Assessing the causes and consequences of co-polymerization in amyloid formation

@inproceedings{Sarell2013AssessingTC,
  title={Assessing the causes and consequences of co-polymerization in amyloid formation},
  author={Claire J. Sarell and Peter G. Stockley and Sheena E Radford},
  booktitle={Prion},
  year={2013}
}
How, and why, different proteins form amyloid fibrils is most often studied in vitro using a single purified protein sequence. However, many amyloid diseases involve co-aggregation of different protein species, including proteins with/without post-translational modifications (e.g., different strains of PrP), proteins of different length (e.g., β₂-microglobulin and ΔN6, Aβ40, and Aβ42), sequence variants (e.g., Aβ and Aβ(ARC)), and proteins from different organisms (e.g., bovine PrP and human… CONTINUE READING

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