Methylation of lysine 4 on histone H3: intricacy of writing and reading a single epigenetic mark
Open accessAbstract
Cells employ elaborate mechanisms to introduce structural and chemical variation into chromatin. Here, we focus on one such element of variation: methylation of lysine 4 in histone H3 (H3K4). We assess a growing body of literature, including treatment of how the mark is established, the patterns of methylation, and the functional consequences of this epigenetic signature. We discuss structural aspects of the H3K4 methyl recognition by the downstream effectors and propose a distinction between sequence-specific recruitment mechanisms and stabilization on chromatin through methyl-lysine recognition. Finally, we hypothesize how the unique properties of the polyvalent chromatin fiber and associated effectors may amplify small differences in methyl-lysine recognition, simultaneously allowing for a dynamic chromatin architecture.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
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?
Bivalent chromatin dynamics accompanies early mESC lineage commitment.
“Moreover, bivalent chromatin dynamics accompanies early mESC lineage commitment (Ruthenburg et al., 2007; Schwartz and Pirrotta 2007; Liu et al., 2016).”
From METTL3 uncouples chromatin accessibility from transcription during retinal development (2025) · cites this paper as Ruthenburg et al., 2007
Cites
2 retracted
Histone methylation by the Drosophila epigenetic transcriptional regulator Ash1
Beisel, C., Imhof, A., Greene, J., Kremmer, E., & Sauer, F. (2002) · Nature · doi:10.1038/nature01126 · Cited by 310 · see citing works
RetractedNoncoding RNAs of Trithorax Response Elements Recruit Drosophila Ash1 to Ultrabithorax
Sánchez-Elsner, T., Gou, D., Kremmer, E., & Sauer, F. (2006) · Science · doi:10.1126/science.1117705 · Cited by 233 · see citing works
RetractedThe language of covalent histone modifications
Strahl, B. D., & Allis, C. D. (2000) · Nature · doi:10.1038/47412 · Cited by 8,679 · see citing works
Self-citationJennifer, C., & Dougherty, D. A. (1997) · Chemical Reviews · doi:10.1021/cr9603744 · Cited by 3,487 · see citing works
Application of a Theory of Enzyme Specificity to Protein Synthesis.
Koshland, D. (1958) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.44.2.98 · Cited by 2,140 · see citing works
Active Genes Are Tri-Methylated at K4 of Histone H3
Santos-Rosa, H., Schneider, R., Bannister, A. J., Sherriff, J., Bernstein, B. E., Emre, N. C. T., Schreiber, S. L., Mellor, J., & Kouzarides, T. (2002) · Nature · doi:10.1038/nature01080 · Cited by 2,138 · see citing works
The diverse functions of histone lysine methylation
Martin, C., & Zhang, Y. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1761 · Cited by 2,066 · see citing works
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 1,509 · see citing works
Genome-wide Map of Nucleosome Acetylation and Methylation in Yeast
Pokholok, D., Harbison, C. T., Levine, S. S., Cole, M. F., Hannett, N. M., Lee, T. I., Bell, G. W., Walker, K., Rolfe, A., Herbolsheimer, E., et al. (2005) · Cell · doi:10.1016/j.cell.2005.06.026 · Cited by 1,433 · see citing works
Joazeiro, C. A. P., & Weissman, A. M. (2000) · Cell · doi:10.1016/s0092-8674(00)00077-5 · Cited by 1,249 · 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
Self-citationShilatifard, A. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142422 · Cited by 1,099 · see citing works
Ng, H., Robert, F., Young, R. A., & Struhl, K. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00092-3 · Cited by 1,097 · see citing works
MLL 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 1,051 · see citing works
Self-citationFacilitated Target Location in Biological Systems
von Hippel, P. H., & Berg, O. G. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84994-3 · Cited by 1,032 · 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
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 · see citing works
Structure of HP1 Chromodomain Bound to a Lysine 9-Methylated Histone H3 Tail
Jacobs, S. A., & Khorasanizadeh, S. (2002) · Science · doi:10.1126/science.1069473 · Cited by 834 · see citing works
Wysocka, J., Swigut, T., Milne, T. A., Dou, Y., Zhang, X., Burlingame, A. L., Roeder, R. G., Brivanlou, A. H., & Allis, C. D. (2005) · Cell · doi:10.1016/j.cell.2005.03.036 · Cited by 820 · see citing works
Self-citationMolecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF
Li, H., Ilin, S., Wang, W., Duncan, E. M., Wysocka, J., Allis, C. D., & Patel, D. J. (2006) · Nature · doi:10.1038/nature04802 · Cited by 816 · see citing works
Self-citationSchübeler, D., MacAlpine, D. M., Scalzo, D., Wirbelauer, C., Kooperberg, C. L., van Leeuwen, F., Gottschling, D. E., O’Neill, L. P., Turner, B. M., Delrow, J. J., et al. (2004) · Genes & Development · doi:10.1101/gad.1198204 · Cited by 795 · see citing works
Histone H3 lysine 4 methylation patterns in higher eukaryotic genes
Schneider, R., Bannister, A. J., Myers, F. A., Thorne, A. W., Crane‐Robinson, C., & Kouzarides, T. (2003) · Nature Cell Biology · doi:10.1038/ncb1076 · Cited by 792 · see citing works
The SET-domain protein superfamily: protein lysine methyltransferases.
Dillon, S. C., Zhang, X. Y., Trievel, R. C., & Cheng, X. (2005) · Genome biology · doi:10.1186/gb-2005-6-8-227 · Cited by 784 · 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
Self-citationSMYD3 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
Dynamic Regulation of Histone Lysine Methylation by Demethylases
Shi, Y., & Whetstine, J. R. (2007) · Molecular Cell · doi:10.1016/j.molcel.2006.12.010 · Cited by 710 · see citing works
Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2
Peña, P. V., Davrazou, F., Shi, X., Walter, K. L., Verkhusha, V. V., Gozani, O., Zhao, R., & Kutateladze, T. G. (2006) · Nature · doi:10.1038/nature04814 · Cited by 685 · see citing works
Protein Dynamics: Implications for Nuclear Architecture and Gene Expression
Misteli, T. (2001) · Science · doi:10.1126/science.291.5505.843 · Cited by 668 · see citing works
Dou, Y., Milne, T. A., Tackett, A. J., Smith, E. R., Fukuda, A., Wysocka, J., Allis, C. D., Chait, B. T., Hess, J. L., & Roeder, R. G. (2005) · Cell · doi:10.1016/j.cell.2005.04.031 · Cited by 665 · see citing works
Self-citationReading protein modifications with interaction domains
Seet, B. T., Đikić, I., Zhou, M., & Pawson, T. J. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1960 · Cited by 662 · see citing works
Yokoyama, A., Wang, Z., Wysocka, J., Sanyal, M., Aufiero, D. J., Kitabayashi, I., Herr, W., & Cleary, M. L. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.13.5639-5649.2004 · Cited by 661 · see citing works
Self-citationDoyon, Y., Cayrou, C., Ullah, M., Landry, A.-J., Côté, V., Selleck, W., Lane, W. S., Tan, S., Yang, X., & Côté, J. (2006) · Molecular Cell · doi:10.1016/j.molcel.2005.12.007 · Cited by 656 · see citing works
Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9
Nielsen, P. R., Nietlispach, D., Mott, H. R., Callaghan, J., Bannister, A. J., Kouzarides, T., Murzin, A. G., Murzina, N. V., & Laue, E. D. (2002) · Nature · doi:10.1038/nature722 · Cited by 656 · see citing works
Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27Preprint
Min, J., Zhang, Y., & Xu, R.-M. (2003) · Genes & Development · doi:10.1101/gad.269603 · Cited by 656 · see citing works
Menin Associates with a Trithorax Family Histone Methyltransferase Complex and with the Hoxc8 Locus
Hughes, C. M., Rozenblatt–Rosen, O., Milne, T. A., Copeland, T. D., Levine, S. S., Lee, J. C., Hayes, D. N., Shanmugam, K. S., Bhattacharjee, A., Biondi, C., et al. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00081-4 · Cited by 645 · see citing works
Chambeyron, S., & Bickmore, W. A. (2004) · Genes & Development · doi:10.1101/gad.292104 · Cited by 618 · see citing works
Briggs, S. D., Bryk, M., Strahl, B. D., Cheung, W. L., Davie, J. K., Dent, S., Winston, F., & Allis, C. D. (2001) · Genes & Development · doi:10.1101/gad.940201 · Cited by 596 · see citing works
Self-citationRoguev, A., Schaft, D., Shevchenko, A., Pijnappel, W. W. M. P., Wilm, M. S., Aasland, R., & Stewart, A. F. (2001) · The EMBO Journal · doi:10.1093/emboj/20.24.7137 · Cited by 594 · 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
Self-citationSolute and macromolecule diffusion in cellular aqueous compartments
Verkman, A. S. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)02003-5 · Cited by 567 · 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
Joshi, A., & Struhl, K. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.11.021 · 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
Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation
Pray-Grant, M. G., Daniel, J. A., Schieltz, D. M., Yates, J. R., & Grant, P. A. (2005) · Nature · doi:10.1038/nature03242 · Cited by 516 · see citing works
Tudor, MBT and chromo domains gauge the degree of lysine methylation
Kim, J., Daniel, J. A., Espejo, A. B., Lake, A., Krishna, M., Li, X., Zhang, Y., & Bedford, M. T. (2006) · EMBO Reports · doi:10.1038/sj.embor.7400625 · Cited by 493 · see citing works
Translational Diffusion of Macromolecule-sized Solutes in Cytoplasm and Nucleus
Seksek, O., Biwersi, J., & Verkman, A. S. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.138.1.131 · Cited by 490 · see citing works
Gozani, O., Karuman, P., Jones, D. R., Ivanov, D., Cha, J., Lugovskoy, A. A., Baird, C. L., Zhu, H., Field, S. J., Lessnick, S. L., et al. (2003) · Cell · doi:10.1016/s0092-8674(03)00480-x · Cited by 487 · see citing works
The Tudor domain ‘Royal Family’: Tudor, plant Agenet, Chromo, PWWP and MBT domains
Maurer‐Stroh, S., Dickens, N. J., Hughes‐Davies, L., Kouzarides, T., Eisenhaber, F., & Ponting, C. P. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(03)00004-5 · Cited by 482 · see citing works
A histone H3 methyltransferase controls epigenetic events required for meiotic prophase
Hayashi, K., Yoshida, K., & Matsui, Y. (2005) · Nature · doi:10.1038/nature04112 · Cited by 472 · see citing works
A hitchhiker's guide to the cullin ubiquitin ligases: SCF and its kin
Willems, A. R., Schwab, M. G., & Tyers, M. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.09.027 · Cited by 461 · see citing works
Recognition of Histone H3 Lysine-4 Methylation by the Double Tudor Domain of JMJD2A
Huang, Y., Fang, J., Bedford, M. T., Zhang, Y., & Xu, R.-M. (2006) · Science · doi:10.1126/science.1125162 · Cited by 446 · see citing works
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
The PHD finger, a nuclear protein-interaction domain
Bienz, M. (2005) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2005.11.001 · Cited by 420 · see citing works
Higa, L. A., Wu, M., Ye, T., Kobayashi, R., Sun, H., & Zhang, H. (2006) · Nature Cell Biology · doi:10.1038/ncb1490 · Cited by 414 · see citing works
Signaling Network Model of Chromatin
Schreiber, S. L., & Bernstein, B. (2002) · Cell · doi:10.1016/s0092-8674(02)01196-0 · Cited by 395 · see citing works
Wysocka, 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
Self-citationLysine acetylation and the bromodomain: a new partnership for signaling
Yang, X. (2004) · BioEssays · doi:10.1002/bies.20104 · Cited by 359 · see citing works
Global and Hox-specific roles for the MLL1 methyltransferase
Guenther, M. G., Jenner, R. G., Chevalier, B. S., Nakamura, T., Croce, C. M., Canaani, E., & Young, R. A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503072102 · Cited by 357 · see citing works
Structural and Sequence Motifs of Protein (Histone) Methylation Enzymes
Cheng, X., Collins, R. E., & Zhang, X. (2005) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.34.040204.144452 · Cited by 349 · see citing works
Lee, J., & Skalnik, D. G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508312200 · Cited by 334 · see citing works
Taverna, S. D., Ilin, S., Rogers, R. S., Tanny, J. C., Lavender, H. F., Li, H., Baker, L. A., Boyle, J., Blair, L. P., Chait, B. T., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.10.026 · Cited by 332 · see citing works
Self-citationMolecular 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
A Trivalent System from Vancomycin· d -Ala- d -Ala with Higher Affinity Than Avidin·Biotin
Rao, J., Lahiri, J., Isaacs, L., Weis, R. M., & Whitesides, G. M. (1998) · Science · doi:10.1126/science.280.5364.708 · Cited by 316 · see citing works
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 289 · see citing works
Petruk, S., Sedkov, Y., Riley, K. M., Hodgson, J. W., Schweisguth, F., Hirose, S., Jaynes, J. B., Brock, H. W., & Mazo, A. (2006) · Cell · doi:10.1016/j.cell.2006.10.039 · Cited by 273 · see citing works
Klymenko, T., & Müller, J. (2004) · EMBO Reports · doi:10.1038/sj.embor.7400111 · Cited by 268 · see citing works
Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex
Ruthenburg, A. J., Wang, W., Graybosch, D. M., Li, H., Allis, C. D., Patel, D. J., & Verdine, G. L. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1119 · Cited by 261 · see citing works
Self-citationMolecular recognition of histone H3 by the WD40 protein WDR5
Couture, J., Collazo, E., & Trievel, R. C. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1116 · Cited by 256 · see citing works
Histone H3 Lys 4 methylation: caught in a bind?Preprint
Sims, R. J., & Reinberg, D. (2006) · Genes & Development · doi:10.1101/gad.1468206 · Cited by 239 · see citing works
The human PAF complex coordinates transcription with events downstream of RNA synthesisPreprint
Zhu, B., Mandal, S. S., Pham, A.-D., Zheng, Y., Erdjument‐Bromage, H., Batra, S. K., Tempst, P., & Reinberg, D. (2005) · Genes & Development · doi:10.1101/gad.1292105 · Cited by 235 · see citing works
Goo, Y., Sohn, Y. C., Kim, D., Kim, S., Kang, M., Jung, D.-J., Kwak, E., Barlev, N. A., Berger, S. L., Chow, V. T. K., et al. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.23.1.140-149.2003 · Cited by 231 · see citing works
MLL associates specifically with a subset of transcriptionally active target genes
Milne, T. A., Dou, Y., Martin, M. E., Brock, H. W., Roeder, R. G., & Hess, J. L. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503630102 · Cited by 230 · see citing works
Gellman, S. H. (1991) · Biochemistry · doi:10.1021/bi00241a001 · Cited by 224 · see citing works
Menin Links Estrogen Receptor Activation to Histone H3K4 Trimethylation
Dreijerink, K. M. A., Mulder, K. W., Winkler, G. S., Höppener, J. W. M., Lips, C. J. M., & Timmers, H. T. M. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-4461 · Cited by 213 · see citing works
Terranova, R., Agherbi, H., Boned, A., Méresse, S., & Djabali, M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507425103 · Cited by 209 · see citing works
Structural basis for molecular recognition and presentation of histone H3 By WDR5
Schuetz, A., Allali‐Hassani, A., Martin, F. A., Loppnau, P., Vedadi, M., Bochkarev, A. V., Plotnikov, A. N., Arrowsmith, C. H., & Min, J. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601316 · Cited by 197 · see citing works
Nuclear PtdIns5P as a Transducer of Stress Signaling: An In Vivo Role for PIP4Kbeta
Jones, D. R., Bultsma, Y., Keune, W., Halstead, J. R., Elouarrat, D., Mohammed, S., Heck, A. J. R., D’Santos, C. S., & Divecha, N. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.07.014 · Cited by 191 · see citing works
Specificity and mechanism of the histone methyltransferase Pr-Set7Preprint
Xiao, B., Jing, C., Kelly, G. P., Walker, P. A., Muskett, F. W., Frenkiel, T. A., Martin, S. R., Sarma, K., Reinberg, D., Gamblin, S. J., et al. (2005) · Genes & Development · doi:10.1101/gad.1315905 · Cited by 185 · see citing works
Fragment‐based Approaches in Drug Discovery
Jahnke, W. (2006) · Methods and principles in medicinal chemistry · doi:10.1002/3527608761 · Cited by 182 · see citing works
Modulation of heat shock gene expression by the TAC1 chromatin-modifying complex
Smith, S. T., Petruk, S., Sedkov, Y., Cho, E., Tillib, S. V., Canaani, E., & Mazo, A. (2004) · Nature Cell Biology · doi:10.1038/ncb1088 · Cited by 181 · see citing works
Dynamic nucleosomes and gene transcription
Mellor, J. (2006) · Trends in Genetics · doi:10.1016/j.tig.2006.03.008 · Cited by 168 · see citing works
Coactivator as a target gene specificity determinant for histone H3 lysine 4 methyltransferases
Lee, S., Lee, D.-K., Dou, Y., Lee, J., Lee, B., Kwak, E., Kong, Y., Lee, S., Roeder, R. G., & Lee, J. W. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607313103 · Cited by 166 · see citing works
Martin, D. G. E., Baetz, K., Shi, X., Walter, K. L., MacDonald, V. E., Wlodarski, M. J., Gozani, O., Hieter, P., & Howe, L. J. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00573-06 · Cited by 161 · see citing works
Krishnamurthy, V. M., Estroff, L. A., & Whitesides, G. M. (2006) · Methods and principles in medicinal chemistry · doi:10.1002/3527608761.ch2 · Cited by 160 · see citing works
Han, Z., Guo, L. P., Wang, H., Shen, Y., Deng, X. W., & Chai, J. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.03.018 · Cited by 159 · see citing works
Identification of the MLL2 Complex as a Coactivator for Estrogen Receptor α
Mo, R., Rao, S. M., & Zhu, Y.-J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513245200 · Cited by 156 · see citing works
Byrd, K. N., & Shearn, A. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1933593100 · Cited by 148 · see citing works
Rank, G., Prestel, M., & Paro, R. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.22.8026-8034.2002 · Cited by 145 · see citing works
Protein Interactions of the MLL PHD Fingers Modulate MLL Target Gene Regulation in Human Cells
Fair, K., Anderson, M., Bulanova, E., Mi, H., Tropschug, M., & Dı́az, M. O. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.10.3589-3597.2001 · Cited by 143 · see citing works
Zhou, Y., & Grummt, I. (2005) · Current Biology · doi:10.1016/j.cub.2005.06.057 · Cited by 135 · see citing works
Nucleosome Binding by the Bromodomain and PHD Finger of the Transcriptional Cofactor p300
Ragvin, A., Valvatne, H., Erdal, S., Årskog, V., Tufteland, K. R., Breen, K., Oyan, A. M., Eberharter, A., Gibson, T. J., Becker, P. B., et al. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.01.051 · Cited by 129 · see citing works
Bae, E., Calhoun, V. C., Levine, M., Lewis, E. B., & Drewell, R. A. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.222671299 · Cited by 129 · see citing works
Phosphatidylinositol 3-phosphate recognition and membrane docking by the FYVE domain
Kutateladze, T. G. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2006.03.011 · Cited by 128 · see citing works
Role of Nucleosome Remodeling Factor NURF in Transcriptional Activation of Chromatin
Mizuguchi, G., Tsukiyama, T., Wiśniewski, J., & Wu, C. (1997) · Molecular Cell · doi:10.1016/s1097-2765(00)80015-5 · Cited by 126 · see citing works
The complexity of chromatin remodeling and its links to cancer
Neely, K. (2002) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/s0304-419x(02)00067-7 · Cited by 124 · see citing works
Hazzalin, C. A., & Mahadevan, L. C. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030393 · Cited by 114 · see citing works
Structure of SET domain proteins: a new twist on histone methylation
Marmorstein, R. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(03)00007-0 · Cited by 111 · see citing works
Mechanisms of Transformation by MLL
Hess, J. L. (2004) · Critical Reviews in Eukaryotic Gene Expression · doi:10.1615/critreveukaryotgeneexpr.v14.i4.10 · Cited by 88 · see citing works
Dehé, P.-M., & Géli, V. (2006) · Biochemistry and Cell Biology · doi:10.1139/o06-081 · Cited by 82 · see citing works
Krajewski, W. A., Nakamura, T., Mazo, A., & Canaani, E. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.5.1891-1899.2005 · Cited by 75 · see citing works
Structure of the Chromo Barrel Domain from the MOF Acetyltransferase
Nielsen, P. R., Nietlispach, D., Buscaino, A., Warner, R. J., Akhtar, A., Murzin, A. G., Murzina, N. V., & Laue, E. D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501347200 · Cited by 56 · see citing works
Sites of in vivo histone methylation in developing trout testis.
Honda, B., Dixon, G. H., & Candido, E. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)40725-4 · Cited by 48 · see citing works
Shi, X., & Gozani, O. (2005) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20625 · Cited by 44 · see citing works
Dynamic regulation of histone methylation by demethylases
Shi, Y. (2008) · The FASEB Journal · doi:10.1096/fasebj.22.1_supplement.258.1 · Cited by 2 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Shrestha, S., & Offer, S. M. (2016) · Medical Epigenetics · doi:10.1159/000444713 · Cited by 8,949 · see citing works
CpG islands and the regulation of transcription
Deaton, A. M., & Bird, A. (2011) · Genes & Development · doi:10.1101/gad.2037511 · Cited by 3,187 · see citing works
Epigenetics: A landscape takes shape
Goldberg, A. D., Allis, C. D., & Bernstein, E. (2007) · Cell · doi:10.1016/j.cell.2007.02.006 · Cited by 2,466 · see citing works
Self-citationA long noncoding RNA maintains active chromatin to coordinate homeotic gene expression
Wang, K., Yang, Y. W., Liu, B., Sanyal, A., Corces, M. R., Chen, Y., Lajoie, B. R., Protacio, A., Flynn, R. A., Gupta, R. A., et al. (2011) · Nature · doi:10.1038/nature09819 · Cited by 1,963 · see citing works
Self-citationModification 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 · see citing works
Self-citationTaverna, S. D., Li, H., Ruthenburg, A. J., Allis, C. D., & Patel, D. J. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1338 · Cited by 1,419 · see citing works
Self-citationMechanisms of Polycomb gene silencing: knowns and unknowns
Simon, J. A., & Kingston, R. E. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2763 · Cited by 1,320 · see citing works
Role of conserved non-coding DNA elements in the Foxp3 gene in regulatory T-cell fate
Zheng, Y., Josefowicz, S. Z., Chaudhry, A., Peng, X. P., Forbush, K. A., & Rudensky, A. Y. (2010) · Nature · doi:10.1038/nature08750 · Cited by 1,170 · see citing works
Covalent histone modifications — miswritten, misinterpreted and mis-erased in human cancers
Chi, P., Allis, C. D., & Wang, G. G. (2010) · Nature reviews. Cancer · doi:10.1038/nrc2876 · Cited by 1,099 · see citing works
Self-citationConrath, U., Beckers, G. J. M., Langenbach, C. J. G., & Jaskiewicz, M. R. (2015) · Annual Review of Phytopathology · doi:10.1146/annurev-phyto-080614-120132 · Cited by 1,073 · see citing works
Multivalent engagement of chromatin modifications by linked binding modules
Ruthenburg, A. J., Li, H., Patel, D. J., & Allis, C. D. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2298 · Cited by 1,015 · see citing works
Self-citationDe 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
Enhancer function: new insights into the regulation of tissue-specific gene expression
Ong, C.-T., & Corces, V. G. (2011) · Nature Reviews Genetics · doi:10.1038/nrg2957 · Cited by 929 · see citing works
Androgen Receptor Regulates a Distinct Transcription Program in Androgen-Independent Prostate Cancer
Wang, Q., Li, W., Zhang, Y., Yuan, X., Xu, K., Yu, J., Chen, Z., Beroukhim, R., Wang, H., Lupien, M., et al. (2009) · Cell · doi:10.1016/j.cell.2009.04.056 · Cited by 897 · see citing works
Selective Anchoring of TFIID to Nucleosomes by Trimethylation of Histone H3 Lysine 4
Vermeulen, M., Mulder, K. W., Denissov, S., Pijnappel, W. W. M. P., van Schaik, F. M. A., Varier, R. A., Baltissen, M. P. A., Stunnenberg, H. G., Mann, M., & Timmers, H. T. M. (2007) · Cell · doi:10.1016/j.cell.2007.08.016 · Cited by 883 · see citing works
Perceiving the epigenetic landscape through histone readers
Musselman, C. A., Lalonde, M., Côté, J., & Kutateladze, T. G. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2436 · Cited by 840 · see citing works
DNA Methylation: Superior or Subordinate in the Epigenetic Hierarchy?
Jin, B., Li, Y., & Robertson, K. D. (2011) · Genes & Cancer · doi:10.1177/1947601910393957 · Cited by 818 · see citing works
A double take on bivalent promotersPreprint
Voigt, P., Tee, W., & Reinberg, D. (2013) · Genes & Development · doi:10.1101/gad.219626.113 · Cited by 811 · see citing works
Molecular aspects of defence priming
Conrath, U. (2011) · Trends in Plant Science · doi:10.1016/j.tplants.2011.06.004 · Cited by 795 · see citing works
Histone Methylation in Higher Plants
Liu, C., Lu, F., Cui, X., & Cao, X. (2010) · Annual Review of Plant Biology · doi:10.1146/annurev.arplant.043008.091939 · Cited by 735 · see citing works
Dynamic Regulation of Histone Lysine Methylation by Demethylases
Shi, Y., & Whetstine, J. R. (2007) · Molecular Cell · doi:10.1016/j.molcel.2006.12.010 · Cited by 710 · see citing works
Histone Methylation Dynamics and Gene Regulation Occur through the Sensing of One-Carbon Metabolism
Mentch, S. J., Mehrmohamadi, M., Huang, L., Liu, X., Gupta, D., Mattocks, D. A. L., Padilla, P. G., Ables, G. P., Bamman, M. M., Thalacker‐Mercer, A. E., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.08.024 · Cited by 706 · see citing works
Allelic reprogramming of the histone modification H3K4me3 in early mammalian development
Zhang, B., Zheng, H., Huang, B., Li, W., Xiang, Y.-L., Peng, X., Jia, M., Wu, X., Zhang, Y., Xu, Q.-H., et al. (2016) · Nature · doi:10.1038/nature19361 · Cited by 627 · see citing works
DNA methylation: The nuts and bolts of repression
Miranda, T. B., & Jones, P. A. (2007) · Journal of Cellular Physiology · doi:10.1002/jcp.21224 · Cited by 685 · see citing works
Epigenetic control of T-helper-cell differentiation
Wilson, C. B., Rowell, E. A., & Sekimata, M. (2009) · Nature reviews. Immunology · doi:10.1038/nri2487 · Cited by 678 · see citing works
Hijacked in cancer: the MLL/KMT2 family of methyltransferases
Rao, R., & Dou, Y. (2015) · Nature Reviews. Cancer · doi:10.1038/nrc3929 · Cited by 558 · see citing works
Broad histone H3K4me3 domains in mouse oocytes modulate maternal-to-zygotic transition
Dahl, J. A., Jung, I., Aanes, H., Greggains, G. D., Manaf, A., Lerdrup, M., Li, G., Kuan, S., Li, B., Lee, A. Y., et al. (2016) · Nature · doi:10.1038/nature19360 · Cited by 628 · see citing works
V(D)J Recombination: Mechanisms of Initiation
Schatz, D. G., & Swanson, P. C. (2011) · Annual Review of Genetics · doi:10.1146/annurev-genet-110410-132552 · Cited by 592 · see citing works
Histone Methylation Regulates Memory Formation
Gupta, S., Kim, S. Y., Artis, S., Molfese, D. L., Schumacher, A., Sweatt, J. D., Paylor, R. E., & Lubin, F. D. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.3732-09.2010 · Cited by 562 · see citing works
Jaskiewicz, M. R., Conrath, U., & Peterhänsel, C. (2010) · EMBO Reports · doi:10.1038/embor.2010.186 · Cited by 560 · see citing works
Kim, J., Guermah, M., McGinty, R. K., Lee, J., Tang, Z., Milne, T. A., Shilatifard, A., Muir, T. W., & Roeder, R. G. (2009) · Cell · doi:10.1016/j.cell.2009.02.027 · Cited by 555 · see citing works
Dynamic histone H3 methylation during gene induction: HYPB/Setd2 mediates all H3K36 trimethylation
Edmunds, J. W., Mahadevan, L. C., & Clayton, A. L. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601967 · Cited by 547 · see citing works
Greer, E. L., Maures, T. J., Hauswirth, A. G., Green, E. M., Leeman, D. S., Maro, G. S., Han, S., Banko, M. R., Gozani, O., & Brunet, A. (2010) · Nature · doi:10.1038/nature09195 · Cited by 543 · 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
Self-citationBrasacchio, 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
Decoding the Epigenetic Language of Neuronal Plasticity
Borrelli, E., Nestler, E. J., Allis, C. D., & Sassone‐Corsi, P. (2008) · Neuron · doi:10.1016/j.neuron.2008.10.012 · Cited by 529 · see citing works
Self-citationLee, J.-E., Wang, C., Xu, S., Cho, Y.-W., Wang, L., Feng, X., Baldridge, A., Sartorelli, V., Zhuang, L., Peng, W., et al. (2013) · eLife · doi:10.7554/elife.01503 · Cited by 522 · see citing works
Aging, Rejuvenation, and Epigenetic Reprogramming: Resetting the Aging Clock
Rando, T. A., & Chang, H. Y. (2012) · Cell · doi:10.1016/j.cell.2012.01.003 · Cited by 520 · see citing works
Is H3K4me3 instructive for transcription activation?
Howe, F. S., Fischl, H., Murray, S. C., & Mellor, J. (2016) · BioEssays · doi:10.1002/bies.201600095 · Cited by 515 · see citing works
Steger, D. J., Lefterova, M. I., Ying, L., Stonestrom, A. J., Schupp, M., Zhuo, D. X., Vakoc, A. L., Kim, J., Chen, J., Lazar, M. A., et al. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.02076-07 · Cited by 499 · see citing works
Histone modification: cause or cog?
Henikoff, S., & Shilatifard, A. (2011) · Trends in Genetics · doi:10.1016/j.tig.2011.06.006 · Cited by 482 · see citing works
H3K4me3 Interactions with TAF3 Regulate Preinitiation Complex Assembly and Selective Gene Activation
Lauberth, S. M., Nakayama, T., Wu, X., Ferris, A. L., Tang, Z., Hughes, S. H., & Roeder, R. G. (2013) · Cell · doi:10.1016/j.cell.2013.01.052 · Cited by 473 · see citing works
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 470 · see citing works
Modulation of p53 Function by SET8-Mediated Methylation at Lysine 382
Shi, X., Kachirskaia, I., Yamaguchi, H., West, L. E., Wen, H., Wang, E. W., Dutta, S. M., Appella, E., & Gozani, O. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.07.012 · Cited by 463 · see citing works
Mechanism and Regulation of Meiotic Recombination InitiationPreprint
Lam, I., & Keeney, S. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016634 · Cited by 457 · see citing works
Nucleosome destabilization in the epigenetic regulation of gene expression
Henikoff, S. (2007) · Nature Reviews Genetics · doi:10.1038/nrg2206 · Cited by 439 · see citing works
Haematopoietic malignancies caused by dysregulation of a chromatin-binding PHD finger
Wang, G. G., Song, J., Wang, Z., Dormann, H. L., Casadio, F., Li, H., Luo, J.-L., Patel, D. J., & Allis, C. D. (2009) · Nature · doi:10.1038/nature08036 · Cited by 439 · see citing works
Self-citationLämke, J., Brzezinka, K., Altmann, S., & Bäurle, I. (2015) · The EMBO Journal · doi:10.15252/embj.201592593 · Cited by 437 · see citing works
Structure and acetyl-lysine recognition of the bromodomain
Mujtaba, S., Zeng, L., & Zhou, M.-M. (2007) · Oncogene · doi:10.1038/sj.onc.1210618 · Cited by 419 · see citing works
Jmjd3 contributes to the control of gene expression in LPS‐activated macrophages
Santa, F. D., Narang, V., Yap, Z. H., Tusi, B. K., Burgold, T., Austenaa, L. M. I., Bucci, G., Cagánová, M., Notarbartolo, S., Casola, S. S., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.271 · Cited by 422 · see citing works
Epigenetic tools (The Writers, The Readers and The Erasers) and their implications in cancer therapy
Biswas, S., & Rao, C. M. (2018) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2018.08.021 · Cited by 402 · see citing works
JARID1B is a histone H3 lysine 4 demethylase up-regulated in prostate cancer
Xiang, Y., Zhu, Z., Han, G., Ye, X., Xu, B., Peng, Z., Ma, Y., Yu, Y., Lin, H., Chen, A. P., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700735104 · Cited by 395 · see citing works
Delcuve, G. P., Rastegar, M., & Davie, J. (2009) · Journal of Cellular Physiology · doi:10.1002/jcp.21678 · Cited by 392 · see citing works
Epigenetics in metal carcinogenesis: nickel, arsenic, chromium and cadmium
Arita, A., & Costa, M. (2009) · Metallomics · doi:10.1039/b903049b · Cited by 388 · see citing works
Histone H3 lysine 4 trimethylation marks meiotic recombination initiation sites
Borde, V., Robine, N., Lin, W., Bonfils, S., Géli, V., & Nicolas, A. G. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.257 · Cited by 380 · see citing works
Quantitative Proteomic Analysis of Histone Modifications
Huang, H., Lin, S., Garcia, B. A., & Zhao, Y. (2015) · Chemical Reviews · doi:10.1021/cr500491u · Cited by 372 · see citing works
OPERating ON Chromatin, a Colorful Language where Context Matters
Gardner, K. E., Allis, C. D., & Strahl, B. D. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.01.040 · Cited by 362 · see citing works
Self-citationArginine methylation at histone H3R2 controls deposition of H3K4 trimethylation
Kirmizis, A., Santos-Rosa, H., Penkett, C. J., Singer, M. A., Vermeulen, M., Mann, M., Bähler, J., Green, R. D., & Kouzarides, T. (2007) · Nature · doi:10.1038/nature06160 · Cited by 355 · see citing works
Recognition of a Mononucleosomal Histone Modification Pattern by BPTF via Multivalent Interactions
Ruthenburg, A. J., Li, H., Milne, T. A., Dewell, S. B., McGinty, R. K., Yuen, M. A., Ueberheide, B. M., Dou, Y., Muir, T. W., Patel, D. J., et al. (2011) · Cell · doi:10.1016/j.cell.2011.03.053 · Cited by 353 · see citing works
Self-citationZhang, T. Y., Labonté, B., Wen, X. L., Turecki, G., & Meaney, M. J. (2013) · Neuropsychopharmacology · doi:10.1038/npp.2012.149 · Cited by 347 · see citing works
Nardini, M., Gnesutta, N., Donati, G., Gatta, R. P., Forni, C., Fossati, A., Vonrhein, C., Moras, D., Romier, C., Bolognesi, M., et al. (2013) · Cell · doi:10.1016/j.cell.2012.11.047 · Cited by 335 · see citing works
Genome-Wide Views of Chromatin Structure
Rando, O. J., & Chang, H. Y. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.071107.134639 · Cited by 323 · see citing works
Chemical Biology of Protein Arginine Modifications in Epigenetic Regulation
Fuhrmann, J., Clancy, K. W., & Thompson, P. R. (2015) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00003 · Cited by 325 · see citing works
PARP-1 Regulates Chromatin Structure and Transcription through a KDM5B-Dependent Pathway
Krishnakumar, R., & Kraus, W. L. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.08.014 · Cited by 328 · see citing works
H3K27 Demethylases, at Long Last
Swigut, T., & Wysocka, J. (2007) · Cell · doi:10.1016/j.cell.2007.09.026 · Cited by 327 · see citing works
Self-citationLiu, F., Quesada, V., Crevillén, P., Bäurle, I., Świeżewski, S., & Dean, C. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.10.018 · Cited by 326 · see citing works
Inhibitors of Protein Methyltransferases and Demethylases
Kanıskan, H. Ü., Martini, M. L., & Jin, J. J. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00801 · Cited by 320 · see citing works
Readout 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
Suppression of the antiviral response by an influenza histone mimic
Marazzi, I., Ho, J., Kim, J., Manicassamy, B., Dewell, S. B., Albrecht, R. A., Seibert, C. W., Schaefer, U., Jeffrey, K. L., Prinjha, R. K., et al. (2012) · Nature · doi:10.1038/nature10892 · Cited by 312 · see citing works
Epigenetic codes in cognition and behaviour
Gräff, J., & Mansuy, I. M. (2008) · Behavioural Brain Research · doi:10.1016/j.bbr.2008.01.021 · Cited by 307 · see citing works
PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylationPreprint
Hyllus, D. M., Stein, C., Schnabel, K., Schiltz, E., Imhof, A., Dou, Y., Hsieh, J. J.-D., & Bauer, U. (2007) · Genes & Development · doi:10.1101/gad.447007 · Cited by 308 · see citing works
Füllgrabe, J., Kavanagh, E. T., & Joseph, B. (2011) · Oncogene · doi:10.1038/onc.2011.121 · Cited by 307 · see citing works
Jiang, H., Shukla, A., Wang, X., Chen, W., Bernstein, B., & Roeder, R. G. (2011) · Cell · doi:10.1016/j.cell.2011.01.020 · Cited by 296 · see citing works
Histone H3 lysine 4 methyltransferase KMT2D
Froimchuk, E., Jang, Y., & Ge, K. (2017) · Gene · doi:10.1016/j.gene.2017.06.056 · Cited by 300 · see citing works
Bivalent histone modifications in early embryogenesis
Vastenhouw, N. L., & Schier, A. F. (2012) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2012.03.009 · Cited by 297 · see citing works
Cancer epigenetics: linking basic biology to clinical medicine
Tsai, H.-C., & Baylin, S. B. (2011) · Cell Research · doi:10.1038/cr.2011.24 · Cited by 298 · see citing works
The In Vivo Pattern of Binding of RAG1 and RAG2 to Antigen Receptor Loci
Ji, Y., Resch, W., Corbett, E., Yamane, A., Casellas, R. C., & Schatz, D. G. (2010) · Cell · doi:10.1016/j.cell.2010.03.010 · Cited by 296 · see citing works
The role of epigenetics in the pathology of diabetic complications
Villeneuve, L. M., & Natarajan, R. D. (2010) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00200.2010 · Cited by 295 · see citing works
The histone methyltransferase MLL1 permits the oscillation of circadian gene expression
Katada, S., & Sassone‐Corsi, P. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1961 · Cited by 291 · see citing works
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 292 · see citing works
Regulation of Estrogen Receptor α by the SET7 Lysine Methyltransferase
Subramanian, K., Jia, D., Kapoor-Vazirani, P., Powell, D. R., Collins, R. E., Sharma, D., Peng, J., Cheng, X., & Vertino, P. M. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.03.022 · Cited by 291 · see citing works
Regulation of hippocampal H3 histone methylation by acute and chronic stress
Hunter, R. G., McCarthy, K. J., Milne, T. A., Pfaff, D. W., & McEwen, B. S. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911143106 · Cited by 290 · see citing works
Is there a code embedded in proteins that is based on post-translational modifications?
Sims, R. J., & Reinberg, D. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2502 · Cited by 289 · see citing works
Polycomb complexes and epigenetic states
Schwartz, Y. B., & Pirrotta, V. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.03.002 · Cited by 283 · see citing works
Liang, Y., Vogel, J. L., Narayanan, A., Peng, H., & Kristie, T. M. (2009) · Nature Medicine · doi:10.1038/nm.2051 · Cited by 283 · see citing works
Epigenetics and Trained Immunity
van der Heijden, C. D. C. C., Noz, M. P., Joosten, L. A. B., Netea, M. G., Riksen, N. P., & Keating, S. T. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7310 · Cited by 284 · see citing works
Resetting histone modifications during human parental-to-zygotic transition
Xia, W., Xu, J., Yu, G., Yao, G., Xu, K., Ma, X., Zhang, N., Liu, B., Li, T., Lin, Z., et al. (2019) · Science · doi:10.1126/science.aaw5118 · Cited by 279 · see citing works
Hamdane, N., Jühling, F., Crouchet, É., Saghire, H. E., Thumann, C., Oudot, M. A., Bandiera, S., Saviano, A., Ponsolles, C., Suarez, A. A. R., et al. (2019) · Gastroenterology · doi:10.1053/j.gastro.2019.02.038 · Cited by 276 · see citing works
Abnormal histone modification patterns in lupus CD4+ T cells.
Hu, N., Qiu, X., Luo, Y., Yuan, J., Li, Y., Lei, W., Zhang, G., Zhou, Y., Su, Y., & Lu, Q. (2008) · PubMed · 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
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 270 · see citing works
Aberrant chromatin at genes encoding stem cell regulators in human mixed-lineage leukemia.Preprint
Guenther, M., Lawton, L. N., Rozovskaia, T., Frampton, G., Levine, S., Volkert, T. L., Croce, C., Nakamura, T., Canaani, E., & Young, R. (2008) · Genes & Development · doi:10.1101/gad.1741408 · Cited by 288 · see citing works
Transcriptional and Epigenomic Regulation of Adipogenesis
Lee, J., Schmidt, H., Lai, B., & Ge, K. (2019) · Molecular and Cellular Biology · doi:10.1128/mcb.00601-18 · Cited by 265 · see citing works
Kerényi, M., Shao, Z., Hsu, Y.-J., Guo, G., Luc, S., O'Brien, K., Fujiwara, Y., Peng, C., Nguyen, M., & Orkin, S. (2013) · eLife · doi:10.7554/elife.00633 · Cited by 264 · see citing works
Epigenetic regulation of Keap1-Nrf2 signaling
Guo, Y., Yu, S., Zhang, C., & Kong, A. T. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.013 · Cited by 261 · see citing works
The Current State of Chromatin Immunoprecipitation
Collas, P. (2010) · Molecular Biotechnology · doi:10.1007/s12033-009-9239-8 · Cited by 254 · see citing works
Epigenetics and Colorectal Cancer Pathogenesis
Bardhan, K., & Liu, K. (2013) · Cancers · doi:10.3390/cancers5020676 · Cited by 253 · see citing works
Acetylation on histone H3 lysine 9 mediates a switch from transcription initiation to elongation
Gates, L. A., Shi, J., Rohira, A. D., Feng, Q. F., Zhu, B., Bedford, M. T., Sagum, C. A., Jung, S. Y., Qin, J., Tsai, M., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.802074 · Cited by 247 · see citing works
ZF-CxxC domain-containing proteins, CpG islands and the chromatin connection
Long, H. K., Blackledge, N. P., & Klose, R. J. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130028 · Cited by 243 · see citing works
Tyagi, S., Chabes, A. L., Wysocka, J., & Herr, W. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.05.030 · Cited by 247 · see citing works
Self-citation
- Authors
- Ruthenburg, A. J., Allis, C. D., & Wysocka, J.
- Affiliations
- Rockefeller University (US)
- Stanford Medicine (US)
- Corresponding author
- Wysocka, Joanna
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2007-01
- Volume
- 25
- Issue
- 1
- Pages
- 15-30
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2024584416
- Cited by
- 1,147
- References
- 104
- Citations by year
- 2026: 23 · 2025: 40 · 2024: 46 · 2023: 39 · 2022: 35 · 2021: 45 · 2020: 51 · 2019: 44 · 2018: 39 · 2017: 54 · 2016: 65 · 2015: 73 · 2014: 68 · 2013: 72 · 2012: 72
- FWCI
- 7.16
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
- Keywords
- H3K4 methylation, H3K4, chromatin epigenetics, chromatin reader proteins, histone methyltransferase, chromatin fiber structure, chromatin structure
- MeSH terms
- Amino Acid Sequence, Animals, Histones, Humans, Lysine, Methylation, Molecular Sequence Data, Homeodomain Proteins, Epigenesis, Genetic, Genes, Developmental
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