Amyloid fibrils from the viewpoint of protein folding

@article{Ohnishi2003AmyloidFF,
  title={Amyloid fibrils from the viewpoint of protein folding},
  author={Satoshi Ohnishi and K. Takano},
  journal={Cellular and Molecular Life Sciences CMLS},
  year={2003},
  volume={61},
  pages={511-524}
}
  • S. Ohnishi, K. Takano
  • Published 2003
  • Chemistry, Medicine
  • Cellular and Molecular Life Sciences CMLS
In amyloid related diseases, proteins form fibrillar aggregates with highly ordered β-sheet structure regardless of their native conformations. Formation of such amyloid fibrils can be reproducible in vitro using isolated proteins/peptides, suggesting that amyloid fibril formation takes place as a result of protein conformational change. In vitro studies revealed that perturbation of the native structure is important for the fibril formation, and it is suggested that the mechanisms of amyloid… Expand
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