Evidence map›Paper›PMID 24751816›Full record

ReviewNature reviews. Drug discovery2014

Targeting bromodomains: epigenetic readers of lysine acetylation.

Panagis Filippakopoulos, Stefan Knapp

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Drug discovery, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 625 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
625citing papers in PubMed, 2 pooled it
64.1field-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

625 citing papers in PubMed, 2 syntheses or guidelines pooled it, 1,228 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Review
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  5. Review
  6. The CTNNB1-TRIM28 complex governs hormone-induced RNA polymerase II dynamics in kidney epithelial cells.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  7. Article
  8. Tuning epigenetics to enhance cancer virotherapy.Acta pharmaceutica Sinica. B · 2026
    Review
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565 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

2 authors at 1 institution in 1 country.

Panagis Filippakopoulos1] Structural Genomics Consortium, Nuffield Department of Clinical Medicine, University of Oxford, Old Road Campus Research Building, Roosevelt Drive, Oxford OX3 7DQ, UK. [2] Ludwig Institute for Cancer Research, Nuffield Department of Clinical Medicine, University of Oxford, Roosevelt Drive, Oxford, OX3 7DQ, UK.
Stefan Knapp1] Structural Genomics Consortium, Nuffield Department of Clinical Medicine, University of Oxford, Old Road Campus Research Building, Roosevelt Drive, Oxford OX3 7DQ, UK. [2] Target Discovery Institute, Nuffield Department of Clinical Medicine, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK.
University of Oxford · GB

Funding

CIHRWellcome Trust 092809Wellcome Trust 092809/Z/10/ZWellcome Trust 095751/Z/11/Z
6 · The paper itself

Abstract

Lysine acetylation is a key mechanism that regulates chromatin structure; aberrant acetylation levels have been linked to the development of several diseases. Acetyl-lysine modifications create docking sites for bromodomains, which are small interaction modules found on diverse proteins, some of which have a key role in the acetylation-dependent assembly of transcriptional regulator complexes. These complexes can then initiate transcriptional programmes that result in phenotypic changes. The recent discovery of potent and highly specific inhibitors for the BET (bromodomain and extra-terminal) family of bromodomains has stimulated intensive research activity in diverse therapeutic areas, particularly in oncology, where BET proteins regulate the expression of key oncogenes and anti-apoptotic proteins. In addition, targeting BET bromodomains could hold potential for the treatment of inflammation and viral infection. Here, we highlight recent progress in the development of bromodomain inhibitors, and their potential applications in drug discovery.

Indexed as

Epigenesis, GeneticAcetylationAnimalsDrug Delivery SystemsHumansLysineProtein BindingProtein Structure, TertiaryLysine

Identifiers

PMID24751816
OpenAlexW2003872705

What OpenQuestion holds

Textmetadata
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.