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

@article{Sunde1997CommonCS,
  title={Common core structure of amyloid fibrils by synchrotron X-ray diffraction.},
  author={M. Sunde and L. Serpell and M. Bartlam and P. Fraser and M. Pepys and C. Blake},
  journal={Journal of molecular biology},
  year={1997},
  volume={273 3},
  pages={
          729-39
        }
}
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… Expand
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The protofilament substructure of amyloid fibrils.
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Structural polymorphism of Alzheimer Aβ and other amyloid fibrils
Direct visualisation of the beta-sheet structure of synthetic Alzheimer's amyloid.
Polymorphism in an amyloid-like fibril-forming model peptide.
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