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={Margaret Sunde and Louise C. Serpell and Mark Bartlam and Paul E. Fraser and Mark B. Pepys and Colin C. F. 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… 

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