AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils
Systemic AA amyloidosis is a protein misfolding disease caused by the formation of amyloid fibrils from serum amyloid A (SAA) protein. Here, the authors present the cryo-EM structures of AA amyloid fibrils isolated from mouse tissue and in vitro formed fibrils, which differ in their structures and t...
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Nature Portfolio
2021-02-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-021-21129-z |
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author | Akanksha Bansal Matthias Schmidt Matthies Rennegarbe Christian Haupt Falk Liberta Sabrina Stecher Ioana Puscalau-Girtu Alexander Biedermann Marcus Fändrich |
author_facet | Akanksha Bansal Matthias Schmidt Matthies Rennegarbe Christian Haupt Falk Liberta Sabrina Stecher Ioana Puscalau-Girtu Alexander Biedermann Marcus Fändrich |
author_sort | Akanksha Bansal |
collection | DOAJ |
description | Systemic AA amyloidosis is a protein misfolding disease caused by the formation of amyloid fibrils from serum amyloid A (SAA) protein. Here, the authors present the cryo-EM structures of AA amyloid fibrils isolated from mouse tissue and in vitro formed fibrils, which differ in their structures and they also show that the ex vivo fibrils are more resistant to proteolysis than the in vitro fibrils and propose that pathogenic amyloid fibrils might originate from proteolytic selection. |
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id | doaj.art-15b5d0653a7f4fee9b6e4b37a7961e1e |
institution | Directory Open Access Journal |
issn | 2041-1723 |
language | English |
last_indexed | 2024-12-19T08:20:15Z |
publishDate | 2021-02-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Nature Communications |
spelling | doaj.art-15b5d0653a7f4fee9b6e4b37a7961e1e2022-12-21T20:29:24ZengNature PortfolioNature Communications2041-17232021-02-011211910.1038/s41467-021-21129-zAA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrilsAkanksha Bansal0Matthias Schmidt1Matthies Rennegarbe2Christian Haupt3Falk Liberta4Sabrina Stecher5Ioana Puscalau-Girtu6Alexander Biedermann7Marcus Fändrich8Institute of Protein Biochemistry, Ulm UniversityInstitute of Protein Biochemistry, Ulm UniversityInstitute of Protein Biochemistry, Ulm UniversityInstitute of Protein Biochemistry, Ulm UniversityInstitute of Protein Biochemistry, Ulm UniversityInstitute of Protein Biochemistry, Ulm UniversityInstitute of Protein Biochemistry, Ulm UniversityInstitute of Protein Biochemistry, Ulm UniversityInstitute of Protein Biochemistry, Ulm UniversitySystemic AA amyloidosis is a protein misfolding disease caused by the formation of amyloid fibrils from serum amyloid A (SAA) protein. Here, the authors present the cryo-EM structures of AA amyloid fibrils isolated from mouse tissue and in vitro formed fibrils, which differ in their structures and they also show that the ex vivo fibrils are more resistant to proteolysis than the in vitro fibrils and propose that pathogenic amyloid fibrils might originate from proteolytic selection.https://doi.org/10.1038/s41467-021-21129-z |
spellingShingle | Akanksha Bansal Matthias Schmidt Matthies Rennegarbe Christian Haupt Falk Liberta Sabrina Stecher Ioana Puscalau-Girtu Alexander Biedermann Marcus Fändrich AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils Nature Communications |
title | AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils |
title_full | AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils |
title_fullStr | AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils |
title_full_unstemmed | AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils |
title_short | AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils |
title_sort | aa amyloid fibrils from diseased tissue are structurally different from in vitro formed saa fibrils |
url | https://doi.org/10.1038/s41467-021-21129-z |
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