Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • News & Views
  • Published:

Escaping amyloid fate

Small molecules that safely antagonize amyloidogenesis are desperately needed for many devastating disorders that plague humankind, including Alzheimer's and Parkinson's diseases. New work brings important mechanistic insights into how one promising candidate, (−)-epigallocatechin-3-gallate (EGCG), diverts amyloid-β and α-synuclein down innocuous folding trajectories at the expense of the deleterious states populated during amyloidogenesis.

This is a preview of subscription content, access via your institution

Relevant articles

Open Access articles citing this article.

Access options

Rent or buy this article

Prices vary by article type

from$1.95

to$39.95

Prices may be subject to local taxes which are calculated during checkout

Figure 1: Structure and mode of action of EGCG.

References

  1. Fink, A.L. Curr. Opin. Struct. Biol. 15, 35–41 (2005).

    Article  CAS  Google Scholar 

  2. Nelson, R. & Eisenberg, D. Adv. Protein Chem. 73, 235–282 (2006).

    Article  CAS  Google Scholar 

  3. Skovronsky, D.M., Lee, V.M.-Y. & Trojanowski, J.Q. Annu. Rev. Pathol. Mech. Dis. 1, 151–170 (2006).

    Article  CAS  Google Scholar 

  4. Dobson, C.M. Nature 432, 824–828 (2004).

    Article  CAS  Google Scholar 

  5. Ehrnhoefer, D.E. et al. Hum. Mol. Genet. 15, 2743–2751 (2006).

    Article  CAS  Google Scholar 

  6. Masuda, M. et al. Biochemistry 45, 6085–6094 (2006).

    Article  CAS  Google Scholar 

  7. Wang, H. et al. Proc. Natl. Acad. Sci. USA 105, 7159–7164 (2008).

    Article  CAS  Google Scholar 

  8. Ehrnhoefer, D.E. et al. Nat. Struct. Mol. Biol. 15, 558–566 (2008).

    Article  CAS  Google Scholar 

  9. Wells, J.A. & McClendon, C.L. Nature 450, 1001–1009 (2007).

    Article  CAS  Google Scholar 

  10. Krishnan, R. & Lindquist, S.L. Nature 435, 765–772 (2005).

    Article  CAS  Google Scholar 

  11. Petkova, A.T. et al. Science 307, 262–265 (2005).

    Article  CAS  Google Scholar 

  12. Kayed, R. et al. Science 300, 486–489 (2003).

    Article  CAS  Google Scholar 

  13. Pardridge, W.M. NeuroRx 2, 3–14 (2005).

    Article  Google Scholar 

  14. Yang, C.S., Maliakal, P. & Meng, X. Annu. Rev. Pharmacol. Toxicol. 42, 25–54 (2002).

    Article  CAS  Google Scholar 

  15. Hammarstrom, P., Wiseman, R.L., Powers, E.T. & Kelly, J.W. Science 299, 713–716 (2003).

    Article  Google Scholar 

  16. Bertoncini, C.W. et al. Proc. Natl. Acad. Sci. USA 102, 1430–1435 (2005).

    Article  CAS  Google Scholar 

  17. Del Mar, C., Greenbaum, E.A., Mayne, L., Englander, S.W. & Woods, V.L., Jr. Proc. Natl. Acad. Sci. USA 102, 15477–15482 (2005).

    Article  CAS  Google Scholar 

  18. Conway, K.A. et al. Proc. Natl. Acad. Sci. USA 97, 571–576 (2000).

    Article  CAS  Google Scholar 

  19. Bitan, G. et al. Proc. Natl. Acad. Sci. USA 100, 330–335 (2003).

    Article  CAS  Google Scholar 

  20. Cheon, M. et al. PLoS Comput. Biol. 3, e173 (2007).

    Article  Google Scholar 

  21. Behrends, C. et al. Mol. Cell 23, 887–897 (2006).

    Article  CAS  Google Scholar 

  22. Shorter, J. & Lindquist, S. Mol. Cell 23, 425–438 (2006).

    Article  CAS  Google Scholar 

  23. Evans, C.G., Wisen, S. & Gestwicki, J.E. J. Biol. Chem. 281, 33182–33191 (2006).

    Article  CAS  Google Scholar 

  24. Mereles, D., Wanker, E.E. & Katus, H.A. Clin. Res. Cardiol. published online, doi:10.1007/s00392-008-0649-6 (3 March 2008).

  25. Carulla, N. et al. Nature 436, 554–558 (2005).

    Article  CAS  Google Scholar 

  26. Shorter, J. & Lindquist, S. Nat. Rev. Genet. 6, 435–450 (2005).

    Article  CAS  Google Scholar 

Download references

Acknowledgements

We thank A. Gitler, M. Lemmon, S. Vashist, E. Sweeny and H. Wang for comments on the manuscript.

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Roberts, B., Shorter, J. Escaping amyloid fate. Nat Struct Mol Biol 15, 544–546 (2008). https://doi.org/10.1038/nsmb0608-544

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1038/nsmb0608-544

This article is cited by

Search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing