Identification of transmissible proteotoxic oligomer-like fibrils that expand conformational diversity of amyloid assemblies

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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Main Authors: Phuong Trang Nguyen, Ximena Zottig, Mathew Sebastiao, Alexandre A. Arnold, Isabelle Marcotte, Steve Bourgault
Format: Article
Language:English
Published: Nature Publishing Group 2021-08-01
Series:Communications Biology
Online Access:https://doi.org/10.1038/s42003-021-02466-7
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spelling doaj-28feaf14cc72438f8c537516bcfa20272021-08-08T11:11:44ZengNature Publishing GroupCommunications Biology2399-36422021-08-014111410.1038/s42003-021-02466-7Identification of transmissible proteotoxic oligomer-like fibrils that expand conformational diversity of amyloid assembliesPhuong Trang Nguyen0Ximena Zottig1Mathew Sebastiao2Alexandre A. Arnold3Isabelle Marcotte4Steve Bourgault5Department of Chemistry, Université du Québec à MontréalDepartment of Chemistry, Université du Québec à MontréalDepartment of Chemistry, Université du Québec à MontréalDepartment of Chemistry, Université du Québec à MontréalDepartment of Chemistry, Université du Québec à MontréalDepartment of Chemistry, Université du Québec à MontréalNguyen 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.https://doi.org/10.1038/s42003-021-02466-7
collection DOAJ
language English
format Article
sources DOAJ
author Phuong Trang Nguyen
Ximena Zottig
Mathew Sebastiao
Alexandre A. Arnold
Isabelle Marcotte
Steve Bourgault
spellingShingle 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
Communications Biology
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 Publishing Group
series Communications Biology
issn 2399-3642
publishDate 2021-08-01
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.
url https://doi.org/10.1038/s42003-021-02466-7
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