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Showing 1–4 of 4 results
Advanced filters: Author: Matthies Rennegarbe Clear advanced filters
  • Systemic AA amyloidosis is caused by misfolding of the acute phase protein serum amyloid A1. Here the authors present the cryo-EM structures of murine and human AA amyloid fibrils that were isolated from tissue samples and describe how the fibrils differ in their fundamental structural properties.

    • Falk Liberta
    • Sarah Loerch
    • Matthias Schmidt
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-10
  • Here, the authors present the cryo-EM structure of in vitro amyloid fibrils from recombinant SAA1.1 protein that were formed by seeding with fibrils purified from systemic AA amyloidosis tissue. This in vitro fibril structure resembles the structure of the ex vivo fibrils but differs from unseeded in vitro fibrils. These findings show that fibril morphologies can be propagated in vitro by seeding.

    • Thomas Heerde
    • Matthies Rennegarbe
    • Marcus Fändrich
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-8
  • 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.

    • Akanksha Bansal
    • Matthias Schmidt
    • Marcus Fändrich
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-9