Identification of a CARM1 Inhibitor with Potent In Vitro and In Vivo Activity in Preclinical Models of Multiple Myeloma
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/s41598-017-18446-z.pdf
Reference65 articles.
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2. Wolf, S. S. The protein arginine methyltransferase family: an update about function, new perspectives and the physiological role in humans. Cell Mol Life Sci 66, 2109–2121, https://doi.org/10.1007/s00018-009-0010-x (2009).
3. Shishkova, E. et al. Global mapping of CARM1 substrates defines enzyme specificity and substrate recognition. Nat Commun 8, 15571, https://doi.org/10.1038/ncomms15571 (2017).
4. Schurter, B. T. et al. Methylation of histone H3 by coactivator-associated arginine methyltransferase 1. Biochemistry 40, 5747–5756, doi:bi002631b [pii] (2001).
5. Wu, J., Cui, N., Wang, R., Li, J. & Wong, J. A role for CARM1-mediated histone H3 arginine methylation in protecting histone acetylation by releasing corepressors from chromatin. PLoS One 7, e34692, https://doi.org/10.1371/journal.pone.0034692PONE-D-11-24591 (2012).
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