Probing the conformation of the prion protein within a single amyloid fibril using a novel immunoconformational assay.

@article{Novitskaya2006ProbingTC,
  title={Probing the conformation of the prion protein within a single amyloid fibril using a novel immunoconformational assay.},
  author={Vera A. Novitskaya and N. Makarava and Anne Bellon and Olga V. Bocharova and Igor B. Bronstein and Richard A. Williamson and Ilia V Baskakov},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 22},
  pages={15536-45}
}
The coexistence of multiple strains or subtypes of the disease-related isoform of prion protein (PrP) in natural isolates, together with the observed conformational heterogeneity of PrP amyloid fibrils generated in vitro, indicates the importance of probing the conformation of single particles within heterogeneous samples. Using an array of PrP-specific antibodies, we report the development of a novel immunoconformational assay. Uniquely, application of this new technology allows the… CONTINUE READING

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