Suppression of inflammation by a synthetic histone mimic

Translating the Histone Code

Jenuwein, T., & Allis, C. D. (2001) · Science · doi:10.1126/science.1063127 · Cited by 9,756 · see citing works

Immunodesign of experimental sepsis by cecal ligation and puncture

Rittirsch, D., Huber-Lang, M. S., Flierl, M. A., & Ward, P. A. (2009) · Nature Protocols · doi:10.1038/nprot.2008.214 · Cited by 2,209 · see citing works

How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers

Taverna, S. D., Li, H., Ruthenburg, A. J., Allis, C. D., & Patel, D. J. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1338 · Cited by 1,419 · see citing works

The Bromodomain Protein Brd4 Is a Positive Regulatory Component of P-TEFb and Stimulates RNA Polymerase II-Dependent Transcription

Jang, M. K., Mochizuki, K., Zhou, M., Jeong, H., Brady, J. N., & Ozato, K. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.06.027 · Cited by 1,301 · see citing works

Distinct Factors Control Histone Variant H3.3 Localization at Specific Genomic Regions

Goldberg, A. D., Banaszynski, L. A., Noh, K., Lewis, P. W., Elsässer, S. J., Stadler, S. C., Dewell, S. B., Law, M. J., Guo, X., Li, X., et al. (2010) · Cell · doi:10.1016/j.cell.2010.01.003 · Cited by 1,281 · see citing works

An extensive network of coupling among gene expression machines

Maniatis, T., & Reed, R. (2002) · Nature · doi:10.1038/416499a · Cited by 1,148 · see citing works

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 · see citing works

Transcriptional control of the inflammatory response

Medzhitov, R., & Horng, T. (2009) · Nature Reviews Immunology · doi:10.1038/nri2634 · Cited by 1,035 · see citing works

Multivalent engagement of chromatin modifications by linked binding modules

Ruthenburg, A. J., Li, H., Patel, D. J., & Allis, C. D. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2298 · Cited by 1,015 · see citing works

Chromatin immunoprecipitation and microarray-based analysis of protein location

Lee, T. I., Johnstone, S. E., & Young, R. A. (2006) · Nature Protocols · doi:10.1038/nprot.2006.98 · Cited by 743 · see citing works

Elongation by RNA polymerase II: the short and long of itPreprint

Sims, R. J., Belotserkovskaya, R., & Reinberg, D. (2004) · Genes & Development · doi:10.1101/gad.1235904 · Cited by 709 · see citing works

Control of RNA Polymerase II Elongation Potential by a Novel Carboxyl-terminal Domain Kinase

Marshall, N. F., Peng, J., Xie, Z., & Price, D. H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.43.27176 · Cited by 662 · see citing works

Control of Inducible Gene Expression by Signal-Dependent Transcriptional Elongation

Hargreaves, D. C., Horng, T., & Medzhitov, R. M. (2009) · Cell · doi:10.1016/j.cell.2009.05.047 · Cited by 649 · see citing works

Brd4 Coactivates Transcriptional Activation of NF-κB via Specific Binding to Acetylated RelA

Huang, B., Yang, X., Zhou, M., Ozato, K., & Chen, L. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01365-08 · Cited by 586 · see citing works

A Unifying Model for the Selective Regulation of Inducible Transcription by CpG Islands and Nucleosome Remodeling

Ramirez-Carrozzi, V. R., Braas, D., Bhatt, D. M., Cheng, C. S., Hong, C., Doty, K. R., Black, J. C., Hoffmann, A., Carey, M., & Smale, S. T. (2009) · Cell · doi:10.1016/j.cell.2009.04.020 · Cited by 581 · see citing works

Selective and antagonistic functions of SWI/SNF and Mi-2beta nucleosome remodeling complexes during an inflammatory response.Preprint

Ramirez-Carrozzi, V., Nazarian, A. A., Li, C.-Y. C., Gore, S., Sridharan, R., Imbalzano, A., & Smale, S. (2006) · Genes & Development · doi:10.1101/gad.1383206 · Cited by 456 · see citing works

The Double Bromodomain Proteins Brd2 and Brd3 Couple Histone Acetylation to Transcription

LeRoy, G., Rickards, B., & Flint, S. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.01.018 · Cited by 374 · see citing works

Selective Transcription in Response to an Inflammatory Stimulus

Smale, S. T. (2010) · Cell · doi:10.1016/j.cell.2010.01.037 · Cited by 318 · see citing works

Mammalian mediator of transcriptional regulation and its possible role as an end-point of signal transduction pathways.

Jiang, Y.-W., Veschambre, P., Erdjument-Bromage, H., Tempst, P., Conaway, J., Conaway, R., & Kornberg, R. (1998) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.95.15.8538 · Cited by 315 · see citing works

Identification of Transcription Complexes that Contain the Double Bromodomain Protein Brd2 and Chromatin Remodeling Machines

Denis, G. V., McComb, M. E., Faller, D. V., Sinha, A., Romesser, P. B., & Costello, C. E. (2006) · Journal of Proteome Research · doi:10.1021/pr050430u · Cited by 144 · see citing works

Structures of the Dual Bromodomains of the P-TEFb-activating Protein Brd4 at Atomic Resolution

Vollmuth, F., Blankenfeldt, W., & Geyer, M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.033712 · Cited by 137 · see citing works

The Short and Long of It: Neural Correlates of Temporal-order Memory for Autobiographical Events

Jacques, P. L. S., Rubin, D. C., LaBar, K. S., & Cabeza, R. E. L. (2008) · Journal of Cognitive Neuroscience · doi:10.1162/jocn.2008.20091 · Cited by 129 · see citing works

Control of NF- B-dependent Transcriptional Responses by Chromatin OrganizationPreprint

Natoli, G. (2009) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000224 · Cited by 96 · see citing works

Pyrin Critical to Macrophage IL-1β Response to Francisella Challenge

Gavrilin, M. A., Mitra, S., Seshadri, S., Nateri, J., Berhe, F., Hall, M. W., & Wewers, M. D. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0803073 · Cited by 88 · see citing works

Brd4 Is Required for Recovery from Antimicrotubule Drug-induced Mitotic Arrest: Preservation of Acetylated Chromatin

Nishiyama, A., Dey, A., Miyazaki, J., & Ozato, K. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-08-0729 · Cited by 78 · see citing works

Expression and characterization of recombinant human acyloxyacyl hydrolase, a leukocyte enzyme that deacylates bacterial lipopolysaccharides

Hagen, F. S., Grant, F. J., Kuijper, J. L., et al. (1991) · Biochemistry · doi:10.1021/bi00098a020 · Cited by 67 · see citing works

Solution structure of the second bromodomain of Brd2 and its specific interaction with acetylated histone tails

Huang, H., Zhang, J., Shen, W., Wang, X., Wu, J., Wu, J., & Shi, Y. (2007) · BMC Structural Biology · doi:10.1186/1472-6807-7-57 · Cited by 62 · see citing works

Structural Basis and Binding Properties of the Second Bromodomain of Brd4 with Acetylated Histone Tails

Liu, Y., Wang, X., Zhang, J., Huang, H., Ding, B., Wu, J., & Shi, Y. (2008) · Biochemistry · doi:10.1021/bi8001659 · Cited by 59 · see citing works

Cancer epigenetics: from mechanism to therapy

Dawson, M. A., & Kouzarides, T. (2012) · Cell · doi:10.1016/j.cell.2012.06.013 · Cited by 3,203 · see citing works

Selective Inhibition of Tumor Oncogenes by Disruption of Super-Enhancers

Lovén, J., Hoke, H. A., Lin, C. Y., Lau, A., Orlando, D. A., Vakoc, C. R., Bradner, J. E., Lee, T. I., & Young, R. A. (2013) · Cell · doi:10.1016/j.cell.2013.03.036 · Cited by 2,961 · see citing works

Trained immunity: A program of innate immune memory in health and– disease

Netea, M. G., Joosten, L. A. B., Latz, E., Mills, K. H. G., Natoli, G., Stunnenberg, H. G., O’Neill, L. A. J., & Xavier, R. J. (2016) · Science · doi:10.1126/science.aaf1098 · Cited by 2,768 · see citing works

The molecular hallmarks of epigenetic control

Allis, C. D., & Jenuwein, T. (2016) · Nature Reviews Genetics · doi:10.1038/nrg.2016.59 · Cited by 2,809 · see citing works

Transcriptional regulation of macrophage polarization: enabling diversity with identity

Lawrence, T., & Natoli, G. (2011) · Nature Reviews Immunology · doi:10.1038/nri3088 · Cited by 2,284 · see citing works

Phthalimide conjugation as a strategy for in vivo target protein degradation

Winter, G. E., Buckley, D. L., Paulk, J., Roberts, J. M., Souza, A., Dhe-Paganon, S., & Bradner, J. E. (2015) · Science · doi:10.1126/science.aab1433 · Cited by 1,760 · see citing works

Histone deacetylases and their inhibitors in cancer, neurological diseases and immune disorders

Falkenberg, K. J., & Johnstone, R. W. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4360 · Cited by 1,564 · see citing works

Epigenetic protein families: a new frontier for drug discovery

Arrowsmith, C. H., Bountra, C., Fish, P. V., Lee, K., & Schapira, M. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3674 · Cited by 1,327 · see citing works

Structural basis of PROTAC cooperative recognition for selective protein degradation

Gadd, M. S., Testa, A., Lucas, X., Chan, K.-H., Chen, W., Lamont, D. J., Zengerle, M., & Ciulli, A. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2329 · Cited by 1,242 · see citing works

Targeting epigenetic regulators for cancer therapy: mechanisms and advances in clinical trials

Cheng, Y., He, C., Wang, M., Ma, X., Mo, F., Yang, S., Han, J., & Wei, X. (2019) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-019-0095-0 · Cited by 1,097 · see citing works

Anti-Inflammatory Therapy in Chronic Disease: Challenges and Opportunities

Tabas, I., & Glass, C. K. (2013) · Science · doi:10.1126/science.1230720 · Cited by 1,093 · see citing works

Selective Small Molecule Induced Degradation of the BET Bromodomain Protein BRD4

Zengerle, M., Chan, K.-H., & Ciulli, A. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00216 · Cited by 1,056 · see citing works

ATP-dependent chromatin remodeling: genetics, genomics and mechanisms

Hargreaves, D. C., & Crabtree, G. R. (2011) · Cell Research · doi:10.1038/cr.2011.32 · Cited by 923 · see citing works

The role of myeloid cells in cancer therapies

Engblom, C., Pfirschke, C., & Pittet, M. J. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.54 · Cited by 788 · see citing works

Tet2 is required to resolve inflammation by recruiting Hdac2 to specifically repress IL-6

Zhang, Q., Zhao, K., Shen, Q., Han, Y., Gu, Y., Li, X., Zhao, D., Liu, Y., Wang, C., Zhang, X., et al. (2015) · Nature · doi:10.1038/nature15252 · Cited by 807 · see citing works

Remodeling of the enhancer landscape during macrophage activation is coupled to enhancer transcription

Kaikkonen, M. U., Spann, N. J., Heinz, S., Romanoski, C. E., Allison, K. A., Stender, J. D., Chun, H. B., Tough, D. F., Prinjha, R. K., Benner, C., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.07.010 · Cited by 672 · see citing works

Modulators of Protein–Protein Interactions

Milroy, L.-G., Grossmann, T. N., Hennig, S., Brunsveld, L., & Ottmann, C. (2014) · Chemical Reviews · doi:10.1021/cr400698c · Cited by 497 · see citing works

BET Proteins as Targets for Anticancer Treatment

Stathis, A., & Bertoni, F. (2018) · Cancer Discovery · doi:10.1158/2159-8290.cd-17-0605 · Cited by 463 · see citing works

Epigenetic mechanisms in neurological disease

Jakovcevski, M., & Akbarian, S. (2012) · Nature Medicine · doi:10.1038/nm.2828 · Cited by 450 · see citing works

BRD4 Connects Enhancer Remodeling to Senescence Immune Surveillance

Tasdemir, N., Banito, A., Roe, J.-S., Alonso-Curbelo, D., Camiolo, M., Tschaharganeh, D. F., Huang, C.-H., Aksoy, O., Bolden, J. E., Chen, C.-C., et al. (2016) · Cancer Discovery · doi:10.1158/2159-8290.cd-16-0217 · Cited by 415 · see citing works

BET Bromodomains Mediate Transcriptional Pause Release in Heart Failure

Anand, P., Brown, J. D., Lin, C. Y., Qi, J., Zhang, R., Artero, P. C., Alaiti, M. A., Bullard, J., Alazem, K., Margulies, K. B., et al. (2013) · Cell · doi:10.1016/j.cell.2013.07.013 · Cited by 406 · see citing works

Selective inhibition of the BD2 bromodomain of BET proteins in prostate cancer

Faivre, E. J., McDaniel, K. F., Albert, D. H., Mantena, S. R., Plotnik, J. P., Wilcox, D., Zhang, L., Bui, M. H., Sheppard, G. S., Wang, L., et al. (2020) · Nature · doi:10.1038/s41586-020-1930-8 · Cited by 408 · see citing works

Requirement for the histone deacetylase Hdac3 for the inflammatory gene expression program in macrophages

Chen, X., Barozzi, I., Termanini, A., Prosperini, E., Recchiuti, A., Dalli, J., Mietton, F., Matteoli, G., Hiebert, S., & Natoli, G. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1121131109 · Cited by 397 · see citing works

Different Neuronal Activity Patterns Induce Different Gene Expression Programs

Tyssowski, K. M., DeStefino, N. R., Cho, J.-H., Dunn, C. J., Poston, R. G., Carty, C. E., Jones, R. D., Chang, S. M., Romeo, P., Wurzelmann, M. K., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.04.001 · Cited by 390 · see citing works

Epigenetic regulation of the innate immune response to infection

Zhang, Q., & Cao, X. (2019) · Nature Reviews Immunology · doi:10.1038/s41577-019-0151-6 · Cited by 366 · see citing works

Light-Induced Protein Degradation with Photocaged PROTACs

Xue, G., Wang, K., Zhou, D., Zhong, H., & Pan, Z. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b06422 · Cited by 377 · see citing works

Synergistic Activation of Inflammatory Cytokine Genes by Interferon-γ-Induced Chromatin Remodeling and Toll-like Receptor Signaling

Qiao, Y., Giannopoulou, E. G., Chan, C. H., Park, S.-H., Gong, S., Chen, J., Hu, X., Elemento, O., & Ivashkiv, L. B. (2013) · Immunity · doi:10.1016/j.immuni.2013.08.009 · Cited by 330 · see citing works

The BET family in immunity and disease

Wang, N., Wu, R., Tang, D., & Kang, R. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00384-4 · Cited by 295 · see citing works

Emerging roles for chromatin as a signal integration and storage platform

Badeaux, A. I., & Shi, Y. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3545 · Cited by 291 · see citing works

Discovery of QCA570 as an Exceptionally Potent and Efficacious Proteolysis Targeting Chimera (PROTAC) Degrader of the Bromodomain and Extra-Terminal (BET) Proteins Capable of Inducing Complete and Durable Tumor Regression

Qin, C., Hu, Y., Zhou, B., Fernandez-Salas, E., Yang, C.-Y., Liu, L., McEachern, D., Przybranowski, S., Wang, M., Stuckey, J., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00506 · Cited by 281 · see citing works

Clinical trials for BET inhibitors run ahead of the science

Andrieu, G., Belkina, A. C., & Denis, G. V. (2016) · Drug Discovery Today: Technologies · doi:10.1016/j.ddtec.2016.06.004 · Cited by 247 · see citing works

A transcriptional switch governs fibroblast activation in heart disease

Alexanian, M., Przytycki, P. F., Micheletti, R., Padmanabhan, A., Ye, L., Travers, J. G., Gonzalez-Teran, B., Silva, A. C., Duan, Q., Ranade, S. S., et al. (2021) · Nature · doi:10.1038/s41586-021-03674-1 · Cited by 238 · see citing works

BRD4 is a novel therapeutic target for liver fibrosis

Ding, N., Hah, N., Yu, R. T., Sherman, M. H., Benner, C., Leblanc, M., He, M., Liddle, C., Downes, M., & Evans, R. M. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1522163112 · Cited by 211 · see citing works

Targeted Protein Degradation by Small Molecules

Bondeson, D. P., & Crews, C. M. (2017) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010715-103507 · Cited by 207 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Modulating PCAF/GCN5 Immune Cell Function through a PROTAC Approach

Bassi, Z. I., Fillmore, M. C., Miah, A. H., Chapman, T. D., Maller, C., Roberts, E. J., Davis, L. C., Lewis, D. E., Galwey, N. W., Waddington, K. E., et al. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.8b00705 · Cited by 186 · see citing works

A mechanism for expansion of regulatory T-cell repertoire and its role in self-tolerance

Feng, Y., van der Veeken, J., Shugay, M., Putintseva, E. V., Osmanbeyoglu, H. U., Dikiy, S., Hoyos, B. E., Moltedo, B., Hemmers, S., Treuting, P., et al. (2015) · Nature · doi:10.1038/nature16141 · Cited by 157 · see citing works

Bromo- and Extraterminal Domain Chromatin Regulators Serve as Cofactors for Murine Leukemia Virus Integration

Gupta, S. S., Maetzig, T., Maertens, G. N., Sharif, A., Rothe, M., Weidner-Glunde, M., Galla, M., Schambach, A., Cherepanov, P., & Schulz, T. F. (2013) · Journal of Virology · doi:10.1128/jvi.01942-13 · Cited by 139 · see citing works

DAMPs, ageing, and cancer: The ‘DAMP Hypothesis’

Huang, J., Xie, Y., Sun, X., Zeh, H. J., Kang, R., Lotze, M. T., & Tang, D. (2015) · Ageing Research Reviews · doi:10.1016/j.arr.2014.10.004 · Cited by 144 · see citing works

Amide-to-Ester Substitution as a Strategy for Optimizing PROTAC Permeability and Cellular Activity

Klein, V. G., Bond, A. G., Craigon, C., Lokey, R. S., & Ciulli, A. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01496 · Cited by 152 · see citing works

Role of Epigenetics in Inflammation-Associated diseases

Shanmugam, M. K., & Sethi, G. (2013) · Subcellular Biochemistry · doi:10.1007/978-94-007-4525-4_27 · Cited by 141 · see citing works

Epigenetic Changes in Diabetes and Cardiovascular Risk

Keating, S. T., Plutzky, J., & El-Osta, A. (2016) · Circulation Research · doi:10.1161/circresaha.116.306819 · Cited by 139 · see citing works

Inhibition of CGAS-STING by JQ1 Alleviates Oxidative Stress-Induced Retina Inflammation and Degeneration

Zou, M., Ke, Q., Nie, Q., Qi, R., Zhu, X., Liu, W., Hu, X., Sun, Q., Fu, J.-L., Tang, X., et al. (2022) · Cell Death & Differentiation · doi:10.1038/s41418-022-00967-4 · Cited by 138 · see citing works

Biophysical regulation of macrophages in health and disease

Meli, V. S., Veerasubramanian, P. K., Atcha, H., Reitz, Z., Downing, T. L., & Liu, W. F. (2019) · Journal of Leukocyte Biology · doi:10.1002/jlb.mr0318-126r · Cited by 133 · see citing works

Chemoproteomics and Chemical Probes for Target Discovery

Drewes, G., & Knapp, S. (2018) · Trends in Biotechnology · doi:10.1016/j.tibtech.2018.06.008 · Cited by 132 · see citing works

Epigenetic targeting of bromodomain protein BRD4 counteracts cancer cachexia and prolongs survival

Segatto, M., Fittipaldi, R., Pin, F., Sartori, R., Dae Ko, K., Zare, H., Fenizia, C., Zanchettin, G., Pierobon, E. S., Hatakeyama, S., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01645-7 · Cited by 101 · see citing works

Proteogenomic characterization and mapping of nucleosomes decoded by Brd and HP1 proteins

LeRoy, G., Chepelev, I., DiMaggio, P. A., Blanco, M. A., Zee, B. M., Zhao, K., & Garcia, B. A. (2012) · Genome Biology · doi:10.1186/gb-2012-13-8-r68 · Cited by 84 · see citing works

Chromatin kinases act on transcription factors and histone tails in regulation of inducible transcription

Josefowicz, S. Z., Shimada, M., Armache, A., Li, C. H., Miller, R. M., Lin, S., Yang, A., Dill, B. D., Molina, H., Park, H.-S., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.09.026 · Cited by 84 · see citing works

Structure of the Brd4 ET domain bound to a C-terminal motif from γ-retroviral integrases reveals a conserved mechanism of interaction

Crowe, B. L., Larue, R. C., Yuan, C., Hess, S., Kvaratskhelia, M., & Foster, M. P. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1516813113 · Cited by 83 · see citing works

BRD4 regulates cellular senescence in gastric cancer cells via E2F/miR-106b/p21 axis

Dong, X., Hu, X., Chen, J., Hu, D., & Chen, L.-F. (2018) · Cell Death & Disease · doi:10.1038/s41419-017-0181-6 · Cited by 75 · see citing works

BET Bromodomain Proteins as Cancer Therapeutic Targets

Shu, S., & Polyak, K. (2016) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2016.81.030908 · Cited by 72 · see citing works

Dual‐target inhibitors of bromodomain and extra‐terminal proteins in cancer: A review from medicinal chemistry perspectives

Feng, L., Wang, G., Chen, Y., He, G., Liu, B., Liu, J., Chiang, C., & Ouyang, L. (2022) · Medicinal Research Reviews · doi:10.1002/med.21859 · Cited by 65 · see citing works

BRD4 (Bromodomain-Containing Protein 4) Interacts with GATA4 (GATA Binding Protein 4) to Govern Mitochondrial Homeostasis in Adult Cardiomyocytes

Padmanabhan, A., Alexanian, M., Linares-Saldana, R., González-Terán, B., Andreoletti, G., Huang, Y., Connolly, A. J., Kim, W., Hsu, A., Duan, Q., et al. (2020) · Circulation · doi:10.1161/circulationaha.120.047753 · Cited by 60 · see citing works

Epigenetic Mechanisms Governing Innate Inflammatory Responses

Perkins, D. J., Patel, M. C., Blanco, J. C. G., & Vogel, S. N. (2016) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2016.0003 · Cited by 51 · see citing works

Targeting protein–protein interactions in hematologic malignancies: still a challenge or a great opportunity for future therapies?

Cierpicki, T., & Grembecka, J. (2015) · Immunological Reviews · doi:10.1111/imr.12244 · Cited by 53 · see citing works

Discovery of novel small molecule induced selective degradation of the bromodomain and extra-terminal (BET) bromodomain protein BRD4 and BRD2 with cellular potencies

Jiang, F., Wei, Q., Li, H., Li, H., Cui, Y., Ma, Y., Chen, H., Cao, P., Lu, T., & Chen, Y. (2020) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2019.115181 · Cited by 48 · see citing works

BRD4 inhibitors block telomere elongation

Wang, S., Pike, A. M., Lee, S. S., Strong, M. A., Connelly, C. J., & Greider, C. W. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx561 · Cited by 45 · see citing works

Protein–Protein Interaction Modulators for Epigenetic Therapies

(2018) · Advances in Protein Chemistry and Structural Biology · doi:10.1016/bs.apcsb.2017.06.002 · Cited by 31 · see citing works

A Src-H3 acetylation signaling axis integrates macrophage mechanosensation with inflammatory response

Veerasubramanian, P. K., Shao, H., Meli, V. S., Phan, T. A. Q., Luu, T. U., Liu, W. F., & Downing, T. L. (2021) · Biomaterials · doi:10.1016/j.biomaterials.2021.121236 · Cited by 28 · see citing works

Selective Targeting of Epigenetic Readers and Histone Deacetylases in Autoimmune and Inflammatory Diseases: Recent Advances and Future Perspectives

Ghiboub, M., Elfiky, A. M. I., de Winther, M. P. J., Harker, N. R., Tough, D. F., & de Jonge, W. J. (2021) · Journal of Personalized Medicine · doi:10.3390/jpm11050336 · Cited by 28 · see citing works

Protein-Protein Interactions as Drug Targets

Wendt, M. D. (2012) · Topics in Medicinal Chemistry · doi:10.1007/978-3-642-28965-1_1 · Cited by 9 · see citing works

Senescence Can Be BETter without the SASP?

Vizioli, M. G., & Adams, P. D. (2016) · Cancer Discovery · doi:10.1158/2159-8290.cd-16-0485 · Cited by 6 · see citing works

Evaluating the Advantages of Using 3D-Enriched Fragments for Targeting BET Bromodomains

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Law, R. P., Atkinson, S. J., Bamborough, P., Chung, C., Demont, E. H., Gordon, L. J., Lindon, M. J., Prinjha, R. K., Watson, A. J. B., & Hirst, D. J. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01666 · Cited by 121 · see citing works

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