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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Bromodomain containing 3

This gene was identified based on its homology to the gene encoding the RING3 protein, a serine/threonine kinase. The gene localizes to 9q34, a region which contains several major histocompatibility complex (MHC) genes. The function of the encoded protein is not known. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: BET, Histone, ACID, BRDT, V1a
Papers on BRD3
The bromodomain inhibitor JQ1 and the histone deacetylase inhibitor panobinostat synergistically reduce N-Myc expression and induce anticancer effects.
Liu et al., Australia. In Clin Cancer Res, Feb 2016
BET bromodomain inhibitors are among the most promising novel anticancer agents by blocking BRD3 and BRD4 from activating oncogene transcription.
Bromodomain and extra-terminal domain bromodomain inhibition prevents synovial inflammation via blocking IκB kinase-dependent NF-κB activation in rheumatoid fibroblast-like synoviocytes.
Xu et al., Guangzhou, China. In Rheumatology (oxford), Jan 2016
RESULTS: Four Brd proteins, including Brd2, Brd3, Brd4 and Brdt, were expressed in FLSs from patients with RA and OA; however, the expression of Brd2 and Brd4 was increased in RA compared with that in OA.
BET protein inhibition mitigates acute myocardial infarction damage in rats via the TLR4/TRAF6/NF-κB pathway.
Song et al., Zhengzhou, China. In Exp Ther Med, Dec 2015
The mRNA and protein expression levels of BRD2, BRD3 and BRD4 were evaluated using quantitative polymerase chain reaction and western blot analysis, respectively.
Targeting the EWS-ETS transcriptional program by BET bromodomain inhibition in Ewing sarcoma.
Richter et al., München, Germany. In Oncotarget, Dec 2015
The effect on this expression program was mimicked by RNA interference with BRD3 or BRD4 expression, indicating that the EWS-FLI1 mediated expression profile is at least in part mediated via such epigenetic readers.
Epigenetic Readers of Lysine Acetylation Regulate Cocaine-Induced Plasticity.
Wahlestedt et al., Miami, United States. In J Neurosci, Dec 2015
Members of the bromodomain and extraterminal (BET) family of epigenetic "reader" proteins (BRD2, BRD3, BRD4, and BRDT) bind acetylated histones and serve as a scaffold for the recruitment of macromolecular complexes to modify chromatin accessibility and transcriptional activity.
Characterization of the Lactobacillus plantarum plasmid pCD033 and generation of the plasmid free strain L. plantarum 3NSH.
Heinl et al., Vienna, Austria. In Plasmid, Sep 2015
A gene encoding a RepB/OrfX-like protein was found to be not essential for plasmid replication.
Selective Small Molecule Induced Degradation of the BET Bromodomain Protein BRD4.
Ciulli et al., Dundee, United Kingdom. In Acs Chem Biol, Sep 2015
The Bromo- and Extra-Terminal (BET) proteins BRD2, BRD3, and BRD4 play important roles in transcriptional regulation, epigenetics, and cancer and are the targets of pan-BET selective bromodomain inhibitor JQ1.
Structure-Based Design of γ-Carboline Analogues as Potent and Specific BET Bromodomain Inhibitors.
Wang et al., Ann Arbor, United States. In J Med Chem, Jul 2015
Small-molecule inhibitors of bromodomain and extra terminal proteins (BET), including BRD2, BRD3, and BRD4 proteins have therapeutic potential for the treatment of human cancers and other diseases and conditions.
Inhibition of BET bromodomains as a therapeutic strategy for cancer drug discovery.
Liu et al., Chengdu, China. In Oncotarget, Apr 2015
Proteins that share the feature of containing two BRDs and an extra-terminal domain belong to BET family, including BRD2, BRD3, BRD4 and BRDT.
BET bromodomain inhibitors: a patent review.
Burns et al., Australia. In Expert Opin Ther Pat, 2014
INTRODUCTION: The bromodomain (BRD) and extra-C terminal domain (BET) protein family consists of four members (BRD2, BRD3, BRD4 and BRDT).
Bromodomains as therapeutic targets in cancer.
Dawson et al., Cambridge, United Kingdom. In Brief Funct Genomics, 2013
Small molecules with high specificity for the Bromodomain and Extra Terminal family of proteins (BRD2, BRD3, BRD4 and BRDT) have recently been shown to have remarkable pre-clinical efficacy in various malignancies.
The importance of diagnosing NUT midline carcinoma.
French, Boston, United States. In Head Neck Pathol, 2013
The rearrangements most often take the form of BRD4-NUT fusions, and in a minority of cases, BRD3-NUT or NUT-variant fusions.
Expression of BET genes in testis of men with different spermatogenic impairments.
Kleiman et al., Ramat Gan, Israel. In Fertil Steril, 2012
The BRDT gene was not expressed in testicular tissue from patients with Sertoli cells only, whereas the other three genes of the BET family retained expression in all the sperm pathologies.
Pathogenesis of NUT midline carcinoma.
French, Boston, United States. In Annu Rev Pathol, 2011
NUT midline carcinoma (NMC), an aggressive form of squamous cell carcinoma, is defined by the presence of acquired chromosomal rearrangements involving NUT, usually BRD4-NUT fusion genes and, less commonly, NUT-variant fusion genes involving BRD3 or still-uncharacterized genes.
Inhibition of BET recruitment to chromatin as an effective treatment for MLL-fusion leukaemia.
Kouzarides et al., Cambridge, United Kingdom. In Nature, 2011
The mode of action of I-BET151 is, at least in part, due to the inhibition of transcription at key genes (BCL2, C-MYC and CDK6) through the displacement of BRD3/4, PAFc and SEC components from chromatin.
Structural basis and specificity of acetylated transcription factor GATA1 recognition by BET family bromodomain protein Brd3.
Mackay et al., Sydney, Australia. In Mol Cell Biol, 2011
the structural basis for GATA1 and Brd3 interaction was described.
Bromodomain protein Brd3 associates with acetylated GATA1 to promote its chromatin occupancy at erythroid target genes.
Blobel et al., Philadelphia, United States. In Proc Natl Acad Sci U S A, 2011
Brd3 associates with acetylated GATA1 to promote its chromatin occupancy at erythroid target genes
The double bromodomain proteins Brd2 and Brd3 couple histone acetylation to transcription.
Flint et al., Princeton, United States. In Mol Cell, 2008
Results report that the double bromodomain proteins Brd2 and Brd3 associate preferentially in vivo with hyperacetylated chromatin along the entire lengths of transcribed genes.
BRD-NUT oncoproteins: a family of closely related nuclear proteins that block epithelial differentiation and maintain the growth of carcinoma cells.
Aster et al., Boston, United States. In Oncogene, 2008
BRD-NUT fusion proteins contribute to carcinogenesis by associating with chromatin and interfering with epithelial differentiation.
fw2.2: a quantitative trait locus key to the evolution of tomato fruit size.
Tanksley et al., Ithaca, United States. In Science, 2000
The cause of the QTL effect is a single gene, ORFX, that is expressed early in floral development, controls carpel cell number, and has a sequence suggesting structural similarity to the human oncogene c-H-ras p21.
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