Protein prenylation plays a key role in the localization and function of many proteins, but the number and identities of prenylated proteins are unknown. A new study uses a multidisciplinary approach to provide a broad yet detailed snapshot of prenylation within the mammalian proteome.
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References
Casey, P.J. Curr. Opin. Cell Biol. 6, 219–225 (1994).
Marshall, C.J. Science 259, 1865–1866 (1993).
Zhang, F.L. & Casey, P.J. Annu. Rev. Biochem. 65, 241–269 (1996).
Sebti, S.M. & Hamilton, A.D. Cancer Drug Discovery and Development Vol. 8 (ed. Teicher, B.A.) 280 (Humana Press, Totowa, New Jersey, USA, 2001).
Gelb, M.H. et al. Nat. Chem. Biol. 2, 518–528 (2006).
Nguyen, U. et al. Nat. Chem. Biol. 5, 227–235 (2009).
Troutman, J.M. et al. Bioconjug. Chem. 16, 1209–1217 (2005).
Kho, Y. et al. Proc. Natl. Acad. Sci. USA 101, 12479–12484 (2004).
Delahunty, C.M. & Yates, J.R. III. Biotechniques 43, 563–569 (2007).
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Hougland, J., Fierke, C. Getting a handle on protein prenylation. Nat Chem Biol 5, 197–198 (2009). https://doi.org/10.1038/nchembio0409-197
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DOI: https://doi.org/10.1038/nchembio0409-197
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