Evidence map›Paper›PMID 27827996›Full record

ReviewInternational journal of molecular sciences2016

The Bromodomain and Extra-Terminal Domain (BET) Family: Functional Anatomy of BET Paralogous Proteins.

Yasushi Taniguchi

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 183 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
183citing papers in PubMed, 1 pooled it
11.7field-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

183 citing papers in PubMed, 1 synthesis or guideline pooled it, 317 citations in OpenAlex.

  1. Pooled it
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  3. Review
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  8. Article
  9. Loop Plasticity Drives Paralog-Specific Recognition in BET ET Domains.Journal of chemical information and modeling · 2026
    Article
  10. Article
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  12. Targeting BRD4-A Promising Therapeutic Option for Glioblastoma?International journal of molecular sciences · 2026
    Review
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  14. Review
  15. Article
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123 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

1 author at 1 institution in 1 country.

Yasushi TaniguchiDivision of Basic Molecular Science and Molecular Medicine, School of Medicine, Tokai University, Isehara, Kanagawa 259-1193, Japan. ytanigu@is.icc.u-tokai.ac.jp.
Tokai University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Bromodomain and Extra-Terminal Domain (BET) family of proteins is characterized by the presence of two tandem bromodomains and an extra-terminal domain. The mammalian BET family of proteins comprises BRD2, BRD3, BRD4, and BRDT, which are encoded by paralogous genes that may have been generated by repeated duplication of an ancestral gene during evolution. Bromodomains that can specifically bind acetylated lysine residues in histones serve as chromatin-targeting modules that decipher the histone acetylation code. BET proteins play a crucial role in regulating gene transcription through epigenetic interactions between bromodomains and acetylated histones during cellular proliferation and differentiation processes. On the other hand, BET proteins have been reported to mediate latent viral infection in host cells and be involved in oncogenesis. Human BRD4 is involved in multiple processes of the DNA virus life cycle, including viral replication, genome maintenance, and gene transcription through interaction with viral proteins. Aberrant BRD4 expression contributes to carcinogenesis by mediating hyperacetylation of the chromatin containing the cell proliferation-promoting genes. BET bromodomain blockade using small-molecule inhibitors gives rise to selective repression of the transcriptional network driven by c-MYC These inhibitors are expected to be potential therapeutic drugs for a wide range of cancers. This review presents an overview of the basic roles of BET proteins and highlights the pathological functions of BET and the recent developments in cancer therapy targeting BET proteins in animal models.

Indexed as

Epigenesis, GeneticAnimalsAntineoplastic AgentsBromodomain Containing ProteinsCell ProliferationChromatinEvolution, MolecularGene DuplicationHistonesHumansLysineMultigene FamilyNeoplasmsProtein DomainsProtein IsoformsProtein Serine-Threonine KinasesAntineoplastic AgentsBRD2 protein, humanBromodomain Containing ProteinsChromatinHistonesLysineProtein IsoformsProtein Serine-Threonine KinasesTranscription FactorsBET inhibitorbromodomainBromodomain and Extra-Terminal Domain (BET)gene transcriptionhistone acetylation

Identifiers

PMID27827996
PMCPMC5133849
OpenAlexW2540133997

What OpenQuestion holds

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LicenceCC BY
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.