Cited by 1,732Genomics and Chromatin DynamicsProtein Degradation and InhibitorsProtein Structure and Dynamics

The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.

Structure and ligand of a histone acetyltransferase bromodomain

Dhalluin, Christophe, Carlson, Justin E., Zeng, Lei, He, Cheng, Aggarwal, Aneel K., Zhou, Ming-Ming, Zhou, Ming-Ming·1999·Nature

DOI 10.1038/20974

Open this paper in CoChat — free account

Abstract

Histone acetylation is important in chromatin remodelling and gene activation. Nearly all known histone-acetyltransferase (HAT)-associated transcriptional co-activators contain bromodomains, which are approximately 110-amino-acid modules found in many chromatin-associated proteins. Despite the wide occurrence of these bromodomains, their three-dimensional structure and binding partners remain unknown. Here we report the solution structure of the bromodomain of the HAT co-activator P/CAF (p300/CBP-associated factor). The structure reveals an unusual left-handed up-and-down four-helix bundle. In addition, we show by a combination of structural and site-directed mutagenesis studies that bromodomains can interact specifically with acetylated lysine, making them the first known protein modules to do so. The nature of the recognition of acetyl-lysine by the P/CAF bromodomain is similar to that of acetyl-CoA by histone acetyltransferase. Thus, the bromodomain is functionally linked to the HAT activity of co-activators in the regulation of gene transcription.

Integrity signals

Registry

Crossref · 10.1038/20974

Cites

30 of 30 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

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
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
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
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
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
Histone acetylation in chromatin structure and transcription
Grunstein, M. (1997) · Nature · doi:10.1038/38664 · Cited by 2,884
Protein modules and signalling networks
Pawson, T. (1995) · Nature · doi:10.1038/373573a0 · Cited by 2,420
The CBP co-activator is a histone acetyltransferase
Bannister, A. J., & Kouzarides, T. (1996) · Nature · doi:10.1038/384641a0 · Cited by 1,828
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
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 1,497

Show all 30 references

Research works printed but not linked: 1

Nicholls, A., Bharadwj, R. & Honig, B. GRASP: Graphical representation and analysis of surface properties. Biophys. J. 64, 166–170 (1993).

Sorted by citations

Items 401–500 of 1,001

Reconstitution of Glucocorticoid Receptor-Dependent Transcription In Vivo
Trotter, K. W., & Archer, T. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.8.3347-3358.2004 · Cited by 107
Functional Involvement of the Brahma/SWI2-related Gene 1 Protein in Cytochrome P4501A1 Transcription Mediated by the Aryl Hydrocarbon Receptor Complex
Wang, S., & Hankinson, O. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110122200 · Cited by 107
Structural Insights into Histone Crotonyl-Lysine Recognition by the AF9 YEATS Domain
Zhang, Q., Zeng, L., Zhao, C., Ju, Y., Konuma, T., & Zhou, M. (2016) · Structure · doi:10.1016/j.str.2016.05.023 · Cited by 106
Self-citation
Structure and function of the SWIRM domain, a conserved protein module found in chromatin regulatory complexes
Da, G., Lenkart, J., Zhao, K., Shiekhattar, R., Cairns, B. R., & Marmorstein, R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510949103 · Cited by 106
A Transient Histone Hyperacetylation Signal Marks Nucleosomes for Remodeling at the PHO8 Promoter In Vivo
Reinke, H., Gregory, P. D., & Hörz, W. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00200-3 · Cited by 106
BRD4 Regulates EZH2 Transcription through Upregulation of C-MYC and Represents a Novel Therapeutic Target in Bladder Cancer
Wu, X., Liu, D., Tao, D., Xiang, W., Xiao, X., Wang, M., Wang, L., Luo, G., Li, Y., Zeng, F., et al. (2016) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-15-0750 · Cited by 111
Expression homeostasis during DNA replication
Voichek, Y., Bar‐Ziv, R., & Barkai, N. (2016) · Science · doi:10.1126/science.aad1162 · Cited by 105
Mechanisms of P/CAF auto-acetylation
Santos-Rosa, H. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg655 · Cited by 105
Keeping it in the family: diverse histone recognition by conserved structural folds
Yap, K. L., & Zhou, M. (2010) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2010.512001 · Cited by 111
Self-citation
The PHD Type Zinc Finger Is an Integral Part of the CBP Acetyltransferase Domain
Kalkhoven, E., Teunissen, H., Houweling, A., Verrijzer, C. P., & ZANTEMA, A. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.7.1961-1970.2002 · Cited by 114
Structures of protein domains that create or recognize histone modifications
Bottomley, M. J. (2004) · EMBO Reports · doi:10.1038/sj.embor.7400146 · Cited by 110
Bromodomain analysis of Brd2-dependent transcriptional activation of cyclin A
Sinha, A., Faller, D. V., & Denis, G. V. (2005) · Biochemical Journal · doi:10.1042/bj20041793 · Cited by 105
Histone acetylation and the cell-cycle in cancer
Wang, C. (2001) · Frontiers in bioscience · doi:10.2741/1wang1 · Cited by 103
Discovery of a Potent, Cell Penetrant, and Selective p300/CBP-Associated Factor (PCAF)/General Control Nonderepressible 5 (GCN5) Bromodomain Chemical Probe
Humphreys, P. G., Bamborough, P., Chung, C., Craggs, P. D., Gordon, L. J., Grandi, P., Hayhow, T. G., Hussain, J., Jones, K. L., Lindon, M. J., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01566 · Cited by 100
Discovery of potent and selective BRD4 inhibitors capable of blocking TLR3-induced acute airway inflammation
Liu, Z., Tian, B., Chen, H., Wang, P., Brasier, A. R., & Zhou, J. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.04.006 · Cited by 104
Histone Modifications in Cancer Biology and Prognosis
Kurdistani, S. K. (2010) · Springer eBooks · doi:10.1007/978-3-7643-8989-5_5 · Cited by 106
The chromatin-targeting protein Brd2 is required for neural tube closure and embryogenesis
Gyuris, A., Donovan, D., Seymour, K. A., Lovasco, L. A., Smilowitz, N. R., Halperin, A. L. P., Klysik, J. E., & Freiman, R. N. (2009) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2009.03.005 · Cited by 102
Extracellular Matrix-Regulated Gene Expression Requires Cooperation of SWI/SNF and \nTranscription Factors
Xu, R., Spencer, V. A., & Bissell, M. J. (2006) · eScholarship (California Digital Library) · Cited by 102
ATP-dependent chromatin remodeling activities
Havas, K. M., Whitehouse, I., & Owen‐Hughes, T. (2001) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000891 · Cited by 102
Transcriptional Control by NF-κB: Elongation in Focus
Diamant, G., & Dikstein, R. (2013) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2013.04.007 · Cited by 101
Real-Time Imaging of Histone H4K12–Specific Acetylation Determines the Modes of Action of Histone Deacetylase and Bromodomain Inhibitors
Ito, T., Umehara, T., Sasaki, K., Nakamura, Y., Nishino, N., Terada, T., Shirouzu, M., Padmanabhan, B., Yokoyama, S., Ito, A., et al. (2011) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.02.009 · Cited by 103
Transcriptional control of erythropoiesis: emerging mechanisms and principles
Kim, S.-I., & Bresnick, E. H. (2007) · Oncogene · doi:10.1038/sj.onc.1210761 · Cited by 113
A new method for mapping macromolecular topography
Mezei, M. (2003) · Journal of Molecular Graphics and Modelling · doi:10.1016/s1093-3263(02)00203-6 · Cited by 101
Interaction between Acetylated MyoD and the Bromodomain of CBP and/or p300
Polesskaya, A., Naguibneva, I., Duquet, A., Bengal, E., Robin, P., & Harel‐Bellan, A. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.16.5312-5320.2001 · Cited by 102
Selective Requirements for Histone H3 and H4 N Termini in p300-Dependent Transcriptional Activation from Chromatin
An, W., Palhan, V. B., Karymov, M. A., Leuba, S. H., & Roeder, R. G. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00497-5 · Cited by 100
The Yin and Yang of Histone Marks in Transcription
Talbert, P. B., & Henikoff, S. (2021) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev-genom-120220-085159 · Cited by 102
Plant orthologs of p300/CBP: conservation of a core domain in metazoan p300/CBP acetyltransferase-related proteins
Bordoli, L. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.3.589 · Cited by 100
p300 Forms a Stable, Template-Committed Complex with Chromatin: Role for the Bromodomain
Manning, E. T., Ikehara, T., Ito, T., Kadonaga, J. T., & Kraus, W. L. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.12.3876-3887.2001 · Cited by 104
Role of plant CBP/p300‐like genes in the regulation of flowering time
Han, S., Song, J., Noh, Y., & Noh, B. (2006) · The Plant Journal · doi:10.1111/j.1365-313x.2006.02939.x · Cited by 102
Analysis of epigenetic modifications of chromatin at specific gene loci by native chromatin immunoprecipitation of nucleosomes isolated using hydroxyapatite chromatography
Brand, M., Rampalli, S., Chaturvedi, C.-P., & Dilworth, F. J. (2008) · Nature Protocols · doi:10.1038/nprot.2008.8 · Cited by 99
Quantitative FRET Analysis by Fast Acquisition Time Domain FLIM at High Spatial Resolution in Living Cells
Padilla‐Parra, S., Audugé, N., Coppey‐Moisan, M., & Tramier, M. (2008) · Biophysical Journal · doi:10.1529/biophysj.108.131276 · Cited by 99
Targeted Histone Acetylation and Altered Nuclease Accessibility over Short Regions of the Pea Plastocyanin Gene
Chua, Y. L., Brown, A. P. C., & Gray, J. C. (2001) · The Plant Cell · doi:10.1105/tpc.13.3.599 · Cited by 99
In vitro transcription system delineates the distinct roles of the coactivators pCAF and p300 during MyoD/E47-dependent transactivation
Dilworth, F. J., Seaver, K. J., Fishburn, A. L., Htet, S. L., & Tapscott, S. J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404192101 · Cited by 99
Solution Structure of the Interacting Domains of the Mad–Sin3 Complex
Brubaker, K., Cowley, S. M., Huang, K., Loo, L. W. M., Yochum, G. S., Ayer, D. E., Eisenman, R. N., & Radhakrishnan, I. (2000) · Cell · doi:10.1016/s0092-8674(00)00168-9 · Cited by 100
Transcriptional Regulation: a Genomic Overview
Riechmann, J. L. (2002) · The Arabidopsis Book · doi:10.1199/tab.0085 · Cited by 98
Bromodomain and Extraterminal Proteins as Novel Epigenetic Targets for Renal Diseases
Morgado‐Pascual, J. L., Rayego‐Mateos, S., Tejedor-Santamaria, L., Suárez-Álvarez, B., & Ruiz‐Ortega, M. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01315 · Cited by 103
GCN5 modulates salicylic acid homeostasis by regulating H3K14ac levels at the 5′ and 3′ ends of its target genes
Kim, S.-K., Piquerez, S. J. M., Ramirez-Prado, J. S., Mastorakis, E., Veluchamy, A., Latrasse, D., Manza-Mianza, D., Brik‐Chaouche, R., Huang, Y., Rodriguez‐Granados, N. Y., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa369 · Cited by 94
An Acetylation Switch in p53 Mediates Holo-TFIID Recruitment
Li, A. G., Piluso, L. G., Cai, X., Gadd, B. J., Ladurner, A. G., & Liu, X. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.09.006 · Cited by 100
Targeting Activity Is Required for SWI/SNF Function In Vivo and Is Accomplished through Two Partially Redundant Activator-Interaction Domains
Prochasson, P., Neely, K. E., Hassan, A. H., Li, B., & Workman, J. L. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00366-6 · Cited by 97
Adenovirus E1B 55-Kilodalton Oncoprotein Inhibits p53 Acetylation by PCAF
Liu, Y., Colosimo, A. L., Yang, X., & Liao, D. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.15.5540-5553.2000 · Cited by 98
BRD4 Inhibitor Inhibits Colorectal Cancer Growth and Metastasis
Hu, Y., Zhou, J., Ye, F., Xiong, H., Peng, L., Zheng, Z., Xu, F., Cui, M., Wei, C., Wang, X., et al. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms16011928 · Cited by 95
Self-citation
Bonus, a Drosophila Homolog of TIF1 Proteins, Interacts with Nuclear Receptors and Can Inhibit βFTZ-F1-Dependent Transcription
Beckstead, R. B., Ortiz, J. A., Sanchez, C., Prokopenko, S. N., Chambon, P., Losson, R., & Bellen, H. J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00220-9 · Cited by 94
Rheostat Control of Gene Expression by Metabolites
Ladurner, A. G. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.09.002 · Cited by 97
The Chromatin-Remodeling BAF Complex Mediates Cellular Antiviral Activities by Promoter Priming
Cui, K., Tailor, P. B., Liu, H., Chen, X., Ozato, K., & Zhao, K. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.10.4476-4486.2004 · Cited by 96
The HIRAN Domain and Recruitment of Chromatin Remodeling and Repair activities to Damaged DNA
Iyer, L. M., Babu, M. M., & Aravind, L. (2006) · Cell Cycle · doi:10.4161/cc.5.7.2629 · Cited by 96
Virp1 Is a Host Protein with a Major Role in Potato Spindle Tuber Viroid Infection in Nicotiana Plants
Kalantidis, K., Denti, M. A., Tzortzakaki, S., Marinou, E., Tabler, M., & Tsagris, M. (2007) · Journal of Virology · doi:10.1128/jvi.00974-07 · Cited by 96
SWI/SNF Displaces SAGA-Acetylated Nucleosomes
Chandy, M., Gutiérrez, J. L., Prochasson, P., & Workman, J. L. (2006) · Eukaryotic Cell · doi:10.1128/ec.00165-06 · Cited by 96
Crosstalk between RNA m6A and DNA methylation regulates transposable element chromatin activation and cell fate in human pluripotent stem cells
Sun, T., Xu, Y., Xiang, Y., Ou, J., Soderblom, E. J., & Diao, Y. (2023) · Nature Genetics · doi:10.1038/s41588-023-01452-5 · Cited by 100
A Signaling Role of Histone-binding Proteins and INHAT Subunits pp32 and Set/TAF-Iβ in Integrating Chromatin Hypoacetylation and Transcriptional Repression
Kutney, S. N., Hong, R., Macfarlan, T. S., & Chakravarti, D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404969200 · Cited by 97
Epigenetic events in malignant melanoma
Rothhammer-Hampl, T., & Bosserhoff, A. (2007) · Pigment Cell Research · doi:10.1111/j.1600-0749.2007.00367.x · Cited by 97
Lysine Acetyltransferase GCN5b Interacts with AP2 Factors and Is Required for Toxoplasma gondii Proliferation
Wang, J., Dixon, S. E., Ting, L.-M., Liu, T., Jeffers, V., Croken, M. M., Calloway, M., Cannella, D., Hakimi, M., Kim, K., et al. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1003830 · Cited by 95
Multiple Mechanistically Distinct Functions of SAGA at the PHO5 Promoter
Barbarić, S., Reinke, H., & Hürz, W. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.10.3468-3476.2003 · Cited by 96
Structure and function of bromodomains in chromatin-regulating complexes
Marmorstein, R., & Berger, S. L. (2001) · Gene · doi:10.1016/s0378-1119(01)00519-4 · Cited by 94
Genome-Scale Acetylation-Dependent Histone Eviction during Spermatogenesis
Goudarzi, A., Shiota, H., Rousseaux, S., & Khochbin, S. (2014) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.02.023 · Cited by 93
A chemical probe toolbox for dissecting the cancer epigenome
Shortt, J., Ott, C. J., Johnstone, R. W., & Bradner, J. E. (2017) · Nature reviews. Cancer · doi:10.1038/nrc.2016.148 · Cited by 94
PROTAC Prodrug‐Integrated Nanosensitizer for Potentiating Radiation Therapy of Cancer
Zhang, S., Lai, Y., Pan, J., Saeed, M., Li, S., Zhou, H., Jiang, X., Gao, J. X., Zhu, Y., Yu, H., et al. (2024) · Advanced Materials · doi:10.1002/adma.202314132 · Cited by 97
The Gcn5 Bromodomain of the SAGA Complex Facilitates Cooperative and Cross-tail Acetylation of Nucleosomes
Li, S., & Shogren‐Knaak, M. A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809617200 · Cited by 98
Hematopoietic-specific activators establish an overlapping pattern of histone acetylation and methylation within a mammalian chromatin domain
Kiekhaefer, C. M., Grass, J. A., Johnson, K. D., Boyer, M. E., & Bresnick, E. H. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.212389499 · Cited by 93
MLL: How complex does it get?
Popovic, R., & Zeleznik‐Le, N. J. (2005) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20430 · Cited by 94
Bromodomain protein 7 interacts with PRMT5 and PRC2, and is involved in transcriptional repression of their target genes
Tae, S., Karkhanis, V. A., VELASCO, K. R., Yaneva, M., Erdjument‐Bromage, H., Tempst, P., & Sif, S. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr170 · Cited by 92
A shifting paradigm: histone deacetylases and transcriptional activation
Smith, C. L. (2008) · Bioessays · doi:10.1002/bies.20687 · Cited by 89
The STAT3 NH2-terminal Domain Stabilizes Enhanceosome Assembly by Interacting with the p300 Bromodomain
Hou, T., Ray, S., Lee, C., & Brasier, A. R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805941200 · Cited by 91
Cyclin D1 Represses p300 Transactivation through a Cyclin-dependent Kinase-independent Mechanism
Fu, M., Wang, C., Rao, M., Wu, X., Bouras, T., Zhang, X., Li, Z., Jiao, X., Yang, J., Li, A., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503188200 · Cited by 91
A histone code in meiosis: the histone kinase, NHK-1, is required for proper chromosomal architecture in Drosophila oocytesPreprint
Ivanovska, I. L., Khandan, T., Ito, T., & Orr‐Weaver, T. L. (2005) · Genes & Development · doi:10.1101/gad.1348905 · Cited by 91
Epigenetics and chemical safety assessment
LeBaron, M. J., Rasoulpour, R. J., Klapacz, J., Ellis‐Hutchings, R. G., Hollnagel, H. M., & Gollapudi, B. B. (2010) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2010.04.003 · Cited by 89
Aberrant lysine acetylation in tumorigenesis: Implications in the development of therapeutics
Kaypee, S., Sudarshan, D., Shanmugam, M. K., Mukherjee, D., Sethi, G., & Kundu, T. K. (2016) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2016.01.011 · Cited by 89
Systematic Profiling of Histone Readers in Arabidopsis thaliana
Zhao, S., Zhang, B., Yang, M., Zhu, J., & Li, H. (2018) · Cell Reports · doi:10.1016/j.celrep.2017.12.099 · Cited by 90
Conserved interaction between distinct Kruppel-associated box domains and the transcriptional intermediary factor 1 beta
Åbrink, M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.041616998 · Cited by 90
Acetylation- and Methylation-Related Epigenetic Proteins in the Context of Their Targets
Javaid, N., & Choi, S. (2017) · Genes · doi:10.3390/genes8080196 · Cited by 97
Mutations in the BRWD3 Gene Cause X-Linked Mental Retardation Associated with Macrocephaly
Field, M. J., Tarpey, P. S., Smith, R., Edkins, S., O’Meara, S., Stevens, C., Tofts, C., Teague, J. W., Butler, A. P., Dicks, E., et al. (2007) · The American Journal of Human Genetics · doi:10.1086/520677 · Cited by 89
Coactivators in transcription initiation: here are your orders
Featherstone, M. (2002) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(02)00280-0 · Cited by 93
ChIPs of the β-globin locus: unraveling gene regulation within an active domain
Bulger, M., Sawado, T., Schübeler, D., & Groudine, M. T. (2002) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(02)00283-6 · Cited by 88
Small-Molecule Targeting of BET Proteins in Cancer
French, C. A. (2016) · Advances in cancer research · doi:10.1016/bs.acr.2016.04.001 · Cited by 89
Histone acetylation and chromatin signature in stem cell identity and cancer
Shukla, V., Vaissière, T., & Herceg, Z. (2007) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2007.07.012 · Cited by 93
Biological function and histone recognition of family IV bromodomain‐containing proteins
Lloyd, J. T., & Glass, K. C. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.26010 · Cited by 88
ATAD2 is an epigenetic reader of newly synthesized histone marks during DNA replication
Koo, S. J., Fernández‐Montalván, A. E., Badock, V., Ott, C. J., Holton, S. J., von Ahsen, O., Toedling, J., Vittori, S., Bradner, J. E., & Gorjánácz, M. (2016) · Oncotarget · doi:10.18632/oncotarget.11855 · Cited by 86
Sequence Analysis of LRPPRC and Its SEC1 Domain Interaction Partners Suggests Roles in Cytoskeletal Organization, Vesicular Trafficking, Nucleocytosolic Shuttling, and Chromosome Activity
Liu, L., & McKeehan, W. L. (2002) · Genomics · doi:10.1006/geno.2001.6679 · Cited by 86
CBP/p300 acetyltransferase activity in hematologic malignancies
Dutta, R., Tiu, B. C., & Sakamoto, K. M. (2016) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2016.06.013 · Cited by 84
A Novel Arabidopsis Acetyltransferase Interacts with the Geminivirus Movement Protein NSP
McGarry, R. C., Barron, Y. D., Carvalho, M. F., Hill, J. E., Gold, D., Cheung, E. C. W., Kraus, W. L., & Lazarowitz, S. G. (2003) · The Plant Cell · doi:10.1105/tpc.012120 · Cited by 85
The therapeutic hope for HDAC6 inhibitors in malignancy and chronic disease
Batchu, S. N., Brijmohan, A. S., & Advani, A. (2016) · Clinical Science · doi:10.1042/cs20160084 · Cited by 86
Histone modification enzymes: novel targets for cancer drugs
Kristeleit, R. S., Stimson, L., Workman, P., & Aherne, W. (2004) · Expert Opinion on Emerging Drugs · doi:10.1517/14728214.9.1.135 · Cited by 86
Gcn5 regulates the dissociation of SWI/SNF from chromatin by acetylation of Swi2/Snf2Preprint
Kim, J., Saraf, A., Florens, L. A., Washburn, M. P., & Workman, J. L. (2010) · Genes & Development · doi:10.1101/gad.1979710 · Cited by 85
Structure-guided drug design identifies a BRD4-selective small molecule that suppresses HIV
Niu, Q., Liu, Z., Alamer, E., Fan, X., Chen, H., Endsley, J. J., Gelman, B. B., Tian, B., Kim, J. H., Michael, N. L., et al. (2019) · Journal of Clinical Investigation · doi:10.1172/jci120633 · Cited by 85
Bromodomains as therapeutic targets in cancer
Barbieri, I., Cannizzaro, E., & Dawson, M. A. (2013) · Briefings in Functional Genomics · doi:10.1093/bfgp/elt007 · Cited by 88
Epigenetic dynamics in psychiatric disorders: Environmental programming of neurodevelopmental processes
Kofink, D., Boks, M. P. M., Timmers, H. T. M., & Kas, M. J. (2013) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2013.03.020 · Cited by 83
Privileged Diazepine Compounds and Their Emergence as Bromodomain Inhibitors
Smith, S. G., Sánchez, R., & Zhou, M. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2014.03.004 · Cited by 83
Self-citation
BET Protein Inhibitor JQ1 Attenuates Myc-Amplified MCC Tumor Growth In Vivo
Shao, Q., Kannan, A., Lin, Z., Stack, B. C., Suen, J. Y., & Gao, L. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-0305 · Cited by 86
The ZZ-type zinc finger of ZZZ3 modulates the ATAC complex-mediated histone acetylation and gene activation
Mi, W., Zhang, Y., Lyu, J., Wang, X., Tong, Q., Peng, D., Xue, Y., Tencer, A. H., Wen, H., Li, W., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-06247-5 · Cited by 83
The bromodomain: a regulator of ATP-dependent chromatin remodeling?
Horn, P. J. (2001) · Frontiers in bioscience · doi:10.2741/horn · Cited by 83
SET-domain proteins of the Su(var)3-9, E(z) and Trithorax families
Álvarez-Venegas, R., & AVRAMOVA, Z. V. (2002) · Gene · doi:10.1016/s0378-1119(02)00401-8 · Cited by 86
Chromatin remodeling complexes: ATP-dependent machines in action.
Johnson, C. N., Adkins, N. L., & Georgel, P. (2005) · Biochemistry and cell biology = Biochimie et biologie cellulaire · doi:10.1139/o05-115 · Cited by 98
Histone acetyl transferases: a role in DNA repair and DNA replication
Hasan, S., & Hottiger, M. O. (2002) · Journal of Molecular Medicine · doi:10.1007/s00109-002-0341-7 · Cited by 82
PBRM1 acts as a p53 lysine-acetylation reader to suppress renal tumor growth
Cai, W., Su, L., Liao, L., Liu, Z. Z., Langbein, L. E., Dulaimi, E., Testa, J. R., Uzzo, R. G., Zhong, Z., Jiang, W., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-13608-1 · Cited by 85
The GCN5: its biological functions and therapeutic potentials
Haque, M. E., Jakaria, M., Akther, M., Cho, D.-Y., Kim, I., & Choi, D. (2021) · Clinical Science · doi:10.1042/cs20200986 · Cited by 83
Molecular Insights into the Recognition of N-Terminal Histone Modifications by the BRPF1 Bromodomain
Poplawski, A., Hu, K., Lee, W., Natesan, S., Peng, D., Carlson, S., Shi, X., Baláž, Š., Markley, J. L., & Glass, K. C. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.12.007 · Cited by 81
Rewiring the Epigenetic Networks in MLL-Rearranged Leukemias: Epigenetic Dysregulation and Pharmacological Interventions
Chan, A., & Chen, C.-W. D. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00081 · Cited by 83
Association of Taf14 with acetylated histone H3 directs gene transcription and the DNA damage responsePreprint
Shanle, E. K., Andrews, F. H., Meriesh, H., McDaniel, S. L., Dronamraju, R., DiFiore, J. V., Jha, D., Wozniak, G. G., Bridgers, J. B., Kerschner, J. L., et al. (2015) · Genes & Development · doi:10.1101/gad.269977.115 · Cited by 82
Chemoselective Synthesis of Lenalidomide-Based PROTAC Library Using Alkylation Reaction
Qiu, X., Sun, N., Kong, Y., Li, Y., Yang, X., & Jiang, B. (2019) · Organic Letters · doi:10.1021/acs.orglett.9b01326 · Cited by 80
Epigenetic mechanisms to propagate histone acetylation by p300/CBP
Kikuchi, M., Morita, S., Wakamori, M., Sato, S., Uchikubo‐Kamo, T., Suzuki, T., Dohmae, N., Shirouzu, M., & Umehara, T. (2023) · Nature Communications · doi:10.1038/s41467-023-39735-4 · Cited by 86
Structures of Metal-Substituted Human Histone Deacetylase 8 Provide Mechanistic Inferences on Biological Function,
Dowling, D., Gattis, S. G., Fierke, C. A., & Christianson, D. W. (2010) · Biochemistry · doi:10.1021/bi1005046 · Cited by 83

Authors: Dhalluin, C., Carlson, J. E., Zeng, L., He, C., Aggarwal, A. K., Zhou, M.-M., & Zhou, M.-M.
Affiliations: Icahn School of Medicine at Mount Sinai (US)
ORCID: Zeng, Lei
Aggarwal, Aneel K.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 1999-06
Volume: 399
Issue: 6735
Pages: 491-496
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/20974
OpenAlex: W1625510017
Cited by: 1,732
References: 30
Citations by year: 2026: 50 · 2025: 58 · 2024: 68 · 2023: 75 · 2022: 64 · 2021: 74 · 2020: 75 · 2019: 80 · 2018: 85 · 2017: 84 · 2016: 100 · 2015: 66 · 2014: 67 · 2013: 63 · 2012: 50
FWCI: 25.15
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
RePEc: Research Papers in Economics (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords: bromodomain, histone acetyltransferase, PCAF, protein structure, four-helix bundle, histone acetylation, transcriptional regulation, acetyl-CoA binding
MeSH terms: p300-CBP-Associated Factor, Acetyltransferases, Amino Acid Sequence, Escherichia coli, Ligands, Lysine, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Conformation, Recombinant Proteins, Transcription Factors, Mutagenesis, Site-Directed, Sequence Homology, Amino Acid, Bromine Compounds, Crystallography, X-Ray, Cell Cycle Proteins, Saccharomyces cerevisiae Proteins, p300-CBP Transcription Factors, Histone Acetyltransferases

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Structure and ligand of a histone acetyltransferase bromodomain

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks