On your histone mark, SET, methylate!

@inproceedings{Binda2013OnYH,
  title={On your histone mark, SET, methylate!},
  author={Olivier Binda},
  booktitle={Epigenetics},
  year={2013}
}
Lysine methylation of histones and non-histone proteins has emerged in recent years as a posttranslational modification with wide-ranging cellular implications beyond epigenetic regulation. The molecular interactions between lysine methyltransferases and their substrates appear to be regulated by posttranslational modifications surrounding the lysine methyl acceptor. Two very interesting examples of this cross-talk between methyl-lysine sites are found in the SET (Su(var)3-9, Enhancer-of-zeste… CONTINUE READING
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References

Publications referenced by this paper.
Showing 1-10 of 81 references

Regulation of DNMT1 stability through SET7-mediated lysine methylation in mammalian cells.

Proceedings of the National Academy of Sciences of the United States of America • 2009
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