Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease
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چکیده
منابع مشابه
Review: structure of amyloid fibril in diseases
Tissue deposition of normally soluble proteins, or their fragments, as insoluble amyloid fibrils causes both acquired and hereditary systemic amyloidoses, which is usually fatal. Amyloid is associated with serious diseases such as Alzheimer’s disease, type 2 diabetes, Parkinson’s Disease, Huntington’s Disease, cancer and the transmissible spongiform encephalopathies. Information concerning the ...
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15 صفحه اولRecent atomic models of amyloid fibril structure.
Despite the difficulties associated with determining atomic-level structures for materials that are fibrous, structural biologists are making headway in understanding the architecture of amyloid-like fibrils. It has long been recognized that these fibrils contain a cross-beta spine, with beta-strands perpendicular to the fibril axis. Recently, atomic structures have been determined for some of ...
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Amyloid fibrils are deposited in a number of diseases, including Alzheimer's disease, Type 2 diabetes, and the transmissible spongiform encephalopathies (TSE). These insoluble deposits are formed from normally soluble proteins that assemble to form fibrous aggregates that accumulate in the tissues. Electron microscopy has been used as a tool to examine the structure and morphology of these aggr...
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ژورنال
عنوان ژورنال: Nature Structural & Molecular Biology
سال: 2015
ISSN: 1545-9993,1545-9985
DOI: 10.1038/nsmb.2991