Back to search

Article

Discovery of a hidden transient state in all bromodomain families

2020-04-01

Abstract excerpt

<h4>ABSTRACT</h4> Bromodomains (BDs) are small protein modules that interact with acetylated marks in histones. These post-translational modifications are pivotal to regulate gene expression, making BDs promising targets to treat several diseases. While the general structure of BDs is well known, their dynamical features and their interplay with other macromolecules are poorly understood, hampering the rational d...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work
4ff80baf-542c-5a19-a8d9-647d00e3fa1c
DOI
10.1101/2020.04.01.019547
Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest
Interactive article relationship graphSelect a related publication card to move it into the centre and load its closest explainable connections. Solid lines are source-backed structured connections. Dashed lines are semantic discovery signals and are not scientific evidence.
Discovery of a hidden transient state in all bromodomain familiesDOI 10.1101/2020.04.01.019547
A distal regulatory region of a class I human histone deacetylase.Semantic proximity
The BRD4-nucleosome interaction is enhanced modestly and non-selectively by histone acetylationSemantic proximity
Bromodomain 4: a cellular Swiss army knifeSemantic proximity
Chemical Epigenetics: The Impact of Chemical and Chemical Biology Techniques on Bromodomain Target ValidationSemantic proximity
Histone Recognition and Large-Scale Structural Analysis of the Human Bromodomain FamilySemantic proximity
The bromodomain: a chromatin browser?Semantic proximity
Structural insights into acetylated histone ligand recognition by the BDP1 bromodomain of <i>Plasmodium falciparum</i>Semantic proximity
mRNA display reveals a class of high-affinity bromodomain-binding motifs that are not found in the human proteomeSemantic proximity
Nucleosome scaffolding by Brd4 tandem bromodomains in acetylation-dependent chromatin compartmentalizationSemantic proximity
The BRPF1 bromodomain is a molecular reader of di-acetyllysineSemantic proximity
Targeting bromodomain-containing proteins: research advances of drug discoverySemantic proximity
Uncovering the Bromodomain Interactome using Site-Specific Azide-Acetyllysine Photochemistry, Proteomic Profiling and Structural CharacterizationSemantic proximity
Select a neighboring publication to make it the new centre.