Influence of C-terminal truncation of murine Serum amyloid A on fibril structure
Abstract Amyloid A (AA) amyloidosis is a systemic protein misfolding disease affecting humans and other vertebrates. While the protein precursor in humans and mice is the acute-phase reactant serum amyloid A (SAA) 1.1, the deposited fibrils consist mainly of C-terminally truncated SAA fragments, ter...
Main Authors: | Matthies Rennegarbe, Inga Lenter, Angelika Schierhorn, Romy Sawilla, Christian Haupt |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Portfolio
2017-07-01
|
Series: | Scientific Reports |
Online Access: | https://doi.org/10.1038/s41598-017-06419-1 |
Similar Items
-
Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids
by: Falk Liberta, et al.
Published: (2019-03-01) -
AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils
by: Akanksha Bansal, et al.
Published: (2021-02-01) -
The AL Amyloid Fibril: Looking for a Link between Fibril Formation and Structure
by: Christian Haupt
Published: (2021-08-01) -
An atlas of amyloid aggregation: the impact of substitutions, insertions, deletions and truncations on amyloid beta fibril nucleation
by: Mireia Seuma, et al.
Published: (2022-11-01) -
A Novel Truncated Form of Serum Amyloid A in Kawasaki Disease.
by: John C Whitin, et al.
Published: (2016-01-01)