Intramembrane proteases have attracted much attention because of their biological and medical value. The first crystal structure of one of these enzymes begins to solve the mystery of how they work.
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
Notes
This article and the paper concerned3 were published online on 11 October 2006.
References
Ehrmann, M. & Clausen, T. Annu. Rev. Genet. 38, 709–724 (2004).
Wolfe, M. S. & Kopan, R. Science 305, 1119–1123 (2004).
Wang, Y., Zhang, Y. & Ha, Y. Nature 444, 179–183 (2006).
Urban, S., Lee, J. R. & Freeman, M. Cell 107, 173–182 (2001).
Wasserman, J. D., Urban, S. & Freeman, M. Genes Dev. 14, 1651–1663 (2000).
Koonin, E. V. et al. Genome Biol. 4, R19 (2003).
Freeman, M. Nature Rev. Mol. Cell Biol. 5, 188–197 (2004).
Fersht, A. Structure and Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding (Freeman, New York, 1999).
Lemberg, M. K. et al. EMBO J. 24, 464–472 (2005).
Urban, S. & Wolfe, M. S. Proc. Natl Acad. Sci. USA 102, 1883–1888 (2005).
Lazarov, V. K. et al. Proc. Natl Acad. Sci. USA 103, 6889–6894 (2006).
Ogura, T. et al. Biochem. Biophys. Res. Commun. 343, 525–534 (2006).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Freeman, M. Enzyme theory holds water. Nature 444, 153–155 (2006). https://doi.org/10.1038/nature05305
Published:
Issue Date:
DOI: https://doi.org/10.1038/nature05305
