A potent and selective inhibitor of protein SUMOylation, a ubiquitin-like post-translational modification, has been developed, shedding light on the potential for developing new classes of anticancer therapeutics.
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References
He, X. et al. Nat. Chem. Biol. 13, 1164–1171 (2017).
Gareau, J.R. & Lima, C.D. Nat. Rev. Mol. Cell Biol. 11, 861–871 (2010).
Geiss-Friedlander, R. & Melchior, F. Nat. Rev. Mol. Cell Biol. 8, 947–956 (2007).
Kessler, J.D. et al. Science 335, 348–353 (2012).
Yu, B. et al. Proc. Natl. Acad. Sci. USA 112, E1724–E1733 (2015).
Brownell, J.E. et al. Mol. Cell 37, 102–111 (2010).
Soucy, T.A. et al. Nature 458, 732–736 (2009).
Demarque, M.D. et al. Gastroenterology 140, 286–296 (2011).
Becker, J. et al. Nat. Struct. Mol. Biol. 20, 525–531 (2013).
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Schneekloth, J. Controlling protein SUMOylation. Nat Chem Biol 13, 1141–1142 (2017). https://doi.org/10.1038/nchembio.2496
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DOI: https://doi.org/10.1038/nchembio.2496