Chromatin modifier enzymes, the histone code and cancer

DNA methylation patterns and epigenetic memory

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The fundamental role of epigenetic events in cancer

Jones, P. A., & Baylin, S. B. (2002) · Nature Reviews Genetics · doi:10.1038/nrg816 · Cited by 5,648

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

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

Histone deacetylases (HDACs): characterization of the classical HDAC family

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

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

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

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The polycomb group protein EZH2 is involved in progression of prostate cancer

Varambally, S., Dhanasekaran, S. M., Zhou, M., Barrette, T. R., Kumar-Sinha, C., Sanda, M. G., Ghosh, D., Pienta, K. J., Sewalt, R. G. A. B., Otte, A. P., et al. (2002) · Nature · doi:10.1038/nature01075 · Cited by 2,717

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

Loss of acetylation at Lys16 and trimethylation at Lys20 of histone H4 is a common hallmark of human cancer

Fraga, M. F., Ballestar, E., Villar-Garea, A., Boix-Chornet, M., Espada, J., Schotta, G., Bonaldi, T., Haydon, C., Ropero, S., Petrie, K., et al. (2005) · Nature Genetics · doi:10.1038/ng1531 · Cited by 1,923

Methylation-Induced Repression— Belts, Braces, and Chromatin

Bird, A. P., & Wolffe, A. P. (1999) · Cell · doi:10.1016/s0092-8674(00)81532-9 · Cited by 1,827

EZH2 is a marker of aggressive breast cancer and promotes neoplastic transformation of breast epithelial cells

Kleer, C. G., Cao, Q., Varambally, S., Shen, R., Ota, I., Tomlins, S. A., Ghosh, D., Sewalt, R. G. A. B., Otte, A. P., Hayes, D. F., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1933744100 · Cited by 1,649

Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein

Kuzmichev, A., Nishioka, K., Erdjument-Bromage, H., Tempst, P., & Reinberg, D. (2002) · Genes & Development · doi:10.1101/gad.1035902 · Cited by 1,596

DNA methylation in cancer: too much, but also too little

Ehrlich, M. (2002) · Oncogene · doi:10.1038/sj.onc.1205651 · Cited by 1,538

The Sir2 Family of Protein Deacetylases

Blander, G., & Guarente, L. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073651 · Cited by 1,495

Estrogen Receptor-α Directs Ordered, Cyclical, and Combinatorial Recruitment of Cofactors on a Natural Target Promoter

Métivier, R., Penot, G., Hübner, M. R., Reid, G., Brand, H., Koš, M., & Gannon, F. (2003) · Cell · doi:10.1016/s0092-8674(03)00934-6 · Cited by 1,431

Histone H3.1 and H3.3 Complexes Mediate Nucleosome Assembly Pathways Dependent or Independent of DNA Synthesis

Tagami, H., Ray-Gallet, D., Almouzni, G., & Nakatani, Y. (2004) · Cell · doi:10.1016/s0092-8674(03)01064-x · Cited by 1,295

G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis

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 1,253

Control of CpNpG DNA methylation by the KRYPTONITE histone H3 methyltransferase

Jackson, J. P., Lindroth, A. M., Cao, X., & Jacobsen, S. E. (2002) · Nature · doi:10.1038/nature731 · Cited by 1,251

Histone and chromatin cross-talk

Fischle, W., Wang, Y., & Allis, C. D. (2003) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(03)00013-9 · Cited by 1,207

EZH2 is downstream of the pRB-E2F pathway, essential for proliferation and amplified in cancer.

Bracken, A. P., Pasini, D., Capra, M., Prosperini, E., Colli, E., & Helin, K. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg542 · Cited by 1,196

Targeted Recruitment of Set1 Histone Methylase by Elongating Pol II Provides a Localized Mark and Memory of Recent Transcriptional Activity

Ng, H. H., Robert, F., Young, R. A., & Struhl, K. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00092-3 · Cited by 1,095

Epigenetic Regulation of Cellular Memory by the Polycomb and Trithorax Group Proteins

Ringrose, L., & Paro, R. (2004) · Annual Review of Genetics · doi:10.1146/annurev.genet.38.072902.091907 · Cited by 1,077

Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast

Sun, Z.-W., & Allis, C. D. (2002) · Nature · doi:10.1038/nature00883 · Cited by 1,072

A histone H3 methyltransferase controls DNA methylation in Neurospora crassa

Tamaru, H., & Selker, E. U. (2001) · Nature · doi:10.1038/35104508 · Cited by 1,038

Gene Dosage–Dependent Embryonic Development and Proliferation Defects in Mice Lacking the Transcriptional Integrator p300

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Human PAD4 Regulates Histone Arginine Methylation Levels via Demethylimination

Wang, Y., Wysocka, J., Sayegh, J., Lee, Y.-H., Perlin, J. R., Leonelli, L., Sonbuchner, L. S., McDonald, C. H., Cook, R. G., Dou, Y., et al. (2004) · Science · doi:10.1126/science.1101400 · Cited by 1,010

Non-CpG methylation is prevalent in embryonic stem cells and may be mediated by DNA methyltransferase 3a

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Rb targets histone H3 methylation and HP1 to promoters

Nielsen, S. J., Schneider, R., Bauer, U.-M., Bannister, A. J., Morrison, A., O'Carroll, D., Firestein, R., Cleary, M., Jenuwein, T., Herrera, R. E., et al. (2001) · Nature · doi:10.1038/35087620 · Cited by 904

Chromatin Acetylation, Memory, and LTP Are Impaired in CBP+/− Mice

Alarcón, J. M., Malleret, G., Touzani, K., Vronskaya, S., Ishii, S., Kandel, E. R., & Barco, A. (2004) · Neuron · doi:10.1016/j.neuron.2004.05.021 · Cited by 892

Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks

Huyen, Y., Zgheib, O., DiTullio Jr, R. A., Gorgoulis, V. G., Zacharatos, P., Petty, T. J., Sheston, E. A., Mellert, H. S., Stavridi, E. S., & Halazonetis, T. D. (2004) · Nature · doi:10.1038/nature03114 · Cited by 884 · cited 1×

Methylation of H3-Lysine 79 Is Mediated by a New Family of HMTases without a SET Domain

Feng, Q., Wang, H., Ng, H. H., Erdjument-Bromage, H., Tempst, P., Struhl, K., & Zhang, Y. (2002) · Current Biology · doi:10.1016/s0960-9822(02)00901-6 · Cited by 865

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

RNAi-mediated pathways in the nucleus

Matzke, M. A., & Birchler, J. A. (2005) · Nature Reviews Genetics · doi:10.1038/nrg1500 · Cited by 844

Histone Deimination Antagonizes Arginine Methylation

Cuthbert, G. L., Daujat, S., Snowden, A. W., Erdjument-Bromage, H., Hagiwara, T., Yamada, M., Schneider, R., Gregory, P. D., Tempst, P., Bannister, A. J., et al. (2004) · Cell · doi:10.1016/j.cell.2004.08.020 · Cited by 839

CBP Histone Acetyltransferase Activity Is a Critical Component of Memory Consolidation

Korzus, E., Rosenfeld, M. G., & Mayford, M. (2004) · Neuron · doi:10.1016/j.neuron.2004.06.002 · Cited by 823

Regulation of p53 activity through lysine methylation

Chuikov, S., Kurash, J. K., Wilson, J. R., Xiao, B., Justin, N., Ivanov, G. S., McKinney, K., Tempst, P., Prives, C., Gamblin, S. J., et al. (2004) · Nature · doi:10.1038/nature03117 · Cited by 816

Methylation of Histone H4 at Arginine 3 Facilitating Transcriptional Activation by Nuclear Hormone Receptor

Wang, H., Huang, Z.-Q., Xia, L., Feng, Q., Erdjument-Bromage, H., Strahl, B. D., Briggs, S. D., Allis, C. D., Wong, J., Tempst, P., et al. (2001) · Science · doi:10.1126/science.1060781 · Cited by 805

Synergistic Coupling of Histone H3 Phosphorylation and Acetylation in Response to Epidermal Growth Factor Stimulation

Cheung, P., Tanner, K. G., Cheung, W. L., Sassone-Corsi, P., Denu, J. M., & Allis, C. D. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80256-7 · Cited by 803

Coordinated histone modifications mediated by a CtBP co-repressor complex

Shi, Y., Sawada, J.-I., Sui, G., Affar, E. B., Whetstine, J. R., Lan, F., Ogawa, H., Po-Shan Luke, M., Nakatani, Y., & Shi, Y. (2003) · Nature · doi:10.1038/nature01550 · Cited by 801

SET Domain-containing Protein, G9a, Is a Novel Lysine-preferring Mammalian Histone Methyltransferase with Hyperactivity and Specific Selectivity to Lysines 9 and 27 of Histone H3

Tachibana, M., Sugimoto, K., Fukushima, T., & Shinkai, Y. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101914200 · Cited by 784

Methylation of histone H3 Lys 4 in coding regions of active genes

Bernstein, B. E., Humphrey, E. L., Erlich, R. L., 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 777

The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a putative acetyltransferase to the CREB–binding protein

Borrow, J., Stanton, V. P., Andresen, J. M., Becher, R., Behm, F. G., Chaganti, R. S. K., Civin, C. I., Disteche, C., Dubé, I., Frischauf, A. M., et al. (1996) · Nature Genetics · doi:10.1038/ng0996-33 · Cited by 771

The DNA methyltransferases associate with HP1 and the SUV39H1 histone methyltransferase

Fuks, F. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg332 · Cited by 760

SUMO and ubiquitin in the nucleus: different functions, similar mechanisms?

Gill, G. (2004) · Genes & Development · doi:10.1101/gad.1214604 · Cited by 756

SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells

Hamamoto, R., Furukawa, Y., Morita, M., Iimura, Y., Silva, F. P., Li, M., Yagyu, R., & Nakamura, Y. (2004) · Nature Cell Biology · doi:10.1038/ncb1151 · Cited by 731

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

Nakamura, T., Mori, T., Tada, S., Krajewski, W., Rozovskaia, T., Wassell, R., Dubois, G., Mazo, A., Croce, C. M., & Canaani, E. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00740-2 · Cited by 721

Transcriptional activation via sequential histone H2B ubiquitylation and deubiquitylation, mediated by SAGA-associated Ubp8

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MOZ-TIF2, but not BCR-ABL, confers properties of leukemic stem cells to committed murine hematopoietic progenitors

Huntly, B. J. P., Shigematsu, H., Deguchi, K., Lee, B. H., Mizuno, S., Duclos, N., Rowan, R., Amaral, S., Curley, D., Williams, I. R., et al. (2004) · Cancer Cell · doi:10.1016/j.ccr.2004.10.015 · Cited by 697

Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex

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Leukemia Proto-Oncoprotein MLL Forms a SET1-Like Histone Methyltransferase Complex with Menin To Regulate Hox Gene Expression

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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. A., et al. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00081-4 · Cited by 645

p300/CBP and cancer

Iyer, N. G., Özdag, H., & Caldas, C. (2004) · Oncogene · doi:10.1038/sj.onc.1207118 · Cited by 638

Phosphorylation of histone H3: a balancing act between chromosome condensation and transcriptional activation

Nowak, S. J., & Corces, V. G. (2004) · Trends in Genetics · doi:10.1016/j.tig.2004.02.007 · Cited by 622

Human SWI/SNF-Associated PRMT5 Methylates Histone H3 Arginine 8 and Negatively Regulates Expression of ST7 and NM23 Tumor Suppressor Genes

Pal, S., Vishwanath, S. N., Erdjument-Bromage, H., Tempst, P., & Sif, S. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.21.9630-9645.2004 · Cited by 592

Mutations truncating the EP300 acetylase in human cancers

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DNA Damage Response Pathway Uses Histone Modification to Assemble a Double-Strand Break-Specific Cohesin Domain

Ünal, E., Arbel-Eden, A., Sattler, U., Shroff, R., Lichten, M., Haber, J. E., & Koshland, D. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.11.027 · Cited by 568

Silent information regulator 2 family of NAD- dependent histone/protein deacetylases generates a unique product, 1- O- acetyl-ADP-ribose

Tanner, K. G., Landry, J., Sternglanz, R., & Denu, J. M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.250422697 · Cited by 555

Methylation of Histone H3 by COMPASS Requires Ubiquitination of Histone H2B by Rad6

Dover, J., Schneider, J., Tawiah-Boateng, M. A., Wood, A., Dean, K., Johnston, M., & Shilatifard, A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200348200 · Cited by 554

Methylation of Histone H4 Lysine 20 Controls Recruitment of Crb2 to Sites of DNA Damage

Sanders, S. L., Portoso, M., Mata, J., Bähler, J., Allshire, R. C., & Kouzarides, T. (2004) · Cell · doi:10.1016/j.cell.2004.11.009 · Cited by 543

Histone Methylation

Bannister, A. J., Schneider, R., & Kouzarides, T. (2002) · Cell · doi:10.1016/s0092-8674(02)00798-5 · Cited by 539

Induction of HDAC2 expression upon loss of APC in colorectal tumorigenesis

Zhu, P., Martin, E., Mengwasser, J., Schlag, P., Janssen, K.-P., & Göttlicher, M. (2004) · Cancer Cell · doi:10.1016/s1535-6108(04)00114-x · Cited by 525

Trans-histone regulatory pathway in chromatin

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Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation

Pray-Grant, M. G., Daniel, J. A., Schieltz, D., Yates, J. R., & Grant, P. A. (2005) · Nature · doi:10.1038/nature03242 · Cited by 515

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

Yang, X.-J. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh252 · Cited by 515

Ordered Cooperative Functions of PRMT1, p300, and CARM1 in Transcriptional Activation by p53

An, W., Kim, J., & Roeder, R. G. (2004) · Cell · doi:10.1016/j.cell.2004.05.009 · Cited by 511

Upregulation and Nuclear Recruitment of HDAC1 in Hormone Refractory Prostate Cancer

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Distribution and Dynamics of Chromatin Modification Induced by a Defined DNA Double-Strand Break

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Histone H3 lysine 9 methylation is an epigenetic imprint of facultative heterochromatin

Peters, A. H. F. M., Mermoud, J. E., O'Carroll, D., Pagani, M., Schweizer, D., Brockdorff, N., & Jenuwein, T. (2002) · Nature Genetics · doi:10.1038/ng789 · Cited by 502

CoREST is an integral component of the CoREST- human histone deacetylase complex

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RNA and Protein Interactions Modulated by Protein Arginine Methylation

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Molecular mechanisms of leukemogenesis mediated by MLL fusion proteins

Ayton, P. M., & Cleary, M. L. (2001) · Oncogene · doi:10.1038/sj.onc.1204639 · Cited by 500

Silencing of human polycomb target genes is associated with methylation of histone H3 Lys 27

Kirmizis, A., Bartley, S. M., Kuzmichev, A., Margueron, R., Reinberg, D., Green, R., & Farnham, P. J. (2004) · Genes & Development · doi:10.1101/gad.1200204 · Cited by 495

Dicer is essential for formation of the heterochromatin structure in vertebrate cells

Fukagawa, T., Nogami, M., Yoshikawa, M., Ikeno, M., Okazaki, T., Takami, Y., Nakayama, T., & Oshimura, M. (2004) · Nature Cell Biology · doi:10.1038/ncb1155 · Cited by 482

Genetic Heterogeneity in Rubinstein-Taybi Syndrome: Mutations in Both the CBP and EP300 Genes Cause Disease

Roelfsema, J. H., White, S. J., Ariyürek, Y., Bartholdi, D., Niedrist, D., Papadia, F., Bacino, C. A., den Dunnen, J. T., van Ommen, G.-J. B., Breuning, M. H., et al. (2005) · The American Journal of Human Genetics · doi:10.1086/429130 · Cited by 478

Menin and MLL cooperatively regulate expression of cyclin-dependent kinase inhibitors

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Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1

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Gene dose-dependent control of hematopoiesis and hematologic tumor suppression by CBP

Kung, A. L., Rebel, V. I., Bronson, R. T., Ch'ng, L.-E., Sieff, C. A., Livingston, D. M., & Yao, T.-P. (2000) · Genes & Development · doi:10.1101/gad.14.3.272 · Cited by 440

Structure of the Catalytic Domain of Human DOT1L, a Non-SET Domain Nucleosomal Histone Methyltransferase

Min, J., Feng, Q., Li, Z., Zhang, Y., & Xu, R.-M. (2003) · Cell · doi:10.1016/s0092-8674(03)00114-4 · Cited by 428

TET1, a member of a novel protein family, is fused to MLL in acute myeloid leukemia containing the t(10;11)(q22;q23)

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Trimethylated lysine 9 of histone H3 is a mark for DNA methylation in Neurospora crassa

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Differentially methylated forms of histone H3 show unique association patterns with inactive human X chromosomes

Boggs, B. A., Cheung, P., Heard, E., Spector, D. L., Chinault, A. C., & Allis, C. D. (2002) · Nature Genetics · doi:10.1038/ng787 · Cited by 378

Histone variants: deviants?

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The Set2 Histone Methyltransferase Functions through the Phosphorylated Carboxyl-terminal Domain of RNA Polymerase II

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Snf1--a Histone Kinase That Works in Concert with the Histone Acetyltransferase Gcn5 to Regulate Transcription

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The c-MYC Oncoprotein Is a Substrate of the Acetyltransferases hGCN5/PCAF and TIP60

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Expression Profile of Histone Deacetylase 1 in Gastric Cancer Tissues

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