Structure and ligand of a histone acetyltransferase bromodomain

AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR

Laskowski, R., Rullmann, J. A., MacArthur, M., Kaptein, R., & Thornton, J. (1996) · Journal of Biomolecular NMR · doi:10.1007/bf00228148 · Cited by 5,502 · see citing works

X-PLOR Version 3.1: A System for X-ray Crystallography and NMR

Brünger, A. T. (1992) · Medical Entomology and Zoology · Cited by 3,424 · see citing works

The Anatomy and Taxonomy of Protein Structure

Richardson, J. S. (1981) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60520-3 · Cited by 3,378 · see citing works

NMR View: A computer program for the visualization and analysis of NMR data

Johnson, B. A., & Blevins, R. A. (1994) · Journal of Biomolecular NMR · doi:10.1007/bf00404272 · Cited by 3,093 · see citing works

The Transcriptional Coactivators p300 and CBP Are Histone Acetyltransferases

Ogryzko, V. V., Schiltz, R. L., Russanova, V., Howard, B. H., & Nakatani, Y. (1996) · Cell · doi:10.1016/s0092-8674(00)82001-2 · Cited by 2,952 · see citing works

Histone acetylation in chromatin structure and transcription

Grunstein, M. (1997) · Nature · doi:10.1038/38664 · Cited by 2,884 · see citing works

Protein modules and signalling networks

Pawson, T. (1995) · Nature · doi:10.1038/373573a0 · Cited by 2,420 · see citing works

The CBP co-activator is a histone acetyltransferase

Bannister, A. J., & Kouzarides, T. (1996) · Nature · doi:10.1038/384641a0 · Cited by 1,824 · see citing works

Tetrahymena Histone Acetyltransferase A: A Homolog to Yeast Gcn5p Linking Histone Acetylation to Gene Activation

Brownell, J. E., Zhou, J., Ranalli, T. A., Kobayashi, R., Edmondson, D. G., Dent, S., & Allis, C. D. (1996) · Cell · doi:10.1016/s0092-8674(00)81063-6 · Cited by 1,636 · see citing works

A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A

Yang, X., Ogryzko, V. V., Nishikawa, J., Howard, B. H., & Nakatani, Y. (1996) · Nature · doi:10.1038/382319a0 · Cited by 1,473 · see citing works

Nuclear Receptor Coactivator ACTR Is a Novel Histone Acetyltransferase and Forms a Multimeric Activation Complex with P/CAF and CBP/p300

Chen, H., Lin, R. J., Schiltz, R. L., Chakravarti, D., Nash, A., Nagy, L., Privalsky, M. L., Nakatani, Y., & Evans, R. M. (1997) · Cell · doi:10.1016/s0092-8674(00)80516-4 · Cited by 1,465 · see citing works

RIBBONS 2.0

Carson, M. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891007240 · Cited by 809 · see citing works

Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines

Kuo, M.-H., Brownell, J. E., Sobel, R. E., Ranalli, T. A., Cook, R. G., Edmondson, D. G., Roth, S. Y., & Allis, C. D. (1996) · Nature · doi:10.1038/383269a0 · Cited by 596 · see citing works

Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional carbon-13 labeling

Neri, D., Szyperski, T., Otting, G., Senn, H., & Kurt Wüthrich, A. (1989) · Biochemistry · doi:10.1021/bi00445a003 · Cited by 563 · see citing works

Special HATs for special occasions: linking histone acetylation to chromatin assembly and gene activation

Brownell, J. E., & Allis, C. D. (1996) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(96)80048-7 · Cited by 534 · see citing works

A Suite of Triple Resonance NMR Experiments for the Backbone Assignment of 15N, 13C, 2H Labeled Proteins with High Sensitivity

Yamazaki, T., Lee, W., Arrowsmith, C. H., Muhandiram, D. R., & Kay, L. E. (1994) · Journal of the American Chemical Society · doi:10.1021/ja00105a005 · Cited by 499 · see citing works

The p300/CBP family: integrating signals with transcription factors and chromatin

Shiama, N. (1997) · Trends in Cell Biology · doi:10.1016/s0962-8924(97)01048-9 · Cited by 481 · see citing works

Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines

Otte, A. P. (1997) · UvA-DARE (University of Amsterdam) · Cited by 480 · see citing works

Differential Roles of p300 and PCAF Acetyltransferases in Muscle Differentiation

Puri, P., Sartorelli, V., Yang, X., Hamamori, Y., Ogryzko, V. V., Howard, B. H., Kedes, L., Wang, J. Y. J., Graessmann, A., Nakatani, Y., et al. (1997) · Molecular Cell · doi:10.1016/s1097-2765(00)80005-2 · Cited by 419 · see citing works

The bromodomain: a conserved sequence found in human,Drosophilaand yeast proteins

Haynes, S. R., Dollard, C. A., Winston, F., Beck, S., Trowsdale, J., & Dawid, I. B. (1992) · Nucleic Acids Research · doi:10.1093/nar/20.10.2603 · Cited by 387 · see citing works

A general method for assigning NMR spectra of denatured proteins using 3D HC(CO)NH-TOCSY triple resonance experiments

Logan, T. M., Olejniczak, E. T., Xu, R., & Fesik, S. (1993) · Journal of Biomolecular NMR · doi:10.1007/bf00178264 · Cited by 301 · see citing works

Sinful repression

Wolffe, A. P. (1997) · Nature · doi:10.1038/387016a0 · Cited by 282 · see citing works

The bromodomain revisited

Jeanmougin, F. (1997) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(97)01042-6 · Cited by 279 · see citing works

[11] Multidimensional heteronuclear nuclear magnetic resonance of proteins

Clore, G. M., & Gronenborn, A. M. (1994) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(94)39013-4 · Cited by 273 · see citing works

Ambiguous NOEs and automated NOE assignment

Nilges, M., & O’Donoghue, S. I. (1998) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/s0079-6565(97)00025-3 · Cited by 233 · see citing works

Structure of the Histone Acetyltransferase Hat1

Dutnall, R. N., Tafrov, S. T., Sternglanz, R., & Ramakrishnan, V. (1998) · Cell · doi:10.1016/s0092-8674(00)81584-6 · Cited by 224 · see citing works

Differential Use of CREB Binding Protein-Coactivator Complexes

Kurokawa, R., Kalafus, D., Ogliastro, M.-H., Kioussi, C., Xu, L., Torchia, J., Rosenfeld, M. G., & Glass, C. K. (1998) · Science · doi:10.1126/science.279.5351.700 · Cited by 213 · see citing works

Structural and functional diversity in 4-α-helical proteins

Weber, P. C., & Salemme, F. R. (1980) · Nature · doi:10.1038/287082a0 · Cited by 213 · see citing works

Topological distribution of four-alpha-helix bundles.

Presnell, S., & Cohen, F. E. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.17.6592 · Cited by 197 · see citing works

Genetic evidence for the interaction of the yeast transcriptional co-activator proteins GCN5 and ADA2

Georgakopoulos, T., Gounalaki, N., & Thireos, G. (1995) · Molecular and General Genetics MGG · doi:10.1007/bf00290718 · Cited by 36 · see citing works

Translating the Histone Code

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

The language of covalent histone modifications

Strahl, B. D., & Allis, C. D. (2000) · Nature · doi:10.1038/47412 · Cited by 8,679 · see citing works

Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain

Bannister, A. J., Zegerman, P., Partridge, J. F., Miska, E. A., Thomas, J. O., Allshire, R. C., & Kouzarides, T. (2001) · Nature · doi:10.1038/35065138 · Cited by 2,903 · see citing works

BET Bromodomain Inhibition as a Therapeutic Strategy to Target c-Myc

Delmore, J. E., Issa, G. C., Lemieux, M. E., Rahl, P. B., Shi, J., Jacobs, H. M., Kastritis, E., Gilpatrick, T., Paranal, R. M., Qi, J., et al. (2011) · Cell · doi:10.1016/j.cell.2011.08.017 · Cited by 2,820 · 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

The complex language of chromatin regulation during transcription

Berger, S. L. (2007) · Nature · doi:10.1038/nature05915 · Cited by 2,768 · see citing works

The diverse functions of histone lysine methylation

Martin, C., & Zhang, Y. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1761 · Cited by 2,066 · see citing works

Histone Acetyltransferases

Dent, S., Denu, J. M., & Allis, C. D. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.81 · Cited by 1,844 · see citing works

Acetylation of Histones and Transcription-Related Factors

Sterner, D. E., & Berger, S. L. (2000) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.64.2.435-459.2000 · Cited by 1,766 · see citing works

Role of Histone H3 Lysine 9 Methylation in Epigenetic Control of Heterochromatin Assembly

Nakayama, J.-I., Rice, J. C., Strahl, B. D., Allis, C. D., & Grewal, S. I. S. (2001) · Science · doi:10.1126/science.1060118 · Cited by 1,739 · see citing works

Histone Recognition and Large-Scale Structural Analysis of the Human Bromodomain Family

Filippakopoulos, P., Picaud, S., Mangos, M., Keates, T., Lambert, J., Baršytė-Lovejoy, D., Felletár, I., Volkmer, R., Müller, S., Pawson, T. J., et al. (2012) · Cell · doi:10.1016/j.cell.2012.02.013 · Cited by 1,719 · see citing works

Functions of Site-Specific Histone Acetylation and Deacetylation

Shahbazian, M. D., & Grunstein, M. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.052705.162114 · Cited by 1,635 · see citing works

Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tailsPreprint

Zhang, Y., & Reinberg, D. (2001) · Genes & Development · doi:10.1101/gad.927301 · Cited by 1,534 · 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

Genome-wide mapping of HATs and HDACs reveals distinct functions in active and inactive genes

Wang, Z., Zang, C., Cui, K., Schones, D. E., Barski, A., Peng, W., & Zhao, K. (2009) · Cell · doi:10.1016/j.cell.2009.06.049 · Cited by 1,344 · see citing works

The growing landscape of lysine acetylation links metabolism and cell signalling

Choudhary, C., Weinert, B. T., Nishida, Y., Verdin, E., & Mann, M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3841 · Cited by 1,324 · 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

Targeting bromodomains: epigenetic readers of lysine acetylation

Filippakopoulos, P., & Knapp, S. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4286 · Cited by 1,274 · see citing works

Histone modifications in transcriptional regulation

Berger, S. L. (2002) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(02)00279-4 · Cited by 1,222 · see citing works

Integrating the MAP kinase signal into the G1 phase cell cycle machinery

Roovers, K., & Assoian, R. K. (2000) · BioEssays · doi:10.1002/1521-1878(200009)22:9 · Cited by 469 · see citing works

A PHD finger of NURF couples histone H3 lysine 4 trimethylation with chromatin remodelling

Wysocka, J., Swigut, T., Xiao, H., Milne, T. A., Kwon, S. Y., Landry, J., Kauer, M., Tackett, A. J., Chait, B. T., Badenhorst, P. W., et al. (2006) · Nature · doi:10.1038/nature04815 · Cited by 1,186 · see citing works

Acetylation: a regulatory modification to rival phosphorylation?

Kouzarides, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.6.1176 · Cited by 1,155 · 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

Histone acetyltransferase complexes: one size doesn't fit all

Lee, K. K. W., & Workman, J. L. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2145 · Cited by 1,091 · 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

Signaling to Chromatin through Histone Modifications

Cheung, P., Allis, C. D., & Sassone-Corsi, P. (2000) · Cell · doi:10.1016/s0092-8674(00)00118-5 · Cited by 989 · see citing works

p300/CBP proteins: HATs for transcriptional bridges and scaffolds

Chan, H. M., & La Thangue, N. B. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.13.2363 · Cited by 1,092 · see citing works

50 years of protein acetylation: from gene regulation to epigenetics, metabolism and beyond

Verdin, E. M., & Ott, M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3931 · Cited by 876 · see citing works

The Mechanisms behind the Therapeutic Activity of BET Bromodomain Inhibition

Shi, J., & Vakoc, C. R. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.05.016 · Cited by 881 · see citing works

Epigenetic Codes for Heterochromatin Formation and Silencing

Richards, E. J., & Elgin, S. C. R. (2002) · Cell · doi:10.1016/s0092-8674(02)00644-x · Cited by 869 · see citing works

MyoD and the transcriptional control of myogenesis

Berkes, C. A., & Tapscott, S. J. (2005) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2005.07.006 · Cited by 848 · see citing works

Structure and Function of a Human TAF II 250 Double Bromodomain Module

Jacobson, R. H., Ladurner, A. G., King, D., & Tjian, R. (2000) · Science · doi:10.1126/science.288.5470.1422 · Cited by 845 · see citing works

Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF‐κB

Chen, L., Mu, Y., & Greene, W. C. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf660 · Cited by 827 · see citing works

Perceiving the epigenetic landscape through histone readers

Musselman, C. A., Lalonde, M., Côté, J., & Kutateladze, T. G. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2436 · Cited by 840 · see citing works

Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF

Li, H., Ilin, S., Wang, W., Duncan, E. M., Wysocka, J., Allis, C. D., & Patel, D. J. (2006) · Nature · doi:10.1038/nature04802 · Cited by 816 · see citing works

Analysis of histone acetyltransferase and histone deacetylase families of Arabidopsis thaliana suggests functional diversification of chromatin modification among multicellular eukaryotes

Pandey, R. (2002) · Nucleic Acids Research · doi:10.1093/nar/gkf660 · Cited by 783 · see citing works

Bromodomain: an acetyl‐lysine binding domain

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

Ordered Recruitment of Chromatin Modifying and General Transcription Factors to the IFN-β Promoter

Agalioti, T., Lomvardas, S., Parekh, B. S., Yie, J., Maniatis, T., & Thanos, D. (2000) · Cell · doi:10.1016/s0092-8674(00)00169-0 · Cited by 737 · see citing works

ATP-Dependent Chromatin-Remodeling Complexes

Vignali, M., Hassan, A. H., Neely, K. E., & Workman, J. L. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.6.1899-1910.2000 · Cited by 731 · see citing works

BET domain co-regulators in obesity, inflammation and cancer

Belkina, A. C., & Denis, G. V. (2012) · Nature reviews. Cancer · doi:10.1038/nrc3256 · Cited by 727 · see citing works

Interpreting the language of histone and DNA modifications

Rothbart, S. B., & Strahl, B. D. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.03.001 · Cited by 721 · see citing works

BRD4 and Cancer: going beyond transcriptional regulation

Donati, B., Lorenzini, E., & Ciarrocchi, A. (2018) · Molecular Cancer · doi:10.1186/s12943-018-0915-9 · Cited by 713 · see citing works

ALL-1 Is a Histone Methyltransferase that Assembles a Supercomplex of Proteins Involved in Transcriptional Regulation

Nakamura, T., Mori, T., Tada, S., Krajewski, W. A., Rozovskaia, T., Wassell, R. P., DuBois, G. C., Mazo, A., Croce, C. M., & Canaani, E. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00740-2 · Cited by 720 · see citing works

Histone methylation versus histone acetylation: new insights into epigenetic regulation

Rice, J. C., & Allis, C. D. (2001) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00208-8 · Cited by 701 · see citing works

p38-dependent marking of inflammatory genes for increased NF-κB recruitment

Saccani, S., Pantano, S., & Natoli, G. (2001) · Nature Immunology · doi:10.1038/ni748 · Cited by 694 · see citing works

Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2

Peña, P. V., Davrazou, F., Shi, X., Walter, K. L., Verkhusha, V. V., Gozani, O., Zhao, R., & Kutateladze, T. G. (2006) · Nature · doi:10.1038/nature04814 · Cited by 685 · see citing works

Histone acetylation and deacetylation in yeast

Kurdistani, S. K., & Grunstein, M. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1075 · Cited by 677 · see citing works

The Nucleosome

Khorasanizadeh, S. (2004) · Cell · doi:10.1016/s0092-8674(04)00044-3 · Cited by 672 · see citing works

The double bromodomain protein Brd4 binds to acetylated chromatin during interphase and mitosis

Dey, A., Chitsaz, F., Abbasi, A., Misteli, T., & Ozato, K. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1433065100 · Cited by 672 · see citing works

Acetylation of non-histone proteins modulates cellular signalling at multiple levels

Spange, S., Wagner, T., Heinzel, T., & Krämer, O. H. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.08.027 · Cited by 661 · see citing works

Mapping Global Histone Acetylation Patterns to Gene Expression

Kurdistani, S. K., Tavazoie, S., & Grunstein, M. R. (2004) · Cell · doi:10.1016/j.cell.2004.05.023 · Cited by 647 · see citing works

Writers and Readers of Histone Acetylation: Structure, Mechanism, and InhibitionPreprint

Marmorstein, R., & Zhou, M. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a018762 · Cited by 643 · see citing works

Deciphering the Transcriptional Histone Acetylation Code for a Human Gene

Agalioti, T., Chen, G., & Thanos, D. (2002) · Cell · doi:10.1016/s0092-8674(02)01077-2 · Cited by 639 · see citing works

Readers of histone modifications

Yun, M., Wu, J., Workman, J. L., & Li, B. (2011) · Cell Research · doi:10.1038/cr.2011.42 · Cited by 626 · see citing works

Protein Lysine Acetylation by p300/CBP

Rabbitts, B. M., & Cole, P. A. (2015) · Chemical Reviews · doi:10.1021/cr500452k · Cited by 620 · see citing works

Functions of bromodomain-containing proteins and their roles in homeostasis and cancer

Fujisawa, T., & Filippakopoulos, P. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.143 · Cited by 589 · 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

Phosphorylation of Serine 10 in Histone H3 Is Functionally Linked In Vitro and In Vivo to Gcn5-Mediated Acetylation at Lysine 14

Lo, W., Trievel, R. C., Rojas, J. R., Duggan, L. J., Hsu, J.-Y., Allis, C. D., Marmorstein, R., & Berger, S. L. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80257-9 · Cited by 573 · see citing works

Transcriptional coactivator complexes.

Näär, A. M., Lemon, B. D., & Tjian, R. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.475 · Cited by 571 · see citing works

The structural basis for the recognition of acetylated histone H4 by the bromodomain of histone acetyltransferase Gcn5p

Owen, D. J., Ornaghi, P., Yang, J., Lowe, N., Evans, P. R., Ballario, P., Neuhaus, D., Filetici, P., & TRAVERS, A. A. (2000) · The EMBO Journal · doi:10.1093/emboj/19.22.6141 · Cited by 543 · see citing works

Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein associationPreprint

Ng, H. H., Feng, Q., Wang, H., Erdjument‐Bromage, H., Tempst, P., Zhang, Y., & Struhl, K. (2002) · Genes & Development · doi:10.1101/gad.1001502 · Cited by 536 · see citing works

Function and Selectivity of Bromodomains in Anchoring Chromatin-Modifying Complexes to Promoter Nucleosomes

Hassan, A. H., Prochasson, P., Neely, K. E., Galasinski, S. C., Chandy, M., Carrozza, M. J., & Workman, J. L. (2002) · Cell · doi:10.1016/s0092-8674(02)01005-x · Cited by 533 · see citing works

Targeting histone deacetylase complexes via KRAB-zinc finger proteins: the PHD and bromodomains of KAP-1 form a cooperative unit that recruits a novel isoform of the Mi-2α subunit of NuRDPreprint

Schultz, D., Friedman, J. R., & Rauscher, F. J. (2001) · Genes & Development · doi:10.1101/gad.869501 · Cited by 530 · see citing works

SIRT1, an antiinflammatory and antiaging protein, is decreased in lungs of patients with chronic obstructive pulmonary disease

Rajendrasozhan, S., Yang, S.-R., Kinnula, V. L., & Rahman, I. (2008) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200708-1269oc · Cited by 520 · see citing works

The diverse superfamily of lysine acetyltransferases and their roles in leukemia and other diseases

Yang, X. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh252 · Cited by 513 · see citing works

Meiotic recombination hot spots and cold spots

Petes, T. D. (2001) · Nature Reviews Genetics · doi:10.1038/35072078 · Cited by 510 · see citing works

The macro domain is an ADP‐ribose binding module

Karras, G. I., Kustatscher, G., Buhecha, H. R., Allen, M. D., Pugieux, C., Sait, F., Bycroft, M., & Ladurner, A. G. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600664 · Cited by 502 · see citing works

Molecular mechanisms of leukemogenesis mediated by MLL fusion proteins

Ayton, P. M., & Cleary, M. L. (2001) · Oncogene · doi:10.1038/sj.onc.1204639 · Cited by 499 · see citing works

Single-Nucleosome Mapping of Histone Modifications in S. cerevisiae

Liu, C. L., Kaplan, T., Kim, M., Buratowski, S., Schreiber, S. L., Friedman, N., & Rando, O. J. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030328 · Cited by 491 · see citing works

Signals and Combinatorial Functions of Histone Modifications

Suganuma, T., & Workman, J. L. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061809-175347 · Cited by 498 · see citing works

CBP and p300: HATs for different occasions

Kalkhoven, E. (2004) · Biochemical Pharmacology · doi:10.1016/j.bcp.2004.03.045 · Cited by 499 · see citing works

A Method for Genetically Installing Site-Specific Acetylation in Recombinant Histones Defines the Effects of H3 K56 Acetylation

Neumann, H., Hancock, S. M., Buning, R., Routh, A. L., Chapman, L., Somers, J., Owen‐Hughes, T., van Noort, J., Rhodes, D., & Chin, J. W. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.07.027 · Cited by 498 · see citing works

Synergism of Xist Rna, DNA Methylation, and Histone Hypoacetylation in Maintaining X Chromosome Inactivation

Csankovszki, G., Nagy, A., & Jaenisch, R. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.4.773 · Cited by 494 · see citing works

Epigenetics and cancer

Lund, A. H., & van Lohuizen, M. (2004) · Genes & Development · doi:10.1101/gad.1232504 · Cited by 489 · see citing works

RVX-208, an inhibitor of BET transcriptional regulators with selectivity for the second bromodomain

Picaud, S., Wells, C. D., Felletár, I., Brotherton, D. H., Martin, S., Savitsky, P. A., Díez-Dacal, B., Philpott, M., Bountra, C., Lingard, H., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1310658110 · Cited by 489 · see citing works

Epigenetic regulation in metabolic diseases: mechanisms and advances in clinical study

Wu, Y., Lin, Z., Li, C., Lin, X. J., Shan, S., Guo, B., Zheng, M.-H., Li, F., Yuan, L., & Li, Z. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01333-7 · Cited by 507 · see citing works

Apoptotic Phosphorylation of Histone H2B Is Mediated by Mammalian Sterile Twenty Kinase

Cheung, W. L., Ajiro, K., Samejima, K., Kloc, M., Cheung, P., Mizzen, C. A., Beeser, A. E., Etkin, L. D., Chernoff, J., Earnshaw, W. C., et al. (2003) · Cell · doi:10.1016/s0092-8674(03)00355-6 · Cited by 487 · see citing works

Concerted Dephosphorylation of the Transcription Factor NFAT1 Induces a Conformational Switch that Regulates Transcriptional Activity

Okamura, H., Aramburu, J. F., García‐Rodríguez, C., Viola, J. P. B., Raghavan, A., Tahiliani, M., Zhang, X., Qin, J., Hogan, P. G., & Rao, A. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00053-8 · Cited by 481 · see citing works

Chromosomal gradient of histone acetylation established by Sas2p and Sir2p functions as a shield against gene silencing

Kimura, A., Umehara, T., & Horikoshi, M. (2002) · Nature Genetics · doi:10.1038/ng993 · Cited by 466 · see citing works

Active chromatin domains are defined by acetylation islands revealed by genome-wide mappingPreprint

Roh, T., Cuddapah, S., & Zhao, K. (2005) · Genes & Development · doi:10.1101/gad.1272505 · Cited by 465 · see citing works

The PHD finger: a versatile epigenome reader

Sánchez, R., & Zhou, M. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.03.005 · Cited by 457 · see citing works

GCN5-Related N-Acetyltransferases: A Structural Overview

Dyda, F., Klein, D. C., & Hickman, A. B. (2000) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.29.1.81 · Cited by 448 · see citing works

Recognition of Histone H3 Lysine-4 Methylation by the Double Tudor Domain of JMJD2A

Huang, Y., Fang, J., Bedford, M. T., Zhang, Y., & Xu, R.-M. (2006) · Science · doi:10.1126/science.1125162 · Cited by 446 · see citing works

Bromodomains as therapeutic targets

Müller, S., Filippakopoulos, P., & Knapp, S. (2011) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399411001992 · Cited by 445 · see citing works

Structure and acetyl-lysine recognition of the bromodomain

Mujtaba, S., Zeng, L., & Zhou, M.-M. (2007) · Oncogene · doi:10.1038/sj.onc.1210618 · Cited by 419 · see citing works

Specificity of the HP1 chromo domain for the methylated N‐terminus of histone H3

Jacobs, S. A., Taverna, S. D., Zhang, Y., Briggs, S. D., Li, J., Eissenberg, J. C., Allis, C. D., & Khorasanizadeh, S. (2001) · The EMBO Journal · doi:10.1093/emboj/20.18.5232 · Cited by 418 · see citing works

Metabolic control of epigenetics in cancer

Kinnaird, A. S., Zhao, S., Wellen, K. E., & Michelakis, E. D. (2016) · Nature reviews. Cancer · doi:10.1038/nrc.2016.82 · Cited by 419 · see citing works

Small-Molecule Inhibition of BRDT for Male Contraception

Matzuk, M. M., McKeown, M. R., Filippakopoulos, P., Li, Q., Ma, L., Agno, J. E., Lemieux, M. E., Picaud, S., Yu, R. N., Qi, J., et al. (2012) · Cell · doi:10.1016/j.cell.2012.06.045 · Cited by 421 · see citing works

BET Protein Function Is Required for Inflammation: Brd2 Genetic Disruption and BET Inhibitor JQ1 Impair Mouse Macrophage Inflammatory Responses

Belkina, A. C., Nikolajczyk, B. S., & Denis, G. V. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1202838 · Cited by 421 · see citing works

Distinct GCN5/PCAF-containing complexes function as co-activators and are involved in transcription factor and global histone acetylation

Nagy, Z., & Tora, L. (2007) · Oncogene · doi:10.1038/sj.onc.1210604 · Cited by 416 · see citing works

p300 and p300/cAMP-response Element-binding Protein-associated Factor Acetylate the Androgen Receptor at Sites Governing Hormone-dependent Transactivation

Fu, M., Wang, C., Reutens, A. T., Wang, J., Angeletti, R. H., Siconolfi-Baez, L., Ogryzko, V. V., Avantaggiati, M. L., & Pestell, R. G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000660200 · Cited by 409 · see citing works

The SANT domain: a unique histone-tail-binding module?

Boyer, L. A., Latek, R. R., & Peterson, C. L. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1314 · Cited by 403 · see citing works

Epigenetics and cardiovascular disease

Ordovás, J. M., & Smith, C. E. (2010) · Nature Reviews Cardiology · doi:10.1038/nrcardio.2010.104 · Cited by 402 · see citing works

Histone acetyltransferases: function, structure, and catalysis

Marmorstein, R., & Dent, S. (2001) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(00)00173-8 · Cited by 401 · see citing works

Targeting Epigenetic Readers in Cancer

Dawson, M. A., Kouzarides, T., & Huntly, B. J. P. (2012) · New England Journal of Medicine · doi:10.1056/nejmra1112635 · Cited by 400 · see citing works

Epigenetic tools (The Writers, The Readers and The Erasers) and their implications in cancer therapy

Biswas, S., & Rao, C. M. (2018) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2018.08.021 · Cited by 402 · 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

Genomic characterization reveals a simple histone H4 acetylation code

Dion, M. F., Altschuler, S. J., Wu, L. F., & Rando, O. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500136102 · Cited by 395 · see citing works

Histones Are First Hyperacetylated and Then Lose Contact with the Activated PHO5 Promoter

Reinke, H., & Hörz, W. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00186-2 · Cited by 394 · see citing works

Sirtuin regulates cigarette smoke-induced proinflammatory mediator release via RelA/p65 NF-κB in macrophages in vitro and in rat lungs in vivo: implications for chronic inflammation and aging

Yang, S.-R., Wright, J., Bauter, M., Seweryniak, K., Kode, A., & Rahman, I. (2007) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00308.2006 · Cited by 391 · see citing works

Structural Insights into Acetylated-Histone H4 Recognition by the Bromodomain-PHD Finger Module of Human Transcriptional Coactivator CBP

Plotnikov, A. N., Yang, S., Zhou, T., Rusinova, E. V., Frasca, A., & Zhou, M. (2013) · Structure · doi:10.1016/j.str.2013.10.021 · Cited by 52 · see citing works

Structural Basis of Site-Specific Histone Recognition by the Bromodomains of Human Coactivators PCAF and CBP/p300

Zeng, L., Zhang, Q., Gerona‐Navarro, G., Moshkina, N., & Zhou, M. (2008) · Structure · doi:10.1016/j.str.2008.01.010 · Cited by 149 · see citing works

Structure and acetyl-lysine recognition of the bromodomain

Mujtaba, S., Zeng, L., & Zhou, M.-M. (2007) · Oncogene · doi:10.1038/sj.onc.1210618 · Cited by 419 · see citing works

Insights into the Molecular Mechanisms of Histone Code Recognition by the BRPF3 Bromodomain

Barman, S., Roy, A., Bardhan, I., Kandasamy, T., Shivani, S., & Sudhamalla, B. (2021) · Chemistry - An Asian Journal · doi:10.1002/asia.202100793 · Cited by 15 · see citing works

Physical Model of p300 Acetyltransferase and Bromodomain (LB89)

Assad, F., Briglall, A., Eusebio, D., Flores, E., Ramirez, H., Simón, M. S., Valentin, T., Zaman, M., Granberry, A., & Houck-Loomis, B. R. (2014) · The FASEB Journal · doi:10.1096/fasebj.28.1_supplement.lb89