Structural diversity of ex vivo amyloid fibrils studied by cryo-electron microscopy.

@article{Jimnez2001StructuralDO,
  title={Structural diversity of ex vivo amyloid fibrils studied by cryo-electron microscopy.},
  author={Jos{\'e} Luis Dom{\'i}nguez Jim{\'e}nez and Glenys A Tennent and Mark B Pepys and Helen R Saibil},
  journal={Journal of molecular biology},
  year={2001},
  volume={311 2},
  pages={241-7}
}
Cryo-electron microscopy studies are presented on amyloid fibrils isolated from amyloidotic organs of two patients with different forms of hereditary non-neuropathic systemic amyloidosis, caused, respectively, by Leu60Arg apolipoprotein AI and Asp67His lysozyme. Although ex vivo amyloid fibrils were thought to be more uniform in structure than those assembled in vitro, our findings show that these fibrils are also quite variable in structure. Structural disorder and variability of the fibrils… CONTINUE READING

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