Evidence map›Paper›PMID 24260471›Full record

ArticlePloS one2013

BRD4 short isoform interacts with RRP1B, SIPA1 and components of the LINC complex at the inner face of the nuclear membrane.

Jude Alsarraj, Farhoud Faraji, Thomas R Geiger, Katherine R Mattaini, Mia Williams, Josephine Wu, Ngoc-Han Ha, Tyler Merlino, Renard C Walker, Allen D Bosley and 11 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

41 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Review
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  4. Impact ofCancers · 2024
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  7. Review
  8. Article
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  11. Article
  12. Article
  13. The BET family in immunity and disease.Signal transduction and targeted therapy · 2021
    Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article
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

21 authors at 7 institutions in 2 countries.

Jude AlsarrajLaboratory of Cancer Biology and Genetics, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland, United States of America.
Farhoud Faraji
Thomas R Geiger
Katherine R Mattaini
Mia Williams
Josephine Wu
Ngoc-Han Ha
Tyler Merlino
Renard C Walker
Allen D Bosley
Zhen Xiao
Thorkell Andresson
Dominic Esposito
Nicholas Smithers
Dave Lugo
Rab Prinjha
Anup Day
Nigel P S Crawford
Keiko Ozato
Kevin Gardner
Kent W Hunter
Center for Cancer Research · USFrederick National Laboratory for Cancer Research · USNational Cancer Institute · USNational Institutes of Health · USGlaxoSmithKline (United Kingdom) · GBEunice Kennedy Shriver National Institute of Child Health and Human Development · USNational Human Genome Research Institute · US

Funding

Genetic Modifiers of Intitiation and Progression of Mammary CancerZIABC011255 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI HUNTER, KENT WILLIAM · 2010 to 2025
$33.2M
Molecular linkages between epigenetic regulation and metabolism in breast cancerZIABC010847 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI GARDNER, KEVIN · 2009 to 2017
$7.7M
Intramural NIH HHS ZIA BC011255NCI NIH HHS ZIA BC 011255
6 · The paper itself

Abstract

Recent studies suggest that BET inhibitors are effective anti-cancer therapeutics. Here we show that BET inhibitors are effective against murine primary mammary tumors, but not pulmonary metastases. BRD4, a target of BET inhibitors, encodes two isoforms with opposite effects on tumor progression. To gain insights into why BET inhibition was ineffective against metastases the pro-metastatic short isoform of BRD4 was characterized using mass spectrometry and cellular fractionation. Our data show that the pro-metastatic short isoform interacts with the LINC complex and the metastasis-associated proteins RRP1B and SIPA1 at the inner face of the nuclear membrane. Furthermore, histone binding arrays revealed that the short isoform has a broader acetylated histone binding pattern relative to the long isoform. These differential biochemical and nuclear localization properties revealed in our study provide novel insights into the opposing roles of BRD4 isoforms in metastatic breast cancer progression.

Indexed as

AnimalsApoptosis Regulatory ProteinsBromodomain Containing ProteinsCell Cycle ProteinsCell Line, TumorCell NucleusChromosomal Proteins, Non-HistoneDisease Models, AnimalFemaleGTPase-Activating ProteinsHeterocyclic Compounds, 4 or More RingsHistonesHumansIntracellular Signaling Peptides and ProteinsMembrane ProteinsMiceApoptosis Regulatory ProteinsBRD4 protein, humanBromodomain Containing ProteinsCell Cycle ProteinsChromosomal Proteins, Non-HistoneGSK1210151AGTPase-Activating ProteinsHeterocyclic Compounds, 4 or More RingsHistonesIntracellular Signaling Peptides and ProteinsMembrane ProteinsMicrotubule-Associated ProteinsNAT10 protein, humanN-Terminal Acetyltransferase EN-Terminal AcetyltransferasesNuclear ProteinsProtein IsoformsRRP1B protein, humanSIPA1 protein, humanSUN1 protein, humanSUN2 protein, humanTranscription Factors

Identifiers

PMID24260471
PMCPMC3834312
OpenAlexW2057519700

What OpenQuestion holds

Textmetadata
LicenceCC0
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.