Results 1 to 10 of about 19,105 (226)

Methylation of BRD4 by PRMT1 regulates BRD4 phosphorylation and promotes ovarian cancer invasion

open access: yesCell Death and Disease, 2023
Bromodomain-containing protein 4 (BRD4), the major component of bromodomain and extra-terminal domain (BET) protein family, has important functions in early embryonic development and cancer development. However, the posttranslational modification of BRD4
Yi Liu   +8 more
doaj   +4 more sources

Interrogating Histone Acetylation and BRD4 as Mitotic Bookmarks of Transcription

open access: yesCell Reports, 2019
Summary: Global changes in chromatin organization and the cessation of transcription during mitosis are thought to challenge the resumption of appropriate transcription patterns after mitosis.
Aaron J Stonestrom   +2 more
exaly   +4 more sources

Recruitment of BRD4 to the ASXL1 genomic targets depends on the extra-terminal domain of BRD4 [PDF]

open access: yesNature Communications
ASXL1 is a well-established driver of a wide range of cancers. Here, we identify a high level of genetic correlation between ASXL1 and the major transcriptional activator BRD4 in cancer cells and characterize the molecular mechanism underlying this ...
Karthik Selvam   +17 more
doaj   +3 more sources

The poly(ADP-ribosyl)ation of BRD4 mediated by PARP1 promoted pathological cardiac hypertrophy

open access: yesActa Pharmaceutica Sinica B, 2021
The bromodomain and extraterminal (BET) family member BRD4 is pivotal in the pathogenesis of cardiac hypertrophy. BRD4 induces hypertrophic gene expression by binding to the acetylated chromatin, facilitating the phosphorylation of RNA polymerases II ...
Zhuoming Li   +2 more
exaly   +3 more sources

BRD4 modulates antimicrobial defense via non-canonical NRF2 activation in macrophages to confer protection against sepsis. [PDF]

open access: yesPLoS Pathogens
Sepsis is a life-threatening condition characterized by dysregulated immune responses and high mortality, driven by persistent pathogens and compromised antimicrobial defenses.
Jinfeng Hu   +16 more
doaj   +2 more sources

Phosphorylation by JNK switches BRD4 functions

open access: yesMolecular Cell
Bromodomain 4 (BRD4), a key regulator with pleiotropic functions, plays crucial roles in cancers and cellular stress responses. It exhibits dual functionality: chromatin-bound BRD4 regulates remodeling through its histone acetyltransferase (HAT) activity, while promoter-associated BRD4 regulates transcription through its kinase activity.
Jie Mu   +2 more
exaly   +3 more sources

Role of the Super-Enhancer Component Bromodomain Protein 4 in the Radiation Response of Human Head and Neck Squamous Cell Carcinoma Cells [PDF]

open access: yesCurrent Issues in Molecular Biology
Radiotherapy is an effective treatment for cancer; however, radioresistant cancer cells result in recurrence. Therefore, elucidating the mechanisms of radioresistance is urgently needed.
Nanami Munakata   +3 more
doaj   +2 more sources

BRD4 Phosphorylation Regulates the Structure of Chromatin Nanodomains. [PDF]

open access: yesCells
The interplay between chromatin structure and phase-separating proteins is an emerging topic in cell biology with implications for understanding disease states. Here, we investigate the functional relationship between bromodomain protein 4 (BRD4) and chromatin architecture.
Seitz C, Fu D, Liu M, Ma H, Liu J.
europepmc   +4 more sources

Molecular dynamics simulations data of six compounds F3J-BRD4/CBP, EX1-BRD4/CBP, and E2T-BRD4/CBP

open access: yesData in Brief, 2021
The data here described are related to the research article entitled "Molecular dynamics insights into binding selectivity of inhibitors toward BRD4 and CBP" [1]. Bromodomain-containing protein 4 (BRD4) and CREB binding protein (CBP) play important roles in tumorigenesis and development.
Shiliang Wu   +4 more
openaire   +3 more sources

Supercharging BRD4 with NUT in carcinoma

open access: yesOncogene, 2021
NUT carcinoma (NC) is an extremely aggressive squamous cancer with no effective therapy. NC is driven, most commonly, by the BRD4-NUT fusion oncoprotein. BRD4-NUT combines the chromatin-binding bromo- and extraterminal domain-containing (BET) protein, BRD4, with an unstructured, poorly understood protein, NUT, which recruits and activates the histone ...
Kyle P. Eagen, Christopher A. French
openaire   +3 more sources

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