Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure. Architecture of Ure2p prion filaments: the N-terminal domains form a central core fiber. Cross-β order and diversity in nanocrystals of an amyloid-forming peptide. An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated β-sheet structure for amyloid. Structure of the cross-β spine of amyloid-like fibrils. General structural motifs of amyloid protofilaments. Aβ amyloid fibrils possess a core structure highly resistant to hydrogen exchange. Mapping Aβ amyloid fibril secondary structure using scanning proline mutagenesis. Polymorphic fibril formation by residues 10–40 of the Alzheimer’s β-amyloid peptide. Structural and dynamic features of Alzheimer’s Aβ peptide in amyloid fibrils studied by site-directed spin labeling. 3D structure of Alzheimer’s amyloid-β(1–42) fibrils. Structural insights into a yeast prion illuminate nucleation and strain diversity. High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy. A structural model for Alzheimer’s β-amyloid fibrils based on experimental constraints from solid state NMR. New model for crystalline polyglutamine assemblies and their connection with amyloid fibrils. Correlation of structural elements and infectivity of the HET-s prion. Common core structure of amyloid fibrils by synchrotron X-ray diffraction. X-ray diffraction studies on amyloid filaments. The structure of amyloid fibrils by electron microscopy and X-ray diffraction. The X-ray interpretation of denaturation and the structure of the seed globulins. Amyloid fibrillogenesis: themes and variations. Electron microscopic observations on a fibrous component in amyloid of diverse origins. Report from the Nomenclature Committee of the International Society of Amyloidosis. Amyloid: toward terminology clarification. Aspects on human amyloid forms and their fibril polypeptides. Structures of 13 of these microcrystals all reveal steric zippers, but with variations that expand the range of atomic architectures for amyloid-like fibrils and offer an atomic-level hypothesis for the basis of prion strains. These include segments from the Alzheimer’s amyloid-β and tau proteins, the PrP prion protein, insulin, islet amyloid polypeptide (IAPP), lysozyme, myoglobin, α-synuclein and β 2-microglobulin, suggesting that common structural features are shared by amyloid diseases at the molecular level. Here we report some 30 other segments from fibril-forming proteins that form amyloid-like fibrils, microcrystals, or usually both. It is a pair of β-sheets, with the facing side chains of the two sheets interdigitated in a dry ‘steric zipper’. The atomic architecture of a spine, from the fibril-forming segment GNNQQNY of the yeast prion protein Sup35, was recently revealed by X-ray microcrystallography. Amyloid fibrils formed from different proteins, each associated with a particular disease, contain a common cross-β spine.
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