Ask about this productRelated genes to: BRDT antibody
- Gene:
- BRDT NIH gene
- Name:
- bromodomain testis associated
- Previous symbol:
- -
- Synonyms:
- BRD6, CT9
- Chromosome:
- 1p22.1
- Locus Type:
- gene with protein product
- Date approved:
- 1997-08-15
- Date modifiied:
- 2016-03-03
Related products to: BRDT antibody
Related articles to: BRDT antibody
- Cyclin-dependent kinase 7 (CDK7) plays key roles in transcription and cell cycle regulation, and its inhibition has been proposed as a potential therapeutic strategy for hepatocellular carcinoma (HCC). The primary research objective of this study is to identify and validate CDK7-associated prognostic genes in HCC using bioinformatics approaches, construct a reliable prognostic risk model, and explore the functional role of CDK7 in HCC progression through and experiments, with a specific focus on its association with RelA/p65 phosphorylation, so as to provide evidence supporting CDK7 as a potential prognostic biomarker and therapeutic target for HCC. Two independent HCC cohorts from The Cancer Genome Atlas (TCGA)-HCC and the Gene Expression Omnibus (dataset GSE14520) were analyzed. Patients were stratified by expression. Differentially expressed genes were identified in both CDK7-based and tumor-versus-normal comparisons, and the intersection of these genes was analyzed. Univariate Cox regression and machine learning were used to screen prognostic genes and construct a risk model. The model's predictive utility was assessed using Kaplan-Meier and receiver operating characteristic (ROC) analyses. Mutation landscapes were compared between risk groups. The functional association of CDK7 was validated through and experiments. Eight prognostic genes (, , , , , , , and ) were screened from 98 intersecting genes via univariate Cox regression and least absolute shrinkage and selection operator regression analyses to construct a risk model. In the TCGA-HCC (374 HCC samples and 50 control samples) and GSE14520 cohorts (222 HCC samples and 212 control samples), patients in the high-risk group had significantly worse overall survival than those in the low-risk group (Hazard Ratio [HR] = 0.003-0.036, 95% Confidence Interval [CI] = 1.01-4.28, < 0.05). The predictive accuracy of the model was moderate, with the areas under the ROC curves (AUCs) for 1-, 3-, and 5-year survival exceeding 0.6 (specifically, 0.69 for 3-year survival). and experiments demonstrated that expression is associated with HCC proliferation, migration, invasion, and tumor growth, and this association might be related to RelA/p65 phosphorylation. This study identified a novel eight-gene prognostic signature linked to CDK7 in HCC and provided experimental evidence that CDK7 promotes tumor aggressiveness. These findings suggest the potential of CDK7 as a prognostic biomarker and therapeutic target for HCC, though further validation of its clinical utility is needed. - Source: PubMed
Publication date: 2026/07/16
Lan BinTan JieWang QingZeng Siyuan - Bromodomain-containing protein 4 (BRD4) is an important therapeutic target for anticancer, antiviral, and anti-inflammatory responses. Although its role in transcription, chromatin dynamics, and epigenetic programs is well recognized, recent studies have expanded the functions of BRD4 and its related bromodomain and extra-terminal (BET) family members (BRD2, BRD3, and BRDT) to other molecular and biological processes. How a universal epigenetic regulator is tailored for context-specific gene/pathway regulation is mechanistically intriguing. In this review, we highlight the importance of protein isoforms and posttranslational modifications, particularly phosphorylation, in generating the protein diversity necessary for selective factor recruitment and context-dependent regulation. Three BRD4 protein isoforms have been identified, including the universally expressed BRD4-L and BRD4-S(a) (simplified as BRD4-S), representing the long and short isoform a, and cell-/stress-specific short isoform b, BRD4-S(b). A phospho-switch mechanism controlling the open/closed state of the bromodomain and BRD4 interaction with partner proteins will also be discussed. Mechanistic understanding of BET protein action has led not only to the development of diverse bromodomain-binding compounds currently used in clinical trials but also to the discovery of a new class of small-molecule inhibitors targeting an intrinsically disordered region (IDR) of phospho-BRD4 to alter specific protein-protein interaction (PPI) networks without globally perturbing transcription programs and chromatin landscapes, thus significantly reducing off-target effects and providing new directions for therapeutic drug development. - Source: PubMed
Publication date: 2026/07/23
Wu Shwu-YuanChiang Cheng-Ming - Bromodomain and extraterminal proteins have emerged as key epigenetic regulators that coordinate transcriptional programs fundamental to cardiovascular physiology and disease. Although bromodomain and extraterminal protein inhibitors exert multiple cardiovascular effects, they cannot fully explain clinical heterogeneity in outcomes and responses, highlighting the need to clarify the context- and disease-specific roles of individual bromodomain and extraterminal protein family members. This narrative review delineates the distinct molecular roles of bromodomain-containing protein 2, bromodomain-containing protein 3, bromodomain-containing protein 4, and bromodomain testis, summarizing their domain architecture and epigenetic regulatory functions. We then synthesize current evidence linking bromodomain and extraterminal protein activity to cardiovascular disease pathogenesis, emphasizing their contributions to major pathological processes, including inflammatory amplification, fibrotic remodeling, dysregulated energy metabolism, aberrant cell proliferation, endothelial-mesenchymal transition, and ferroptotic cell death. Furthermore, we evaluate advances in bromodomain and extraterminal protein inhibitors across preclinical and clinical research, highlighting agents that demonstrate anti-inflammatory, antifibrotic, and cardioprotective efficacy in animal models of cardiovascular disease. By integrating mechanistic and translational evidence, this review provides a framework for understanding bromodomain and extraterminal proteins in cardiovascular diseases and guides the rational design of targeted therapies. - Source: PubMed
Publication date: 2026/07/09
Zhang KaixuanFan YangkaiWang Yuan - The engineered formation of ternary complexes, in which two proteins are bridged by small molecules such as PROTACs or molecular glues, is a prerequisite for the targeted enzymatic degradation of pathogenic proteins; however, the combined analysis of these ternary interactions during the drug discovery process remains challenging. Here, we introduce a proximity binding assay for the simultaneous measurement of binary and ternary interaction kinetics on a biosensor surface. Target proteins and the substrate binding subunit of ubiquitin E3 ligase are tethered to mobile swivel arms of a Y-shaped DNA scaffold. The Y-structure induces spatial proximity between the proteins and presents them to PROTAC analytes flown across the sensor. PROTAC-induced ternary complex formation is measured by fluorescence energy transfer (FRET), while binary interactions are detected by fluorescence quenching. The assay is applied to cereblon (CRBN) and von Hippel-Lindau (VHL) as E3 ligase substrate receptors, a range of compounds including AT1, MZ1, dBETs, and ARV-825 as PROTACs, and the two bromodomains of BRD2, BRD3, BRD4, and BRDT proteins as targets. Automated workflows enable the measurement of 384 real-time sensorgrams in a single run using picomole sample quantities. The insights into proximity-mediated binding kinetics can enable the development of PROTACs and molecular glues with improved properties for targeted protein degradation. - Source: PubMed
Publication date: 2026/04/21
Ponzo IreneSoldà AliceCrowe CharlotteDahl GöranJahodová TerezaHeerwig AndreasGeschwindner StefanCiulli AlessioRant Ulrich - The first bromodomain of the BET protein BRDT (BRDT-BD1) possesses a unique Arg54 residue at the terminus of the ZA channel, absent in other BET family members. We explored this structural uniqueness with 23 analogs of the BET/kinase inhibitor , each bearing an amino acid side chain to enable potential interactions between the positively charged arginine group and the negatively charged carboxylate groups. In an AlphaScreen assay, serine analog showed 35-fold selectivity for BRDT-T over BRD4-T. The BRDT-BD1 cocrystal structure with glutamic acid analog showed no interaction with Arg54, suggesting that the observed preference may be related to differences in the structured water molecules. Compound displayed exceptional in vitro metabolic stability but had limited cellular permeability in MDCK-MDR1 cells. Compounds and are among the best BRDT-BD1-preferring inhibitors reported to date and demonstrate a significant step toward identifying highly selective BRDT inhibitors for male contraception. - Source: PubMed
Publication date: 2026/04/15
Liang TaimengGuan XianghongChan AliceKalra PrakritiShi RuiSolberg JonathanSigua Logan HQi JunPomerantz William C KSchönbrunn ErnstHawkinson Jon EGeorg Gunda I