Phosphorylation by p44 MAP Kinase/ERK1 Stimulates CBP Histone Acetyl Transferase Activity in Vitro
- 19 August 1999
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 262 (1), 157-162
- https://doi.org/10.1006/bbrc.1999.1132
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- The CREB-binding Protein (CBP) Cooperates with the Serum Response Factor for Transactivation of the c-fos Serum Response ElementJournal of Biological Chemistry, 1997
- The CBP co-activator is a histone acetyltransferaseNature, 1996
- CREB-binding Protein Activates Transcription through Multiple DomainsJournal of Biological Chemistry, 1996
- The Transcriptional Coactivators p300 and CBP Are Histone AcetyltransferasesCell, 1996
- The nuclear hormone receptor coactivator SRC-1 is a specific target of p300.Proceedings of the National Academy of Sciences, 1996
- A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1ANature, 1996
- Adaptor-mediated Recruitment of RNA Polymerase II to a Signal-dependent ActivatorJournal of Biological Chemistry, 1996
- Nuclear protein CBP is a coactivator for the transcription factor CREBNature, 1994
- Activation of cAMP and mitogen responsive genes relies on a common nuclear factorNature, 1994
- Phosphorylated CREB binds specifically to the nuclear protein CBPNature, 1993