Bromodomain: an acetyl‐lysine binding domain

By L. Zeng, Ming‐Ming Zhou. FEBS Letters, 2002

778 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/52d66d24b36b7943590a32592b9b4e75f4b43e6a

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In Molecular Biology

Citations in the corpus

The interplay of histone modifications – writers that read (2015, neutral): “There are also accessory proteins that can associate with the core PRC2 complex to form two types of PRC2: PRC2.”
Molecular docking: a powerful approach for structure-based drug discovery. (2011, background): “Several enzyme families also involve loop rearrangement within the active site responsible for ligand binding, such as Bromodomain, an extensive family related to acetyl-lysine binding, or Dihydrofolate reductase, responsible for the maintenance of the cellular pools of tetrahydrofolate, as well as ”
Histone and chromatin cross-talk. (2003, background): “Bromodomains (brm [brahma]-like domains) are present in several HATs and chromatin remodeling proteins, as well as in the general transcription factor TAF250, and bind acetylated lysines (for review see [48]).”
Shaping the nuclear action of NF-κB (2004, background): “Bromodomains specifically recognize acetylated lysine residues and are present in many chromatin-associated proteins as well as nearly all known nuclear histone acetyltransferase”
How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers (2007, background): “Bromodomains are protein modules found in chromatin-associated proteins, especially nuclear histone acetyltransferases (HATs) such as Gcn5p, and components of certain remodeling complexes, in which they have key roles in transcriptional activation and chromatin remodelin”
Regulation of nucleosome dynamics by histone modifications (2013, neutral): “Bromodomains are found in a wide range of chromatin-associated proteins, including lysine acetyltransferases and chromatin remodeling proteins 28 .”
Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification (2011, background): “Second, histone PTMs regulate chromatin structure and function by recruiting PTM-specific binding proteins, which recognize modified histones via specialized structural folds such as bromo-, chromo- andPHDdomains (Wysocka et al., 2005, 2006; Zeng and Zhou, 2002).”