Amyloid fibril structure from the vascular variant of systemic AA amyloidosis

التفاصيل البيبلوغرافية
العنوان:	Amyloid fibril structure from the vascular variant of systemic AA amyloidosis
المؤلفون:	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
بيانات النشر:	Universität Ulm
سنة النشر:	2022
المجموعة:	OPARU (OPen Access Repository of Ulm University)
مصطلحات موضوعية:	Cryoelectron microscopy, Protein aggregation, PROTEIN AA, BETA, PATTERN, Pathogenesis, Pathogenese
الوصف:	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.
نوع الوثيقة:	article in journal/newspaper
وصف الملف:	application/pdf
اللغة:	English
Relation:	http://dx.doi.org/10.18725/OPARU-49156; http://nbn-resolving.de/urn:nbn:de:bsz:289-oparu-49232-4
DOI:	10.18725/OPARU-49156
الاتاحة:	https://doi.org/10.18725/OPARU-49156 http://nbn-resolving.de/urn:nbn:de:bsz:289-oparu-49232-4
Rights:	https://creativecommons.org/licenses/by/4.0/
رقم الانضمام:	edsbas.C5825A71
قاعدة البيانات:	BASE

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الوصف
DOI:	10.18725/OPARU-49156