Various aberrant protein forms are the subject of intense research. It is not easy to probe their structures, but studies that have done so provide telling information about their biological properties.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
References
Dobson, C. M. Nature 426, 884–890 (2003).
Prusiner, S. Science 278, 245–251 (1997).
Tuite, M. F. & Cox, B. S. Nature Rev. Mol. Cell Biol. 4, 878–890 (2003).
Nelson, R. et al. Nature 435, 773–778 (2005).
Ritter, C. et al. Nature 435, 844–848 (2005).
Krishnan, R. & Lindquist, S. L. Nature 435, 765–772 (2005).
Selkoe, D. J. Nature 426, 900–904 (2003).
Caughey, B. Nature Med. 6, 751–754 (2000).
Sunde, M. & Blake, C. C. F. Adv. Protein Chem. 50, 123–159 (1997).
Jímenez, J. L. et al. Proc. Natl Acad. Sci. USA 99, 9196–9201 (2002).
Tanaka, M., Chien, P., Naber, N., Cooke, R. & Weissman, J. S. Nature 428, 323–328 (2004).
Petkova, A. T. et al. Science 307, 262–265 (2005).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Dobson, C. Prying into prions. Nature 435, 747–748 (2005). https://doi.org/10.1038/435747a
Published:
Issue Date:
DOI: https://doi.org/10.1038/435747a
This article is cited by
-
Molecular modeling to investigate the binding of Congo red toward GNNQQNY protofibril and in silico virtual screening for the identification of new aggregation inhibitors
Journal of Molecular Modeling (2013)
-
Failure of Alzheimer’s Aβ(1–40) amyloid nanofibrils under compressive loading
JOM (2010)
-
Koch’s postulates and infectious proteins
Acta Neuropathologica (2006)
