- Abstract:
-
Histone lysine acetylation is a key component of epigenetic regulation of gene transcription. Bromodomains, found in histone acetyl transferases and other chromatin-associated proteins, bind selectively to acetylated lysines, acting as "readers" of the histone code, and have recently been shown to contain a druggable binding pocket. Here we report the development of high-throughput assays that quantify the binding of bromodomains to acetylated histone peptides. We have used these assays to sc...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1039/c1mb05099k
-
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- Journal:
- Molecular bioSystems
- Volume:
- 7
- Issue:
- 10
- Pages:
- 2899-2908
- Publication date:
- 2011-10-05
- DOI:
- EISSN:
-
1742-2051
- ISSN:
-
1742-206X
- URN:
-
uuid:4ed79667-f0f6-4799-960a-850e7ce4fd28
- Source identifiers:
-
177354
- Local pid:
- pubs:177354
- Language:
- English
- Keywords:
- Copyright date:
- 2011
Journal article
Bromodomain-peptide displacement assays for interactome mapping and inhibitor discovery.
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