Complex folding and misfolding effects of deer-specific amino acid substitutions in the β2-α2 loop of murine prion protein-Reference-Cited by-同舟云学术

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Complex folding and misfolding effects of deer-specific amino acid substitutions in the β2-α2 loop of murine prion protein

Published:2015-10-22 Issue:1 Volume:5 Page:
ISSN:2045-2322
Container-title:Scientific Reports
language:en
Short-container-title:Sci Rep

Author:

Agarwal Sonya,Döring Kristina,Gierusz Leszek A.,Iyer Pooja,Lane Fiona M.,Graham James F.,Goldmann Wilfred,Pinheiro Teresa J. T.,Gill Andrew C.

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/srep15528.pdf

Reference50 articles.

1. Gill, A. C., Lane, F. M., Alibhai, J., Manson, J. C. & McCutcheon, S. The mechanisms of Prion disease. CAB reviews 6, No. 55 (2011).

2. Prusiner, S. B. Prions. Proceedings of the National Academy of Sciences of the United States of America 95, 13363–13383 (1998).

3. Gill, A. C. et al. Post-translational hydroxylation at the N-terminus of the prion protein reveals presence of PPII structure in vivo. EMBO Journal 19, 5324–5331 (2000).

4. Taubner, L. M., Bienkiewicz, E. A., Copie, V. & Caughey, B. Structure of the Flexible Amino-Terminal Domain of Prion Protein Bound to a Sulfated Glycan. Journal of Molecular Biology 395, 475–490, 10.1016/j.jmb.2009.10.075 (2010).

5. Haire, L. F. et al. The crystal structure of the globular domain of sheep prion protein. Journal of Molecular Biology 336, 1175–1183 (2004).

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