Polymorphism in an amyloid-like fibril-forming model peptide.

@article{Verel2008PolymorphismIA,
  title={Polymorphism in an amyloid-like fibril-forming model peptide.},
  author={Ren{\'e} Verel and Ivan T Tomka and Carlo Bertozzi and Riccardo Cadalbert and Richard A. Kammerer and Michel O. Steinmetz and Beat H Meier},
  journal={Angewandte Chemie},
  year={2008},
  volume={47 31},
  pages={5842-5}
}
The conversion of peptides or proteins from their soluble forms into amyloid fibrils is frequently associated with pathological conditions ranging from neurodegenerative disorders to systemic amyloidoses. Although amyloid fibrils and non-disease-associated amyloid-like fibrils can be formed by peptides and proteins that share no sequence identity, they display several common properties. One hallmark of amyloid and amyloid-like fibrils is their highly ordered organization into a laminated cross… CONTINUE READING
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