Epigenetic Changes in Diabetes and Cardiovascular Risk
Open accessAbstract
Cardiovascular complications remain the leading causes of morbidity and premature mortality in patients with diabetes mellitus. Studies in humans and preclinical models demonstrate lasting gene expression changes in the vasculopathies initiated by previous exposure to high glucose concentrations and the associated overproduction of reactive oxygen species. The molecular signatures of chromatin architectures that sensitize the genome to these and other cardiometabolic risk factors of the diabetic milieu are increasingly implicated in the biological memory underlying cardiovascular complications and now widely considered as promising therapeutic targets. Atherosclerosis is a complex heterocellular disease where the contributing cell types possess distinct epigenomes shaping diverse gene expression. Although the extent that pathological chromatin changes can be manipulated in human cardiovascular disease remains to be established, the clinical applicability of epigenetic interventions will be greatly advanced by a deeper understanding of the cell type–specific roles played by writers, erasers, and readers of chromatin modifications in the diabetic vasculature. This review details a current perspective of epigenetic mechanisms of macrovascular disease in diabetes mellitus and highlights recent key descriptions of chromatinized changes associated with persistent gene expression in endothelial, smooth muscle, and circulating immune cells relevant to atherosclerosis. Furthermore, we discuss the challenges associated with pharmacological targeting of epigenetic networks to correct abnormal or deregulated gene expression as a strategy to alleviate the clinical burden of diabetic cardiovascular disease.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
The sand rat (Psammomys obesus) is a diurnal, well-accepted and extensively studied model for T2DM.
“A diurnal, well‐accepted and extensively studied model for T2DM 48, 51, 100, 101, 102, 103 is the sand rat, (Psammomys obesus).”
From The Circadian Syndrome: is the Metabolic Syndrome and much more! (2019) · cites this paper as [48]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
1 retracted
GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis
Fujiki, R., Chikanishi, T., Hashiba, W., Ito, H., Takada, I., Roeder, R. G., Kitagawa, H., & Kato, S. (2009) · Nature · doi:10.1038/nature07954 · Cited by 168 · see citing works
RetractedAtherosclerosis--an inflammatory disease
Ross, R. (1999) · New England Journal of Medicine · doi:10.1056/nejm199901143400207 · Cited by 21,725 · see citing works
An integrated encyclopedia of DNA elements in the human genome
The ENCODE Project Consortium (2012) · Nature · doi:10.1038/nature11247 · Cited by 18,072 · see citing works
Chromatin modifications and their function
Kouzarides, T. (2007) · Cell · doi:10.1016/j.cell.2007.02.005 · Cited by 10,883 · see citing works
Biochemistry and molecular cell biology of diabetic complications
Brownlee, M. (2001) · Nature · doi:10.1038/414813a · Cited by 9,107 · see citing works
Turner, R. C., Fox, C., Matthews, McElroy, H. H., Cull, C. A., Holman, R. R., Neil, P., Hadden, D. R., Wright, D., Manley, E., et al. (1998) · The Lancet · Cited by 8,419 · see citing works
10-year follow-up of intensive glucose control in type 2 diabetes
Holman, R. R., Paul, S. K., Bethel, M. A., Matthews, D. R., & Neil, H. A. W. (2008) · New England Journal of Medicine · doi:10.1056/nejmoa0806470 · Cited by 7,751 · see citing works
Intensive blood glucose control and vascular outcomes in patients with type 2 diabetes
(2008) · New England Journal of Medicine · doi:10.1056/nejmoa0802987 · Cited by 7,397 · see citing works
DNA methylation patterns and epigenetic memory
Bird, A. (2002) · Genes & Development · doi:10.1101/gad.947102 · Cited by 7,124 · see citing works
Integrative analysis of 111 reference human epigenomes
Roadmap Epigenomics Consortium, Kundaje, A., Meuleman, W., Ernst, J., Bilenky, M., Yen, A., Heravi-Moussavi, A., Kheradpour, P., Zhang, Z., Wang, J., et al. (2015) · Nature · doi:10.1038/nature14248 · Cited by 6,368 · see citing works
Functions of DNA methylation: islands, start sites, gene bodies and beyond
Jones, P. A. (2012) · Nature Reviews Genetics · doi:10.1038/nrg3230 · Cited by 6,061 · see citing works
Regulation of chromatin by histone modifications
Bannister, A. J., & Kouzarides, T. (2011) · Cell Research · doi:10.1038/cr.2011.22 · Cited by 6,012 · see citing works
Chen, X., Xiu, M., Xing, J., Yu, S., Min, D., & Guo, F. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479439 · Cited by 5,759 · see citing works
Glucose control and vascular complications in veterans with type 2 diabetes
Duckworth, W., Abraira, C., Moritz, T., Reda, D., Emanuele, N., Reaven, P. D., Zieve, F. J., Marks, J., Davis, S. N., Hayward, R., et al. (2009) · New England Journal of Medicine · doi:10.1056/nejmoa0808431 · Cited by 4,762 · see citing works
Genome-wide methylation profiles reveal quantitative views of human aging rates
Hannum, G., Guinney, J., Zhao, L., Zhang, L., Hughes, G., Sadda, S., Klotzle, B., Bibikova, M., Fan, J.-B., Gao, Y., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.10.016 · Cited by 4,270 · see citing works
Master Transcription Factors and Mediator Establish Super-Enhancers at Key Cell Identity Genes
Whyte, W. A., Orlando, D. A., Hnisz, D., Abraham, B. J., Lin, C. Y., Kagey, M. H., Rahl, P. B., Lee, T. I., & Young, R. A. (2013) · Cell · doi:10.1016/j.cell.2013.03.035 · Cited by 4,143 · see citing works
Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
Shi, Y., Lan, F., Matson, C., Mulligan, P., Whetstine, J. R., Cole, P. A., Casero, R. A., & Shi, Y. (2004) · Cell · doi:10.1016/j.cell.2004.12.012 · Cited by 4,051 · see citing works
Gupta, A., & Uribarri, J. (2016) · Hormone Research in Paediatrics · doi:10.1159/000444053 · Cited by 4,019 · see citing works
Monocyte Chemoattractant Protein-1 (MCP-1): An Overview
Deshmane, S. L., Kremlev, S., Amini, S., & Sawaya, B. E. (2009) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2008.0027 · Cited by 3,889 · see citing works
Super-enhancers in the control of cell identity and disease
Hnisz, D., Abraham, B. J., Lee, T. I., Lau, A., Saint-André, V., Sigova, A. A., Hoke, H. A., & Young, R. A. (2013) · Cell · doi:10.1016/j.cell.2013.09.053 · Cited by 3,662 · see citing works
Heintzman, N. D., Stuart, R. K., Hon, G., Fu, Y., Ching, C. W., Hawkins, R. D., Barrera, L. O., Van Calcar, S., Qu, C., Ching, K. A., et al. (2007) · Nature Genetics · doi:10.1038/ng1966 · Cited by 3,398 · see citing works
Long Noncoding RNA as Modular Scaffold of Histone Modification Complexes
Tsai, M.-C., Manor, O., Wan, Y., Mosammaparast, N., Wang, J. K., Lan, F., Shi, Y., Segal, E., & Chang, H. Y. (2010) · Science · doi:10.1126/science.1192002 · Cited by 3,290 · cited 1× · see citing works
“In addition, recent reports describe a role for long noncoding RNA transcripts in localizing chromatin signatures.(200) Furthermore, it is increasingly appreciated that the enzymes responsible for writing and removing chromatin modifications also interact with, modify, and modulate transcription factors, representing…”
Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
Lachner, M., O'Carroll, D., Rea, S., Mechtler, K., & Jenuwein, T. (2001) · Nature · doi:10.1038/35065132 · Cited by 2,868 · see citing works
Genomic DNA methylation: the mark and its mediators.
Klose, R. J., & Bird, A. P. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2005.12.008 · Cited by 2,501 · see citing works
Histone demethylation by a family of JmjC domain-containing proteins
Tsukada, Y.-I., Fang, J., Erdjument‐Bromage, H., Warren, M., Borchers, C. H., Tempst, P., & Zhang, Y. (2005) · Nature · doi:10.1038/nature04433 · Cited by 2,171 · see citing works
Function and information content of DNA methylation
Schübeler, D. (2015) · Nature · doi:10.1038/nature14192 · Cited by 2,060 · see citing works
Epigenetic programming of monocyte-to-macrophage differentiation and trained innate immunity
Saeed, S., Quintin, J., Kerstens, H. H. D., Rao, N. A., Aghajanirefah, A., Matarese, F., Cheng, S.-C., Ratter, J., Berentsen, K., van der Ent, M. A., et al. (2014) · Science · doi:10.1126/science.1251086 · Cited by 1,761 · see citing works
Cloning and characterization of a family of novel mammalian DNA (cytosine-5) methyltransferases
Okano, M., Xie, S., & Li, E. (1998) · Nature Genetics · doi:10.1038/890 · Cited by 1,643 · see citing works
Kuzmichev, A., Nishioka, K., Erdjument-Bromage, H., Tempst, P., & Reinberg, D. (2002) · Genes & Development · doi:10.1101/gad.1035902 · Cited by 1,596 · see citing works
Suppression of inflammation by a synthetic histone mimic
Nicodeme, E., Jeffrey, K. L., Schaefer, U., Beinke, S., Dewell, S., Chung, C.-W., Chandwani, R., Marazzi, I., Wilson, P., Coste, H., et al. (2010) · Nature · doi:10.1038/nature09589 · Cited by 1,563 · see citing works
Lewis, J. D., Meehan, R. R., Henzel, W. J., Maurer-Fogy, I., Jeppesen, P., Klein, F., & Bird, A. (1992) · Cell · doi:10.1016/0092-8674(92)90610-o · Cited by 1,371 · see citing works
Hydroxylation of 5-Methylcytosine by TET1 Promotes Active DNA Demethylation in the Adult Brain
Guo, J. U., Su, Y., Zhong, C., Ming, G., & Song, H. (2011) · Cell · doi:10.1016/j.cell.2011.03.022 · Cited by 1,355 · see citing works
Identification and Characterization of a Family of Mammalian Methyl-CpG Binding Proteins
Hendrich, B., & Bird, A. P. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.11.6538 · Cited by 1,352 · see citing works
Gene-specific control of inflammation by TLR-induced chromatin modifications
Foster, S. L., Hargreaves, D. C., & Medzhitov, R. (2007) · Nature · doi:10.1038/nature05836 · Cited by 1,344 · see citing works
Schultz, D. C., Ayyanathan, K., Negorev, D., Maul, G. G., & Rauscher, F. J. (2002) · Genes & Development · doi:10.1101/gad.973302 · Cited by 1,313 · see citing works
Gosselin, D., Link, V. M., Romanoski, C. E., Fonseca, G. J., Eichenfield, D. Z., Spann, N. J., Stender, J. D., Chun, H. B., Garner, H., Geissmann, F., et al. (2014) · Cell · doi:10.1016/j.cell.2014.11.023 · Cited by 1,307 · see citing works
Impaired hydroxylation of 5-methylcytosine in myeloid cancers with mutant TET2
Ko, M., Huang, Y., Jankowska, A. M., Pape, U. J., Tahiliani, M., Bandukwala, H. S., An, J., Lamperti, E. D., Koh, K. P., Ganetzky, R. D., et al. (2010) · Nature · doi:10.1038/nature09586 · Cited by 1,294 · 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
DNA methylation age of blood predicts all-cause mortality in later life
Marioni, R. E., Shah, S., McRae, A. F., Chen, B. H., Colicino, E., Harris, S. E., Gibson, J., Henders, A. K., Redmond, P., Cox, S. R., et al. (2015) · Genome Biology · doi:10.1186/s13059-015-0584-6 · Cited by 1,261 · 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
El-Osta, A., Brasacchio, D., Yao, D., Pocai, A., Jones, P. L., Roeder, R. G., Cooper, M. E., & Brownlee, M. (2008) · The Journal of Experimental Medicine · doi:10.1084/jem.20081188 · Cited by 1,115 · see citing works
Self-citationMacrophage infiltration in acute coronary syndromes. Implications for plaque rupture.
Moreno, P., Falk, E., Palacios, I. F., Newell, J. B., Fuster, V., & Fallon, J. T. (1994) · Circulation · doi:10.1161/01.cir.90.2.775 · Cited by 1,105 · see citing works
Regulation of Alternative Splicing by Histone Modifications
Luco, R. F., Pan, Q., Tominaga, K., Blencowe, B. J., Pereira‐Smith, O. M., & Misteli, T. (2010) · Science · doi:10.1126/science.1184208 · Cited by 1,099 · see citing works
Reversal of Histone Lysine Trimethylation by the JMJD2 Family of Histone Demethylases
Whetstine, J. R., Nottke, A. C., Lan, F., Huarte, M., Smolikov, S., Chen, Z., Spooner, E., Li, E., Zhang, G., Colaiácovo, M. P., et al. (2006) · Cell · doi:10.1016/j.cell.2006.03.028 · Cited by 1,046 · see citing works
Reinius, L. E., Acevedo, N., Joerink, M., Pershagen, G., Dahlén, S., Greco, D., Söderhäll, C., Scheynius, A., & Kere, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041361 · Cited by 1,019 · see citing works
Xue, Y., Wong, J., Moreno, G. T., Young, M. K., Côté, J., & Wang, W. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80299-3 · Cited by 983 · see citing works
Gæde, P., Vedel, P., Parving, H.-H., & Pedersen, O. (1999) · The Lancet · doi:10.1016/s0140-6736(98)07368-1 · Cited by 981 · see citing works
Botuyan, M. V., Lee, J., Ward, I. M., Kim, J., Thompson, J. R., Chen, J., & Mer, G. (2006) · Cell · doi:10.1016/j.cell.2006.10.043 · Cited by 973 · see citing works
De Santa, F., Totaro, M. G., Prosperini, E., Notarbartolo, S., Testa, G., & Natoli, G. (2007) · Cell · doi:10.1016/j.cell.2007.08.019 · Cited by 965 · see citing works
ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression
Shi, X., Hong, T., Walter, K. L., Ewalt, M. D., Michishita, E., Hung, T., Carney, D., Peña, P. V., Lan, F., Kaadige, M. R., et al. (2006) · Nature · doi:10.1038/nature04835 · Cited by 944 · see citing works
Ezh1 and Ezh2 Maintain Repressive Chromatin through Different Mechanisms
Margueron, R., Li, G., Sarma, K., Blais, A., Zavadil, J., Woodcock, C. L. F., Dynlacht, B. D., & Reinberg, D. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.11.004 · Cited by 889 · see citing works
Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks
Huyen, Y., Zgheib, O., DiTullio Jr, R. A., Gorgoulis, V. G., Zacharatos, P., Petty, T. J., Sheston, E. A., Mellert, H. S., Stavridi, E. S., & Halazonetis, T. D. (2004) · Nature · doi:10.1038/nature03114 · Cited by 884 · 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
Latent Enhancers Activated by Stimulation in Differentiated Cells
Ostuni, R., Piccolo, V., Barozzi, I., Polletti, S., Termanini, A., Bonifacio, S., Curina, A., Prosperini, E., Ghisletti, S., & Natoli, G. (2013) · Cell · doi:10.1016/j.cell.2012.12.018 · Cited by 867 · see citing works
Methylation of H3-Lysine 79 Is Mediated by a New Family of HMTases without a SET Domain
Feng, Q. F., Wang, H., Ng, H., Erdjument‐Bromage, H., Tempst, P., Struhl, K., & Zhang, Y. (2002) · Current Biology · doi:10.1016/s0960-9822(02)00901-6 · Cited by 866 · see citing works
Yamane, K., Toumazou, C., Tsukada, Y.-I., Erdjument‐Bromage, H., Tempst, P., Wong, J., & Zhang, Y. (2006) · Cell · doi:10.1016/j.cell.2006.03.027 · Cited by 840 · see citing works
Vermeulen, M., Eberl, H. C., Matarese, F., Marks, H., Denissov, S., Butter, F., Lee, K. K., Olsen, J. V., Hyman, A. A., Stunnenberg, H. G., et al. (2010) · Cell · doi:10.1016/j.cell.2010.08.020 · Cited by 806 · see citing works
Tachibana, M., Sugimoto, K., Fukushima, T., & Shinkai, Y. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101914200 · Cited by 784 · see citing works
A histone H3 lysine 27 demethylase regulates animal posterior development
Lan, F., Bayliss, P. E., Rinn, J. L., Whetstine, J. R., Wang, J. K., Chen, S., Iwase, S., Alpatov, R., Issaeva, I., Canaani, E., et al. (2007) · Nature · doi:10.1038/nature06192 · Cited by 782 · see citing works
Regulation of MLL1 H3K4 methyltransferase activity by its core components
Dou, Y., Milne, T. A., Ruthenburg, A. J., Lee, S., Lee, J. W., Verdine, G. L., Allis, C. D., & Roeder, R. G. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1128 · Cited by 764 · see citing works
Replication of smooth muscle cells in vascular disease.
Schwartz, S. M., CAMPBELL, G. R., & Campbell, J. H. (1986) · Circulation Research · doi:10.1161/01.res.58.4.427 · Cited by 762 · see citing works
JMJD6 Is a Histone Arginine Demethylase
Chang, B., Chen, Y., Zhao, Y., & Bruick, R. K. (2007) · Science · doi:10.1126/science.1145801 · Cited by 746 · see citing works
Pott, S., & Lieb, J. D. (2014) · Nature Genetics · doi:10.1038/ng.3167 · Cited by 745 · see citing works
SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells
Hamamoto, R., Furukawa, Y., Morita, M., Iimura, Y., Pittella-Silva, F., Li, M., Yagyu, R., & Nakamura, Y. (2004) · Nature Cell Biology · doi:10.1038/ncb1151 · Cited by 738 · see citing works
Bekkering, S., Quintin, J., Joosten, L. A. B., van der Meer, J. W. M., Netea, M. G., & Riksen, N. P. (2014) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.114.303887 · Cited by 735 · see citing works
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
Follow-up of glycemic control and cardiovascular outcomes in type 2 diabetes
Hayward, R. A., Reaven, P. D., Wiitala, W. L., Bahn, G. D., Reda, D. J., Ge, L., McCarren, M., Duckworth, W. C., & Emanuele, N. V. (2015) · New England Journal of Medicine · doi:10.1056/nejmoa1414266 · Cited by 668 · see citing works
Parker, S. C. J., Stitzel, M. L., Taylor, D. L., Orozco, J. M., Erdos, M. R., Akiyama, J. A., van Bueren, K. L., Chines, P. S., Narisu, N., Program, N. C. S., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1317023110 · Cited by 665 · see citing works
Identification of a mammalian protein that binds specifically to DNA containing methylated CpGs
Meehan, R. R., Lewis, J., McKay, S. J., Kleiner, E., & Bird, A. P. (1989) · Cell · doi:10.1016/0092-8674(89)90430-3 · Cited by 659 · see citing works
NF-κB Directs Dynamic Super Enhancer Formation in Inflammation and Atherogenesis
Brown, J. D., Lin, C. Y., Duan, Q., Griffin, G., Federation, A. J., Paranal, R. M., Bair, S., Newton, G., Lichtman, A. H., Kung, A. L., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.08.024 · Cited by 614 · see citing works
Self-citationPal, S., Vishwanath, S. N., Erdjument‐Bromage, H., Tempst, P., & Sif, S. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.21.9630-9645.2004 · Cited by 599 · see citing works
Nishioka, K., Rice, J. C., Sarma, K., Erdjument‐Bromage, H., Werner, J. K., Wang, Y., Chuikov, S., Valenzuela, P., Tempst, P., Steward, R., et al. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00548-8 · Cited by 580 · see citing works
Transdifferentiation of Vascular Smooth Muscle Cells to Macrophage-Like Cells During Atherogenesis
Feil, S., Fehrenbacher, B., Lukowski, R., Essmann, F., Schulze-Osthoff, K., Schaller, M., & Feil, R. (2014) · Circulation Research · doi:10.1161/circresaha.115.304634 · Cited by 578 · see citing works
Iguchi-Ariga, S. M., & Schaffner, W. (1989) · Genes & Development · doi:10.1101/gad.3.5.612 · Cited by 559 · see citing works
Genome-wide Profiling of 5-Formylcytosine Reveals Its Roles in Epigenetic Priming
Song, C., Szulwach, K. E., Dai, Q., Fu, Y., Mao, S.-Q., Lin, L., Street, C., Li, Y., Poidevin, M., Wu, H., et al. (2013) · Cell · doi:10.1016/j.cell.2013.04.001 · Cited by 545 · see citing works
Purification and Functional Characterization of a Histone H3-Lysine 4-Specific Methyltransferase
Wang, H., Cao, R., Li, X., Erdjument‐Bromage, H., Borchers, C. H., Tempst, P., & Zhang, Y. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00405-1 · Cited by 539 · see citing works
Zhao, Q., Rank, G., Tan, Y., Li, H., Moritz, R. L., Simpson, R. J., Cerruti, L., Curtis, D. J., Patel, D. J., Allis, C. D., et al. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1568 · Cited by 539 · see citing works
Brasacchio, D., Okabe, J., Tikellis, C., Balcerczyk, A., George, P., Baker, E. K., Calkin, A. C., Brownlee, M., Cooper, M. E., & El‐Osta, A. (2009) · Diabetes · doi:10.2337/db08-1666 · Cited by 533 · see citing works
Self-citationBernstein, E., Duncan, E. M., Masui, O., Gil, J., Heard, É., & Allis, C. D. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.7.2560-2569.2006 · Cited by 531 · see citing works
Double chromodomains cooperate to recognize the methylated histone H3 tail
Flanagan, J. F., Mi, L.-Z., Chruszcz, M., Cymborowski, M., Clines, K. L., Kim, Y., Minor, W., Rastinejad, F., & Khorasanizadeh, S. (2005) · Nature · doi:10.1038/nature04290 · Cited by 528 · see citing works
PTIP Associates with MLL3- and MLL4-containing Histone H3 Lysine 4 Methyltransferase Complex
Cho, Y., Hong, T., Hong, S., Guo, H. W., Yu, H., Kim, D., Guszczynski, T., Dressler, G. R., Copeland, T. D., Kalkum, M., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701574200 · Cited by 528 · see citing works
Bliss, M. (1982) · doi:10.1007/978-1-349-09612-1 · Cited by 524 · see citing works
KDM1B is a histone H3K4 demethylase required to establish maternal genomic imprints
Ciccone, D. N., Su, H., Hevi, S., Gay, F., Lei, H., Bajko, J., Xu, G., Li, E., & Chen, T. (2009) · Nature · doi:10.1038/nature08315 · Cited by 514 · see citing works
Chronic Infections and the Risk of Carotid Atherosclerosis
Kiechl, S. J., Egger, G., Mayr, M., Wiedermann, C. J., Bonora, E., Oberhollenzer, F., Muggeo, M., Xu, Q., Wick, G., Poewe, W. H., et al. (2001) · Circulation · doi:10.1161/01.cir.103.8.1064 · Cited by 508 · see citing works
Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive
Guccione, E., Bassi, C., Casadio, F., Martinato, F., Cesaroni, M., Schuchlautz, H., Lüscher, B., & Amati, B. B. (2007) · Nature · doi:10.1038/nature06166 · Cited by 495 · see citing works
Yamane, K., Tateishi, K., Klose, R. J., Fang, J., Fabrizio, L. A., Erdjument‐Bromage, H., Taylor‐Papadimitriou, J., Tempst, P., & Zhang, Y. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.03.001 · Cited by 493 · see citing works
Progression of Incipient Diabetic Retinopathy During Good Glycemic Control
Engerman, R. L., & Kern, T. S. (1987) · Diabetes · doi:10.2337/diab.36.7.808 · Cited by 490 · cited 1× · see citing works
“5 years of insulin therapy and effective glycemic control.(11) Similarly”
The DCCT Research Group (1986) · Diabetes · doi:10.2337/diabetes.35.5.530 · Cited by 465 · see citing works
Strahl, B. D., Briggs, S. D., Brame, C. J., Caldwell, J., Koh, S. S., Ma, H., Cook, R. G., Shabanowitz, J., Hunt, D. F., Stallcup, M. R., et al. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00294-9 · Cited by 457 · see citing works
Macrophage expression of active MMP-9 induces acute plaque disruption in apoE-deficient mice
Gough, P. J. (2005) · Journal of Clinical Investigation · doi:10.1172/jci25074 · Cited by 453 · see citing works
The Retinoblastoma Binding Protein RBP2 Is an H3K4 Demethylase
Klose, R. J., Yan, Q., Tóthová, Z., Yamane, K., Erdjument‐Bromage, H., Tempst, P., Gilliland, D. G., Zhang, Y., & Kaelin, W. G. (2007) · Cell · doi:10.1016/j.cell.2007.02.013 · Cited by 446 · see citing works
Duivenvoorden, R., Tang, J., Cormode, D. P., Mieszawska, A. J., Izquierdo‐Garcia, D., Ozcan, C., Otten, M. J., Zaidi, N., Lobatto, M. E., van Rijs, S. M., et al. (2014) · Nature Communications · doi:10.1038/ncomms4065 · Cited by 444 · see citing works
The histone H3K4 demethylase SMCX links REST target genes to X-linked mental retardation
Tahiliani, M., Mei, P., Fang, R., Leonor, T., Rutenberg, M. S., Shimizu, F., Li, J., Rao, A., & Shi, Y. G. (2007) · Nature · doi:10.1038/nature05823 · Cited by 429 · see citing works
Sims, R. J., Chen, C.-F., Santos-Rosa, H., Kouzarides, T., Patel, S. S., & Reinberg, D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500395200 · Cited by 423 · see citing works
Villeneuve, L. M., Reddy, M. A., Lanting, L. L., Wang, M., Li, M., & Natarajan, R. D. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803623105 · Cited by 412 · 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
Self-citationWysocka, J., Myers, M. P., Laherty, C. D., Eisenman, R. N., & Herr, W. (2003) · Genes & Development · doi:10.1101/gad.252103 · Cited by 390 · see citing works
Beamish, J. A., He, P., Kottke‐Marchant, K., & Marchant, R. E. (2010) · Tissue Engineering Part B Reviews · doi:10.1089/ten.teb.2009.0630 · Cited by 383 · see citing works
Association of UHRF1 with methylated H3K9 directs the maintenance of DNA methylation
Rothbart, S. B., Krajewski, K., Nady, N., Tempel, W., Xue, S., Badeaux, A. I., Baršytė-Lovejoy, D., Martínez-Márquez, J. Y., Bedford, M. T., Fuchs, S. M., et al. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2391 · Cited by 381 · see citing works
Jayashree, B., Bibin, Y. S., Prabhu, D., Shanthirani, C. S., Gokulakrishnan, K., Lakshmi, B. S., Mohan, V., & Balasubramanyam, M. (2014) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-013-1911-4 · Cited by 353 · see citing works
Epigenetic regulatory functions of DNA modifications: 5-methylcytosine and beyond
Breiling, A., & Lyko, F. (2015) · Epigenetics & Chromatin · doi:10.1186/s13072-015-0016-6 · Cited by 353 · see citing works
Li, Y., Reddy, M. A., Miao, F., Shanmugam, N., Yee, J.-K., Hawkins, D., Ren, B., & Natarajan, R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802800200 · Cited by 353 · see citing works
L3MBTL1, a Histone-Methylation-Dependent Chromatin Lock
Trojer, P., Li, G., Sims, R. J., Vaquero, A., Kalakonda, N., Boccuni, P., Lee, D., Erdjument‐Bromage, H., Tempst, P., Nimer, S. D., et al. (2007) · Cell · doi:10.1016/j.cell.2007.03.048 · Cited by 343 · see citing works
The Diabetes Control and Complications Trial (DCCT)/Epidemiology of Diabetes Interventions and Complications (EDIC) Research Group (2015) · Diabetes · doi:10.2337/db14-0930 · Cited by 333 · see citing works
Molecular regulation of H3K4 trimethylation by ASH2L, a shared subunit of MLL complexes
Steward, M., Lee, J., O’Donovan, A., Wyatt, M., Bernstein, B., & Shilatifard, A. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1131 · Cited by 325 · see citing works
Keating, S. T., & El‐Osta, A. (2015) · Circulation Research · doi:10.1161/circresaha.116.303936 · Cited by 315 · see citing works
Self-citationReadout of Epigenetic Modifications
Patel, D. J., & Wang, Z. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-072711-165700 · Cited by 315 · see citing works
Brown, M. A., Sims, R. J., Gottlieb, P. D., & Tucker, P. W. (2006) · Molecular Cancer · doi:10.1186/1476-4598-5-26 · Cited by 314 · see citing works
Solution Structure of the Methyl-CpG Binding Domain of Human MBD1 in Complex with Methylated DNA
Ohki, I., Shimotake, N., Fujita, N., Jee, J.-G., Ikegami, T., Nakao, M., & Shirakawa, M. (2001) · Cell · doi:10.1016/s0092-8674(01)00324-5 · Cited by 313 · see citing works
Bradshaw, E. M., Raddassi, K., Elyaman, W., Orban, T., Gottlieb, P. A., Kent, S. C., & Hafler, D. A. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0900576 · Cited by 295 · see citing works
Increased Monocytic Activity and Biomarkers of Inflammation in Patients With Type 1 Diabetes
Devaraj, S., Glaser, N. S., Griffen, S., Wang, J. F., Miguelino, E., & Jialal, I. (2006) · Diabetes · doi:10.2337/diabetes.55.03.06.db05-1417 · Cited by 293 · see citing works
Ten-Eleven Translocation-2 (TET2) Is a Master Regulator of Smooth Muscle Cell Plasticity
Liu, R., Yu, J. H., Tang, W. H., Qin, L., Zhang, X., Tellides, G., Hwa, J., Yu, J., & Martin, K. A. (2013) · Circulation · doi:10.1161/circulationaha.113.002887 · Cited by 289 · see citing works
Control of SRF binding to CArG box chromatin regulates smooth muscle gene expression in vivo
McDonald, O. G. (2005) · Journal of Clinical Investigation · doi:10.1172/jci26505 · Cited by 284 · see citing works
Zhou, S., Chen, H., Wan, Y.-Z., Zhang, Q.-J., Wei, Y.-S., Huang, S., Liu, J., Lu, Y., Zhang, Z., Yang, R., et al. (2011) · Circulation Research · doi:10.1161/circresaha.111.243592 · Cited by 273 · see citing works
Liu, Y., Subrahmanyam, R., Chakraborty, T., Sen, R., & Desiderio, S. V. (2007) · Immunity · doi:10.1016/j.immuni.2007.09.005 · Cited by 271 · see citing works
Shen, L., Inoue, A., He, J., Liu, Y., Lu, F., & Zhang, Y. (2014) · Cell stem cell · doi:10.1016/j.stem.2014.09.002 · Cited by 268 · see citing works
Identification and Characterization of the Human Set1B Histone H3-Lys4 Methyltransferase Complex
Lee, J., Tate, C. M., You, J., & Skalnik, D. G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609809200 · Cited by 266 · see citing works
Novel Long Noncoding RNAs Are Regulated by Angiotensin II in Vascular Smooth Muscle Cells
Leung, A., Trac, C., Jin, W. L., Lanting, L. L., Akbany, A., Sætrom, P., Schones, D. E., & Natarajan, R. D. (2013) · Circulation Research · doi:10.1161/circresaha.112.300849 · Cited by 266 · see citing works
DNA Methylation Map of Human Atherosclerosis
Zaina, S., Heyn, H., Carmona, F. J., Varol, N., Sayols, S., Condom, E., Ramírez, J., Gómez, A., Gonçalves, I., Morán, S., et al. (2014) · Circulation Cardiovascular Genetics · doi:10.1161/circgenetics.113.000441 · Cited by 265 · see citing works
Identification and Characterization of a Novel Human Histone H3 Lysine 36-specific Methyltransferase
Sun, X., Wei, J., Wu, X., Hu, M., Wang, L., Wang, H.-H., Zhang, Q.-H., Chen, S., Huang, Q.-H., & Chen, Z. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504012200 · Cited by 260 · see citing works
Isolation and characterization of the cDNA encoding human DNA methyltransferase
Yen, R.-W. C., Vertino, P. M., Nelkin, B. D., Yu, J. J., El‐Deiry, W. S., Cumaraswamy, A., Lennon, G. G., Trask, B. J., Celano, P., & Baylin, S. B. (1992) · Nucleic Acids Research · doi:10.1093/nar/20.9.2287 · Cited by 256 · see citing works
Paneni, F., Mocharla, P. S., Akhmedov, A. T., Costantino, S., Osto, E., Volpe, M., Lüscher, T. F., & Cosentino, F. (2012) · Circulation Research · doi:10.1161/circresaha.112.266593 · Cited by 256 · see citing works
Lee, M. G., Norman, J. A., Shilatifard, A., & Shiekhattar, R. (2007) · Cell · doi:10.1016/j.cell.2007.02.004 · Cited by 254 · see citing works
Detection of histone modifications at specific gene loci in single cells in histological sections
Gomez, D., Shankman, L. S., Nguyen, A. T., & Owens, G. K. (2013) · Nature Methods · doi:10.1038/nmeth.2332 · Cited by 253 · see citing works
Evaluating the Role of Epigenetic Histone Modifications in the Metabolic Memory of Type 1 Diabetes
Miao, F., Chen, Z., GENUTH, S. M., Paterson, A. D., Zhang, L., Wu, X., Li, S. M., Cleary, P. A., Riggs, A. D., Harlan, D. M., et al. (2014) · Diabetes · doi:10.2337/db13-1251 · Cited by 253 · see citing works
Structure and function insights into the NuRD chromatin remodeling complex
Torchy, M., Hamiche, A., & Klaholz, B. P. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1880-8 · Cited by 244 · see citing works
TDRD3 Is an Effector Molecule for Arginine-Methylated Histone Marks
Yang, Y., Lu, Y., Espejo, A. B., Wu, J., Xu, W., Liang, S., & Bedford, M. T. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.11.024 · Cited by 242 · see citing works
Sobue, K., Hayashi, K., & Nishida, W. (1999) · Molecular and Cellular Biochemistry · doi:10.1023/a:1006941621170 · Cited by 239 · see citing works
Pena, O. M., Pistolic, J., Raj, D., Fjell, C. D., & Hancock, R. E. W. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1001952 · Cited by 238 · see citing works
Clouaire, T., & Stancheva, I. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-7324-y · Cited by 237 · see citing works
Raiber, E., Beraldi, D., Ficz, G., Burgess, H. E., Branco, M. R., Murat, P., Oxley, D., Booth, M. J., Reik, W., & Balasubramanian, S. (2012) · Genome biology · doi:10.1186/gb-2012-13-8-r69 · Cited by 230 · see citing works
Therapeutic potential for HDAC inhibitors in the heart
McKinsey, T. A. (2012) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010611-134712 · Cited by 230 · see citing works
Reactive oxygen species mediate a cellular ‘memory’ of high glucose stress signalling
Ihnat, M. A., Thorpe, J. E., Kamat, C. D., Szabó, C., Green, D. E., Warnke, L. A., Lacza, Z., Cselenyák, A., Ross, K., Shakir, S. F., et al. (2007) · Diabetologia · doi:10.1007/s00125-007-0684-2 · Cited by 225 · see citing works
Kocher, O. N., Gabbiani, F., Gabbiani, G., et al. (1991) · PubMed · Cited by 225 · see citing works
Inhibiting macrophage proliferation suppresses atherosclerotic plaque inflammation
Tang, J., Lobatto, M. E., Hassing, L., van der Staay, S. E. M., van Rijs, S. M., Calcagno, C., Braza, M. S., Baxter, S., Fay, F., Sánchez-Gaytán, B. L., et al. (2015) · Science Advances · doi:10.1126/sciadv.1400223 · Cited by 223 · see citing works
MECP2 disorders: from the clinic to mice and back
Lombardi, L. M., Baker, S. A., & Zoghbi, H. Y. (2015) · Journal of Clinical Investigation · doi:10.1172/jci78167 · Cited by 221 · cited 1× · see citing works
“Such complexes contain enzymes that remove transcriptionally permissive histone acetylation marks and enzymes that write transcriptionally repressive histone methylation marks, linking DNA methylation with post-translational histone modifications (discussed further below).(96) In contrast, mechanistically distinct DNA…”
Pirola, L., Balcerczyk, A., Tothill, R. W., Haviv, I., Kaspi, A., Lunke, S., Ziemann, M., Karagiannis, T. C., Tonna, S. J., Kowalczyk, A., et al. (2011) · Genome Research · doi:10.1101/gr.116095.110 · Cited by 220 · see citing works
Self-citationTan, X., Rotllant, J., Li, H., Deyne, P. G. D., & Du, S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509503103 · Cited by 214 · see citing works
Diabetes Accelerates Smooth Muscle Accumulation in Lesions of Atherosclerosis
Suzuki, L. A., Poot, M., Gerrity, R. G., & Bornfeldt, K. (2001) · Diabetes · doi:10.2337/diabetes.50.4.851 · Cited by 210 · see citing works
Abu‐Farha, M., Lambert, J., Madhoun, A. S. A., Elisma, F., Skerjanc, I. S., & Figeys, D. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700271-mcp200 · Cited by 199 · see citing works
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 198 · see citing works
PRMT7, a New Protein Arginine Methyltransferase That Synthesizes Symmetric Dimethylarginine
Lee, J., Cook, J. R., Yang, Z.-H., Mirochnitchenko, O. V., Gunderson, S., Felix, A. M., Herth, N., Hoffmann, R., & Pestka, S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405295200 · Cited by 197 · see citing works
Hsia, D. A., Tepper, C. G., Pochampalli, M. R., Hsia, E. Y. C., Izumiya, C., Huerta, S. B., Wright, M. E., Chen, H.-W., Kung, H.-J., & Izumiya, Y. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1000401107 · Cited by 197 · see citing works
A Suv39h‐dependent mechanism for silencing S‐phase genes in differentiating but not in cycling cells
Ait‐Si‐Ali, S., Guasconi, V., Fritsch, L., Yahi, H., Sekhri, R., Naguibneva, I., Robin, P., Cabon, F., Polesskaya, A., & Harel‐Bellan, A. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600074 · Cited by 190 · see citing works
( R )-PFI-2 is a potent and selective inhibitor of SETD7 methyltransferase activity in cells
Baršytė-Lovejoy, D., Li, F., Oudhoff, M. J., Tatlock, J. H., Dong, A., Zeng, H., Wu, H., Freeman, S. A., Schapira, M., Senisterra, G. A., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1407358111 · Cited by 187 · see citing works
Villeneuve, L. M., Kato, M., Reddy, M. A., Wang, M., Lanting, L., & Natarajan, R. (2010) · Diabetes · doi:10.2337/db10-0208 · Cited by 186 · see citing works
Bromodomain-Containing Protein 4
Meloche, J., Potus, F., Vaillancourt, M., et al. (2015) · Circulation Research · doi:10.1161/circresaha.115.307004 · Cited by 183 · see citing works
Piga, R., Naito, Y., Kokura, S., Handa, O., & Yoshikawa, T. (2006) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2006.09.016 · Cited by 182 · see citing works
Distinguishing Hyperglycemic Changes by Set7 in Vascular Endothelial Cells
Okabe, J., Orlowski, C., Balcerczyk, A., Tikellis, C., Thomas, M. C., Cooper, M. E., & El-Osta, A. (2012) · Circulation Research · doi:10.1161/circresaha.112.266171 · Cited by 180 · see citing works
Self-citationTargeting macrophage Histone deacetylase 3 stabilizes atherosclerotic lesions
Hoeksema, M. A., Gijbels, M. J., den Bossche, J. V., van der Velden, S., Sijm, A., Neele, A. E., Seijkens, T. T. P., Stöger, J. L., Meiler, S. U., Boshuizen, M. C. S., et al. (2014) · EMBO Molecular Medicine · doi:10.15252/emmm.201404170 · Cited by 179 · see citing works
Paneni, F., Costantino, S., Battista, R., Castello, L., Capretti, G., Chiandotto, S., Scavone, G., Villano, A., Pitocco, D., Lanza, G. A., et al. (2014) · Circulation Cardiovascular Genetics · doi:10.1161/circgenetics.114.000671 · Cited by 176 · see citing works
Zampetaki, A., Zeng, L., Margariti, A., Xiao, Q., Li, H., Zhang, Z., Pepe, A. E., Wang, G., Habi, O., DEFALCO, E., et al. (2009) · Circulation · doi:10.1161/circulationaha.109.890491 · Cited by 173 · see citing works
Genomic patterns and context specific interpretation of DNA methylation
Baubec, T., & Schübeler, D. (2014) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2013.11.015 · Cited by 163 · see citing works
Sinha, K. M., Yasuda, H., Coombes, M. M., Dent, S., & Crombrugghe, B. D. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.332 · Cited by 160 · see citing works
KDM7 is a dual demethylase for histone H3 Lys 9 and Lys 27 and functions in brain development
Tsukada, Y.-I., Ishitani, T., & Nakayama, K. I. (2010) · Genes & Development · doi:10.1101/gad.1864410 · Cited by 158 · see citing works
Ostos, M. A., Recalde, D., Zakin, M. M., & Scott‐Algara, D. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02692-3 · Cited by 152 · see citing works
Lee, S., Oshige, M., Durant, S. T., Rasila, K. K., Williamson, E. A., Ramsey, H. E., Corwin, L. K., Nickoloff, J. A., & Hromas, R. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503676102 · Cited by 150 · see citing works
Activator-Mediated Recruitment of the MLL2 Methyltransferase Complex to the β-Globin Locus
Demers, C., Chaturvedi, C.-P., Ranish, J. A., Juban, G., Lai, P., Morlé, F., Aebersold, R. H., Dilworth, F. J., Groudine, M. T., & Brand, M. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.06.022 · Cited by 143 · see citing works
Trichostatin A Exacerbates Atherosclerosis in Low Density Lipoprotein Receptor–Deficient Mice
Choi, J., Nam, K., Kim, J.-Y., Baek, M. W., Park, J.-E., Park, H., Kwon, H. J., Kwon, O., Kim, D.-Y., & Oh, G. T. (2005) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000184758.07257.88 · Cited by 142 · see citing works
Epigenetic regulation of smooth muscle cell plasticity
Liu, R., Leslie, K. L., & Martin, K. A. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.06.004 · Cited by 140 · see citing works
Findeisen, H. M., Gizard, F., Zhao, Y., 青华, Heywood, E. B., Jones, K. L., Cohn, D. M., & Bruemmer, D. (2011) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.110.221952 · Cited by 137 · see citing works
HP1 Binding to Chromatin Methylated at H3K9 Is Enhanced by Auxiliary Factors
Eskeland, R., Eberharter, A., & Imhof, A. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01576-06 · Cited by 136 · see citing works
Diabetes Adversely Affects Macrophages During Atherosclerotic Plaque Regression in Mice
Parathath, S., Grauer, L., Huang, L., Sanson, M., Distel, E., Goldberg, I. J., & Fisher, E. A. A. (2011) · Diabetes · doi:10.2337/db10-0778 · Cited by 135 · see citing works
Jahagirdar, R., Zhang, H., Azhar, S., Tobin, J., Attwell, S., Yu, R., Wu, J., McLure, K. G., Hansen, H. C., Wagner, G. S., et al. (2014) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2014.06.008 · Cited by 134 · see citing works
Balancing chromatin remodeling and histone modifications in transcription
Petty, E. L., & Pillus, L. (2013) · Trends in Genetics · doi:10.1016/j.tig.2013.06.006 · Cited by 119 · see citing works
SIRT1, p66Shc, and Set7/9 in Vascular Hyperglycemic Memory
Paneni, F., Volpe, M., Lüscher, T. F., & Cosentino, F. (2013) · Diabetes · doi:10.2337/db12-1648 · Cited by 118 · see citing works
Substrate Preferences of the EZH2 Histone Methyltransferase Complex
Martin, C. C., Cao, R., & Zhang, Y. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513425200 · Cited by 107 · see citing works
Strategic Approaches to Unraveling Genetic Causes of Cardiovascular Diseases
Marian, A. J., & Belmont, J. W. (2011) · Circulation Research · doi:10.1161/circresaha.110.236067 · Cited by 107 · see citing works
The DNA methylation drift of the atherosclerotic aorta increases with lesion progression
Valencia-Morales, M. D. P., Zaina, S., Heyn, H., Carmona, F. J., Varol, N., Sayols, S., Condom, E., Ramírez, J., Gómez, A., Morán, S., et al. (2015) · BMC Medical Genomics · doi:10.1186/s12920-015-0085-1 · Cited by 104 · see citing works
Histone Methyltransferase SETD3 Regulates Muscle Differentiation
Eom, G. H., Kim, K., Kim, J. H., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.203307 · Cited by 101 · see citing works
The transcriptional regulator network of human inflammatory macrophages is defined by open chromatin
Schmidt, S. V., Krebs, W., Ulas, T., Xue, J., Bassler, K. E., Günther, P. S., Hardt, A.-L., Schultze, H., Sander, J., Klee, K., et al. (2016) · Cell Research · doi:10.1038/cr.2016.1 · Cited by 101 · see citing works
Epigenome Microarray Platform for Proteome-Wide Dissection of Chromatin-Signaling Networks
Bua, D. J., Kuo, A. J., Cheung, P., Liu, C. L., Migliori, V., Espejo, A. B., Casadio, F., Bassi, C., Amati, B. B., Bedford, M. T., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006789 · Cited by 98 · see citing works
Vascular histone deacetylation by pharmacological HDAC inhibitionPreprint
Rafehi, H., Balcerczyk, A., Lunke, S., Kaspi, A., Ziemann, M., Kurup, H. K. N., Okabe, J., Khurana, I., Ooi, J. Y. Y., Khan, A. W., et al. (2014) · Genome Research · doi:10.1101/gr.168781.113 · Cited by 94 · see citing works
Self-citationPHF8 is a histone H3K9me2 demethylase regulating rRNA synthesis
Zhu, Z., Wang, Y., Li, X., Wang, Y., Xu, L., Wang, X., Sun, T., Dong, X., Chen, L., Mao, H., et al. (2010) · Cell Research · doi:10.1038/cr.2010.75 · Cited by 92 · see citing works
Transcriptional regulation by the Set7 lysine methyltransferase
Keating, S. T., & El‐Osta, A. (2013) · Epigenetics · doi:10.4161/epi.24234 · Cited by 91 · see citing works
Self-citationKapoor-Vazirani, P., Kagey, J. D., & Vertino, P. M. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.00524-10 · Cited by 89 · see citing works
Islet transplantation inhibits diabetic retinopathy in the sucrose-fed diabetic Cohen rat.
Hammes, H., Klinzing, I., Wiegand, S., et al. (1993) · PubMed · Cited by 84 · see citing works
Histone target selection within chromatin: an exemplary case of teamworkPreprint
Lalonde, M., Cheng, X., & Côté, J. (2014) · Genes & Development · doi:10.1101/gad.236331.113 · Cited by 83 · see citing works
CLLD8/KMT1F Is a Lysine Methyltransferase That Is Important for Chromosome Segregation
Falandry, C., Fourel, G., Galy, V., Ristriani, T., Horard, B., Simon, E. B., Salles, G., Gilson, É., & Magdinier, F. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.052399 · Cited by 81 · see citing works
Abbas, A., Aukrust, P., Russell, D., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0084935 · Cited by 80 · see citing works
Ananthanarayanan, M., Li, S., Balasubramaniyan, N., Suchy, F. J., & Walsh, M. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410021200 · Cited by 76 · see citing works
Kim, S. M., Kee, H. J., Eom, G. H., Choe, N., Kim, J. Y., Kim, Y. S., Kim, S. K., Kook, H., Kook, H., & Seo, S. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.04.095 · Cited by 73 · see citing works
Epigenetic pathways in macrophages emerge as novel targets in atherosclerosis
Neele, A. E., den Bossche, J. V., Hoeksema, M. A., & de Winther, M. P. J. (2015) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2015.03.101 · Cited by 70 · see citing works
Inhibiting epigenetic enzymes to improve atherogenic macrophage functions
den Bossche, J. V., Neele, A. E., Hoeksema, M. A., de Heij, F., Boshuizen, M. C. S., van der Velden, S., de Boer, V. C. J., Reedquist, K. A., & de Winther, M. P. J. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.11.029 · Cited by 70 · see citing works
Mathiyalagan, P., Okabe, J., Chang, L., Su, Y. R., Du, X., & El‐Osta, A. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt896 · Cited by 69 · see citing works
Self-citationWu, H., Zhao, M., Yoshimura, A., Chang, C., & Lu, Q. (2016) · Clinical Reviews in Allergy & Immunology · doi:10.1007/s12016-016-8534-y · Cited by 69 · see citing works
Sukmawati, D., & Tanaka, R. (2015) · PubMed Central · Cited by 68 · see citing works
Metabolic Regulation of Histone Acetyltransferases by Endogenous Acyl-CoA Cofactors
Montgomery, D. C., Sorum, A. W., Guasch, L., Nicklaus, M. C., & Meier, J. L. (2015) · Chemistry & Biology · doi:10.1016/j.chembiol.2015.06.015 · Cited by 67 · see citing works
He, S., Owen, D. R., Jelinsky, S. A., & Lin, L.-L. (2015) · Scientific Reports · doi:10.1038/srep14368 · Cited by 67 · see citing works
The Epigenetic Memory of Monocytes and Macrophages as a Novel Drug Target in Atherosclerosis
Bekkering, S., Joosten, L. A. B., van der Meer, J. W. M., Netea, M. G., & Riksen, N. P. (2015) · Clinical Therapeutics · doi:10.1016/j.clinthera.2015.01.008 · Cited by 65 · see citing works
BET Bromodomain Blockade Mitigates Intimal Hyperplasia in Rat Carotid Arteries
Wang, B., Zhang, M., Takayama, T., Shi, X., Roenneburg, D. A., Kent, K. C., & Guo, L. (2015) · EBioMedicine · doi:10.1016/j.ebiom.2015.09.045 · Cited by 64 · see citing works
Transcriptional Regulation of Endothelial Arginase 2 by Histone Deacetylase 2
Pandey, D., Sikka, G., Bergman, Y., Kim, J. H., Ryoo, S., Romer, L. H., & Berkowitz, D. E. (2014) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.114.303685 · Cited by 63 · see citing works
Epigenomic profiling of DNA methylation in paired prostate cancer versus adjacent benign tissue
Geybels, M. S., Zhao, S., Wong, C.-J., Bibikova, M. V., Klotzle, B., Wu, M. C., Ostrander, E. A., Fan, J., Feng, Z., & Stanford, J. L. (2015) · The Prostate · doi:10.1002/pros.23093 · Cited by 58 · see citing works
Nomoto, H., Miyoshi, H., Furumoto, T., Oba, K., Tsutsui, H., Miyoshi, A., Kondo, T., Tsuchida, K., Atsumi, T., Manda, N., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0135854 · Cited by 52 · see citing works
Denis, G. V., Nikolajczyk, B. S., & Schnitzler, G. R. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.05.030 · Cited by 39 · see citing works
Choi, I., Kim, R., Lim, H., Kaestner, K. H., & Won, K. (2014) · BMC Genomics · doi:10.1186/1471-2164-15-670 · Cited by 38 · see citing works
Coupling circadian rhythms of metabolism and chromatin remodelling
Masri, S., Orozco-Solís, R., Aguilar‐Arnal, L., Cervantes, M., & Sassone‐Corsi, P. (2015) · Diabetes Obesity and Metabolism · doi:10.1111/dom.12509 · Cited by 37 · see citing works
Genome architecture: from linear organisation of chromatin to the 3D assembly in the nucleus
Sequeira‐Mendes, J., & Gutiérrez, C. (2015) · Chromosoma · doi:10.1007/s00412-015-0538-5 · Cited by 36 · see citing works
Flagged first, then by citations
Research works printed but not linked: 1
- [37]Keating ST El-Osta A Epigenetics and Metabolism. Circulation research 2015 116 715 736 25677519
Cited by
Sorted by citations
Reactive oxygen species (ROS) in macrophage activation and function in diabetes
Rendra, E., Riabov, V., Mossel, D. M., Sevastyanova, T., Harmsen, M. C., & Kzhyshkowska, J. (2019) · Immunobiology · doi:10.1016/j.imbio.2018.11.010 · Cited by 636 · see citing works
The Circadian Syndrome: is the Metabolic Syndrome and much more!
Zimmet, P., Alberti, K. G. M. M., Stern, N., Bilu, C., El‐Osta, A., Einat, H., & Kronfeld‐Schor, N. (2019) · Journal of Internal Medicine · doi:10.1111/joim.12924 · Cited by 387 · see citing works
Self-citationType 2 diabetes mellitus and cardiovascular disease: Genetic and epigenetic links
De Rosa, S., Arcidiacono, B., Chiefari, E., Brunetti, A., Indolfi, C., & Foti, D. P. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00002 · Cited by 369 · see citing works
The epigenetic landscape related to reactive oxygen species formation in the cardiovascular system
Kietzmann, T., Petry, A., Shvetsova, A., Gerhold, J. M., & Görlach, A. (2017) · British Journal of Pharmacology · doi:10.1111/bph.13792 · Cited by 253 · see citing works
Obesity, Diabetes, and Cardiovascular Diseases: A Compendium
Scherer, P. E., & Hill, J. A. (2016) · Circulation Research · doi:10.1161/circresaha.116.308999 · Cited by 237 · see citing works
Epigenetics in diabetic nephropathy, immunity and metabolism
Keating, S. T., van Diepen, J. A., Riksen, N. P., & El-Osta, A. (2018) · Diabetologia · doi:10.1007/s00125-017-4490-1 · Cited by 82 · see citing works
Self-citationResveratrol improves sperm DNA quality and reproductive capacity in type 1 diabetes
Simas, J. N., Mendes, T. B., Fischer, L. W., Vendramini, V., & Miraglia, S. M. (2021) · Andrology · doi:10.1111/andr.12891 · Cited by 39 · see citing works
- Authors
- Keating, S. T., Plutzky, J., & El-Osta, A.
- Affiliations
- Brigham and Women's Hospital (US)
- From the Epigenetics in Human Health and Disease Laboratory (S.T.K., A.E.-O.) and Epigenomics Profiling Facility (A.E.-O.), Baker IDI Heart and Diabetes Institute, The Alfred Medical Research and Education Precinct, Melbourne, Victoria, Australia; Division of Cardiovascular Medicine, Brigham and Women’s Hospital, Harvard Medical School, Boston, MA (J.P.); Department of Pathology, The University of Melbourne, Victoria, Australia (A.E.-O.); and Central Clinical School, Department of Medicine, Monash...
- Venue
- Circulation Research
- Published
- 2016-05-27
- Volume
- 118
- Issue
- 11
- Pages
- 1706-1722
- ISSN
- 0009-7330 (ISSN-L)
- 1524-4571
- PMC
- PMC5593074
- OpenAlex
- W2401080925
- Cited by
- 139
- References
- 205
- Citations by year
- 2026: 7 · 2025: 12 · 2024: 17 · 2023: 9 · 2022: 12 · 2021: 13 · 2020: 16 · 2019: 14 · 2018: 19 · 2017: 16 · 2016: 4
- FWCI
- 9.18
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Circulation Research (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Minerva Access (University of Melbourne) (submittedVersion)
- Funders
- State Government of Victoria
- National Institutes of Health
- Medical Research Council
- National Health and Medical Research Council
- National Heart, Lung, and Blood Institute (R56HL125894, P01HL048743)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Diabetes, Cardiovascular Risks, and Lipoproteins
- Keywords
- epigenetics, diabetes mellitus, cardiovascular disease, atherosclerosis, diabetic vascular complications, chromatin modification, endothelial cells, vascular smooth muscle cells, immune cells, high glucose, reactive oxygen species, epigenetic drug targets, gene expression regulation
- MeSH terms
- Animals, Diabetes Mellitus, Diabetic Angiopathies, Humans, Chromatin Assembly and Disassembly, Epigenesis, Genetic
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
