Selective inhibition of BET bromodomains

Efficacy and Safety of a Specific Inhibitor of the BCR-ABL Tyrosine Kinase in Chronic Myeloid Leukemia

Druker, B. J., Talpaz, M., Resta, D. J., Peng, B., Buchdunger, E., Ford, J., Lydon, N., Kantarjian, H. M., Capdeville, R., Ohno-Jones, S., et al. (2001) · New England Journal of Medicine · doi:10.1056/nejm200104053441401 · Cited by 5,237

Effects of a selective inhibitor of the Abl tyrosine kinase on the growth of Bcr–Abl positive cells

Druker, B. J., Tamura, S., Buchdunger, E., Ohno-Jones, S., Segal, G. M., Fanning, S., Zimmermann, J., & Lydon, N. (1996) · Nature Medicine · doi:10.1038/nm0596-561 · Cited by 3,652

Use of all-trans retinoic acid in the treatment of acute promyelocytic leukemia

Huang, M., Ye, Y., Chen, S. R., Chai, J., Lu, J., Zhoa, L., Gu, L.-J., & Wang, Z.-Y. (1988) · Blood · doi:10.1182/blood.v72.2.567.567 · Cited by 2,445

The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability

Niesen, F., Berglund, H., & Vedadi, M. (2007) · Nature Protocols · doi:10.1038/nprot.2007.321 · Cited by 2,420

Structural Mechanism for STI-571 Inhibition of Abelson Tyrosine Kinase

Schindler, T. H., Bornmann, W. G., Pellicena, P., Miller, W. T., Clarkson, B., & Kuriyan, J. (2000) · Science · doi:10.1126/science.289.5486.1938 · Cited by 1,785

c-Myc Regulates Transcriptional Pause Release

Rahl, P. B., Lin, C. Y., Seila, A. C., Flynn, R. A., McCuine, S., Burge, C. B., Sharp, P. A., & Young, R. A. (2010) · Cell · doi:10.1016/j.cell.2010.03.030 · Cited by 1,279

Recruitment of P-TEFb for Stimulation of Transcriptional Elongation by the Bromodomain Protein Brd4

Yang, Z., Yik, J. H. N., Chen, R., He, N., Jang, M. K., Ozato, K., & Zhou, Q. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.06.029 · Cited by 1,141

Inhibition of the Abl protein-tyrosine kinase in vitro and in vivo by a 2-phenylaminopyrimidine derivative.

Buchdunger, E., Zimmermann, J., Mett, H., Meyer, T., Müller, M., Druker, B. J., & Lydon, N. (1996) · PubMed · Cited by 1,057

Bromodomain: an acetyl‐lysine binding domain

Zeng, L., & Zhou, M. (2002) · FEBS Letters · doi:10.1016/s0014-5793(01)03309-9 · Cited by 751

Regulation of the glucocorticoid receptor via a BET-dependent enhancer drives antiandrogen resistance in prostate cancer

Shah, N., Wang, P., Wongvipat, J., Karthaus, W. R., Abida, W. M., Armenia, J., Rockowitz, S., Drier, Y., Bernstein, B., Long, H. W., et al. (2017) · eLife · doi:10.7554/elife.27861 · Cited by 207

The oncogenic BRD4-NUT chromatin regulator drives aberrant transcription within large topological domainsPreprint

Alekseyenko, A. A., Walsh, E. M., Wang, X., Grayson, A. R., Hsi, P. T., Kharchenko, P. V., Kuroda, M. I., & French, C. A. (2015) · Genes & Development · doi:10.1101/gad.267583.115 · Cited by 205

RNA cytosine methylation and methyltransferases mediate chromatin organization and 5-azacytidine response and resistance in leukaemia

Cheng, J. X., Chen, L., Li, Y., Cloe, A., Yue, M., Wei, J., Watanabe, K. A., Shammo, J. M., Anastasi, J., Shen, Q. J., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-03513-4 · Cited by 204

Synthetic Lethal and Resistance Interactions with BET Bromodomain Inhibitors in Triple-Negative Breast Cancer

Shu, S., Wu, H., Ge, J. Y., Zeid, R., Harris, I. S., Jovanović, B., Murphy, K. C., Wang, B., Qiu, X., Endress, J. E., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.04.027 · Cited by 204

Dissecting Fragment-Based Lead Discovery at the von Hippel-Lindau Protein:Hypoxia Inducible Factor 1α Protein-Protein Interface

Molle, I. V., Thomann, A., Buckley, D. L., So, E. C., Lang, S., Crews, C. M., & Ciulli, A. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.08.015 · Cited by 203

Eusocial insects as emerging models for behavioural epigenetics

Yan, H., Simola, D. F., Bonasio, R., Liebig, J., Berger, S. L., & Reinberg, D. (2014) · Nature Reviews Genetics · doi:10.1038/nrg3787 · Cited by 203

The bromodomain: From epigenome reader to druggable target

Sánchez, R., Meslamani, J. E., & Zhou, M. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.03.011 · Cited by 201

Rational Chemical Design of Molecular Glue Degraders

Toriki, E. S., Papatzimas, J. W., Nishikawa, K., Dovala, D., Frank, A. O., Hesse, M. J., Danková, D., Song, J.-G., Bruce-Smythe, M., Struble, H., et al. (2023) · ACS Central Science · doi:10.1021/acscentsci.2c01317 · Cited by 202

Strategies targeting cellular senescence

Ovadya, Y., & Krizhanovsky, V. (2018) · Journal of Clinical Investigation · doi:10.1172/jci95149 · Cited by 200

Identification of a Chemical Probe for Bromo and Extra C-Terminal Bromodomain Inhibition through Optimization of a Fragment-Derived Hit

Fish, P. V., Filippakopoulos, P., Bish, G., Brennan, P. E., Bunnage, M. E., Cook, A. S., Federov, O., Gerstenberger, B. S., Jones, H. M., Knapp, S., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm3010515 · Cited by 200

In Silico Modeling of PROTAC-Mediated Ternary Complexes: Validation and Application

Drummond, M. L., & Williams, C. I. (2019) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.8b00872 · Cited by 199

Targeted Degradation of BET Proteins in Triple-Negative Breast Cancer

Bai, L., Zhou, B., Yang, C.-Y., Ji, J., McEachern, D., Przybranowski, S., Jiang, H., Hu, J., Xu, F., Zhao, Y., et al. (2017) · Cancer Research · doi:10.1158/0008-5472.can-16-2622 · Cited by 199

RVX-208, an Inducer of ApoA-I in Humans, Is a BET Bromodomain Antagonist

McLure, K. G., Gesner, E. M., Tsujikawa, L. M., Kharenko, O. A., Attwell, S., Campeau, E., Wasiak, S., Stein, A. J., White, A., Fontano, E., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0083190 · Cited by 200

Opposing Functions of BRD4 Isoforms in Breast Cancer

Wu, S.-Y., Lee, C.-F., Lai, H., Yu, C., Lee, J., Zuo, H., Tsai, S. Y., Tsai, M., Ge, K., Wan, Y., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.04.034 · Cited by 201

METTL3 Inhibitors for Epitranscriptomic Modulation of Cellular Processes

Moroz, E., Danzhi Huang, A., Bedi, R. K., Cheriyamkunnel, S. J., Bochenkova, E., Dolbois, A., Rzeczkowski, M. D., Li, Y., Wiedmer, L., & Caflisch, A. (2021) · ChemMedChem · doi:10.1002/cmdc.202100291 · Cited by 199

Place your BETs: the therapeutic potential of bromodomains

Prinjha, R. K., Witherington, J., & Lee, K. (2012) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2011.12.002 · Cited by 197

BacPROTACs mediate targeted protein degradation in bacteria

Morreale, F. E., Kleine, S., Leodolter, J., Junker, S., Hoi, D. M., Ovchinnikov, S., Okun, A., Kley, J., Kurzbauer, R., Junk, L., et al. (2022) · Cell · doi:10.1016/j.cell.2022.05.009 · Cited by 196

Targeting Protein-Protein Interaction by Small Molecules

Jin, L., Wang, W., & Fang, G. (2014) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-011613-140028 · Cited by 195

Highly Active Combination of BRD4 Antagonist and Histone Deacetylase Inhibitor against Human Acute Myelogenous Leukemia Cells

Fiskus, W. C., Sharma, S., Qi, J., Valenta, J. A., Schaub, L. J., Shah, B., Peth, K., Portier, B. P., Rodríguez, M., Devaraj, S. G. T., et al. (2014) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-13-0770 · Cited by 195

EGFR Mutation Promotes Glioblastoma through Epigenome and Transcription Factor Network Remodeling

Liu, F., Hon, G. C., Villa, G. R., Turner, K. M., Ikegami, S., Yang, H., Ye, Z., Li, B., Kuan, S., Lee, A. Y., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.09.002 · Cited by 194

Inducible In Vivo Silencing of Brd4 Identifies Potential Toxicities of Sustained BET Protein Inhibition

Bolden, J. E., Tasdemir, N., Dow, L. E., van Es, J. H., Wilkinson, J. E., Zhao, Z., Clevers, H. C., & Lowe, S. W. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.08.025 · Cited by 194

Disrupting Acetyl-Lysine Recognition: Progress in the Development of Bromodomain Inhibitors

Romero, F. A., Taylor, A. M., Crawford, T. D., Tsui, V., Côté, A., & Magnuson, S. R. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01514 · Cited by 194

Re-programing Chromatin with a Bifunctional LSD1/HDAC Inhibitor Induces Therapeutic Differentiation in DIPG

Anastas, J. N., Zee, B. M., Kalin, J. H., Kim, M., Guo, R., Alexandrescu, S., Blanco, M. A., Giera, S., Gillespie, S. M., Das, J., et al. (2019) · Cancer Cell · doi:10.1016/j.ccell.2019.09.005 · Cited by 197

Phosphorylation-Inducing Chimeric Small Molecules

Siriwardena, S. U., Godage, D. N. P. M., Shoba, V. M., Lai, S., Shi, M., Wu, P., Chaudhary, S. K., Schreiber, S. L., & Choudhary, A. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c05537 · Cited by 195

BET proteins promote efficient murine leukemia virus integration at transcription start sites

Sharma, A., Larue, R. C., Plumb, M. R., Malani, N., Male, F., Slaughter, A., Kessl, J. J., Shkriabai, N., Coward, E., Aiyer, S. S., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1307157110 · Cited by 193

A rationale to target the SWI/SNF complex for cancer therapy

Hohmann, A. F., & Vakoc, C. R. (2014) · Trends in Genetics · doi:10.1016/j.tig.2014.05.001 · Cited by 193

Lysine acetylation and cancer: A proteomics perspective

Gil, J., Ramírez-Torres, A., & Encarnación‐Guevara, S. (2016) · Journal of Proteomics · doi:10.1016/j.jprot.2016.10.003 · Cited by 191

Tudor: a versatile family of histone methylation ‘readers’

Lu, R., & Wang, G. G. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.08.002 · Cited by 190

Targeting MYCN-Driven Transcription By BET-Bromodomain Inhibition

Henssen, A. G., Althoff, K., Odersky, A., Beckers, A., Koche, R. P., Speleman, F., Schäfers, S., Bell, E., Nortmeyer, M., Westermann, F., et al. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-15-1449 · Cited by 190

Sensitivity and engineered resistance of myeloid leukemia cells to BRD9 inhibition

Hohmann, A. F., Martin, L. J., Minder, J. L., Roe, J., Shi, J., Steurer, S., Bader, G., McConnell, D. B., Pearson, M. A., Gerstberger, T., et al. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2115 · Cited by 190

Fragment-Based Discovery of Bromodomain Inhibitors Part 1: Inhibitor Binding Modes and Implications for Lead Discovery

Chung, C., Dean, A. W., Woolven, J. M., & Bamborough, P. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm201320w · Cited by 189

The Role of Bromodomain Proteins in Regulating Gene Expression

Josling, G. A., Selvarajah, S. A., Petter, M., & Duffy, M. F. (2012) · Genes · doi:10.3390/genes3020320 · Cited by 189

The Discovery of I-BET726 (GSK1324726A), a Potent Tetrahydroquinoline ApoA1 Up-Regulator and Selective BET Bromodomain Inhibitor

Gosmini, R. L., Nguyen, V. L., Toum, J., Simon, C., Brusq, J.-M. G., Krysa, G., Mirguet, O., Riou, A. M., Boursier, E. V., Trottet, L., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm5010539 · Cited by 189

Bromodomain Protein BRD4 Is Required for Estrogen Receptor-Dependent Enhancer Activation and Gene Transcription

Nagarajan, S., Hossan, T., Alawi, M., Najafova, Z., Indenbirken, D., Bedi, U., Taipaleenmäki, H., Batalla, I. B., Scheller, M., Loges, S., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.06.016 · Cited by 189

Bromodomain-Containing Protein 4

Meloche, J., Potus, F., Vaillancourt, M., Bourgeois, A., Johnson, I., Deschamps, L., Chabot, S., Ruffenach, G., Henry, S., Breuils‐Bonnet, S., et al. (2015) · Circulation Research · doi:10.1161/circresaha.115.307004 · Cited by 188

MYC, a downstream target of BRD-NUT, is necessary and sufficient for the blockade of differentiation in NUT midline carcinoma

Grayson, A. R., Walsh, E. M., Cameron, M. J., Godec, J., Ashworth, T. D., Ambrose, J. M., Aserlind, A. B., Wang, H., Evan, G. I., Kluk, M., et al. (2013) · Oncogene · doi:10.1038/onc.2013.126 · Cited by 187

Blockade of oncogenic IκB kinase activity in diffuse large B-cell lymphoma by bromodomain and extraterminal domain protein inhibitors

Ceribelli, M., Kelly, P. N., Shaffer, A. L., Wright, G. W., Xiao, W., Yang, Y., Griner, L. A. M., Guha, R., Shinn, P., Keller, J. M., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1411701111 · Cited by 187

Protein-Observed Fluorine NMR: A Bioorthogonal Approach for Small Molecule Discovery

Arntson, K. E., & Pomerantz, W. C. K. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01447 · Cited by 187

Targeting Cancer Cells with BET Bromodomain InhibitorsPreprint

Xu, Y., & Vakoc, C. R. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026674 · Cited by 187

TP63, SOX2, and KLF5 Establish a Core Regulatory Circuitry That Controls Epigenetic and Transcription Patterns in Esophageal Squamous Cell Carcinoma Cell Lines

Jiang, Y., Jiang, Y., Li, C.-Q., Zhang, Y., Dakle, P., Hp, K., Deng, J.-W., Lin, R. Y., Yan, Y., Xie, J.-J., et al. (2020) · Gastroenterology · doi:10.1053/j.gastro.2020.06.050 · Cited by 186

Cancer-associated IDH2 mutants drive an acute myeloid leukemia that is susceptible to Brd4 inhibitionPreprint

Chen, C., Liu, Y., Lü, C., Cross, J. R., Morris, J. P., Shroff, A., Ward, P. S., Bradner, J. E., Thompson, C. B., & Lowe, S. W. (2013) · Genes & Development · doi:10.1101/gad.226613.113 · Cited by 186

Bromodomain-containing Protein 4 (BRD4) Regulates RNA Polymerase II Serine 2 Phosphorylation in Human CD4+ T Cells

Weishi, Z., Prakash, C., Sum, C., Gong, Y., Li, Y., Kwok, J. J. T., Thiessen, N., Pettersson, S., Jones, S. J. M., Knapp, S., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.413047 · Cited by 185

Opposing effects of cancer-type-specific SPOP mutants on BET protein degradation and sensitivity to BET inhibitors

Janoušková, H., Tekle, G. E., Bellini, E., Udeshi, N. D., Rinaldi, A. M., Ulbricht, A., Bernasocchi, T., Civenni, G., Losa, M., Svinkina, T., et al. (2017) · Nature Medicine · doi:10.1038/nm.4372 · Cited by 185

Visualizing biologically active small molecules in cells using click chemistry

Cañeque, T., Müller, S., & Rodriguez, R. (2018) · Nature Reviews Chemistry · doi:10.1038/s41570-018-0030-x · Cited by 185

Selective inhibition of CD4 + T-cell cytokine production and autoimmunity by BET protein and c-Myc inhibitors

Bandukwala, H. S., Gagnon, J. D., Togher, S., Greenbaum, J., Lamperti, E. D., Parr, N. J., Molesworth, A. M. H., Smithers, N. N., Lee, K. C., Witherington, J. J., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1212264109 · Cited by 184

Mass Spectrometry-Based Proteomics in Preclinical Drug Discovery

Schirle, M., Bantscheff, M., & Küster, B. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.01.002 · Cited by 184

Hot spots in protein–protein interfaces: Towards drug discovery

Cukuroglu, E., Engin, H. B., Gürsoy, A., & Keskin, Ö. (2014) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2014.06.003 · Cited by 184

Progress in the Development and Application of Small Molecule Inhibitors of Bromodomain–Acetyl-lysine Interactions

Hewings, D. S., Rooney, T. P. C., Jennings, L. E., Hay, D. A., Schofield, C. J., Brennan, P. E., Knapp, S., & Conway, S. J. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300915b · Cited by 184

Cell of Origin and Genetic Alterations in the Pathogenesis of Multiple Myeloma

Barwick, B. G., Gupta, V. A., Vertino, P. M., & Boise, L. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01121 · Cited by 184

Distinct chromatin functional states correlate with HIV latency reactivation in infected primary CD4+ T cells

Battivelli, E., Dahabieh, M. S., Abdel‐Mohsen, M., Svensson, J. P., da Silva, I. T., Cohn, L. B., Gramatica, A., Deeks, S. G., Greene, W. C., Pillai, S. K., et al. (2018) · eLife · doi:10.7554/elife.34655 · Cited by 183

RNAs interact with BRD4 to promote enhanced chromatin engagement and transcription activation

Rahnamoun, H., Lee, J. H., Sun, Z., Lu, H., Ramsey, K. M., Komives, E. A., & Lauberth, S. M. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0102-0 · Cited by 184

Interactome Rewiring Following Pharmacological Targeting of BET Bromodomains

Lambert, J., Picaud, S., Fujisawa, T., Hou, H., Savitsky, P. A., Uusküla-Reimand, L., Gupta, G. D., Abdouni, H. S., Lin, Z., Tucholska, M., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.11.006 · Cited by 183

Genome-wide localization of small molecules

Anders, L., Guenther, M. G., Qi, J., Fan, Z. P., Marineau, J., Rahl, P. B., Lovén, J., Sigova, A. A., Smith, W. B., Lee, T. I., et al. (2013) · Nature Biotechnology · doi:10.1038/nbt.2776 · Cited by 182

BRD4 Coordinates Recruitment of Pause Release Factor P-TEFb and the Pausing Complex NELF/DSIF To Regulate Transcription Elongation of Interferon-Stimulated Genes

Patel, M. C., Debrosse, M., Smith, M. D., Dey, A., Huynh, W., Sarai, N., Heightman, T. D., Tamura, T., & Ozato, K. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01180-12 · Cited by 182

Targeting smooth muscle cell phenotypic switching in vascular disease

Chakraborty, R., Chatterjee, P., Dave, J. M., Ostriker, A. C., Greif, D. M., Rzucidlo, E. M., & Martin, K. A. (2021) · JVS Vascular Science · doi:10.1016/j.jvssci.2021.04.001 · Cited by 182

Greater Than the Sum of Parts: Complexity of the Dynamic Epigenome

Soshnev, A. A., Josefowicz, S. Z., & Allis, C. D. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.05.004 · Cited by 181

Role of MYC in medulloblastoma

Roussel, M. F., & Robinson, G. W. (2013) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a014308 · Cited by 180

Enhancer Remodeling during Adaptive Bypass to MEK Inhibition Is Attenuated by Pharmacologic Targeting of the P-TEFb Complex

Zawistowski, J. S., Bevill, S. M., Goulet, D. R., Stuhlmiller, T. J., Beltran, A. S., Olivares-Quintero, J. F., Singh, D., Sciaky, N., Parker, J. S., Rashid, N. U., et al. (2017) · Cancer Discovery · doi:10.1158/2159-8290.cd-16-0653 · Cited by 180

Targeting the differential addiction to anti-apoptotic BCL-2 family for cancer therapy

Inoue‐Yamauchi, A., Jeng, P., Kim, K., Chen, H., Han, S., Ganesan, Y. T., Ishizawa, K., Jebiwott, S., Dong, Y., Pietanza, M. C., et al. (2017) · Nature Communications · doi:10.1038/ncomms16078 · Cited by 180

Dynamic Chromatin Targeting of BRD4 Stimulates Cardiac Fibroblast Activation

Stratton, M. S., Bagchi, R. A., Felisbino, M. B., Hirsch, R. A., Smith, H. E., Riching, A. S., Enyart, B. Y., Koch, K. A., Cavasin, M. A., Alexanian, M., et al. (2019) · Circulation Research · doi:10.1161/circresaha.119.315125 · Cited by 179

Potent BRD4 inhibitor suppresses cancer cell-macrophage interaction

Yin, M., Guo, Y., Hu, R., Cai, W. L., Li, Y., Pei, S., Sun, H., Peng, C., Li, J., Ye, R., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15290-0 · Cited by 179

Identifying drug targets in tissues and whole blood with thermal-shift profiling

Perrin, J., Werner, T., Kurzawa, N., Rutkowska, A., Childs, D. D., Kalxdorf, M., Poeckel, D., Stonehouse, E., Strohmer, K., Heller, B., et al. (2020) · Nature Biotechnology · doi:10.1038/s41587-019-0388-4 · Cited by 178

MYC in pancreatic cancer: novel mechanistic insights and their translation into therapeutic strategies

Heßmann, E., Schneider, G., Ellenrieder, V., & Siveke, J. T. (2015) · Oncogene · doi:10.1038/onc.2015.216 · Cited by 178

“Minimalist” Cyclopropene-Containing Photo-Cross-Linkers Suitable for Live-Cell Imaging and Affinity-Based Protein Labeling

Li, Z., Wang, D., Li, L., Pan, S., Na, Z., Tan, C. Y. J., & Yao, S. Q. (2014) · Journal of the American Chemical Society · doi:10.1021/ja502780z · Cited by 178

Feedback Activation of Leukemia Inhibitory Factor Receptor Limits Response to Histone Deacetylase Inhibitors in Breast Cancer

Zeng, H., Qu, J., Jin, N., Xu, J., Lin, C., Chen, Y., Yang, X., He, X., Tang, S., Lan, X., et al. (2016) · Cancer Cell · doi:10.1016/j.ccell.2016.08.001 · Cited by 178

Targeting epigenetics and non-coding RNAs in atherosclerosis: from mechanisms to therapeutics

Xu, S., Kamato, D., Little, P. J., Nakagawa, S., Pelisek, J., & Jin, Z. G. (2018) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.11.003 · Cited by 178

Therapeutic targets for cardiac fibrosis: from old school to next-gen

Travers, J. G., Tharp, C. A., Rubino, M., & McKinsey, T. A. (2022) · Journal of Clinical Investigation · doi:10.1172/jci148554 · Cited by 179

Reawakening fetal hemoglobin: prospects for new therapies for the β-globin disorders

Bauer, D. E., Kamran, S. C., & Orkin, S. H. (2012) · Blood · doi:10.1182/blood-2012-06-292078 · Cited by 177

Small Molecule Inhibitors of Bromodomain–Acetyl-lysine Interactions

Brand, M. J. D., Measures, A. M., Wilson, B. G., Cortopassi, W. A., Alexander, R. P., Höss, M., Hewings, D. S., Rooney, T. P. C., Paton, R. S., & Conway, S. J. (2014) · ACS Chemical Biology · doi:10.1021/cb500996u · Cited by 177

Topoisomerase 1 inhibition suppresses inflammatory genes and protects from death by inflammation

Rialdi, A., Campisi, L., Zhao, N., Lagda, A. C., Pietzsch, C. A., Ho, J., Martínez‐Gil, L., Fenouil, R., Chen, X., Edwards, M. R., et al. (2016) · Science · doi:10.1126/science.aad7993 · Cited by 177

Fragment-Based Discovery of Bromodomain Inhibitors Part 2: Optimization of Phenylisoxazole Sulfonamides

Bamborough, P., Diallo, H., Goodacre, J. D., Gordon, L. J., Lewis, A. J., Seal, J. T., Wilson, D. M., Woodrow, M. D., & Chung, C. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm201283q · Cited by 176

ZMYND8 acetylation mediates HIF-dependent breast cancer progression and metastasis

Chen, Y., Zhang, B., Bao, L., Jin, L., Yang, M., Peng, Y., Kumar, A., Wang, J. E., Wang, C., Zou, X., et al. (2018) · Journal of Clinical Investigation · doi:10.1172/jci95089 · Cited by 176

The BET Family of Proteins Targets Moloney Murine Leukemia Virus Integration near Transcription Start Sites

De Rijck, J., de Kogel, C., Demeulemeester, J., Vets, S., El Ashkar, S., Malani, N., Bushman, F. D., Landuyt, B., Husson, S. J., Busschots, K., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.09.040 · Cited by 175

Chromatin Accessibility Landscape of Cutaneous T Cell Lymphoma and Dynamic Response to HDAC Inhibitors

Qu, K., Zaba, L. C., Satpathy, A. T., Giresi, P. G., Li, R., Jin, Y., Armstrong, R. J., Chen, J., Schmitt, N., Rahbar, Z., et al. (2017) · Cancer Cell · doi:10.1016/j.ccell.2017.05.008 · Cited by 175

Epigenetics of hematopoiesis and hematological malignanciesPreprint

Hu, D., & Shilatifard, A. (2016) · Genes & Development · doi:10.1101/gad.284109.116 · Cited by 175

BET acetyl-lysine binding proteins control pathological cardiac hypertrophy

Spiltoir, J. I., Stratton, M. S., Cavasin, M. A., Demos-Davies, K., Reid, B. G., Qi, J., Bradner, J. E., & McKinsey, T. A. (2013) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2013.07.017 · Cited by 174

Antibody-Mediated Delivery of Chimeric BRD4 Degraders. Part 2: Improvement of In Vitro Antiproliferation Activity and In Vivo Antitumor Efficacy

Dragovich, P. S., Pillow, T. H., Blake, R. A., Sadowsky, J. D., Adaligil, E., Adhikari, P., Chen, J., Corr, N., dela Cruz-Chuh, J., Del Rosario, G., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01846 · Cited by 174

Histone Deacetylases Positively Regulate Transcription through the Elongation Machinery

Greer, C. B., Tanaka, Y., Kim, Y. J., Xie, P., Zhang, M. Q., Park, I.-H., & Kim, T. H. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.10.013 · Cited by 174

Inhibition of bromodomain and extra-terminal proteins (BET) as a potential therapeutic approach in haematological malignancies: emerging preclinical and clinical evidence

Chaidos, A., Caputo, V. S., & Karadimitris, A. (2015) · Therapeutic Advances in Hematology · doi:10.1177/2040620715576662 · Cited by 174

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Karakashev, S. V., Zhu, H., Yokoyama, Y., Zhao, B., Fatkhutdinov, N., Kossenkov, A. V., Wilson, A. J., Simpkins, F. A., Speicher, D. W., Khabele, D., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.11.095 · Cited by 174

Tumor Burden and Immunotherapy: Impact on Immune Infiltration and Therapeutic Outcomes

Kim, S. I., Cassella, C. R., & Byrne, K. T. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.629722 · Cited by 178

Rewiring cancer drivers to activate apoptosis

Gourisankar, S. P., Krokhotin, A., Ji, W., Liu, X., Chang, C.-Y., Kim, S. H., Li, Z., Wenderski, W., Simanauskaite, J., Yang, H., et al. (2023) · Nature · doi:10.1038/s41586-023-06348-2 · Cited by 174

Epstein-Barr Virus Oncoprotein Super-enhancers Control B Cell Growth

Zhou, H., Schmidt, S. C. S., Jiang, S., Willox, B., Bernhardt, K., Liang, J., Johannsen, E., Kharchenko, P. V., Gewurz, B. E., Kieff, E. D., et al. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2014.12.013 · Cited by 174

Direct observation of a condensate effect on super-enhancer controlled gene bursting

Du, M., Stitzinger, S. H., Spille, J.-H., Cho, W., Lee, C., Hijaz, M., Quintana, A., & Cissé, I. I. (2024) · Cell · doi:10.1016/j.cell.2023.12.005 · Cited by 176

Regulation ofMYCgene expression by aberrant Wnt/β-catenin signaling in colorectal cancer

Rennoll, S. A. (2015) · World Journal of Biological Chemistry · doi:10.4331/wjbc.v6.i4.290 · Cited by 174

Exploiting ferroptosis vulnerabilities in cancer

Nakamura, T., & Conrad, M. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01425-8 · Cited by 172

NF-κB: master regulator of cellular responses in health and disease

Hoffmann, A., Cheng, G., & Baltimore, D. (2025) · Immunity & Inflammation · doi:10.1007/s44466-025-00014-0 · Cited by 173

An in-tumor genetic screen reveals that the BET bromodomain protein, BRD4, is a potential therapeutic target in ovarian carcinoma

Baratta, M. G., Schinzel, A. C., Zwang, Y., Bandopadhayay, P., Bowman-Colin, C., Kutt, J., Curtis, J. D., Piao, H., Wong, L. C., Kung, A. L., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1422165112 · Cited by 171

Discovery of a chemical probe for the L3MBTL3 methyllysine reader domain

James, L. I., Baršytė-Lovejoy, D., Zhong, N., Krichevsky, L., Korboukh, V. K., Herold, J. M., MacNevin, C. J., Norris, J. L., Sagum, C. A., Tempel, W., et al. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1157 · Cited by 170

A poised fragment library enables rapid synthetic expansion yielding the first reported inhibitors of PHIP(2), an atypical bromodomain

Cox, O. B., Krojer, T. J., Collins, P. M., Monteiro, O., Talon, R., Bradley, A. R., Fedorov, O., Amin, J., Marsden, B. D., Spencer, J., et al. (2015) · Chemical Science · doi:10.1039/c5sc03115j · Cited by 170

Gain of function of ASXL1 truncating protein in the pathogenesis of myeloid malignancies

Yang, H., Kurtenbach, S., Guo, Y., Lohse, I., Durante, M. A., Li, J., Li, Z., Al‐Ali, H., Li, L., Chen, Z., et al. (2017) · Blood · doi:10.1182/blood-2017-06-789669 · Cited by 170

BET Bromodomain Inhibition Releases the Mediator Complex from Select cis-Regulatory Elements

Bhagwat, A. S., Roe, J., Mok, B. Y., Hohmann, A. F., Shi, J., & Vakoc, C. R. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.03.054 · Cited by 169

Epigenetics in rheumatoid arthritis

Klein, K., & Gay, S. (2014) · Current Opinion in Rheumatology · doi:10.1097/bor.0000000000000128 · Cited by 169

Learning the chemical grammar of biomolecular condensates

Kilgore, H. R., & Young, R. A. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01046-y · Cited by 174

DNA Hypomethylating Drugs in Cancer TherapyPreprint

Sato, T., Issa, J. J., & Kropf, P. L. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026948 · Cited by 169

Structure-Guided Design of IACS-9571, a Selective High-Affinity Dual TRIM24-BRPF1 Bromodomain Inhibitor

Palmer, W. S., Poncet-Montange, G., Liu, G., Petrocchi, A., Reyna, N., Subramanian, G., Theroff, J., Yau, A., Kost-Alimova, M., Bardenhagen, J. P., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00405 · Cited by 168

Discovery and Characterization of GSK2801, a Selective Chemical Probe for the Bromodomains BAZ2A and BAZ2B

Chen, P., Chaikuad, A., Bamborough, P., Bantscheff, M., Bountra, C., Chung, C., Fedorov, O., Grandi, P., Jung, D. K., Leśniak, R. K., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00209 · Cited by 168

DUB3 Promotes BET Inhibitor Resistance and Cancer Progression by Deubiquitinating BRD4

Jin, X., Yan, Y., Wang, D., Ding, D., Ma, T., Ye, Z., Jiménez, R. E., Wang, L., Wu, H., & Huang, H. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.06.036 · Cited by 169

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Jung, M., Gelato, K. A., Fernández‐Montalván, A. E., Siegel, S., & Haendler, B. (2015) · Epigenomics · doi:10.2217/epi.14.91 · Cited by 167

Comprehensive lysine acetylomes emerging from bacteria to humans

Kim, G.-W., & Yang, X. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.10.001 · Cited by 167

Abstract 2318: BET bromodomain inhibitors for cancer therapy

Qi, J., Filippakopoulos, P., McKeown, M. R., Shaw, K. L., Smith, W. B., French, C. A., Kung, A. L., Knapp, S., & Bradner, J. E. (2011) · Cancer Research · doi:10.1158/1538-7445.am2011-2318

Abstract IA16: Chemical inhibition of bromodomains

Bradner, J. E. (2012) · Cancer Research · doi:10.1158/1538-7445.csb12-ia16

Discovery and Characterization of Small Molecule Inhibitors of the BET Family Bromodomains

Chung, C., Coste, H., White, J. H. M., Mirguet, O., Wilde, J. I., Gosmini, R. L., Delves, C. J., Magny, S. D., Woodward, R., Hughes, S. A., et al. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm200108t · Cited by 338

Bromodomains: Structure, function and pharmacology of inhibition

Ferri, E., Petosa, C., & McKenna, C. E. (2015) · Biochemical Pharmacology · doi:10.1016/j.bcp.2015.12.005 · Cited by 249

Bromodomain Inhibition and Its Application to Human Disease

Dupper, N. J., Zhou, Y., Govin, J., & McKenna, C. E. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-813939-4.00011-5 · Cited by 2