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.
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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).
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Freeman, M. Enzyme theory holds water. Nature 444, 153–155 (2006). https://doi.org/10.1038/nature05305
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DOI: https://doi.org/10.1038/nature05305