ArticleBiochemistry2022
Alternative Mechanisms for DNA Engagement by BET Bromodomain-Containing Proteins.
Article in Biochemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 14 citations in OpenAlex.
- BRD4 binds the nucleosome via both histone and DNA interactions.Molecular cell · 2026Article
- Direct Readout of Multivalent Chromatin Reader-Nucleosome Interactions by Nucleosome Mass Spectrometry.ACS central science · 2026Article
- Structural Genomics Defines PBRM1 Bromodomain Variant Function in ccRCC.Human mutation · 2026Article
- The BRD4-nucleosome interaction is enhanced modestly and non-selectively by histone acetylation.Nucleic acids research · 2025Article
- Mechanistic insights into DNA binding by BD1 of the TAF1 tandem bromodomain module.The Biochemical journal · 2025Article
- BAHCC1 binds H4K20me1 to facilitate the MCM complex loading and DNA replication.Nature communications · 2025Article
- A "Goldilocks Zone" for Recruiting BET Proteins with Bromodomain-1-Selective Ligands.ACS chemical biology · 2024Article
- Rewriting cellular fate: epigenetic interventions in obesity and cellular programming.Molecular medicine (Cambridge, Mass.) · 2024Review
- Beyond the tail: the consequence of context in histone post-translational modification and chromatin research.The Biochemical journal · 2024Article
- Article
- Origin of the multi-phasic quenching dynamics in the BLUF domains across the species.Nature communications · 2024Article
- PBRM1 bromodomains associate with RNA to facilitate chromatin association.Nucleic acids research · 2023Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Epigenetic reader domains regulate chromatin structure and modulate gene expression through the recognition of post-translational modifications on histones. Recently, reader domains have also been found to harbor double-stranded (ds) DNA-binding activity, which is as functionally critical as histone association. Here, we explore the dsDNA recognition of the N-terminal bromodomain of the bromodomain and extra-terminal (BET) protein, BRD4. Using protein-observed
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.