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- W2167869105 abstract "Amyloid fibrils are ordered polymers in which constituent polypeptides adopt a non-native fold. Despite their importance in degenerative human diseases, the overall structure of amyloid fibrils remains unknown. High-resolution studies of model peptide assemblies have identified residues forming cross-beta-strands and have revealed some details of local beta-strand packing. However, little is known about the assembly contacts that define the fibril architecture. Here we present a set of three-dimensional structures of amyloid fibrils formed from full-length beta(2)-microglobulin, a 99-residue protein involved in clinical amyloidosis. Our cryo-electron microscopy maps reveal a hierarchical fibril structure built from tetrameric units of globular density, with at least three different subunit interfaces in this homopolymeric assembly. These findings suggest a more complex superstructure for amyloid than hitherto suspected and prompt a re-evaluation of the defining features of the amyloid fold." @default.
- W2167869105 created "2016-06-24" @default.
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- W2167869105 date "2009-05-01" @default.
- W2167869105 modified "2023-09-27" @default.
- W2167869105 title "Globular Tetramers of β2-Microglobulin Assemble into Elaborate Amyloid Fibrils" @default.
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- W2167869105 doi "https://doi.org/10.1016/j.jmb.2009.03.066" @default.
- W2167869105 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2726924" @default.
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- W2167869105 hasPublicationYear "2009" @default.
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