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Roles and regulation of histone methylation in animal development
Open accessAbstract
Histone methylation can occur at various sites in histone proteins, primarily on lysine and arginine residues, and it can be governed by multiple positive and negative regulators, even at a single site, to either activate or repress transcription. It is now apparent that histone methylation is critical for almost all stages of development, and its proper regulation is essential for ensuring the coordinated expression of gene networks that govern pluripotency, body patterning and differentiation along appropriate lineages and organogenesis. Notably, developmental histone methylation is highly dynamic. Early embryonic systems display unique histone methylation patterns, prominently including the presence of bivalent (both gene-activating and gene-repressive) marks at lineage-specific genes that resolve to monovalent marks during differentiation, which ensures that appropriate genes are expressed in each tissue type. Studies of the effects of methylation on embryonic stem cell pluripotency and differentiation have helped to elucidate the developmental roles of histone methylation. It has been revealed that methylation and demethylation of both activating and repressive marks are essential for establishing embryonic and extra-embryonic lineages, for ensuring gene dosage compensation via genomic imprinting and for establishing body patterning via HOX gene regulation. Not surprisingly, aberrant methylation during embryogenesis can lead to defects in body patterning and in the development of specific organs. Human genetic disorders arising from mutations in histone methylation regulators have revealed their important roles in the developing skeletal and nervous systems, and they highlight the overlapping and unique roles of different patterns of methylation in ensuring proper development.
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“and (ii) some methyltransferases methylating multiple classes of macromolecule 20 , as described above.”
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1 retracted
Sarraf, S. A., & Stancheva, I. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.06.043 · Cited by 501
RetractedComprehensive Mapping of Long-Range Interactions Reveals Folding Principles of the Human Genome
Lieberman-Aiden, E., van Berkum, N. L., Williams, L., Imakaev, M., Ragoczy, T., Telling, A., Amit, I., Lajoie, B. R., Sabo, P. J., Dorschner, M. O., et al. (2009) · Science · doi:10.1126/science.1181369 · Cited by 8,898
The language of covalent histone modifications
Strahl, B. D., & Allis, C. D. (2000) · Nature · doi:10.1038/47412 · Cited by 8,679
High-Resolution Profiling of Histone Methylations in the Human Genome
Barski, A., Cuddapah, S., Cui, K., Roh, T.-Y., Schones, D. E., Wang, Z., Wei, G., Chepelev, I., & Zhao, K. (2007) · Cell · doi:10.1016/j.cell.2007.05.009 · Cited by 6,845
Topological domains in mammalian genomes identified by analysis of chromatin interactions
Dixon, J. R., Selvaraj, S., Yue, F., Kim, A., Li, Y., Shen, Y., Hu, M., Liu, J. S., & Ren, B. (2012) · Nature · doi:10.1038/nature11082 · Cited by 6,829
A bivalent chromatin structure marks key developmental genes in embryonic stem cells
Bernstein, B. E., Mikkelsen, T. S., Xie, X., Kamal, M., Huebert, D. J., Cuff, J., Fry, B., Meissner, A., Wernig, M., Plath, K., et al. (2006) · Cell · doi:10.1016/j.cell.2006.02.041 · Cited by 5,361
Genome-wide maps of chromatin state in pluripotent and lineage-committed cells
Mikkelsen, T. S., Ku, M., Jaffe, D. B., Issac, B., Lieberman, E., Giannoukos, G., Alvarez, P., Brockman, W., Kim, T.-K., Koche, R. P., et al. (2007) · Nature · doi:10.1038/nature06008 · Cited by 4,129
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
Self-citationA gene complex controlling segmentation in Drosophila
Lewis, E. B. (1978) · Nature · doi:10.1038/276565a0 · Cited by 3,813
Role of Histone H3 Lysine 27 Methylation in Polycomb-Group Silencing
Cao, R., Wang, L., Wang, H., Xia, L., Erdjument-Bromage, H., Tempst, P., Jones, R. S., & Zhang, Y. (2002) · Science · doi:10.1126/science.1076997 · Cited by 3,775
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
Epigenetics in human disease and prospects for epigenetic therapy
Egger, G., Liang, G., Aparicio, A., & Jones, P. A. (2004) · Nature · doi:10.1038/nature02625 · Cited by 3,232
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
Regulation of chromatin structure by site-specific histone H3 methyltransferases
Rea, S., Eisenhaber, F., O'Carroll, D., Strahl, B. D., Sun, Z.-W., Schmid, M., Opravil, S., Mechtler, K., Ponting, C. P., Allis, C. D., et al. (2000) · Nature · doi:10.1038/35020506 · Cited by 2,845
Synaptic, transcriptional and chromatin genes disrupted in autism
Study, T. D., De Rubeis, S., Autism, H. M. C. F., UK10K Consortium, The Autism Sequencing Consortium, He, X., Goldberg, A. P., Poultney, C. S., Samocha, K., Ercument Cicek, A., et al. (2014) · Nature · doi:10.1038/nature13772 · Cited by 2,746
Combinatorial patterns of histone acetylations and methylations in the human genome
Wang, Z., Zang, C., Rosenfeld, J. A., Schones, D. E., Barski, A., Cuddapah, S., Cui, K., Roh, T.-Y., Peng, W., Zhang, M. Q., et al. (2008) · Nature Genetics · doi:10.1038/ng.154 · Cited by 2,331
Control of Developmental Regulators by Polycomb in Human Embryonic Stem Cells
Lee, T. I., Jenner, R. G., Boyer, L. A., Guenther, M. G., Levine, S. S., Kumar, R., Chevalier, B. S., Johnstone, S. E., Cole, M. F., Isono, K., et al. (2006) · Cell · doi:10.1016/j.cell.2006.02.043 · Cited by 2,296
The diverse roles of DNA methylation in mammalian development and disease
Greenberg, M., & Bourc’his, D. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0159-6 · Cited by 2,272
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 2,244
LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription
Metzger, E., Wissmann, M., Yin, N., Müller, J. M., Schneider, R., Peters, A. H. F. M., Günther, T., Buettner, R., & Schüle, R. (2005) · Nature · doi:10.1038/nature04020 · Cited by 1,780
Loss of the Suv39h Histone Methyltransferases Impairs Mammalian Heterochromatin and Genome Stability
Peters, A. H. F. M., O'Carroll, D., Scherthan, H., Mechtler, K., Sauer, S., Schöfer, C., Weipoltshammer, K., Pagani, M., Lachner, M., Kohlmaier, A., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00542-6 · Cited by 1,766
DNMT3L connects unmethylated lysine 4 of histone H3 to de novo methylation of DNA
Ooi, S. K. T., Qiu, C., Bernstein, E., Li, K., Jia, D., Yang, Z., Erdjument‐Bromage, H., Tempst, P., Lin, S., Allis, C. D., et al. (2007) · Nature · doi:10.1038/nature05987 · Cited by 1,648
Kuzmichev, A., Nishioka, K., Erdjument-Bromage, H., Tempst, P., & Reinberg, D. (2002) · Genes & Development · doi:10.1101/gad.1035902 · Cited by 1,596
Genomic Maps and Comparative Analysis of Histone Modifications in Human and Mouse
Bernstein, B., Kamal, M., Lindblad‐Toh, K., Bekiranov, S., Bailey, D. K., Huebert, D. J., McMahon, S., Karlsson, E. K., Kulbokas, E. J., Gingeras, T., et al. (2005) · Cell · doi:10.1016/j.cell.2005.01.001 · Cited by 1,567
Histone Methyltransferase Activity of a Drosophila Polycomb Group Repressor Complex
Müller, J., Hart, C. M., Francis, N. J., Vargas, M. L., Sengupta, A. K., Wild, B., Miller, E., O’Connor, M. B., Kingston, R. E., & Simon, J. A. (2002) · Cell · doi:10.1016/s0092-8674(02)00976-5 · Cited by 1,553
Mutations affecting the pattern of the larval cuticle inDrosophila melanogaster
N�sslein-Volhard, C., Wieschaus, E. F., & Kluding, H. (1984) · Development Genes and Evolution · doi:10.1007/bf00848156 · Cited by 1,552
RAG-1 and RAG-2, Adjacent Genes That Synergistically Activate V(D)J Recombination
Oettinger, M. A., Schatz, D. G., Gorka, C., & Baltimore, D. (1990) · Science · doi:10.1126/science.2360047 · Cited by 1,506
Modification of Enhancer Chromatin: What, How, and Why?
Calo, E., & Wysocka, J. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.01.038 · Cited by 1,457
UTX and JMJD3 are histone H3K27 demethylases involved in HOX gene regulation and development
Agger, K., Cloos, P. A., Christensen, J. F., Pasini, D., Rose, S., Rappsilber, J., Issaeva, I., Canaani, E., Salcini, A. E., & Helin, K. (2007) · Nature · doi:10.1038/nature06145 · Cited by 1,392
Exome sequencing identifies MLL2 mutations as a cause of Kabuki syndrome
Ng, S. B. H., Bigham, A. W., Buckingham, K. J., Hannibal, M., McMillin, M. J., Gildersleeve, H. I. S., Beck, A. E., Tabor, H. K., Cooper, G. M., Mefford, H. C., et al. (2010) · Nature Genetics · doi:10.1038/ng.646 · Cited by 1,349
Tachibana, M., Sugimoto, K., Nozaki, M., Ueda, J., Ohta, T., Ohki, M., Fukuda, M., Takeda, N., Niida, H., Kato, H., et al. (2002) · Genes & Development · doi:10.1101/gad.989402 · Cited by 1,294
Lehnertz, B., Ueda, Y., Derijck, A. A. H. A., Braunschweig, U., Perez-Burgos, L., Kubicek, S., Chen, T., Li, E., Jenuwein, T., & Peters, A. H. F. M. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00432-9 · Cited by 1,289
Role of Histone H3 Lysine 27 Methylation in X Inactivation
Plath, K., Fang, J., Mlynarczyk‐Evans, S., Cao, R., Worringer, K. A., Wang, H., de la Cruz, C. C., Otte, A. P., Panning, B., & Zhang, Y. (2003) · Science · doi:10.1126/science.1084274 · Cited by 1,241
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 1,226
Regulation of Transcription by a Protein Methyltransferase
Chen, D., Ma, H., Hong, H., Koh, S. S., Huang, S., Schurter, B. T., Aswad, D. W., & Stallcup, M. R. (1999) · Science · doi:10.1126/science.284.5423.2174 · Cited by 1,214
Partitioning and Plasticity of Repressive Histone Methylation States in Mammalian Chromatin
Peters, A. H. F. M., Kubicek, S., Mechtler, K., O’Sullivan, R. J., Derijck, A. A. H. A., Perez-Burgos, L., Kohlmaier, A., Opravil, S., Tachibana, M., Shinkai, Y., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00477-5 · Cited by 1,208
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 1,075
Self-citationMLL Targets SET Domain Methyltransferase Activity to Hox Gene Promoters
Milne, T. A., Briggs, S. D., Brock, H. W., Martin, M. E., Gibbs, D. Y., Allis, C. D., & Hess, J. L. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00741-4 · Cited by 1,071
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 970
Self-citationSuz12 is essential for mouse development and for EZH2 histone methyltransferase activity
Pasini, D., Bracken, A. P., Jensen, M. R., Denchi, E. L., & Helin, K. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600402 · Cited by 963
The Polycomb-Group GeneEzh2 Is Required for Early Mouse Development
O’Carroll, D., Erhardt, S., Pagani, M., Barton, S. C., Surani, M. A., & Jenuwein, T. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.13.4330-4336.2001 · Cited by 908
Regulation of LSD1 Histone Demethylase Activity by Its Associated Factors
Shi, Y.-J., Matson, C., Lan, F., Iwase, S., Baba, T., & Shi, Y. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.08.027 · Cited by 906
Self-citationMethylation 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 897
Altered Hox expression and segmental identity in Mll-mutant mice
Yu, B., Hess, J. L., Horning, S. E., Brown, G. A. J., & Korsmeyer, S. J. (1995) · Nature · doi:10.1038/378505a0 · Cited by 872
Dot1p Modulates Silencing in Yeast by Methylation of the Nucleosome Core
van Leeuwen, F., Gafken, P. R., & Gottschling, D. E. (2002) · Cell · doi:10.1016/s0092-8674(02)00759-6 · Cited by 853
Rice, J. C., Briggs, S. D., Ueberheide, B. M., Barber, C. M., Shabanowitz, J., Hunt, D. F., Shinkai, Y., & Allis, C. D. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00479-9 · Cited by 849
Regulation of p53 activity through lysine methylation
Chuikov, S., Kurash, J. K., Wilson, J. R., Xiao, B., Justin, N., Ivanov, G. S., McKinney, K. M., Tempst, P., Prives, C. L., Gamblin, S. J., et al. (2004) · Nature · doi:10.1038/nature03117 · Cited by 846
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 844
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 808
Self-citationDistinct epigenomic landscapes of pluripotent and lineage-committed human cells
Hawkins, R. D., Hon, G. C., Lee, L. K., Ngo, Q., Lister, R., Pelizzola, M., Edsall, L. E., Kuan, S., Luu, Y., Klugman, S., et al. (2010) · Cell stem cell · doi:10.1016/j.stem.2010.03.018 · Cited by 806
Demethylation of H3K27 Regulates Polycomb Recruitment and H2A Ubiquitination
Lee, M. G., Villa, R., Trojer, P., Norman, J. A., Yan, K.-P., Reinberg, D., Croce, L. D., & Shiekhattar, R. (2007) · Science · doi:10.1126/science.1149042 · Cited by 789
Tachibana, M., Sugimoto, K., Fukushima, T., & Shinkai, Y. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101914200 · Cited by 784
van der Lugt, N. M. T., Domen, J., Linders, K., van ROON, M. A., Robanus-Maandag, E. C., Riele, H. T., van der Valk, M., Deschamps, J., Sofroniew, M. V., & van Lohuizen, M. (1994) · Genes & Development · doi:10.1101/gad.8.7.757 · Cited by 781
Methylation of histone H3 Lys 4 in coding regions of active genes
Bernstein, B., Humphrey, E. L., Erlich, R., Schneider, R., Bouman, P., Liu, J. S., Kouzarides, T., & Schreiber, S. L. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.082249499 · Cited by 778
The putative oncogene GASC1 demethylates tri- and dimethylated lysine 9 on histone H3
Cloos, P. A., Christensen, J., Agger, K., Maiolica, A., Rappsilber, J., Antal, T., Hansen, K. H., & Helin, K. (2006) · Nature · doi:10.1038/nature04837 · Cited by 756
Identification of JmjC domain-containing UTX and JMJD3 as histone H3 lysine 27 demethylases
Hong, S., Cho, Y., Yu, L., Yu, H., Veenstra, T. D., & Ge, K. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707292104 · Cited by 716
Whole-Genome Analysis of Histone H3 Lysine 4 and Lysine 27 Methylation in Human Embryonic Stem Cells
Pan, G., Tian, S., Nie, J., Yang, C., Ruotti, V., Wei, H., Jonsdottir, G. A., Stewart, R., & Thomson, J. A. (2007) · Cell Stem Cell · doi:10.1016/j.stem.2007.08.003 · Cited by 711
Allelic reprogramming of the histone modification H3K4me3 in early mammalian development
Zhang, B., Zheng, H., Huang, B., Li, W., Xiang, Y., Xu, P., Ming, J., Wu, X., Zhang, Y., Xu, Q., et al. (2016) · Nature · doi:10.1038/nature19361 · Cited by 703
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 699
Facultative Heterochromatin: Is There a Distinctive Molecular Signature?
Trojer, P., & Reinberg, D. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.09.011 · Cited by 686
Mutations affecting the pattern of the larval cuticle inDrosophila melanogaster
J�rgens, G., Wieschaus, E. F., N�sslein-Volhard, C., & Kluding, H. (1984) · Development Genes and Evolution · doi:10.1007/bf00848157 · Cited by 683
The regulation, functions and clinical relevance of arginine methylation
Guccione, E., & Richard, S. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0155-x · Cited by 662
The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36
Klose, R. J., Yamane, K., Bae, Y., Zhang, D., Erdjument‐Bromage, H., Tempst, P., Wong, J., & Zhang, Y. (2006) · Nature · doi:10.1038/nature04853 · Cited by 648
Cui, K., Zang, C., Roh, T., Schones, D. E., Childs, R. W., Peng, W., & Zhao, K. (2009) · Cell stem cell · doi:10.1016/j.stem.2008.11.011 · Cited by 646
Wen, B., Wu, H., Shinkai, Y., Irizarry, R. A., & Feinberg, A. P. (2009) · Nature Genetics · doi:10.1038/ng.297 · Cited by 634
Zhao, X. D., Han, X., Chew, J. L., Liu, J., Chiu, K. P., Choo, A. B. H., Orlov, Y. L., Sung, W.-K. K., Shahab, A., Kuznetsov, V. A., et al. (2007) · Cell stem cell · doi:10.1016/j.stem.2007.08.004 · Cited by 626
CpG islands influence chromatin structure via the CpG-binding protein Cfp1
Thomson, J. P., Skene, P. J., Selfridge, J., Clouaire, T., Guy, J., Webb, S., Kerr, A. R. W., Deaton, A., Andrews, R., James, K. D., et al. (2010) · Nature · doi:10.1038/nature08924 · Cited by 625
Enhancer decommissioning by LSD1 during embryonic stem cell differentiation
Whyte, W. A., Bilodeau, S., Orlando, D. A., Hoke, H. A., Frampton, G. M., Foster, C. T., Cowley, S. M., & Young, R. A. (2012) · Nature · doi:10.1038/nature10805 · Cited by 602
Step-wise methylation of histone H3K9 positions heterochromatin at the nuclear periphery
Towbin, B. D., González-Aguilera, C., Sack, R., Gaidatzis, D., Kalck, V., Meister, P., Askjaer, P., & Gasser, S. M. (2012) · Cell · doi:10.1016/j.cell.2012.06.051 · Cited by 597
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 595
A subset of p53-deficient embryos exhibit exencephaly
Sah, V. P., Attardi, L. D., Mulligan, G., Williams, B. O., Bronson, R. T., & Jacks, T. (1995) · Nature Genetics · doi:10.1038/ng0695-175 · Cited by 594
Histone arginine methylation regulates pluripotency in the early mouse embryo
Torres‐Padilla, M., Parfitt, D.-E., Kouzarides, T., & Zernicka‐Goetz, M. (2007) · Nature · doi:10.1038/nature05458 · Cited by 592
Opposing LSD1 complexes function in developmental gene activation and repression programmes
Wang, J., Scully, K. M., Zhu, X., Cai, L., Zhang, J., Préfontaine, G. G., Krones, A., Ohgi, K. A., Zhu, P., García-Bassets, I., et al. (2007) · Nature · doi:10.1038/nature05671 · Cited by 580
Nishioka, K., Chuikov, S., Sarma, K., Erdjument‐Bromage, H., Allis, C. D., Tempst, P., & Reinberg, D. (2002) · Genes & Development · doi:10.1101/gad.967202 · Cited by 579
Tschiersch, B., Hofmann, A., Krauss, V., Dorn, R., Korge, G., & Reuter, G. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06693.x · Cited by 567
Ang, Y.-S., Tsai, S., Lee, D., Monk, J. M., Su, J., Ratnakumar, K., Ding, J., Ge, Y., Darr, H., Chang, B., et al. (2011) · Cell · doi:10.1016/j.cell.2011.03.003 · Cited by 559
Mutations affecting the pattern of the larval cuticle inDrosophila melanogaster
Wieschaus, E. F., N�sslein-Volhard, C., & J�rgens, G. (1984) · Development Genes and Evolution · doi:10.1007/bf00848158 · Cited by 556
Genome-wide Chromatin State Transitions Associated with Developmental and Environmental Cues
Zhu, J., Adli, M., Zou, J., Verstappen, G., Coyne, M. J., Zhang, X., Durham, T., Miri, M., Deshpande, V., Jager, P. L. D., et al. (2013) · Cell · doi:10.1016/j.cell.2012.12.033 · Cited by 551
The roles of DNA, RNA and histone methylation in ageing and cancer
Michalak, E. M., Burr, M. L., Bannister, A. J., & Dawson, M. A. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0143-1 · Cited by 549
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 547
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 546
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 534
The Occurrence of iε-N-Methyl Lysine in Histones
Murray, K. (1964) · Biochemistry · doi:10.1021/bi00889a003 · Cited by 521
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
Molecular implementation and physiological roles for histone H3 lysine 4 (H3K4) methylation
Shilatifard, A. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.03.019 · Cited by 495
RAG2 PHD finger couples histone H3 lysine 4 trimethylation with V(D)J recombination
Matthews, A. G. W., Kuo, A. J., Ramón‐Maiques, S., Han, S., Glass, K. C., Ivanov, D., Gallardo, M., Carney, D., Cheung, P., Ciccone, D. N., et al. (2007) · Nature · doi:10.1038/nature06431 · Cited by 492
Self-citationPRMT1 Is the Predominant Type I Protein Arginine Methyltransferase in Mammalian Cells
Tang, J., Frankel, A., Cook, R. J., Kim, S., Paik, W. K., Williams, K. R., Clarke, S. G., & Herschman, H. R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.11.7723 · Cited by 486
Comprehensive Catalog of Currently Documented Histone ModificationsPreprint
Zhao, Y., & Garcia, B. A. (2015) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a025064 · Cited by 484
Maternal H3K27me3 controls DNA methylation-independent imprinting
Inoue, A., Jiang, L., Lu, F., Suzuki, T., & Zhang, Y. (2017) · Nature · doi:10.1038/nature23262 · Cited by 483
De novo DNA methylation promoted by G9a prevents reprogramming of embryonically silenced genes
Epsztejn‐Litman, S., Feldman, N., Abu-Remaileh, M., Shufaro, Y., Gerson, A., Ueda, J., Deplus, R., Fuks, F., Shinkai, Y., Cedar, H., et al. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1476 · Cited by 478
High-frequency developmental abnormalities in p53-deficient mice
Armstrong, J. F., Kaufman, M. H., Harrison, D. J., & Clarke, A. R. (1995) · Current Biology · doi:10.1016/s0960-9822(95)00183-7 · Cited by 473
Spatial Distribution of Di- and Tri-methyl Lysine 36 of Histone H3 at Active Genes
Bannister, A. J., Schneider, R., Myers, F. A., Thorne, A. W., Crane‐Robinson, C., & Kouzarides, T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500796200 · Cited by 459
Lin, W., Gary, J. D., Yang, M. C., Clarke, S. G., & Herschman, H. R. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.25.15034 · Cited by 455
Jmjd1a and Jmjd2c histone H3 Lys 9 demethylases regulate self-renewal in embryonic stem cells
Loh, Y.-H., Zhang, W., Chen, X., George, J., & Ng, H.-H. (2007) · Genes & Development · doi:10.1101/gad.1588207 · Cited by 443
Role of Jhdm2a in regulating metabolic gene expression and obesity resistance
Tateishi, K., Okada, Y., Kallin, E. M., & Zhang, Y. (2009) · Nature · doi:10.1038/nature07777 · Cited by 442
Hu, D., Gao, X., Morgan, M. A., Herz, H.-M., Smith, E. R., & Shilatifard, A. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01181-13 · Cited by 439
Resetting Epigenetic Memory by Reprogramming of Histone Modifications in Mammals
Zheng, H., Huang, B., Zhang, B., Xiang, Y., Du, Z., Xu, Q., Li, Y., Wang, Q., Ma, J., Xu, P., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.08.032 · Cited by 439
Recognition of unmethylated histone H3 lysine 4 links BHC80 to LSD1-mediated gene repression
Lan, F., Collins, R. E., Cegli, R. D., Alpatov, R., Horton, J. R., Shi, X., Gozani, O., Cheng, X., & Shi, Y. (2007) · Nature · doi:10.1038/nature06034 · Cited by 432
Self-citationA Transcriptional Switch Mediated by Cofactor Methylation
Xu, W., Chen, H.-W., Du, K., Asahara, H., Tini, M., Emerson, B. M., Montminy, M., & Evans, R. M. (2001) · Science · doi:10.1126/science.1065961 · Cited by 418
tudor, a gene required for assembly of the germ plasm in Drosophila melanogaster
Boswell, R. E. (1985) · Cell · doi:10.1016/0092-8674(85)90015-7 · Cited by 409
Saleque, S., Kim, J., Rooke, H. M., & Orkin, S. H. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.06.039 · Cited by 401
Histone H3-K9 Methyltransferase ESET Is Essential for Early Development
Dodge, J. E., Kang, Y., Beppu, H., Lei, H., & Li, E. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.6.2478-2486.2004 · Cited by 400
Chromatin remodelling factor Mll1 is essential for neurogenesis from postnatal neural stem cells
Lim, D. A., Huang, Y.-C., Swigut, T., Mirick, A. L., García‐Verdugo, J. M., Wysocka, J., Ernst, P., & Álvarez-Buylla, A. (2009) · Nature · doi:10.1038/nature07726 · Cited by 390
Horton, J. R., Upadhyay, A. K., Qi, H. H., Zhang, X., Shi, Y., & Cheng, X. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1753 · Cited by 389
Self-citationHistone demethylase JHDM2A is critical for Tnp1 and Prm1 transcription and spermatogenesis
Okada, Y., Scott, G. J., Ray, M. K., Mishina, Y. M., & Zhang, Y. (2007) · Nature · doi:10.1038/nature06236 · Cited by 388
Issaeva, I., Zonis, Y. A., Rozovskaia, T., Orlovsky, K., Croce, C. M., Nakamura, T., Mazo, A., Eisenbach, L., & Canaani, E. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01506-06 · Cited by 386
A histone H3 lysine 36 trimethyltransferase links Nkx2-5 to Wolf–Hirschhorn syndrome
Nimura, K., Ura, K., Shiratori, H., Ikawa, M., Okabe, M., Schwartz, R. J., & Kaneda, Y. (2009) · Nature · doi:10.1038/nature08086 · Cited by 379
Miller, S. A., Mohn, S. E., & Weinmann, A. S. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.028 · Cited by 373
Jensen, L. R., Amende, M., Gurok, U., Moser, B., Gimmel, V., Tzschach, A., Janecke, A. R., Tariverdian, G., Chelly, J., Fryns, J.-P., et al. (2005) · The American Journal of Human Genetics · doi:10.1086/427563 · Cited by 373
A gene product required for correct initiation of segmental determination in Drosophila
Struhl, G. (1981) · Nature · doi:10.1038/293036a0 · Cited by 367
Tee, W., Pardo, M., Theunissen, T. W., Yu, L., Choudhary, J. S., Hájková, P., & Surani, M. A. (2010) · Genes & Development · doi:10.1101/gad.606110 · Cited by 365
Ezhkova, E., Lien, W.-H., Stokes, N., Pasolli, H. A., Silva, J. M., & Fuchs, E. (2011) · Genes & Development · doi:10.1101/gad.2019811 · Cited by 357
Pawlak, M. R., Scherer, C., Chen, J., Roshon, M. J., & Ruley, H. E. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.13.4859-4869.2000 · Cited by 355
Chromatin analysis in human early development reveals epigenetic transition during ZGA
Wu, J., Xu, J., Liu, B., Yao, G., Wang, P., Lin, Z., Huang, B., Wang, X., Li, T., Shi, S., et al. (2018) · Nature · doi:10.1038/s41586-018-0080-8 · Cited by 351
LSD1 regulates the balance between self-renewal and differentiation in human embryonic stem cells
Adamo, A., Sesé, B., Boué, S., Castaño, J., Paramonov, I., Barrero, M. J., & Belmonte, J. C. I. (2011) · Nature Cell Biology · doi:10.1038/ncb2246 · Cited by 348
Imprinted X inactivation maintained by a mouse Polycomb group gene
Wang, J., Mager, J., Chen, Y., Schneider, E., Cross, J. C., Nagy, A., & Magnuson, T. (2001) · Nature Genetics · doi:10.1038/ng574 · Cited by 338
Unique and Independent Roles for MLL in Adult Hematopoietic Stem Cells and Progenitors
Jude, C. D., Climer, L. K., Xu, D., Artinger, E. L., Fisher, J. K., & Ernst, P. (2007) · Cell stem cell · doi:10.1016/j.stem.2007.05.019 · Cited by 329
Mutations in EZH2 Cause Weaver Syndrome
Gibson, W. T., Hood, R. L., Zhan, S. H., Bulman, D. E., Fejes, A. P., Moore, R. A., Mungall, A. J. J., Eydoux, P., Babul‐Hirji, R., An, J., et al. (2011) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2011.11.018 · Cited by 328
Proteome-wide analysis of arginine monomethylation reveals widespread occurrence in human cells
Buch-Larsen, S. C., Sylvestersen, K. B., Mund, A., Lyon, D. B., Mullari, M., Madsen, M. V., Daniel, J. A., Jensen, L. J., & Nielsen, M. L. (2016) · Science Signaling · doi:10.1126/scisignal.aaf7329 · Cited by 326
Molecular Regulation of H3K4 Trimethylation by Wdr82, a Component of Human Set1/COMPASS
Wu, M., Wang, P. F., Lee, J. S., Martin‐Brown, S., Florens, L. A., Washburn, M. P., & Shilatifard, A. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00976-08 · Cited by 324
UTX and UTY Demonstrate Histone Demethylase-Independent Function in Mouse Embryonic Development
Shpargel, K. B., Sengoku, T., Yokoyama, S., & Magnuson, T. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002964 · Cited by 320
Deciphering arginine methylation: Tudor tells the tale
Chen, C., Nott, T. J., Jin, J., & Pawson, T. J. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3185 · Cited by 307
Histone H4K20/H3K9 demethylase PHF8 regulates zebrafish brain and craniofacial development
Qi, H. H., Sarkissian, M., Hu, G., Wang, Z., Bhattacharjee, A., Gordon, D. B., Gonzales, M., Lan, F., Ongusaha, P. P., Huarte, M., et al. (2010) · Nature · doi:10.1038/nature09261 · Cited by 305
Self-citationSimon, J. A., Chiang, A., & Bender, W. W. (1992) · Development · doi:10.1242/dev.114.2.493 · Cited by 304
PRC2 directly methylates GATA4 and represses its transcriptional activityPreprint
He, A., Shen, X., Ma, Q., Cao, J., von Gise, A., Zhou, P., Wang, G., Márquez, V. E., Orkin, S. H., & Pu, W. T. (2012) · Genes & Development · doi:10.1101/gad.173930.111 · Cited by 304
Bezzi, M., Teo, S. X., Müller, J., Mok, W. C., Sahu, S. K., Vardy, L. A., Bonday, Z., & Guccione, E. (2013) · Genes & Development · doi:10.1101/gad.219899.113 · Cited by 302
Yu, B., Hanson, R. D., Hess, J. L., Horning, S. E., & Korsmeyer, S. J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.18.10632 · Cited by 302
Douglas, J. B., Hanks, S., Temple, I. K., Davies, S. J., Murray, A., Upadhyaya, M., Tomkins, S. E., Hughes, H. E., Cole, R. P. T., & Rahman, N. (2003) · The American Journal of Human Genetics · doi:10.1086/345647 · Cited by 301
A Histone Mutant Reproduces the Phenotype Caused by Loss of Histone-Modifying Factor Polycomb
Pengelly, A. R., Copur, Ö., Jäckle, H., Herzig, A., & Müller, J. (2013) · Science · doi:10.1126/science.1231382 · Cited by 297
Denissov, S., Hofemeister, H., Marks, H., Kranz, A., Ciotta, G., Singh, S., Anastassiadis, K., Stunnenberg, H. G., & Stewart, A. F. (2014) · Development · doi:10.1242/dev.102681 · Cited by 297
The eed mutation disrupts anterior mesoderm production in mice
Faust, C. J., Schumacher, A., Holdener, B. C., & Magnuson, T. (1995) · Development · doi:10.1242/dev.121.2.273 · Cited by 295
Multiple epigenetic maintenance factors implicated by the loss of Mll2 in mouse development
Glaser, S. P., Schaft, J., Lubitz, S., Vintersten, K., van der Hoeven, F., Tufteland, K. R., Aasland, R., Anastassiadis, K., Ang, S., & Stewart, A. F. (2006) · Development · doi:10.1242/dev.02302 · Cited by 294
Yadav, N., Lee, J. H., Kim, J., Shen, J., Hu, M. C. ‐., Aldaz, C. M., & Bedford, M. T. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1232272100 · Cited by 288
Mll Has a Critical Role in Fetal and Adult Hematopoietic Stem Cell Self-Renewal
McMahon, K. A., Hiew, S., Hadjur, S., Veiga‐Fernandes, H., Menzel, U., Price, A. J., Kioussis, D., Williams, O., & Brady, H. J. M. (2007) · Cell stem cell · doi:10.1016/j.stem.2007.07.002 · Cited by 286
De Novo Mutations in MLL Cause Wiedemann-Steiner Syndrome
Jones, W. D., Dafou, D., McEntagart, M., Woollard, W. J., Elmslie, F., Holder‐Espinasse, M., Irving, M. D., Saggar, A. K., Smithson, S., Trembath, R. C., et al. (2012) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2012.06.008 · Cited by 283
Altered distributions of Ultrabithorax transcripts in extra sex combs mutant embryos of Drosophila.
Struhl, G., & Akam, M. E. (1985) · The EMBO Journal · doi:10.1002/j.1460-2075.1985.tb04075.x · Cited by 281
Yang, L., Xia, L., Wu, D. Y., Wang, H., Chansky, H. A., Schubach, W. H., Hickstein, D. D., & Zhang, Y. (2002) · Oncogene · doi:10.1038/sj.onc.1204998 · Cited by 274
Histone Lysine Methylases and Demethylases in the Landscape of Human Developmental Disorders
Faùndes, V., Newman, W. G., Bernardini, L., Canham, N. L. E., Clayton‐Smith, J., Dallapiccola, B., Davies, S. J., Demos, M. K., Goldman, A. P., Gill, H., et al. (2017) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2017.11.013 · Cited by 274
MLL2 Is Required in Oocytes for Bulk Histone 3 Lysine 4 Trimethylation and Transcriptional Silencing
Andreu‐Vieyra, C., Chen, R., Agno, J. E., Glaser, S. P., Anastassiadis, K., Stewart, A. F., & Matzuk, M. M. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000453 · Cited by 272
Klymenko, T., & Müller, J. (2004) · EMBO Reports · doi:10.1038/sj.embor.7400111 · Cited by 270
Kerenyi, M. A., Shao, Z., Hsu, Y., Guo, G., Luc, S., O’Brien, K., Fujiwara, Y., Peng, C., Nguyen, M., & Orkin, S. H. (2013) · eLife · doi:10.7554/elife.00633 · Cited by 267
Definitive Hematopoiesis Requires the Mixed-Lineage Leukemia Gene
Ernst, P., Fisher, J. K., Avery, W., Wade, S., Foy, D. S., & Korsmeyer, S. J. (2004) · Developmental Cell · doi:10.1016/s1534-5807(04)00061-9 · Cited by 265
Disruption of an EHMT1-Associated Chromatin-Modification Module Causes Intellectual Disability
Kleefstra, T., Kramer, J. M., Neveling, K., Willemsen, M. H., Koemans, T. S., Vissers, L. E. L. M., Wissink-Lindhout, W. M., Fencková, M., van den Akker, W. M. R., Kasri, N. N., et al. (2012) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2012.05.003 · Cited by 264
Lee, S., Lee, J. W., & Lee, S. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.11.009 · Cited by 260
Epigenetic Regulation of Mouse Sex Determination by the Histone Demethylase Jmjd1a
Kuroki, S., Matoba, S., Akiyoshi, M., Matsumura, Y., Miyachi, H., Mise, N., Abe, K., Ogura, A., Wilhelm, D., Koopman, P. A., et al. (2013) · Science · doi:10.1126/science.1239864 · Cited by 259
Epigenetic Temporal Control of Mouse Hox Genes in Vivo
Soshnikova, N. V., & Duboule, D. (2009) · Science · doi:10.1126/science.1171468 · Cited by 257
Gene-Specific Modulation of TAF10 Function by SET9-Mediated Methylation
Kouskouti, A., Scheer, E., Staub, A., Tora, L., & Talianidis, I. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00182-0 · Cited by 255
Defects in Yolk Sac Hematopoiesis in Mll-Null Embryos
Hess, J. L., Yu, B., Li, B., Hanson, R., & Korsmeyer, S. J. (1997) · Blood · doi:10.1182/blood.v90.5.1799 · Cited by 254
Functional Interplay between Histone Demethylase and Deacetylase Enzymes
Lee, M. G., Wynder, C., Bochar, D. A., Hakimi, M., Cooch, N. S., & Shiekhattar, R. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00723-06 · Cited by 252
Zurita‐Lopez, C. I., Sandberg, T. E., Kelly, R. L., & Clarke, S. G. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.336271 · Cited by 249
Wang, S., Tang, Z., Chen, C.-W. D., Shimada, M., Koche, R. P., Wang, L.-H., Nakadai, T., Chramiec, A. G., Krivtsov, A. V., Armstrong, S. A., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.06.028 · Cited by 249
Spatially Regulated Expression of Homeotic Genes in Drosophila
Harding, K. W., Wedeen, C. J., McGinnis, W. J., & Levine, M. (1985) · Science · doi:10.1126/science.3898362 · Cited by 245
Mutations in the histone methyltransferase gene KMT2B cause complex early-onset dystonia
Meyer, E., Study, D. D. D., Carss, K., Rankin, J., Nichols, J. M. E., Grozeva, D., Joseph, A. P., Mencacci, N. E., Papandreou, A., Ng, J., et al. (2016) · Nature Genetics · doi:10.1038/ng.3740 · Cited by 245
Growth Disturbance in Fetal Liver Hematopoiesis of Mll-Mutant Mice
Yagi, H., Deguchi, K., Aono, A., et al. (1998) · Blood · doi:10.1182/blood.v92.1.108.413k11_108_117 · Cited by 240
H3K9me3-heterochromatin loss at protein-coding genes enables developmental lineage specification
Nicetto, D., Donahue, G., Jain, T., Peng, T., Sidoli, S., Sheng, L., Montavon, T., Becker, J. S., Grindheim, J. M., Blahnik, K. R., et al. (2019) · Science · doi:10.1126/science.aau0583 · Cited by 240
Role of the Polycomb Repressive Complex 2 (PRC2) in Transcriptional Regulation and CancerPreprint
Laugesen, A., Højfeldt, J. W., & Helin, K. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026575 · Cited by 225
PHF8 activates transcription of rRNA genes through H3K4me3 binding and H3K9me1/2 demethylation
Feng, W., Yonezawa, M., Ye, J., Jenuwein, T., & Grummt, I. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1778 · Cited by 224
GFI1 proteins orchestrate the emergence of haematopoietic stem cells through recruitment of LSD1
Thambyrajah, R., Mazan, M. M., Patel, R., Moignard, V., Stefańska, M., Marinopoulou, E., Li, Y., Lancrin, C., Clapes, T., Möröy, T., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3276 · Cited by 219
Molecular basis of histone H3K36me3 recognition by the PWWP domain of Brpf1
Vezzoli, A., Bonadies, N., Allen, M. D., Freund, S. M. V., Santiveri, C. M., Kvinlaug, B. T., Huntly, B. J. P., Göttgens, B., & Bycroft, M. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1797 · Cited by 218
Mutations in PHF8 are associated with X linked mental retardation and cleft lip/cleft palate
Laumonnier, F., Holbert, S., Ronce, N., Faravelli, F., Lenzner, S., Schwartz, C. E., Lespinasse, J., Esch, H. V., Lacombe, D., Goizet, C., et al. (2005) · Journal of Medical Genetics · doi:10.1136/jmg.2004.029439 · Cited by 218
Prepatterning of Developmental Gene Expression by Modified Histones before Zygotic Genome Activation
Lindeman, L. C., Andersen, I. S., Reiner, A. H., Li, N., Aanes, H., Østrup, O., Winata, C. L., Mathavan, S., Müller, F., Aleström, P., et al. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.10.008 · Cited by 213
Ramón‐Maiques, S., Kuo, A. J., Carney, D., Matthews, A. G. W., Oettinger, M. A., Gozani, O., & Yang, W. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709170104 · Cited by 211
Sprüssel, A., Schulte, J. H., Weber, S., Necke, M., Händschke, K., Thor, T., Pajtler, K. W., Schramm, A., König, K., Diehl, L., et al. (2012) · Leukemia · doi:10.1038/leu.2012.157 · Cited by 203
The Role of Nuclear Receptor–Binding SET Domain Family Histone Lysine Methyltransferases in CancerPreprint
Bennett, R. L., Swaroop, A., Troche, C., & Licht, J. D. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026708 · Cited by 203
Kleefstra, T., Smidt, M. P., Banning, M. J. G., Oudakker, A. R., Esch, H. V., de Brouwer, A. P. M., Nillesen, W., Sistermans, E. A., Hamel, B. C. J., de Bruijn, D., et al. (2005) · Journal of Medical Genetics · doi:10.1136/jmg.2004.028464 · Cited by 201
Lysine-Specific Demethylase 1 Regulates the Embryonic Transcriptome and CoREST Stability
Foster, C. T., Dovey, O. M., Lezina, L., Luo, J., Gant, T. W., Barlev, N. A., Bradley, A., & Cowley, S. M. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00521-10 · Cited by 198
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
Faust, C. J., Lawson, K. A., Schork, N. J., Thiel, B., & Magnuson, T. (1998) · Development · doi:10.1242/dev.125.22.4495 · Cited by 194
Miranda, T. B., Miranda, M., Frankel, A., & Clarke, S. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312904200 · Cited by 194
Spectrum of MLL2 (ALR) mutations in 110 cases of Kabuki syndrome
Hannibal, M., Buckingham, K. J., Ng, S. B. H., Ming, J. E., Beck, A. E., McMillin, M. J., Gildersleeve, H. I. S., Bigham, A. W., Tabor, H. K., Mefford, H. C., et al. (2011) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.34074 · Cited by 194
Bledau, A. S., Schmidt, K., Neumann, K., Hill, U., Ciotta, G., Gupta, A. K., Torres, D. C., Fu, J., Kranz, A., Stewart, A. F., et al. (2014) · Development · doi:10.1242/dev.098152 · Cited by 192
Dacwag, C. S., Ohkawa, Y., Pal, S., Sif, S., & Imbalzano, A. N. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01528-06 · Cited by 191
Obesity and metabolic syndrome in histone demethylase JHDM2a‐deficient mice
Inagaki, T., Tachibana, M., Magoori, K., Kudo, H., Tanaka, T., Okamura, M., Naito, M., Kodama, T., Shinkai, Y., & Sakai, J. (2009) · Genes to Cells · doi:10.1111/j.1365-2443.2009.01326.x · Cited by 183
Glaser, S. P., Lubitz, S., Loveland, K. L., Ohbo, K., Robb, L., Schwenk, F., Seibler, J., Roellig, D., Kranz, A., Anastassiadis, K., et al. (2009) · Epigenetics & Chromatin · doi:10.1186/1756-8935-2-5 · Cited by 176
Interrogating the Function of Metazoan Histones using Engineered Gene Clusters
McKay, D. J., Klusza, S., Penke, T. J. R., Meers, M. P., Curry, K. P., McDaniel, S. L., Malek, P. Y., Cooper, S. W., Tatomer, D. C., Lieb, J. D., et al. (2015) · Developmental Cell · doi:10.1016/j.devcel.2014.12.025 · Cited by 173
Arensbergen, J., García-Hurtado, J., Moran, I., Maestro, M. A., Xu, X., de Casteele, M. V., Skoudy, A. L., Palassini, M., Heimberg, H., & Ferrer, J. (2010) · Genome Research · doi:10.1101/gr.101709.109 · Cited by 167
Byrd, K. N., & Shearn, A. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1933593100 · Cited by 159
study, T. D., Akawi, N. A., McRae, J. F., Ansari, M., Balasubramanian, M., Blyth, M., Brady, A. F., Clayton, S., Cole, T. R. P., Deshpande, C., et al. (2015) · Nature Genetics · doi:10.1038/ng.3410 · Cited by 158
Ingham, P. W., & Whittle, R. (1980) · Molecular and General Genetics MGG · doi:10.1007/bf00271751 · Cited by 155
Breaking Colinearity in the Mouse HoxD Complex
Kondo, T., & Duboule, D. (1999) · Cell · doi:10.1016/s0092-8674(00)80749-7 · Cited by 149
Genomic imprinting of Xist by maternal H3K27me3Preprint
Inoue, A., Jiang, L., Lu, F., & Zhang, Y. (2017) · Genes & Development · doi:10.1101/gad.304113.117 · Cited by 149
Tudor domain proteins in development
Pek, J. W., Anand, A., & Kai, T. (2012) · Development · doi:10.1242/dev.073304 · Cited by 148
CARM1 and Paraspeckles Regulate Pre-implantation Mouse Embryo Development
Hupalowska, A., Jędrusik, A., Zhu, M., Bedford, M. T., Glover, D. M., & Zernicka‐Goetz, M. (2018) · Cell · doi:10.1016/j.cell.2018.11.027 · Cited by 145
Jiang, W., Wang, J., & Zhang, Y. (2012) · Cell Research · doi:10.1038/cr.2012.119 · Cited by 142
MLL4 Is Required to Maintain Broad H3K4me3 Peaks and Super-Enhancers at Tumor Suppressor Genes
Dhar, S. S., Zhao, D., Lin, T., Gu, B., Pal, K., Wu, S. J., Alam, H., Lv, J., Yun, K., Gopalakrishnan, V., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.04.028 · Cited by 142
Global mapping of CARM1 substrates defines enzyme specificity and substrate recognition
Shishkova, E., Zeng, H., Liu, F., Kwiecien, N. W., Hebert, A. S., Coon, J. J., & Xu, W. (2017) · Nature Communications · doi:10.1038/ncomms15571 · Cited by 141
Ugarte, F., Sousae, R., Cinquin, B. P., Martin, E. W., Krietsch, J., Sanchez, G., Inman, M., Tsang, H., Warr, M. R., Passegue, E. A., et al. (2015) · Stem Cell Reports · doi:10.1016/j.stemcr.2015.09.009 · Cited by 140
KMT2D regulates specific programs in heart development via histone H3 lysine 4 di-methylation
Ang, S., Uebersohn, A., Spencer, C. I., Huang, Y., Lee, J., Ge, K., & Bruneau, B. G. (2016) · Development · doi:10.1242/dev.132688 · Cited by 140
Park, D. H., Hong, S. J., Salinas, R. D., Liu, S. J., Sun, S. W., Sgualdino, J., Testa, G., Matzuk, M. M., Iwamori, N., & Lim, D. A. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.07.060 · Cited by 139
Ancelin, K., Syx, L., Borensztein, M., Ranisavljevic, N., Vassilev, I., Briseño-Roa, L., Liu, T., Metzger, E., Servant, N., Barillot, E., et al. (2016) · eLife · doi:10.7554/elife.08851 · Cited by 139
The Polycomb-group homolog Bmi-1 is a regulator of murine Hox gene expression
van der Lugt, N. M. T., Alkema, M. J., Berns, A. J. M., & Deschamps, J. (1996) · Mechanisms of Development · doi:10.1016/s0925-4773(96)00570-9 · Cited by 134
Spectrum of NSD1 mutations in Sotos and Weaver syndromes
Rio, M., Clech, L., Amiel, J., Faivre, L. O., Lyonnet, S., Merrer, M. F. L., Odent, S., Lacombe, D., Edery, P., Brauner, R., et al. (2003) · Journal of Medical Genetics · doi:10.1136/jmg.40.6.436 · Cited by 134
Qiu, Y., Liu, L., Zhao, C., Han, C., Li, F., Zhang, J., Wang, Y., Li, G., Mei, Y., Wu, M., et al. (2012) · Genes & Development · doi:10.1101/gad.188359.112 · Cited by 134
Self-citationIwase, S., Brookes, E., Agarwal, S., Badeaux, A. I., Ito, H., Vallianatos, C. N., Tomassy, G. S., Kasza, T., Lin, G. R., Thompson, A., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2015.12.091 · Cited by 132
Self-citationLaue, K., Daujat, S., Crump, J. G., Plaster, N. M., Roehl, H. H., Kimmel, C. B., Schneider, R., & Hammerschmidt, M. (2008) · Development · doi:10.1242/dev.017160 · Cited by 130
Inoue, A., Chen, Z., Yin, Q., & Zhang, Y. (2018) · Genes & Development · doi:10.1101/gad.318675.118 · Cited by 130
Antagonism between DNA and H3K27 Methylation at the Imprinted Rasgrf1 Locus
Lindroth, A. M., Park, Y. J., McLean, C. M., Dokshin, G. A., Persson, J., Herman, H., Pasini, D., Miró, X., Donohoe, M. E., Lee, J. T., et al. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000145 · Cited by 127
Ablation of PRMT6 reveals a role as a negative transcriptional regulator of the p53 tumor suppressor
Neault, M., Mallette, F. A., Vogel, G., Michaud‐Levesque, J., & Richard, S. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks764 · Cited by 126
CARM1 is Required in Embryonic Stem Cells to Maintain Pluripotency and Resist Differentiation
Wu, Q., Bruce, A. W., Jędrusik, A., Ellis, P. D., Andrews, R., Langford, C. F., Glover, D. M., & Zernicka‐Goetz, M. (2009) · Stem Cells · doi:10.1002/stem.131 · Cited by 123
Protein Interfaces in Signaling Regulated by Arginine Methylation
Boisvert, F., Chénard, C. A., & Richard, S. (2005) · Science s STKE · doi:10.1126/stke.2712005re2 · Cited by 122
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Metadata
- Authors
- Jambhekar, A., Dhall, A., & Shi, Y.
- Affiliations
- Boston Children's Hospital (US)
- Corresponding author
- Jambhekar, Ashwini
- Shi, Yang
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2019-07-02
- Volume
- 20
- Issue
- 10
- Pages
- 625-641
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- PMC
- PMC6774358
- OpenAlex
- W2955543783
- Cited by
- 556
- References
- 271
- Citations by year
- 2026: 43 · 2025: 81 · 2024: 113 · 2023: 93 · 2022: 90 · 2021: 80 · 2020: 52 · 2019: 4
- FWCI
- 4.99
- Type
- journal article
- Language
- en
- Update notices
- correction (2019-11-07)
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- American Cancer Society
- Constellation Pharmaceuticals
- National Institute of Mental Health (R01MH096066)
- National Cancer Institute (R35CA210104)
- National Institute of General Medical Sciences (R01GM117264)
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
- Keywords
- histone methylation, animal development, lysine methylation, arginine methylation, transcriptional regulation, pluripotency, embryonic stem cells, lineage differentiation, genomic imprinting, gene dosage compensation, body patterning, Hox genes, organogenesis, histone demethylation, developmental disorders, skeletal development, brain development
- MeSH terms
- Animals, Cell Differentiation, Histones, Humans, Methylation, Protein Processing, Post-Translational, Gene Expression Regulation, Developmental, Body Patterning, Pluripotent Stem Cells, Embryonic Development
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