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      Common core structure of amyloid fibrils by synchrotron X-ray diffraction.

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          Abstract

          Tissue deposition of normally soluble proteins as insoluble amyloid fibrils is associated with serious diseases including the systemic amyloidoses, maturity onset diabetes, Alzheimer's disease and transmissible spongiform encephalopathy. Although the precursor proteins in different diseases do not share sequence homology or related native structure, the morphology and properties of all amyloid fibrils are remarkably similar. Using intense synchrotron sources we observed that six different ex vivo amyloid fibrils and two synthetic fibril preparations all gave similar high-resolution X-ray fibre diffraction patterns, consistent with a helical array of beta-sheets parallel to the fibre long axis, with the strands perpendicular to this axis. This confirms that amyloid fibrils comprise a structural superfamily and share a common protofilament substructure, irrespective of the nature of their precursor proteins.

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          Author and article information

          Journal
          J Mol Biol
          Journal of molecular biology
          Elsevier BV
          0022-2836
          0022-2836
          Oct 31 1997
          : 273
          : 3
          Affiliations
          [1 ] University of Oxford, Rex Richards Building, South Parks Road, Oxford, OX1 3QU, UK.
          Article
          S0022-2836(97)91348-6
          10.1006/jmbi.1997.1348
          9356260
          6d52b394-2532-4508-a8ff-660d8d6a4bd4
          Copyright 1997 Academic Press Limited.
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