mAM Facilitates Conversion by ESET of Dimethyl to Trimethyl Lysine 9 of Histone H3 to Cause Transcriptional Repression
- 1 August 2003
- journal article
- research article
- Published by Elsevier in Molecular Cell
- Vol. 12 (2) , 475-487
- https://doi.org/10.1016/j.molcel.2003.08.007
Abstract
No abstract availableKeywords
This publication has 37 references indexed in Scilit:
- Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste proteinGenes & Development, 2002
- Role of Histone H3 Lysine 27 Methylation in Polycomb-Group SilencingScience, 2002
- Histone Methyltransferase Activity of a Drosophila Polycomb Group Repressor ComplexCell, 2002
- Drosophila Enhancer of Zeste/ESC Complexes Have a Histone H3 Methyltransferase Activity that Marks Chromosomal Polycomb SitesCell, 2002
- Active genes are tri-methylated at K4 of histone H3Nature, 2002
- Epigenetic Codes for Heterochromatin Formation and SilencingCell, 2002
- Molecular cloning of ESET, a novel histone H3-specific methyltransferase that interacts with ERG transcription factorOncogene, 2002
- Correlation Between Histone Lysine Methylation and Developmental Changes at the Chicken β-Globin LocusScience, 2001
- Transitions in Distinct Histone H3 Methylation Patterns at the Heterochromatin Domain BoundariesScience, 2001
- SET Domain-containing Protein, G9a, Is a Novel Lysine-preferring Mammalian Histone Methyltransferase with Hyperactivity and Specific Selectivity to Lysines 9 and 27 of Histone H3Journal of Biological Chemistry, 2001