Rational design of potent human transthyretin amyloid disease inhibitors

@article{Klabunde2000RationalDO,
  title={Rational design of potent human transthyretin amyloid disease inhibitors},
  author={Thomas Klabunde and H. Michael Petrassi and Vibha B. Oza and Prakash Raman and Jeffery W Kelly and James C. Sacchettini},
  journal={Nature Structural Biology},
  year={2000},
  volume={7},
  pages={312-321}
}
The human amyloid disorders, familial amyloid polyneuropathy, familial amyloid cardiomyopathy and senile systemic amyloidosis, are caused by insoluble transthyretin (TTR) fibrils, which deposit in the peripheral nerves and heart tissue. Several nonsteroidal anti-inflammatory drugs and structurally similar compounds have been found to strongly inhibit the formation of TTR amyloid fibrils in vitro. These include flufenamic acid, diclofenac, flurbiprofen, and resveratrol. Crystal structures of the… CONTINUE READING
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