Search Results - "Rennegarbe, Matthies"

AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils by Bansal, Akanksha, Schmidt, Matthias, Rennegarbe, Matthies, Haupt, Christian, Liberta, Falk, Stecher, Sabrina, Puscalau-Girtu, Ioana, Biedermann, Alexander, Fändrich, Marcus

“…Systemic AA amyloidosis is a world-wide occurring protein misfolding disease of humans and animals. It arises from the formation of amyloid fibrils from serum…”
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Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids by Liberta, Falk, Loerch, Sarah, Rennegarbe, Matthies, Schierhorn, Angelika, Westermark, Per, Westermark, Gunilla T., Hazenberg, Bouke P. C., Grigorieff, Nikolaus, Fändrich, Marcus, Schmidt, Matthias

“…Systemic AA amyloidosis is a worldwide occurring protein misfolding disease of humans and animals. It arises from the formation of amyloid fibrils from the…”
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Cryo-EM demonstrates the in vitro proliferation of an ex vivo amyloid fibril morphology by seeding by Heerde, Thomas, Rennegarbe, Matthies, Biedermann, Alexander, Savran, Dilan, Pfeiffer, Peter B., Hitzenberger, Manuel, Baur, Julian, Puscalau-Girtu, Ioana, Zacharias, Martin, Schwierz, Nadine, Haupt, Christian, Schmidt, Matthias, Fändrich, Marcus

“…Several studies showed that seeding of solutions of monomeric fibril proteins with ex vivo amyloid fibrils accelerated the kinetics of fibril formation in…”
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Influence of C-terminal truncation of murine Serum amyloid A on fibril structure by Rennegarbe, Matthies, Lenter, Inga, Schierhorn, Angelika, Sawilla, Romy, Haupt, Christian

“…Amyloid A (AA) amyloidosis is a systemic protein misfolding disease affecting humans and other vertebrates. While the protein precursor in humans and mice is…”
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Morphological and primary structural consistency of fibrils from different AA patients (common variant) by Liberta, Falk, Rennegarbe, Matthies, Rösler, Reinhild, Bijzet, Johan, Wiese, Sebastian, Hazenberg, Bouke P.C., Fändrich, Marcus

“…Aims: To test the hypothesis that the fibril morphology and the fibril protein primary structure are conserved across different patients suffering from the…”
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