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Banerjee, Sambhasan; Baur, Julian; Daniel, Christoph; Pfeiffer, Peter Benedikt; Hitzenberger, Manuel; Kuhn, Lukas; Wiese, Sebastian; Bijzet, Johan; Haupt, Christian; Amann, Kerstin U; Zacharias, Martin; Hazenberg, Bouke P C; Westermark, Gunilla T; Schmidt, Matthias; Fändrich, Marcus
Nature communications, 11/2022, Letnik: 13, Številka: 1Journal Article
Systemic AA amyloidosis is a debilitating protein misfolding disease in humans and animals. In humans, it occurs in two variants that are called 'vascular' and 'glomerular', depending on the main amyloid deposition site in the kidneys. Using cryo electron microscopy, we here show the amyloid fibril structure underlying the vascular disease variant. Fibrils purified from the tissue of such patients are mainly left-hand twisted and contain two non-equal stacks of fibril proteins. They contrast in these properties to the fibrils from the glomerular disease variant which are right-hand twisted and consist of two structurally equal stacks of fibril proteins. Our data demonstrate that the different disease variants in systemic AA amyloidosis are associated with different fibril morphologies.
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Dostop do baze podatkov JCR je dovoljen samo uporabnikom iz Slovenije. Vaš trenutni IP-naslov ni na seznamu dovoljenih za dostop, zato je potrebna avtentikacija z ustreznim računom AAI.
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JCR | SNIP | JCR | SNIP | JCR | SNIP | JCR | SNIP |
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in: SICRIS
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