Physical and Functional Interactions of Monoubiquitylated Transactivators with the Proteasome
Open Access
- 1 August 2008
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 283 (31) , 21789-21798
- https://doi.org/10.1074/jbc.m803075200
Abstract
No abstract availableKeywords
This publication has 40 references indexed in Scilit:
- Activation Domain-dependent Monoubiquitylation of Gal4 Protein Is Essential for Promoter Binding in VivoJournal of Biological Chemistry, 2008
- Label Transfer Chemistry for the Characterization of Protein−Protein InteractionsJournal of the American Chemical Society, 2007
- The role of the proteasomal ATPases and activator monoubiquitylation in regulating Gal4 binding to promotersGenes & Development, 2006
- Chemistry of Periodate-Mediated Cross-Linking of 3,4-Dihydroxylphenylalanine-Containing Molecules to ProteinsJournal of the American Chemical Society, 2006
- Proteasomal ATPases Link Ubiquitylation of Histone H2B to Methylation of Histone H3Molecular Cell, 2004
- Toward a General Chemical Method for Rapidly Mapping Multi-Protein ComplexesJournal of Proteome Research, 2004
- The Gal4 Activation Domain Binds Sug2 Protein, a Proteasome Component, in Vivo and in VitroJournal of Biological Chemistry, 2001
- Evidence That Proteolysis of Gal4 Cannot Explain the Transcriptional Effects of Proteasome ATPase MutationsJournal of Biological Chemistry, 2001
- The Glucocorticoid Receptor: Rapid Exchange with Regulatory Sites in Living CellsScience, 2000
- Specific Covalent Labeling of Recombinant Protein Molecules Inside Live CellsScience, 1998