Identification of transmissible proteotoxic oligomer-like fibrils that expand conformational diversity of amyloid assemblies
Nguyen et al identified cytotoxic amyloid fibrils with oligomer-like characteristics, which were assembled from an islet amyloid polypeptide (IAPP) derivative containing an Asn-to-Gln substitution (N21Q). They presented evidence to show that these stable fibrils expand the conformational diversity o...
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Nature Portfolio
2021
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oai:doaj.org-article:28feaf14cc72438f8c537516bcfa20272021-12-02T18:49:23ZIdentification of transmissible proteotoxic oligomer-like fibrils that expand conformational diversity of amyloid assemblies10.1038/s42003-021-02466-72399-3642https://doaj.org/article/28feaf14cc72438f8c537516bcfa20272021-08-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-02466-7https://doaj.org/toc/2399-3642Nguyen et al identified cytotoxic amyloid fibrils with oligomer-like characteristics, which were assembled from an islet amyloid polypeptide (IAPP) derivative containing an Asn-to-Gln substitution (N21Q). They presented evidence to show that these stable fibrils expand the conformational diversity of amyloid assemblies, which represents an opportunity to elucidate the structural basis of amyloid disorders.Phuong Trang NguyenXimena ZottigMathew SebastiaoAlexandre A. ArnoldIsabelle MarcotteSteve BourgaultNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-14 (2021) |
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Biology (General) QH301-705.5 |
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Biology (General) QH301-705.5 Phuong Trang Nguyen Ximena Zottig Mathew Sebastiao Alexandre A. Arnold Isabelle Marcotte Steve Bourgault Identification of transmissible proteotoxic oligomer-like fibrils that expand conformational diversity of amyloid assemblies |
description |
Nguyen et al identified cytotoxic amyloid fibrils with oligomer-like characteristics, which were assembled from an islet amyloid polypeptide (IAPP) derivative containing an Asn-to-Gln substitution (N21Q). They presented evidence to show that these stable fibrils expand the conformational diversity of amyloid assemblies, which represents an opportunity to elucidate the structural basis of amyloid disorders. |
format |
article |
author |
Phuong Trang Nguyen Ximena Zottig Mathew Sebastiao Alexandre A. Arnold Isabelle Marcotte Steve Bourgault |
author_facet |
Phuong Trang Nguyen Ximena Zottig Mathew Sebastiao Alexandre A. Arnold Isabelle Marcotte Steve Bourgault |
author_sort |
Phuong Trang Nguyen |
title |
Identification of transmissible proteotoxic oligomer-like fibrils that expand conformational diversity of amyloid assemblies |
title_short |
Identification of transmissible proteotoxic oligomer-like fibrils that expand conformational diversity of amyloid assemblies |
title_full |
Identification of transmissible proteotoxic oligomer-like fibrils that expand conformational diversity of amyloid assemblies |
title_fullStr |
Identification of transmissible proteotoxic oligomer-like fibrils that expand conformational diversity of amyloid assemblies |
title_full_unstemmed |
Identification of transmissible proteotoxic oligomer-like fibrils that expand conformational diversity of amyloid assemblies |
title_sort |
identification of transmissible proteotoxic oligomer-like fibrils that expand conformational diversity of amyloid assemblies |
publisher |
Nature Portfolio |
publishDate |
2021 |
url |
https://doaj.org/article/28feaf14cc72438f8c537516bcfa2027 |
work_keys_str_mv |
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