Results 1 to 10 of about 277,221 (202)
AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils
Nature Communications, 2021 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 ...
Akanksha Bansal +8 more
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Polymorphism of Amyloid Fibrils In Vivo [PDF]
Angewandte Chemie International Edition, 2016 AbstractPolymorphism is a wide‐spread feature of amyloid‐like fibrils formed in vitro, but it has so far remained unclear whether the fibrils formed within a patient are also affected by this phenomenon. In this study we show that the amyloid fibrils within a diseased individual can vary considerably in their three‐dimensional architecture.
Karthikeyan, Annamalai +10 more
openaire +3 more sources
Interfacial Electrostatic Self‐Assembly of Amyloid Fibrils into Multifunctional Protein Films
Advanced Science, 2023 Amyloid fibrils have generated steadily increasing traction in the development of natural and artificial materials. However, it remains a challenge to construct bulk amyloid films directly from amyloid fibrils due to their intrinsic brittleness.
Yangyang Han +2 more
exaly +2 more sources
Cryo-EM structure and polymorphism of Aβ amyloid fibrils purified from Alzheimer’s brain tissue
Nature Communications, 2019 Alzheimer’s disease is characterised by the deposition of Aβ amyloid fibrils and tau protein neurofibrillary tangles. Here the authors use cryo-EM to structurally characterise brain derived Aβ amyloid fibrils and find that they are polymorphic and right ...
Marius Kollmer +9 more
doaj +2 more sources
Structural diversity and polymorphism in amyloid fibrils from single organs and single patients with AL amyloidosis [PDF]
Structural DynamicsAmyloidogenic light chain (AL) amyloidosis is a complicated disease that results from aggregation of antibody light chain proteins into amyloid fibrils, that then disrupt organ function.
Parker T Bassett +4 more
doaj +2 more sources
Scientific Reports, 2017 Fluorescence of thioflavin T (ThT) is a proven tool for amyloid fibrils study. The correct model of ThT binding to fibrils is crucial to clarify amyloid fibrils structure and mechanism of their formation.
Anna I. Sulatskaya +4 more
doaj +2 more sources
Amyloid Fibrils from Hemoglobin [PDF]
Biomolecules, 2017 Amyloid fibrils are a class of insoluble protein nanofibers that are formed via the self-assembly of a wide range of peptides and proteins. They are increasingly exploited for a broad range of applications in bionanotechnology, such as biosensing and ...
Nadishka Jayawardena +7 more
doaj +3 more sources
Cathepsin B prevents cell death by fragmentation and destruction of pathological amyloid fibrils [PDF]
Cell Death DiscoveryAmyloid fibrils cause organ and tissue dysfunction in numerous severe diseases. Despite the prevalence and severity of amyloidoses, there is still no effective and safe anti-amyloid therapy.
Maksim I. Sulatsky +4 more
doaj +2 more sources
Food amyloid fibrils are safe nutrition ingredients based on in-vitro and in-vivo assessment
Nature Communications, 2023 Food protein amyloid fibrils have superior technological, nutritional, sensorial, and physical properties compared to native monomers, but there is as yet insufficient understanding of their digestive fate and safety for wide consumption.
Dan Xu +12 more
semanticscholar +1 more source
Plant Protein Amyloid Fibrils for Multifunctional Sustainable Materials
Advanced Sustainable Systems, 2023 Artificial functional materials based on amyloid fibrils are proven to be a promising strategy toward functional materials. However, scaling‐up applications present sustainability concerns, as animal proteins are the main sources for fabricating amyloid ...
Ting Li +8 more
semanticscholar +1 more source