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Artikel ; Online: Conditional Human BRD4 Knock-In Transgenic Mouse Genotyping and Protein Isoform Detection.

Lewis, Michael Paul / Wu, Shwu-Yuan / Chiang, Cheng-Ming

2022 Band 12, Heft 7

Abstract: Bromodomain-containing protein 4 (BRD4) is an acetyl-lysine reader protein and transcriptional regulator implicated in chromatin dynamics and cancer development. Several BRD4 isoforms have been detected in humans with the long isoform (BRD4-L, aa 1-1,362) ...

Abstract	Bromodomain-containing protein 4 (BRD4) is an acetyl-lysine reader protein and transcriptional regulator implicated in chromatin dynamics and cancer development. Several BRD4 isoforms have been detected in humans with the long isoform (BRD4-L, aa 1-1,362) playing a tumor-suppressive role and a major short isoform (BRD4-S, aa 1-722) having oncogenic activity in breast cancer development.
Sprache	Englisch
Erscheinungsdatum	2022-04-05
Erscheinungsland	United States
Dokumenttyp	Journal Article
ZDB-ID	2833269-6
ISSN	2331-8325 ; 2331-8325
ISSN (online)	2331-8325
ISSN	2331-8325
DOI	10.21769/BioProtoc.4374
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Novel BRD4-p53 Inhibitor SDU-071 Suppresses Proliferation and Migration of MDA-MB-231 Triple-Negative Breast Cancer Cells.

Wang, Shumei / Lei, Kang / Lai, Hsien-Tsung / Liu, Tingting / Du, Lupei / Wu, Shwu-Yuan / Ye, Xiaohan / Chiang, Cheng-Ming / Li, Minyong

ACS pharmacology & translational science

2024 Band 7, Heft 4, Seite(n) 1178–1190

Abstract: A promising alternative for cancer treatment involves targeted inhibition of the epigenetic regulator bromodomain-containing protein 4 (BRD4); however, available BRD4 inhibitors are constrained by their potency, oral bioavailability, and cytotoxicity. ... ...

Abstract	A promising alternative for cancer treatment involves targeted inhibition of the epigenetic regulator bromodomain-containing protein 4 (BRD4); however, available BRD4 inhibitors are constrained by their potency, oral bioavailability, and cytotoxicity. Herein, to overcome the drawback of the translational BRD4 inhibitors, we describe a novel BRD4-p53 inhibitor, SDU-071, which suppresses BRD4 interaction with the p53 tumor suppressor and its biological activity in MDA-MB-231 triple-negative breast cancer (TNBC) cells in vitro and in vivo. This novel small-molecule BRD4-p53 inhibitor suppresses cell proliferation, migration, and invasion by downregulating the expression of BRD4-targeted genes, such as c-Myc and Mucin 5AC, and inducing cell cycle arrest and apoptosis, as demonstrated in cultured MDA-MB-231 TNBC cells. Its antitumor activity is illustrated in an orthotopic mouse xenograft mammary tumor model. Overall, our results show that SDU-071 is a viable option for potentially treating TNBC as a new BRD4-p53 inhibitor.
Sprache	Englisch
Erscheinungsdatum	2024-03-12
Erscheinungsland	United States
Dokumenttyp	Journal Article
ISSN	2575-9108
ISSN (online)	2575-9108
DOI	10.1021/acsptsci.4c00057
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: The matrix protein of respiratory syncytial virus suppresses interferon signaling via RACK1 association.

Cao, Jingjing / Shi, Menghan / Zhu, Lina / Li, Xiangzhi / Li, Aiying / Wu, Shwu-Yuan / Chiang, Cheng-Ming / Zhang, Youming

Journal of virology

2023 Band 97, Heft 10, Seite(n) e0074723

Abstract: Importance: Respiratory syncytial virus (RSV) matrix (M) protein is indispensable for virion assembly and release. It is localized to the nucleus during early infection to perturb host transcription. However, the function of RSV M protein in other ... ...

Abstract	Importance: Respiratory syncytial virus (RSV) matrix (M) protein is indispensable for virion assembly and release. It is localized to the nucleus during early infection to perturb host transcription. However, the function of RSV M protein in other cellular activities remains poorly understood. In this study, several interferon response-associated host factors, including RACK1, were identified by proteomic analysis as RSV M interactors. Knockdown of RACK1 attenuates RSV-restricted IFN signaling leading to enhanced host defense against RSV infection, unraveling a role of M protein in antagonizing IFN response via association with RACK1. Our study uncovers a previously unrecognized mechanism of immune evasion by RSV M protein and identifies RACK1 as a novel host factor recruited by RSV, highlighting RACK1 as a potential new target for RSV therapeutics development.
Mesh-Begriff(e)	Humans ; Interferons ; Neoplasm Proteins/genetics ; Proteins ; Proteomics ; Receptors for Activated C Kinase/metabolism ; Respiratory Syncytial Virus Infections/metabolism ; Respiratory Syncytial Virus Infections/virology ; Respiratory Syncytial Virus, Human/genetics ; Viral Matrix Proteins/metabolism
Chemische Substanzen	Interferons (9008-11-1) ; Neoplasm Proteins ; Proteins ; RACK1 protein, human ; Receptors for Activated C Kinase ; Viral Matrix Proteins
Sprache	Englisch
Erscheinungsdatum	2023-09-15
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/jvi.00747-23
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: An investigation of the influence of reactive oxygen species produced from riboflavin-5'-phosphate by blue or violet light on the inhibition of WiDr colon cancer cells.

Chiu, Chi-Ming / Lee, Shwu-Yuan / Chen, Pin-Rong / Zhan, Shao-Qi / Yuann, Jeu-Ming P / Huang, Shiuh-Tsuen / Wu, Ming-Fang / Cheng, Chien-Wei / Chang, Yu-Chung / Liang, Ji-Yuan

Photodiagnosis and photodynamic therapy

2023 Band 44, Seite(n) 103810

Abstract: Riboflavin-5'-phosphate (FMN), an innocuous product of riboflavin (RF) phosphorylation, is vital for humans. FMN is sensitive to light illumination, as indicated by reactive oxygen species (ROS) formation. This investigation was undertaken to evaluate ... ...

Abstract	Riboflavin-5'-phosphate (FMN), an innocuous product of riboflavin (RF) phosphorylation, is vital for humans. FMN is sensitive to light illumination, as indicated by reactive oxygen species (ROS) formation. This investigation was undertaken to evaluate the influence of blue light illumination (BLI) and violet light illumination (VLI) upon FMN to develop a method to inhibit WiDr colon cancer cells by FMN photolysis. When FMN is subjected to BLI and VLI, it inhibits WiDr colon cancer cells by generating superoxide radical anions (O
Mesh-Begriff(e)	Humans ; Reactive Oxygen Species/metabolism ; Light ; Photochemotherapy/methods ; Photosensitizing Agents/pharmacology ; Riboflavin/pharmacology ; Colonic Neoplasms/drug therapy ; Phosphates
Chemische Substanzen	Reactive Oxygen Species ; Photosensitizing Agents ; Riboflavin (TLM2976OFR) ; Phosphates
Sprache	Englisch
Erscheinungsdatum	2023-09-23
Erscheinungsland	Netherlands
Dokumenttyp	Journal Article
ZDB-ID	2149918-4
ISSN	1873-1597 ; 1572-1000
ISSN (online)	1873-1597
ISSN	1572-1000
DOI	10.1016/j.pdpdt.2023.103810
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Direct interaction with the BRD4 carboxyl-terminal motif (CTM) and TopBP1 is required for human papillomavirus 16 E2 association with mitotic chromatin and plasmid segregation function.

Prabhakar, Apurva T / James, Claire D / Fontan, Christian T / Otoa, Raymonde / Wang, Xu / Bristol, Molly L / Yeager, Calvin / Hill, Ronald D / Dubey, Aanchal / Wu, Shwu-Yuan / Chiang, Cheng-Ming / Morgan, Iain M

Journal of virology

2023 Band 97, Heft 10, Seite(n) e0078223

Abstract: Importance: Human papillomavirus 16 (HPV16) is a causative agent in around 3%-4% of all human cancers, and currently, there are no anti-viral therapeutics available for combating this disease burden. In order to identify new therapeutic targets, we must ...

Abstract	Importance: Human papillomavirus 16 (HPV16) is a causative agent in around 3%-4% of all human cancers, and currently, there are no anti-viral therapeutics available for combating this disease burden. In order to identify new therapeutic targets, we must increase our understanding of the HPV16 life cycle. Previously, we demonstrated that an interaction between E2 and the cellular protein TopBP1 mediates the plasmid segregation function of E2, allowing distribution of viral genomes into daughter nuclei following cell division. Here, we demonstrate that E2 interaction with an additional host protein, BRD4, is also essential for E2 segregation function, and that BRD4 exists in a complex with TopBP1. Overall, these results enhance our understanding of a critical part of the HPV16 life cycle and presents several therapeutic targets for disruption of the viral life cycle.
Mesh-Begriff(e)	Humans ; Bromodomain Containing Proteins ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Chromatin/metabolism ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Human papillomavirus 16/genetics ; Human papillomavirus 16/metabolism ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Oncogene Proteins, Viral/genetics ; Oncogene Proteins, Viral/metabolism ; Plasmids/genetics ; Transcription Factors/genetics ; Transcription Factors/metabolism
Chemische Substanzen	BRD4 protein, human ; Bromodomain Containing Proteins ; Cell Cycle Proteins ; Chromatin ; DNA-Binding Proteins ; Nuclear Proteins ; Oncogene Proteins, Viral ; Transcription Factors ; E2 protein, Human papillomavirus type 16 ; TOPBP1 protein, human
Sprache	Englisch
Erscheinungsdatum	2023-09-15
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/jvi.00782-23
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel: Direct interaction with the BRD4 carboxyl-terminal motif (CTM) and TopBP1 is required for human papillomavirus 16 E2 association with mitotic chromatin and plasmid segregation function.

Prabhakar, Apurva T / James, Claire D / Fontan, Christian T / Otoa, Raymonde / Wang, Xu / Bristol, Molly L / Hill, Ronald D / Dubey, Aanchal / Wu, Shwu-Yuan / Chiang, Cheng-Ming / Morgan, Iain M

bioRxiv : the preprint server for biology

2023

Abstract: During the human papillomavirus 16 life cycle, the E2 protein binds simultaneously to the viral genome and host chromatin throughout mitosis, ensuring viral genomes reside in daughter cell nuclei following cell division. Previously, we demonstrated that ... ...

Abstract	During the human papillomavirus 16 life cycle, the E2 protein binds simultaneously to the viral genome and host chromatin throughout mitosis, ensuring viral genomes reside in daughter cell nuclei following cell division. Previously, we demonstrated that CK2 phosphorylation of E2 on serine 23 promotes interaction with TopBP1, and that this interaction is required for optimum E2 mitotic chromatin association and plasmid segregation function. Others have implicated BRD4 in mediating the plasmid segregation function of E2 and we have demonstrated that there is a TopBP1-BRD4 complex in the cell. We therefore further investigated the role of the E2-BRD4 interaction in mediating E2 association with mitotic chromatin and plasmid segregation function. Using a combination of immunofluorescence and our novel plasmid segregation assay in U2OS and N/Tert-1 cells stably expressing a variety of E2 mutants, we report that direct interaction with the BRD4 carboxyl-terminal motif (CTM) and TopBP1 is required for E2 association with mitotic chromatin and plasmid segregation. We also identify a novel TopBP1 mediated interaction between E2 and the BRD4 extra-terminal (ET) domain Importance: HPV16 is a causative agent in around 3-4% of all human cancers and currently there are no anti-viral therapeutics available for combating this disease burden. In order to identify new therapeutic targets, we must increase our understanding of the HPV16 life cycle. Previously, we demonstrated that an interaction between E2 and the cellular protein TopBP1 mediates the plasmid segregation function of E2, allowing distribution of viral genomes into daughter nuclei following cell division. Here, we demonstrate that E2 interaction with an additional host protein, BRD4, is also essential for E2 segregation function, and that BRD4 exists in a complex with TopBP1. Overall, these results enhance our understanding of a critical part of the HPV16 life cycle and presents several therapeutic targets for disruption of the viral life cycle.
Sprache	Englisch
Erscheinungsdatum	2023-05-26
Erscheinungsland	United States
Dokumenttyp	Preprint
DOI	10.1101/2023.05.25.542291
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: IDR-targeting compounds suppress HPV genome replication via disruption of phospho-BRD4 association with DNA damage response factors.

Wu, Shwu-Yuan / Lai, Hsien-Tsung / Sanjib Banerjee, N / Ma, Zonghui / Santana, Juan F / Wei, Shuguang / Liu, Xisheng / Zhang, Meirong / Zhan, Jian / Chen, Haiying / Posner, Bruce / Chen, Yadong / Price, David H / Chow, Louise T / Zhou, Jia / Chiang, Cheng-Ming

Molecular cell

2023 Band 84, Heft 2, Seite(n) 202–220.e15

Abstract: Compounds binding to the bromodomains of bromodomain and extra-terminal (BET) family proteins, particularly BRD4, are promising anticancer agents. Nevertheless, side effects and drug resistance pose significant obstacles in BET-based therapeutics ... ...

Abstract	Compounds binding to the bromodomains of bromodomain and extra-terminal (BET) family proteins, particularly BRD4, are promising anticancer agents. Nevertheless, side effects and drug resistance pose significant obstacles in BET-based therapeutics development. Using high-throughput screening of a 200,000-compound library, we identified small molecules targeting a phosphorylated intrinsically disordered region (IDR) of BRD4 that inhibit phospho-BRD4 (pBRD4)-dependent human papillomavirus (HPV) genome replication in HPV-containing keratinocytes. Proteomic profiling identified two DNA damage response factors-53BP1 and BARD1-crucial for differentiation-associated HPV genome amplification. pBRD4-mediated recruitment of 53BP1 and BARD1 to the HPV origin of replication occurs in a spatiotemporal and BRD4 long (BRD4-L) and short (BRD4-S) isoform-specific manner. This recruitment is disrupted by phospho-IDR-targeting compounds with little perturbation of the global transcriptome and BRD4 chromatin landscape. The discovery of these protein-protein interaction inhibitors (PPIi) not only demonstrates the feasibility of developing PPIi against phospho-IDRs but also uncovers antiviral agents targeting an epigenetic regulator essential for virus-host interaction and cancer development.
Mesh-Begriff(e)	Humans ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Human Papillomavirus Viruses ; Papillomavirus Infections/drug therapy ; Papillomavirus Infections/genetics ; Proteomics ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Papillomaviridae/genetics ; Papillomaviridae/metabolism ; Viral Proteins/genetics ; Virus Replication/physiology ; DNA Repair ; Bromodomain Containing Proteins
Chemische Substanzen	Transcription Factors ; Nuclear Proteins ; Cell Cycle Proteins ; Viral Proteins ; BRD4 protein, human ; Bromodomain Containing Proteins
Sprache	Englisch
Erscheinungsdatum	2023-12-15
Erscheinungsland	United States
Dokumenttyp	Journal Article
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2023.11.022
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Discovery, X-ray Crystallography, and Anti-inflammatory Activity of Bromodomain-containing Protein 4 (BRD4) BD1 Inhibitors Targeting a Distinct New Binding Site.

Liu, Zhiqing / Li, Yi / Chen, Haiying / Lai, Hsien-Tsung / Wang, Pingyuan / Wu, Shwu-Yuan / Wold, Eric A / Leonard, Paul G / Joseph, Sarah / Hu, Haitao / Chiang, Cheng-Ming / Brasier, Allan R / Tian, Bing / Zhou, Jia

Journal of medicinal chemistry

2022 Band 65, Heft 3, Seite(n) 2388–2408

Abstract: Bromodomain-containing protein 4 (BRD4) is an emerging epigenetic drug target for intractable inflammatory disorders. The lack of highly selective inhibitors among BRD4 family members has stalled the collective understanding of this critical system and ... ...

Abstract	Bromodomain-containing protein 4 (BRD4) is an emerging epigenetic drug target for intractable inflammatory disorders. The lack of highly selective inhibitors among BRD4 family members has stalled the collective understanding of this critical system and the progress toward clinical development of effective therapeutics. Here we report the discovery of a potent BRD4 bromodomain 1 (BD1)-selective inhibitor ZL0590 (
Mesh-Begriff(e)	Animals ; Anti-Inflammatory Agents/chemical synthesis ; Anti-Inflammatory Agents/metabolism ; Anti-Inflammatory Agents/pharmacokinetics ; Anti-Inflammatory Agents/pharmacology ; Binding Sites ; Cell Cycle Proteins/antagonists & inhibitors ; Cell Cycle Proteins/metabolism ; Cell Line ; Crystallography, X-Ray ; Gene Expression/drug effects ; Humans ; Interleukin-6/genetics ; Interleukin-6/metabolism ; Male ; Mice, Inbred C57BL ; Nuclear Proteins/antagonists & inhibitors ; Oxidoreductases Acting on CH-CH Group Donors/genetics ; Oxidoreductases Acting on CH-CH Group Donors/metabolism ; Phenylurea Compounds/chemical synthesis ; Phenylurea Compounds/metabolism ; Phenylurea Compounds/pharmacokinetics ; Phenylurea Compounds/pharmacology ; Protein Binding ; Protein Domains ; Rats ; Transcription Factors/antagonists & inhibitors ; Transcription Factors/metabolism ; Mice
Chemische Substanzen	Anti-Inflammatory Agents ; BRD4 protein, human ; Brd4 protein, mouse ; Cell Cycle Proteins ; IL6 protein, human ; Interleukin-6 ; Nuclear Proteins ; Phenylurea Compounds ; Transcription Factors ; Oxidoreductases Acting on CH-CH Group Donors (EC 1.3.-) ; RSAD2 protein, human (EC 1.3.-)
Sprache	Englisch
Erscheinungsdatum	2022-01-04
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	218133-2
ISSN	1520-4804 ; 0022-2623
ISSN (online)	1520-4804
ISSN	0022-2623
DOI	10.1021/acs.jmedchem.1c01851
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel: The Influence of the Degradation of Tetracycline by Free Radicals from Riboflavin-5'-Phosphate Photolysis on Microbial Viability.

Huang, Shiuh-Tsuen / Lee, Shwu-Yuan / Wang, Song-Hua / Wu, Chun-Yi / Yuann, Jeu-Ming P / He, Sin / Cheng, Chien-Wei / Liang, Ji-Yuan

Microorganisms

2019 Band 7, Heft 11

Abstract: Tetracycline (TC) is a broad-spectrum antibiotic compound. Wastewater with TC may have an adverse effect on ecosystems. Riboflavin-5'-phosphate (FMN or flavin mononucleotide) is a non-toxic product of the phosphorylation of vitamin ... ...

Abstract	Tetracycline (TC) is a broad-spectrum antibiotic compound. Wastewater with TC may have an adverse effect on ecosystems. Riboflavin-5'-phosphate (FMN or flavin mononucleotide) is a non-toxic product of the phosphorylation of vitamin B
Sprache	Englisch
Erscheinungsdatum	2019-10-28
Erscheinungsland	Switzerland
Dokumenttyp	Journal Article
ZDB-ID	2720891-6
ISSN	2076-2607
ISSN	2076-2607
DOI	10.3390/microorganisms7110500
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Involvement of Brd4 in different steps of the papillomavirus life cycle.

Iftner, Thomas / Haedicke-Jarboui, Juliane / Wu, Shwu-Yuan / Chiang, Cheng-Ming

Virus research

2017 Band 231, Seite(n) 76–82

Abstract: Bromodomain-containing protein 4 (Brd4) is a cellular chromatin-binding factor and transcriptional regulator that recruits sequence-specific transcription factors and chromatin modulators to control target gene transcription. Papillomaviruses (PVs) have ... ...

Abstract	Bromodomain-containing protein 4 (Brd4) is a cellular chromatin-binding factor and transcriptional regulator that recruits sequence-specific transcription factors and chromatin modulators to control target gene transcription. Papillomaviruses (PVs) have evolved to hijack Brd4's activity in order to create a facilitating environment for the viral life cycle. Brd4, in association with the major viral regulatory protein E2, is involved in multiple steps of the PV life cycle including replication initiation, viral gene transcription, and viral genome segregation and maintenance. Phosphorylation of Brd4, regulated by casein kinase II (CK2) and protein phosphatase 2A (PP2A), is critical for viral gene transcription as well as E1- and E2-dependent origin replication. Thus, pharmacological agents regulating Brd4 phosphorylation and inhibitors blocking phospho-Brd4 functions are promising candidates for therapeutic intervention in treating human papillomavirus (HPV) infections as well as associated disease.
Sprache	Englisch
Erscheinungsdatum	2017-03-02
Erscheinungsland	Netherlands
Dokumenttyp	Journal Article ; Review
ZDB-ID	605780-9
ISSN	1872-7492 ; 0168-1702
ISSN (online)	1872-7492
ISSN	0168-1702
DOI	10.1016/j.virusres.2016.12.006
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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