The DOI matches its Crossref record; 106 of the 106 references it cites were found in a registry or an index.
The bromodomain interaction module
Open accessAbstract
ε‐N‐acetylation of lysine residues (K ac) is one of the most abundant post‐translation modifications (PTMs) in the human proteome. In the nucleus, acetylation of histones has been linked to transcriptional activation of genes but the functional consequences of most acetylation events and proteins recruited to these sites remains largely unknown. Bromodomains (BRDs) are small helical interaction modules that specifically recognize acetylation sites in proteins. BRDs have recently emerged as interesting targets for the development of specific protein interaction inhibitors, enabling a novel exiting strategy for the development of new therapies. This review provides an overview over sequence requirements of BRDs, known substrates and the structural mechanisms of specific K ac recognition.
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Cites
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Cited by
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Mechanisms of action and regulation of ATP-dependent chromatin-remodelling complexes
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Metadata
- Authors
- Filippakopoulos, P., & Knapp, S.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2012-05-03
- Volume
- 586
- Issue
- 17
- Pages
- 2692-2704
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W1974631163
- Cited by
- 374
- References
- 106
- FWCI
- 12.78
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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