Structure of the Catalytic Domain of Human DOT1L, a Non-SET Domain Nucleosomal Histone Methyltransferase
- 1 March 2003
- Vol. 112 (5), 711-723
- https://doi.org/10.1016/s0092-8674(03)00114-4
Abstract
No abstract availableKeywords
This publication has 42 references indexed in Scilit:
- Structure and Catalytic Mechanism of a SET Domain Protein MethyltransferaseCell, 2002
- Active genes are tri-methylated at K4 of histone H3Nature, 2002
- Disruptor of Telomeric Silencing-1 Is a Chromatin-specific Histone H3 MethyltransferaseJournal of Biological Chemistry, 2002
- Methylation of Histone H3 by COMPASS Requires Ubiquitination of Histone H2B by Rad6Journal of Biological Chemistry, 2002
- Set2 Is a Nucleosomal Histone H3-Selective Methyltransferase That Mediates Transcriptional RepressionMolecular and Cellular Biology, 2002
- Crystal structure of a protein repair methyltransferase from Pyrococcus furiosus with its l-isoaspartyl peptide substrateJournal of Molecular Biology, 2001
- Methylation of Histone H4 at Arginine 3 Facilitating Transcriptional Activation by Nuclear Hormone ReceptorScience, 2001
- The language of covalent histone modificationsNature, 2000
- [20] Processing of X-ray diffraction data collected in oscillation modeMethods in Enzymology, 1997
- Crystal structure of catechol O-methyltransferaseNature, 1994