A Mammalian bromodomain protein, brd4, interacts with replication factor C and inhibits progression to S phase - Wikidata - wikimedia - TriplyDB

A Mammalian bromodomain protein, brd4, interacts with replication factor C and inhibits progression to S phase

A Mammalian bromodomain protein, brd4, interacts with replication factor C and inhibits progression to S phase

http://www.wikidata.org/entity/Q24540065

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Brd4 maintains constitutively active NF-κB in cancer cells by binding to acetylated RelA Brd4 coactivates transcriptional activation of NF-kappaB via specific binding to acetylated RelA The mitotic chromosome binding activity of the papillomavirus E2 protein correlates with interaction with the cellular chromosomal protein, Brd4.Bromodomain protein Brd4 binds to GTPase-activating SPA-1, modulating its activity and subcellular localization Brd4-independent transcriptional repression function of the papillomavirus e2 proteins Cloned fusion product from a rare t(15;19)(q13.2;p13.1) inhibit S phase in vitro Kaposi's sarcoma-associated herpesvirus latency-associated nuclear antigen interacts with bromodomain protein Brd4 on host mitotic chromosomes Brd4 links chromatin targeting to HPV transcriptional silencing Acetylation-dependent chromatin reorganization by BRDT, a testis-specific bromodomain-containing protein A peek into the complex realm of histone phosphorylation Chromatin targeting drugs in cancer and immunity Structures of the Dual Bromodomains of the P-TEFb-activating Protein Brd4 at Atomic Resolution Inhibition of BET recruitment to chromatin as an effective treatment for MLL-fusion leukaemia RVX-208, an inhibitor of BET transcriptional regulators with selectivity for the second bromodomain BRD4 is an atypical kinase that phosphorylates serine2 of the RNA polymerase II carboxy-terminal domain BET domain co-regulators in obesity, inflammation and cancer Brd4 associates with mitotic chromosomes throughout early zebrafish embryogenesis Activation of JNK triggers release of Brd4 from mitotic chromosomes and mediates protection from drug-induced mitotic stress Bromodomain protein Brd4 plays a key role in Merkel cell polyomavirus DNA replication Brd4 is required for recovery from antimicrotubule drug-induced mitotic arrest: preservation of acetylated chromatin BRD4 short isoform interacts with RRP1B, SIPA1 and components of the LINC complex at the inner face of the nuclear membrane The double bromodomain protein Brd4 binds to acetylated chromatin during interphase and mitosis RNA Polymerase II Regulates Topoisomerase 1 Activity to Favor Efficient Transcription.Abrogation of the Brd4-positive transcription elongation factor B complex by papillomavirus E2 protein contributes to viral oncogene repression Papillomavirus interaction with cellular chromatin.BET proteins are a key component of immunoglobulin gene expression.Interaction of bovine papillomavirus E2 protein with Brd4 stabilizes its association with chromatin.Role of BRD4 in hematopoietic differentiation of embryonic stem cells.Brd2/RING3 interacts with a chromatin-binding domain in the Kaposi's Sarcoma-associated herpesvirus latency-associated nuclear antigen 1 (LANA-1) that is required for multiple functions of LANA-1.BET inhibition as a single or combined therapeutic approach in primary paediatric B-precursor acute lymphoblastic leukaemia.Recruitment of Brd4 to the human papillomavirus type 16 DNA replication complex is essential for replication of viral DNA.Use of epigenetic drugs in disease: an overview.Small-molecular modulators of cancer-associated epigenetic mechanisms.Mechanistic analysis of the role of bromodomain-containing protein 4 (BRD4) in BRD4-NUT oncoprotein-induced transcriptional activation.Brd4 is displaced from HPV replication factories as they expand and amplify viral DNA Brd4 is required for e2-mediated transcriptional activation but not genome partitioning of all papillomaviruses.Kaposi's sarcoma-associated herpesvirus LANA-1 interacts with the short variant of BRD4 and releases cells from a BRD4- and BRD2/RING3-induced G1 cell cycle arrest.Perturbation of BRD4 protein function by BRD4-NUT protein abrogates cellular differentiation in NUT midline carcinoma Replication and partitioning of papillomavirus genomes.Bromodomain-Containing Protein 4: A Dynamic Regulator of Breast Cancer Metastasis through Modulation of the Extracellular Matrix.

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A Mammalian bromodomain protein, brd4, interacts with replication factor C and inhibits progression to S phase

http://www.wikidata.org/entity/Q24540065

description

2002 nî lūn-bûn

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2002 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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2002 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2002年の論文

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A Mammalian bromodomain protei ...... nhibits progression to S phase

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A Mammalian bromodomain protei ...... nhibits progression to S phase

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A Mammalian bromodomain protei ...... nhibits progression to S phase

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MCB.22.18.6509-6520.2002

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Molecular and Cellular Biology

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A Mammalian bromodomain protei ...... nhibits progression to S phase

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Andrea Farina

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Anup Dey

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JaeHun Cheong

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Jerard Hurwitz

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Jon Shuman

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Keiko Ozato

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Selvaggia Sciortino

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Tetsuo Maruyama

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Tomohiko Tamura

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Vladimir P Bermudez

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P2860

Structure and ligand of a histone acetyltransferase bromodomain

A bromodomain protein, MCAP, associates with mitotic chromosomes and affects G(2)-to-M transition

Replication factor C interacts with the C-terminal side of proliferating cell nuclear antigen

Reconstitution of recombinant human replication factor C (RFC) and identification of an RFC subcomplex possessing DNA-dependent ATPase activity

A multifunctional DNA-binding protein that promotes the formation of serum response factor/homeodomain complexes: identity to TFII-I

cDNAs encoding the large subunit of human replication factor C

A conserved domain of the large subunit of replication factor C binds PCNA and acts like a dominant negative inhibitor of DNA replication in mammalian cells

RING3 kinase transactivates promoters of cell cycle regulatory genes through E2F

The structural basis for the recognition of acetylated histone H4 by the bromodomain of histone acetyltransferase gcn5p

BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures

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