Evidence map›Paper›PMID 24686119›Full record

ReviewBiochimica et biophysica acta2014

The bromodomain: from epigenome reader to druggable target.

Roberto Sanchez, Jamel Meslamani, Ming-Ming Zhou

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
10.7field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

84 citing papers in PubMed, 193 citations in OpenAlex.

  1. Article
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  15. Construction of Histone-Protein Complex Structures by Peptide Growing.International journal of molecular sciences · 2023
    Article
  16. Review
  17. Review
  18. Review
  19. Article
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24 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Roberto SanchezDepartment of Structural and Chemical Biology, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA.
Jamel MeslamaniDepartment of Structural and Chemical Biology, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA.
Ming-Ming ZhouDepartment of Structural and Chemical Biology, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA.
Icahn School of Medicine at Mount Sinai · US

Funding

Chemical Genomics Paradigm for Epigentic RegulationR01HG004508 · NHGRI · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI ZHOU, MING-MING · 2008 to 2014
$6.7M
STRUCTURE OF PROTEIN MODULES IN CHROMATIN REMODELINGR01CA087658 · NCI · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI ZHOU, MING-MING · 2000 to 2016
$4.8M
NCI NIH HHS R01 CA087658NHGRI NIH HHS R01 HG004508
6 · The paper itself

Abstract

Lysine acetylation is a fundamental post-translational modification that plays an important role in the control of gene transcription in chromatin in an ordered fashion. The bromodomain, the conserved structural module present in transcription-associated proteins, functions exclusively to recognize acetyl-lysine on histones and non-histone proteins. The structural analyses of bromodomains' recognition of lysine-acetylated peptides derived from histones and cellular proteins provide detailed insights into the differences and unifying features of biological ligand binding selectivity by the bromodomains. Newly developed small-molecule inhibitors targeting bromodomain proteins further highlight the functional importance of bromodomain/acetyl-lysine binding as a key mechanism in orchestrating molecular interactions and regulation in chromatin biology and gene transcription. These new studies argue that modulating bromodomain/acetyl-lysine interactions with small-molecule chemicals offer new opportunities to control gene expression in a wide array of human diseases including cancer and inflammation. This article is part of a Special Issue entitled: Molecular mechanisms of histone modification function.

Indexed as

Epigenesis, GeneticProtein Processing, Post-TranslationalAcetylationCardiovascular DiseasesHistonesHIV InfectionsHumansLysineModels, MolecularNeoplasmsProtein ConformationProtein Interaction Domains and MotifsProtein Structure, TertiarySmall Molecule LibrariesTranscription FactorsHistonesLysineSmall Molecule LibrariesTranscription FactorsBromodomainGene transcriptionSmall molecule inhibitors

Identifiers

PMID24686119
PMCPMC4099289
OpenAlexW2040932281

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.