Direct Association of p300 with Unmodified H3 and H4 N Termini Modulates p300-dependent Acetylation and Transcription of Nucleosomal Templates
Authors:
- Robert G. RoederRRRobert G. Roeder
Open Access
- 1 January 2003
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 278 (3) , 1504-1510
Abstract
No abstract availableKeywords
This publication has 43 references indexed in Scilit:
- Histone H3 Lysine 4 Methylation Disrupts Binding of Nucleosome Remodeling and Deacetylase (NuRD) Repressor ComplexJournal of Biological Chemistry, 2002
- Biochemical Analysis of Chromatin Containing RecombinantDrosophila Core HistonesJournal of Biological Chemistry, 2002
- Translating the Histone CodeScience, 2001
- p300 Forms a Stable, Template-Committed Complex with Chromatin: Role for the BromodomainMolecular and Cellular Biology, 2001
- Solution structure and acetyl-lysine binding activity of the GCN5 bromodomainJournal of Molecular Biology, 2000
- The language of covalent histone modificationsNature, 2000
- The bromodomain of Gcn5p interacts in vitro with specific residues in the N terminus of histone H4 1 1Edited by T. RichmondJournal of Molecular Biology, 1999
- Characterization of nucleosome core particles containing histone proteins made in bacteria 1 1Edited by A. KlugJournal of Molecular Biology, 1997
- The bromodomain revisitedTrends in Biochemical Sciences, 1997
- The Transcriptional Coactivators p300 and CBP Are Histone AcetyltransferasesCell, 1996