141
Views
3
CrossRef citations to date
0
Altmetric
Original Articles

Structural Characterization of Amyloidotic Antifreeze Protein Fibrils and Intermediates

&
Pages 1030-1033 | Published online: 20 Aug 2009

REFERENCES

  • Baskakov, I. V., Aagaard, C., Mehlhorn, I., Wille, H., Groth, D., Baldwin, M. A., Prusiner, S. B., and Cohen, F. E., 2000. Self-assembly of recombinant prion protein of 106 residues, Biochemistry 39 (2000), pp. 2792–2804.
  • Bendheim, P. E., Barry, R. A., DeArmond, S. J., Stites, D. P., and Prusiner, S. B., 1984. Antibodies to a scrapie prion protein, Nature 310 (1984), pp. 418–421.
  • http://www.statcan.ca/english/research/11-621-MIE/11-621-MIE2004010.htm, Boame, A., Parsons, W., and Trant, M. 2004. Mad cow disease and beef trade: An update.
  • Collinge, J., 2001. Prion diseases of humans and animals: Their causes and molecular basis, Annu. Rev. Neurosci. 24 (2001), pp. 519–550.
  • Egelman, E. H., 2007. Single-particle reconstruction from EM images of helical filaments, Curr. Opin. Struct. Biol. 17 (2007), pp. 556–561.
  • Eghiaian, F., 2005. Structuring the puzzle of prion propagation, Curr. Opin. Struct. Biol. 15 (2005), pp. 724–730.
  • Eghiaian, F., Grosclaude, J., Lesceu, S., Debey, P., Doublet, B., Treguer, E., Rezaei, H., and Knossow, M., 2004. Insight into the PrPC→PrPSc conversion from the structures of antibody-bound ovine prion scrapie-susceptibility variants, Proc. Natl. Acad. Sci. USA 101 (2004), pp. 10254–10259.
  • Graether, S. P., Slupsky, C. M., Davies, P. L., and Sykes, B. D., 2001. Structure of type I antifreeze protein and mutants in supercooled water, Biophys. J. 81 (2001), pp. 1677–1683.
  • Graether, S. P., Slupsky, C. M., and Sykes, B. D., 2003. Freezing of a fish antifreeze protein results in amyloid fibril formation, Biophys. J. 84 (2003), pp. 552–557.
  • Guo, M., Gorman, P. M., Rico, M., Chakrabartty, A., and Laurents, D. V., 2005. Charge substitution shows that repulsive electrostatic interactions impede the oligomerization of Alzheimer amyloid peptides, FEBS. Lett. 579 (2005), pp. 3574–3578.
  • Harrison, R. S., Sharpe, P. C., Singh, Y., and Fairlie, D. P., 2007. Amyloid peptides and proteins in review, Rev. Physiol. Biochem. Pharmacol. 159 (2007), pp. 1–77.
  • Hun, L. K., Nguyen, T. N., Damo, S. M., Mazur, T., Ball, H. L., Prusiner, S. B., Pines, A., and Wemmer, D. E., 2005. Solid-state NMR structural studies of the fibril form of a mutant mouse prion peptide PrP(89–143)(P101L), Solid State Nucl. Magn. Reson 29 (2005), pp. 183–190, .
  • Jeffrey, M., Goodbrand, I. A., and Goodsir, C. M., 1995. Pathology of the transmissible spongiform encephalopathies with special emphasis on ultrastructure, Micron 26 (1995), pp. 277–298.
  • Novitskaya, V., Bocharova, O. V., Bronstein, I., and Baskakov, I. V., 2006. Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons, J. Biol. Chem. 281 (2006), pp. 13828–13836.
  • Prusiner, S. B., 1997. Prion diseases and the BSE crisis, Science 278 (1997), pp. 245–251.
  • Sunde, M., Serpell, L. C., Bartlam, M., Fraser, P. E., Pepys, M. B., and Blake, C. C., 1997. Common core structure of amyloid fibrils by synchrotron X-ray diffraction, J. Mol. Biol. 273 (1997), pp. 729–739.
  • Walsh, D. M., and Selkoe, D. J., 2007. A beta oligomers—A decade of discovery, J. Neurochem. 101 (2007), pp. 1172–1184.
  • Wishart, D. S., and Sykes, B. D., 1994. The 13C chemical-shift index: A simple method for the identification of protein secondary structure using 13C chemical shifts, J. Biomol. NMR 4 (1994), pp. 171–180.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.