmark of some of the most prevalent neurodegenerative diseases. More recently, the process of amyloid formation has been demystified through a number of key mechanistic findings, some of which are highlighted in this themed collection. |
format | Online Article Text |
id | pubmed-10284024 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | The Royal Society of Chemistry |
record_format | MEDLINE/PubMed |
spelling | pubmed-102840242023-06-22 Amyloids and protein aggregation Linse, Sara Knowles, Tuomas Chem Sci Chemistry A general discovery in protein science in the past few decades has been the finding that a number of unrelated proteins and peptides all have a marked propensity to form amyloid fibrils in vivo and in vitro. These structures have become known as the pathological hallmark of some of the most prevalent neurodegenerative diseases. More recently, the process of amyloid formation has been demystified through a number of key mechanistic findings, some of which are highlighted in this themed collection. The Royal Society of Chemistry 2023-06-06 /pmc/articles/PMC10284024/ /pubmed/37350828 http://dx.doi.org/10.1039/d2sc90225g Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by/3.0/ |
spellingShingle | Chemistry Linse, Sara Knowles, Tuomas Amyloids and protein aggregation |
title | Amyloids and protein aggregation |
title_full | Amyloids and protein aggregation |
title_fullStr | Amyloids and protein aggregation |
title_full_unstemmed | Amyloids and protein aggregation |
title_short | Amyloids and protein aggregation |
title_sort | amyloids and protein aggregation |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10284024/ https://www.ncbi.nlm.nih.gov/pubmed/37350828 http://dx.doi.org/10.1039/d2sc90225g |
work_keys_str_mv | AT linsesara amyloidsandproteinaggregation AT knowlestuomas amyloidsandproteinaggregation |