Chemical mechanisms of histone lysine and arginine modifications

Translating the Histone Code

Jenuwein, T., & Allis, C. D. (2001) · Science · doi:10.1126/science.1063127 · Cited by 9,756 · see citing works

Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase

Imai, S.-I., Armstrong, C. M., Kaeberlein, M., & Guarente, L. (2000) · Nature · doi:10.1038/35001622 · Cited by 3,510 · see citing works

Histone demethylation by a family of JmjC domain-containing proteins

Tsukada, Y.-I., Fang, J., Erdjument‐Bromage, H., Warren, M., Borchers, C. H., Tempst, P., & Zhang, Y. (2005) · Nature · doi:10.1038/nature04433 · Cited by 2,171 · see citing works

Histone Acetyltransferases

Dent, S., Denu, J. M., & Allis, C. D. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.81 · Cited by 1,844 · see citing works

Twenty-Five Years of the Nucleosome, Fundamental Particle of the Eukaryote Chromosome

Kornberg, R. D., & Lorch, Y. (1999) · Cell · doi:10.1016/s0092-8674(00)81958-3 · Cited by 1,833 · see citing works

Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis

Gregoretti, I., Lee, Y.-M., & Goodson, H. V. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.02.006 · Cited by 1,456 · see citing works

Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins

Frye, R. A. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3000 · Cited by 1,409 · see citing works

Histones and histone modifications

Peterson, C. L., & Laniel, M.-A. (2004) · Current Biology · doi:10.1016/j.cub.2004.07.007 · Cited by 1,313 · see citing works

Dimethyl sulfoxide to vorinostat: development of this histone deacetylase inhibitor as an anticancer drug

Marks, P. A., & Breslow, R. (2007) · Nature Biotechnology · doi:10.1038/nbt1272 · Cited by 1,198 · see citing works

SIRT4 Inhibits Glutamate Dehydrogenase and Opposes the Effects of Calorie Restriction in Pancreatic β Cells

Haigis, M. C., Mostoslavsky, R., Haigis, K. M., Fahie, K., Christodoulou, D. C., Murphy, A. J., Valenzuela, D. M., Yancopoulos, G. D., Karow, M., Blander, G., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.057 · Cited by 1,162 · see citing works

SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin

Michishita, E., McCord, R. A., Berber, E., Kioi, M., Padilla-Nash, H., Damian, M., Cheung, P., Kusumoto, R., Kawahara, T. L. A., Barrett, J. C., et al. (2008) · Nature · doi:10.1038/nature06736 · Cited by 1,111 · see citing works

Arginine Methylation

Bedford, M. T., & Richard, S. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.003 · Cited by 1,106 · see citing works

Chromatin Modifications by Methylation and Ubiquitination: Implications in the Regulation of Gene Expression

Shilatifard, A. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142422 · Cited by 1,099 · see citing works

Histone deacetylases and cancer

Glozak, M. A., & Seto, E. (2007) · Oncogene · doi:10.1038/sj.onc.1210610 · Cited by 1,031 · see citing works

Human PAD4 Regulates Histone Arginine Methylation Levels via Demethylimination

Wang, Y., Wysocka, J., Sayegh, J., Lee, Y., 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 1,013 · see citing works

SMART 4.0: towards genomic data integration

Letunić, I. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkh088 · Cited by 997 · see citing works

PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease

Vossenaar, E. R., Zendman, A. J. W., VENROOIJ, W. J. V., & Pruijn, G. J. M. (2003) · BioEssays · doi:10.1002/bies.10357 · Cited by 986 · see citing works

The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases

Landry, J., Sutton, A., Tafrov, S. T., Heller, R. C., Stebbins, J., Pillus, L., & Sternglanz, R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.110148297 · Cited by 970 · see citing works

New nomenclature for chromatin-modifying enzymes

Allis, C. D., Berger, S. L., Cote, J., Dent, S., Jenuwien, T., Kouzarides, T., Pillus, L., Reinberg, D., Shi, Y., Shiekhattar, R., et al. (2007) · Cell · doi:10.1016/j.cell.2007.10.039 · Cited by 957 · see citing works

Fe(II)/α-Ketoglutarate-Dependent Hydroxylases and Related Enzymes

Hausinger, R. P. (2004) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230490440541 · Cited by 937 · see citing works

Many paths to methyltransfer: a chronicle of convergence

Schubert, H. L., Blumenthal, R. M., & Cheng, X. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(03)00090-2 · Cited by 876 · see citing works

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

Feng, Q. F., Wang, H., Ng, H., Erdjument‐Bromage, H., Tempst, P., Struhl, K., & Zhang, Y. (2002) · Current Biology · doi:10.1016/s0960-9822(02)00901-6 · Cited by 866 · see citing works

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 · see citing works

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 840 · see citing works

Characterization of Five Human cDNAs with Homology to the Yeast SIR2 Gene: Sir2-like Proteins (Sirtuins) Metabolize NAD and May Have Protein ADP-Ribosyltransferase Activity

Frye, R. A. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0897 · Cited by 809 · see citing works

Lysine propionylation and butyrylation are novel post-translational modifications in histones

Chen, Y., Sprung, R., Tang, Y., Ball, H., Sangras, B., Kim, S. C., Falck, J. R., Peng, J., Gu, W., & Zhao, Y. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700021-mcp200 · Cited by 764 · see citing works

Enzymatic Activity Associated with Class II HDACs Is Dependent on a Multiprotein Complex Containing HDAC3 and SMRT/N-CoR

Fischle, W., Dequiedt, F., Hendzel, M. J., Guenther, M. G., Lazar, M. A., Voelter, W., & Verdin, E. (2002) · Molecular Cell · doi:10.1016/s1097-2765(01)00429-4 · Cited by 754 · see citing works

JMJD6 Is a Histone Arginine Demethylase

Chang, B., Chen, Y., Zhao, Y., & Bruick, R. K. (2007) · Science · doi:10.1126/science.1145801 · Cited by 746 · see citing works

Measuring conformational dynamics of biomolecules by single molecule fluorescence spectroscopy.

Weiss, S. (2000) · Nature Structural Biology · doi:10.1038/78941 · Cited by 723 · see citing works

Structural Snapshots of Human HDAC8 Provide Insights into the Class I Histone Deacetylases

Somoza, J. R., Skene, R. J., Katz, B. A., Mol, C., Ho, J. D., Jennings, A. J., Luong, C., Arvai, A., Buggy, J. J., Chi, E., et al. (2004) · Structure · doi:10.1016/j.str.2004.04.012 · Cited by 710 · cited 5× · 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 versus histone acetylation: new insights into epigenetic regulation

Rice, J. C., & Allis, C. D. (2001) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00208-8 · Cited by 701 · see citing works

Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going?

Hassa, P. O., Haenni, S. S., Elser, M., & Hottiger, M. O. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00040-05 · Cited by 682 · see citing works

Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor

Vannini, A., Volpari, C., Filocamo, G., Casavola, E. C., Brunetti, M., Renzoni, D., Chakravarty, P., Paolini, C., De Francesco, R., Gallinari, P., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404603101 · Cited by 638 · see citing works

Sirtuins in aging and age-related disease

Longo, V. D., & Kennedy, B. K. (2006) · Cell · doi:10.1016/j.cell.2006.07.002 · Cited by 628 · see citing works

The Occurence of C–H · · · O Hydrogen Bonds in Proteins

Derewenda, Z. S., Lee, L., & Derewenda, U. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1995.0492 · Cited by 568 · see citing works

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. W., Sternglanz, R., & Denu, J. M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.250422697 · Cited by 557 · see citing works

Mouse Sir2 Homolog SIRT6 Is a Nuclear ADP-ribosyltransferase

Liszt, G., Ford, E., Kurtev, M., & Guarente, L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413296200 · Cited by 548 · see citing works

Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein associationPreprint

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 536 · see citing works

Something about SUMO inhibits transcription

Gill, G. (2005) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2005.07.004 · Cited by 498 · see citing works

The structural basis of protein acetylation by the p300/CBP transcriptional coactivator

Liu, X., Wang, L., Zhao, K., Thompson, P. R., Hwang, Y., Marmorstein, R., & Cole, P. A. (2008) · Nature · doi:10.1038/nature06546 · Cited by 454 · see citing works

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

Min, J., Feng, Q. F., Li, Z., Zhang, Y., & Xu, R.-M. (2003) · Cell · doi:10.1016/s0092-8674(03)00114-4 · Cited by 431 · see citing works

Structural basis for Ca2+-induced activation of human PAD4

Arita, K., Hashimoto, H., Shimizu, T., Nakashima, K., Yamada, M., & Sato, M. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb799 · Cited by 425 · 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

An Enzymatic Activity in the Yeast Sir2 Protein that Is Essential for Gene Silencing

Tanny, J. C., Dowd, G. J., Huang, J., Hilz, H., & Moazed, D. (1999) · Cell · doi:10.1016/s0092-8674(00)81671-2 · Cited by 391 · see citing works

Fluorescence and optical characteristics of reduced flavines and flavoproteins

Ghisla, S., Massey, V., Lhoste, J., & Mayhew, S. G. (1974) · Biochemistry · doi:10.1021/bi00700a029 · Cited by 387 · see citing works

Structure and catalytic mechanism of the human histone methyltransferase SET7/9

Xiao, B., Jing, C., Wilson, J. R., Walker, P. A., Vasisht, N., Kelly, G. P., Howell, S. A., Taylor, I. A., Blackburn, G. M., & Gamblin, S. J. (2003) · Nature · doi:10.1038/nature01378 · Cited by 384 · see citing works

Structure of the Predominant Protein Arginine Methyltransferase PRMT1 and Analysis of Its Binding to Substrate Peptides

Zhang, X., & Cheng, X. (2003) · Structure · doi:10.1016/s0969-2126(03)00071-6 · Cited by 361 · 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

Regulation of histone deacetylase activities

Sengupta, N., & Seto, E. (2004) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20179 · Cited by 348 · see citing works

The Novel Human Protein Arginine N-Methyltransferase PRMT6 Is a Nuclear Enzyme Displaying Unique Substrate Specificity

Frankel, A., Yadav, N., Lee, J. H., Branscombe, T. L., Clarke, S. G., & Bedford, M. T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108786200 · Cited by 337 · see citing works

Structural Basis for the Product Specificity of Histone Lysine Methyltransferases

Zhang, X., Yang, Z., Khan, S. I., Horton, J. R., Tamaru, H., Selker, E. U., & Cheng, X. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00224-7 · Cited by 330 · see citing works

Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity

Ng, S. S., Kavanagh, K. L., McDonough, M. A., Butler, D. S., Pilka, E. S., Liénard, B. M. R., Bray, J. E., Savitsky, P. A., Gileadi, O., von Delft, F., et al. (2007) · Nature · doi:10.1038/nature05971 · Cited by 329 · see citing works

PRMT 3, a Type I Protein Arginine N-Methyltransferase That Differs from PRMT1 in Its Oligomerization, Subcellular Localization, Substrate Specificity, and Regulation

Tang, J., Gary, J. D., Clarke, S. G., & Herschman, H. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.27.16935 · Cited by 317 · see citing works

SET domain protein lysine methyltransferases: Structure, specificity and catalysis

Qian, C., & Zhou, M. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-006-6274-5 · Cited by 316 · see citing works

Crystal structure of the conserved core of protein arginine methyltransferase PRMT3

Zhang, X., Zhou, L., & Cheng, X. (2000) · The EMBO Journal · doi:10.1093/emboj/19.14.3509 · Cited by 314 · see citing works

Strength of the CαH··O Hydrogen Bond of Amino Acid Residues

Scheiner, S., Kar, T., & Gu, Y. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010770200 · Cited by 306 · see citing works

Chemistry of Gene Silencing: The Mechanism of NAD+-Dependent Deacetylation Reactions

Sauve, A. A., Celic, I., Avalos‬, J. L., Deng, H., Boeke, J. D., & Schramm, V. L. (2001) · Biochemistry · doi:10.1021/bi011858j · Cited by 301 · see citing works

Splicing regulates NAD metabolite binding to histone macroH2A

Kustatscher, G., Hothorn, M., Pugieux, C., Scheffzek, K., & Ladurner, A. G. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb956 · Cited by 300 · see citing works

Disruptor of Telomeric Silencing-1 Is a Chromatin-specific Histone H3 Methyltransferase

Lacoste, N., Utley, R. T., Hunter, J. M., Poirier, G. G., & Côté, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200366200 · Cited by 298 · see citing works

Inhibitors and Inactivators of Protein Arginine Deiminase 4: Functional and Structural Characterization ,

Luo, Y., Arita, K., Bhatia, M., Knuckley, B., Lee, Y., Stallcup, M. R., Sato, M., & Thompson, P. R. (2006) · Biochemistry · doi:10.1021/bi061180d · Cited by 293 · see citing works

CALCIUM IN CELL INJURY AND DEATH

Dong, Z., Saikumar, P., Weinberg, J. M., & Venkatachalam, M. A. (2006) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev.pathol.1.110304.100218 · Cited by 293 · see citing works

Unsafe SETs: histone lysine methyltransferases and cancer

Schneider, R., Bannister, A. J., & Kouzarides, T. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)02141-2 · Cited by 287 · see citing works

Histone demethylation catalysed by LSD1 is a flavin‐dependent oxidative process

Forneris, F., Binda, C., Vanoni, M. A., Mattevi, A., & Battaglioli, E. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.03.015 · Cited by 284 · see citing works

Purification and partial characterization of a nucleolar scleroderma antigen (Mr = 34,000; pI, 8.5) rich in NG,NG-dimethylarginine.

Lischwe, M. A., Ochs, R. L., Reddy, R., Cook, R. G., Yeoman, L. C., Tan, E. M., Reichlin, M., & Busch, H. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38718-5 · Cited by 276 · see citing works

Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase

Couture, J., Collazo, E., Ortiz-Tello, P. A., Brunzelle, J. S., & Trievel, R. C. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1273 · Cited by 276 · see citing works

The Sirtuin family: therapeutic targets to treat diseases of aging

Milne, J. C., & Denu, J. M. (2008) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2008.01.019 · Cited by 271 · see citing works

Chemistry of acetyl transfer by histone modifying enzymes: structure, mechanism and implications for effector design

Hodawadekar, S. C., & Marmorstein, R. (2007) · Oncogene · doi:10.1038/sj.onc.1210619 · Cited by 271 · see citing works

Assembly of the SIR Complex and Its Regulation by O-Acetyl-ADP-Ribose, a Product of NAD-Dependent Histone Deacetylation

Liou, G., Tanny, J. C., Kruger, R. G., Walz, T., & Moazed, D. (2005) · Cell · doi:10.1016/j.cell.2005.03.035 · Cited by 260 · see citing works

Substrate binding to histone deacetylases as shown by the crystal structure of the HDAC8–substrate complex

Vannini, A., Volpari, C., Gallinari, P., Jones, P., Mattu, M., Carfí, A., De Francesco, R., Steinkühler, C., & Di Marco, S. (2007) · The EMBO Reports · doi:10.1038/sj.embor.7401047 · Cited by 256 · see citing works

Structure of the Neurospora SET Domain Protein DIM-5, a Histone H3 Lysine Methyltransferase

Zhang, X., Tamaru, H., Khan, S. I., Horton, J. R., Keefe, L. J., Selker, E. U., & Cheng, X. (2002) · Cell · doi:10.1016/s0092-8674(02)00999-6 · Cited by 250 · see citing works

Increased Citrullination of Histone H3 in Multiple Sclerosis Brain and Animal Models of Demyelination: A Role for Tumor Necrosis Factor-Induced Peptidylarginine Deiminase 4 Translocation

Mastronardi, F. G., Wood, D. D., Jiang, M., Raijmakers, R., Tseveleki, V., Dosch, H., Probert, L., Casaccia‐Bonnefil, P., & Moscarello, M. A. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.3349-06.2006 · Cited by 250 · see citing works

Structural Basis of LSD1-CoREST Selectivity in Histone H3 Recognition

Forneris, F., Binda, C., Adamo, A., Battaglioli, E., & Mattevi, A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.c700100200 · Cited by 239 · see citing works

Mechanism of Nicotinamide Inhibition and Transglycosidation by Sir2 Histone/Protein Deacetylases

Jackson, M. D., Schmidt, M. T., Oppenheimer, N. J., & Denu, J. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306552200 · Cited by 238 · see citing works

Histone arginine methylation and its dynamic regulation

Wysocka, J. (2006) · Frontiers in bioscience · doi:10.2741/1802 · Cited by 233 · see citing works

Nucleosome and chromatin fiber dynamics

Luger, K., & Hansen, J. C. (2005) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2005.03.006 · Cited by 227 · see citing works

Catalytic Mechanism and Function of Invariant Glutamic Acid 173 from the Histone Acetyltransferase GCN5 Transcriptional Coactivator

Tanner, K. G., Trievel, R. C., Kuo, M., Howard, R. M., Berger, S. L., Allis, C. D., Marmorstein, R., & Denu, J. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.26.18157 · Cited by 221 · see citing works

Sir2 Regulation by Nicotinamide Results from Switching between Base Exchange and Deacetylation Chemistry

Sauve, A. A., & Schramm, V. L. (2003) · Biochemistry · doi:10.1021/bi034959l · Cited by 216 · see citing works

Non-heme dioxygenases: cellular sensors and regulators jelly rolled into one?

Ozer, A., & Bruick, R. K. (2007) · Nature Chemical Biology · doi:10.1038/nchembio863 · Cited by 214 · see citing works

Substrate Specificity and Kinetic Mechanism of the Sir2 Family of NAD+-Dependent Histone/Protein Deacetylases

Borra, M. T., Langer, M. R., Slama, J. T., & Denu, J. M. (2004) · Biochemistry · doi:10.1021/bi049592e · Cited by 214 · see citing works

Kinetic Characterization of Protein Arginine Deiminase 4: A Transcriptional Corepressor Implicated in the Onset and Progression of Rheumatoid Arthritis

Kearney, P. L., Bhatia, M., Jones, N. G., Yuan, L., Glascock, M. C., Catchings, K. L., Yamada, M., & Thompson, P. R. (2005) · Biochemistry · doi:10.1021/bi050292m · Cited by 213 · see citing works

Structural Identification of 2′- and 3′-O-Acetyl-ADP-ribose as Novel Metabolites Derived from the Sir2 Family of β-NAD+-dependent Histone/Protein Deacetylases

Jackson, M. D., & Denu, J. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200671200 · Cited by 212 · see citing works

How does the histone code work?

Cosgrove, M. S., & Wolberger, C. (2005) · Biochemistry and Cell Biology · doi:10.1139/o05-137 · Cited by 210 · see citing works

Aberrant expression of CARM1, a transcriptional coactivator of androgen receptor, in the development of prostate carcinoma and androgen‐independent status

Hong, H., Kao, C. H., Jeng, M., Eble, J. N., Koch, M. O., Gardner, T. A., Zhang, S., Li, L., Pan, C.-X., Hu, Z., et al. (2004) · Cancer · doi:10.1002/cncr.20327 · Cited by 205 · see citing works

N-Lysine Propionylation Controls the Activity of Propionyl-CoA Synthetase

Garrity, J., Gardner, J. G., Hawse, W. F., Wolberger, C., & Escalante‐Semerena, J. C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704409200 · Cited by 203 · see citing works

PRMT7 Is a Member of the Protein Arginine Methyltransferase Family with a Distinct Substrate Specificity

Miranda, T. B., Miranda, M., Frankel, A., & Clarke, S. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312904200 · Cited by 194 · see citing works

Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD + -dependent Sir2 histone/protein deacetylases

Zhao, K., Harshaw, R. B., Chai, X., & Marmorstein, R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401057101 · Cited by 186 · 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

SET domains and histone methylation

Xiao, B., Wilson, J. R., & Gamblin, S. J. (2003) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2003.10.003 · Cited by 165 · see citing works

Functional insights from structures of coactivator‐associated arginine methyltransferase 1 domains

Troffer-Charlier, N., Cura, V., Hassenboehler, P., Moras, D., & Cavarelli, J. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601855 · Cited by 165 · see citing works

Crystal Structure of Yeast Esa1 Suggests a Unified Mechanism for Catalysis and Substrate Binding by Histone Acetyltransferases

Yan, Y. C., Barlev, N. A., Haley, R., Berger, S. L., & Marmorstein, R. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00116-7 · Cited by 164 · see citing works

Methylation of Arginine Residues Interferes with Citrullination by Peptidylarginine Deiminases in vitro

Raijmakers, R., Zendman, A. J. W., Egberts, W. V., Vossenaar, E. R., Raats, J., Soede-Huijbregts, C., Rutjes, F. P. J. T., van Veelen, P. A., Drijfhout, J. W., & Pruijn, G. J. M. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.01.054 · Cited by 163 · see citing works

The structure and oligomerization of the yeast arginine methyltransferase, Hmt1.

Silver, P. A., Hogle, J. M., Weiss, V. H., McBride, A. E., Soriano, M. A., & Filman, D. J. (2000) · Nature Structural Biology · doi:10.1038/82028 · Cited by 161 · see citing works

Histone Citrullination by Protein Arginine Deiminase: Is Arginine Methylation a Green Light or a Roadblock?

Thompson, P. R., & Fast, W. L. (2006) · ACS Chemical Biology · doi:10.1021/cb6002306 · Cited by 157 · see citing works

The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate

Yuan, Y., Harper, S. L., Speicher, D. W., & Marmorstein, R. (2002) · Nature Structural Biology · doi:10.1038/nsb849 · Cited by 156 · see citing works

Conserved Enzymatic Production and Biological Effect of O-Acetyl-ADP-ribose by Silent Information Regulator 2-like NAD+-dependent Deacetylases

Borra, M. T., O'Neill, F. J., Jackson, M. D., Marshall, B. L., Verdin, E. M., Foltz, K. R., & Denu, J. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111830200 · Cited by 155 · see citing works

Metabolite of SIR2 Reaction Modulates TRPM2 Ion Channel

Grubisha, O., Rafty, L. A., Takanishi, C. L., Xu, X., Tong, L., Perraud, A., Scharenberg, A. M., & Denu, J. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513741200 · Cited by 154 · see citing works

A Fluoroacetamidine-Based Inactivator of Protein Arginine Deiminase 4: Design, Synthesis, and in Vitro and in Vivo Evaluation

Luo, Y., Knuckley, B., Lee, Y., Stallcup, M. R., & Thompson, P. R. (2006) · Journal of the American Chemical Society · doi:10.1021/ja0576233 · Cited by 153 · see citing works

Structure and Mechanism of Lysine-specific Demethylase Enzymes

Anand, R., & Marmorstein, R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.r700027200 · Cited by 153 · see citing works

Structural Basis for the Mechanism and Regulation of Sir2 Enzymes

Avalos‬, J. L., Boeke, J. D., & Wolberger, C. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00082-6 · Cited by 152 · see citing works

Catalytic Activity and Inhibition of Human Histone Deacetylase 8 Is Dependent on the Identity of the Active Site Metal Ion

Gantt, S. L., Gattis, S. G., & Fierke, C. A. (2006) · Biochemistry · doi:10.1021/bi060212u · Cited by 151 · see citing works

Neuronal protection by sirtuins in Alzheimer's disease

Anekonda, T. S., & Reddy, P. H. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03492.x · Cited by 150 · see citing works

Substrate Specificity and Kinetic Mechanism of Mammalian G9a Histone H3 Methyltransferase

Patnaik, D., Chin, H. G., Estève, P., Benner, J. S., Jacobsen, S. E., & Pradhan, S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409604200 · Cited by 147 · see citing works

Kinetic Mechanism of the Histone Acetyltransferase GCN5 from Yeast

Tanner, K. G., Langer, M. R., Kim, Y., & Denu, J. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002893200 · Cited by 146 · see citing works

Unusual Sites of Arginine Methylation in Poly(A)-binding Protein II and in Vitro Methylation by Protein Arginine Methyltransferases PRMT1 and PRMT3

Smith, J. J., Rücknagel, K. P., Schierhorn, A., Tang, J., Németh, A., Linder, M., Herschman, H. R., & Wahle, E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.19.13229 · Cited by 146 · see citing works

Involvement of arginine methyltransferase CARM1 in androgen receptor function and prostate cancer cell viability

Majumder, S., Liu, Y., Ford, O. H., Mohler, J. L., & Whang, Y. E. (2006) · The Prostate · doi:10.1002/pros.20438 · Cited by 146 · see citing works

Mechanism-Based Inhibition of Sir2 Deacetylases by Thioacetyl-Lysine Peptide

Smith, B. C., & Denu, J. M. (2007) · Biochemistry · doi:10.1021/bi7013294 · Cited by 144 · see citing works

LSD1 and the chemistry of histone demethylation

Culhane, J. C., & Cole, P. A. (2007) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2007.07.014 · Cited by 143 · see citing works

Structural basis of the recognition of a methylated histone tail by JMJD2A

Chen, Z., Zang, J., Kappler, J. W., Hong, X., Crawford, F., Wang, Q., Lan, F., Jiang, C., Whetstine, J. R., Dai, S., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0704525104 · Cited by 142 · see citing works

Insights into the Sirtuin Mechanism from Ternary Complexes Containing NAD+ and Acetylated Peptide

Hoff, K. G., Avalos‬, J. L., Sens, K. L., & Wolberger, C. (2006) · Structure · doi:10.1016/j.str.2006.06.006 · Cited by 141 · see citing works

Acetyl-lysine Analog Peptides as Mechanistic Probes of Protein Deacetylases

Smith, B. C., & Denu, J. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707878200 · Cited by 139 · see citing works

Catalytic Mechanism and Product Specificity of the Histone Lysine Methyltransferase SET7/9: An ab Initio QM/MM-FE Study with Multiple Initial Structures

Hu, P., & Zhang, Y. (2006) · Journal of the American Chemical Society · doi:10.1021/ja056153+ · Cited by 138 · see citing works

Stopped-Flow Kinetic Analysis ofEscherichia coliTaurine/α-Ketoglutarate Dioxygenase: Interactions with α-Ketoglutarate, Taurine, and Oxygen

Ryle, M. J., Padmakumar, R., & Hausinger, R. P. (1999) · Biochemistry · doi:10.1021/bi9912746 · Cited by 137 · see citing works

Clustering of glycine and NG,NG-dimethylarginine in nucleolar protein C23

Lischwe, M. A., Cook, R. G., Ahn, Y. S., Yeoman, L. C., & Busch, H. (1985) · Biochemistry · doi:10.1021/bi00343a001 · Cited by 136 · see citing works

A Highly Specific Mechanism of Histone H3-K4 Recognition by Histone Demethylase LSD1

Forneris, F., Binda, C., Dall'Aglio, A., Fraaije, M. W., Battaglioli, E., & Mattevi, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607411200 · Cited by 135 · see citing works

Protein Arginine Methyltransferase 1: Positively Charged Residues in Substrate Peptides Distal to the Site of Methylation Are Important for Substrate Binding and Catalysis

Osborne, T. C., Obianyo, O., Zhang, X., Cheng, X., & Thompson, P. R. (2007) · Biochemistry · doi:10.1021/bi701558t · Cited by 135 · see citing works

Insights into histone code syntax from structural and biochemical studies of CARM1 methyltransferase

Yue, W. W., Hassler, M., Roe, S. M., Thompson-Vale, V., & Pearl, L. H. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601856 · Cited by 134 · see citing works

Catalytic Mechanism of a MYST Family Histone Acetyltransferase

Berndsen, C., Albaugh, B. N., Tan, S., & Denu, J. M. (2006) · Biochemistry · doi:10.1021/bi602513x · Cited by 133 · see citing works

Fungal Rtt109 histone acetyltransferase is an unexpected structural homolog of metazoan p300/CBP

Tang, Y., Holbert, M. A., Würtele, H., Meeth, K. M., Rocha, W., Gharib, M., Jiang, E., Thibault, P., Verreault, A., Cole, P. A., et al. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1448 · Cited by 133 · see citing works

Transcriptional Coactivator Protein p300

Thompson, P. R., Kurooka, H., Nakatani, Y., & Cole, P. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104736200 · Cited by 132 · see citing works

Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT

Trievel, R. C., Flynn, E. M., Houtz, R. L., & Hurley, J. H. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb946 · Cited by 128 · see citing works

A chromosomal SIR2 homologue with both histone NAD‐dependent ADP‐ribosyltransferase and deacetylase activities is involved in DNA repair in Trypanosoma brucei

Garcia-Salcedo, J. A., Gijón, P., Nolan, D. P., Tebabi, P., & Pays, E. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg553 · Cited by 127 · see citing works

Structure of the Conserved Core of the Yeast Dot1p, a Nucleosomal Histone H3 Lysine 79 Methyltransferase

Sawada, K., Yang, Z., Horton, J. R., Collins, R. E., Zhang, X., & Cheng, X. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405902200 · Cited by 126 · see citing works

Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9—AdoMet

Kwon, T., Chang, J. H., Kwak, E., Lee, C. W., Joachimiak, A., Kim, Y. C., Lee, J. W., & Cho, Y. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg025 · Cited by 125 · see citing works

A mechanism for mitochondrial monoamine oxidase catalyzed amine oxidation

Silverman, R. B., Hoffman, S. J., & Catus, W. B. (1980) · Journal of the American Chemical Society · doi:10.1021/ja00543a052 · Cited by 123 · see citing works

The active site of the SET domain is constructed on a knot

Jacobs, S. A., Harp, J. M., Devarakonda, S., Kim, Y., Rastinejad, F., & Khorasanizadeh, S. (2002) · Nature Structural Biology · doi:10.1038/nsb861 · Cited by 117 · see citing works

Epigenetic Regulation of Chromatin Structure and Gene Function by Biotin

Hassan, Y. I., & Zempleni, J. (2006) · Journal of Nutrition · doi:10.1093/jn/136.7.1763 · Cited by 113 · see citing works

Citrullination by Peptidylarginine Deiminase in Rheumatoid Arthritis

Suzuki, A., Yamada, R., & Yamamoto, K. (2007) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1422.034 · Cited by 112 · see citing works

Unexpected Deacetylation Mechanism Suggested by a Density Functional Theory QM/MM Study of Histone-Deacetylase-Like Protein

Corminbœuf, C., Hu, P., Tuckerman, M. E., & Zhang, Y. (2006) · Journal of the American Chemical Society · doi:10.1021/ja0600882 · Cited by 108 · see citing works

Coincidences, decarboxylation, and electrostatic effects

Westheimer, F. H. (1995) · Tetrahedron · doi:10.1016/0040-4020(94)00865-r · Cited by 107 · see citing works

Phosphorylation-mediated inactivation of coactivator-associated arginine methyltransferase 1

Higashimoto, K., Kuhn, P., Desai, D., Cheng, X., & Xu, W. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0610792104 · Cited by 105 · see citing works

Sir2 Protein Deacetylases: Evidence for Chemical Intermediates and Functions of a Conserved Histidine

Smith, B. C., & Denu, J. M. (2005) · Biochemistry · doi:10.1021/bi052014t · Cited by 101 · see citing works

Benzoate 1,2-Dioxygenase from Pseudomonas putida: Single Turnover Kinetics and Regulation of a Two-Component Rieske Dioxygenase

Wolfe, M. D., Altier, D. J., Stubna, A., Popescu, C. V., Münck, E., & Lipscomb, J. D. (2002) · Biochemistry · doi:10.1021/bi025912n · Cited by 101 · see citing works

Mechanistic Analysis of a Suicide Inactivator of Histone Demethylase LSD1

Szewczuk, L. M., Culhane, J. C., Yang, M., Majumdar, A. K., Yu, H., & Cole, P. A. (2007) · Biochemistry · doi:10.1021/bi700414b · Cited by 100 · see citing works

Mechanism of histone methylation catalyzed by protein lysine methyltransferase SET7/9 and origin of product specificity

Guo, H., & Guo, H. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702981104 · Cited by 98 · see citing works

Protein Arginine Deiminase 4: Evidence for a Reverse Protonation Mechanism

Knuckley, B., Bhatia, M., & Thompson, P. R. (2007) · Biochemistry · doi:10.1021/bi700095s · Cited by 98 · see citing works

Effect of Solvent upon CH···O Hydrogen Bonds with Implications for Protein Folding

Scheiner, S., & Kar, T. (2005) · The Journal of Physical Chemistry B · doi:10.1021/jp0446736 · Cited by 97 · see citing works

Expression of nitric oxide related enzymes in coronary heart disease

Chen, X., Niroomand, F., Liu, Z., Zankl, A. R., Katus, H. A., Jahn, L., & Tiefenbacher, C. (2006) · Basic Research in Cardiology · doi:10.1007/s00395-006-0592-5 · Cited by 97 · see citing works

Crystal Structures of Arginine Deiminase with Covalent Reaction Intermediates

Das, K., Butler, G. H., Kwiatkowski, V., Clark, A. D., Yadav, P. N., & Arnold, E. (2004) · Structure · doi:10.1016/j.str.2004.02.017 · Cited by 90 · see citing works

Kinetics and Comparative Reactivity of Human Class I and Class IIb Histone Deacetylases

Schultz, B. E., Misialek, S., Wu, J., Tang, J., Conn, M. T., Tahilramani, R., & Wong, L. (2004) · Biochemistry · doi:10.1021/bi0494471 · Cited by 88 · see citing works

Transition State Structure for the Hydrolysis of NAD+Catalyzed by Diphtheria Toxin

Berti, P. J., Blanke, S. R., & Schramm, V. L. (1997) · Journal of the American Chemical Society · doi:10.1021/ja971317a · Cited by 85 · see citing works

Catalytic Roles for Carbon-Oxygen Hydrogen Bonding in SET Domain Lysine Methyltransferases

Couture, J., Hauk, G., Thompson, M. J., Blackburn, G. M., & Trievel, R. C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602257200 · Cited by 83 · see citing works

Enzymatic demethylation of calf thymus histones

Paik, W. K., & Kim, S. (1973) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(73)91383-1 · Cited by 82 · see citing works

How Do SET-Domain Protein Lysine Methyltransferases Achieve the Methylation State Specificity? Revisited by Ab Initio QM/MM Molecular Dynamics Simulations

Hu, P., Wang, S., & Zhang, Y. (2008) · Journal of the American Chemical Society · doi:10.1021/ja075896n · Cited by 81 · see citing works

Sir2 Deacetylases Exhibit Nucleophilic Participation of Acetyl-Lysine in NAD+ Cleavage

Smith, B. C., & Denu, J. M. (2007) · Journal of the American Chemical Society · doi:10.1021/ja070162w · Cited by 81 · see citing works

Steady-State and Transient Kinetic Analyses of Taurine/α-Ketoglutarate Dioxygenase: Effects of Oxygen Concentration, Alternative Sulfonates, and Active-Site Variants on the FeIV-oxo Intermediate

Grzyska, P. K., Ryle, M. J., Monterosso, G. R., Liu, J., Ballou, D. P., & Hausinger, R. P. (2005) · Biochemistry · doi:10.1021/bi048746n · Cited by 76 · see citing works

Catalytic Properties and Kinetic Mechanism of Human Recombinant Lys-9 Histone H3 Methyltransferase SUV39H1: Participation of the Chromodomain in Enzymatic Catalysis

Chin, H. G., Patnaik, D., Estève, P., Jacobsen, S. E., & Pradhan, S. (2006) · Biochemistry · doi:10.1021/bi051997r · Cited by 74 · see citing works

Formaldehyde Cycle and the Phases of Stress Syndrome

Tyihák, E., Trézl, L., & Szende, B. (1998) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1998.tb09001.x · Cited by 66 · see citing works

Crystal Structures Representing the Michaelis Complex and the Thiouronium Reaction Intermediate of Pseudomonas aeruginosa Arginine Deiminase

Galkin, A. G., Lü, X., Dunaway‐Mariano, D., & Herzberg, O. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505471200 · Cited by 66 · see citing works

Transition State Analysis of NAD+Hydrolysis by the Cholera Toxin Catalytic Subunit

Rising, K. A., & Schramm, V. L. (1997) · Journal of the American Chemical Society · doi:10.1021/ja9621915 · Cited by 61 · see citing works

Acetylation-dependent ADP-ribosylation by Trypanosoma brucei Sir2

Kowieski, T. M., Lee, S., & Denu, J. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707613200 · Cited by 58 · see citing works

Functional analysis of the N- and C-terminus of mammalian G9a histone H3 methyltransferase

Esteve, P. O. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki635 · Cited by 57 · see citing works

Kinetic studies of Escherichia coli AlkB using a new fluorescence-based assay for DNA demethylation

Roy, T. W., & Bhagwat, A. S. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm1031 · Cited by 56 · see citing works

Transition-State Structure for the ADP-Ribosylation of Recombinant Giα1 Subunits by Pertussis Toxin

Scheuring, J., Berti, P. J., & Schramm, V. L. (1998) · Biochemistry · doi:10.1021/bi972594x · Cited by 51 · see citing works

[51] Fluorescence and optical characteristics of reduced flavins and flavoproteins

Ghisla, S. (1980) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(80)66481-7 · Cited by 51 · see citing works

Mechanistic Studies of the Flavoenzyme Tryptophan 2-Monooxygenase: Deuterium and 15N Kinetic Isotope Effects on Alanine Oxidation by an l -Amino Acid Oxidase

Ralph, E. C., Anderson, M. A., Cleland, W. W., & Fitzpatrick, P. F. (2006) · Biochemistry · doi:10.1021/bi061894o · Cited by 50 · see citing works

Transition State Structure for ADP-Ribosylation of Eukaryotic Elongation Factor 2 Catalyzed by Diphtheria Toxin

Parikh, S. L., & Schramm, V. L. (2004) · Biochemistry · doi:10.1021/bi035907z · Cited by 49 · see citing works

Pertussis Toxin: Transition State Analysis for ADP-Ribosylation of G-Protein Peptide αi3C20

Scheuring, J., & Schramm, V. L. (1997) · Biochemistry · doi:10.1021/bi970379a · Cited by 48 · see citing works

Biochemical Analysis of the Arginine Methylation of High Molecular Weight Fibroblast Growth Factor-2

Klein, S., Carroll, J. A., Chen, Y., Henry, M. F., Henry, P. A., Ortonowski, I. E., Pintucci, G., Beavis, R. C., Burgess, W. H., & Rifkin, D. B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.5.3150 · Cited by 47 · see citing works

Histone Lysine Methyltransferase SET7/9: Formation of a Water Channel Precedes Each Methyl Transfer

Zhang, X., & Bruice, T. C. (2007) · Biochemistry · doi:10.1021/bi7014579 · Cited by 46 · see citing works

Theoretical study revealing the functioning of a novel combination of catalytic motifs in histone deacetylase

Vanommeslaeghe, K., Proft, F. D., Loverix, S., Tourwé, D. A., & Geerlings, P. (2005) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2005.04.001 · Cited by 46 · see citing works

Kinetic Isotope Effect Characterization of the Transition State for Oxidized Nicotinamide Adenine Dinucleotide Hydrolysis by Pertussis Toxin

Scheuring, J., & Schramm, V. L. (1997) · Biochemistry · doi:10.1021/bi962841h · Cited by 43 · see citing works

Kinetic Manifestation of Processivity during Multiple Methylations Catalyzed by SET Domain Protein Methyltransferases

Dirk, L. M. A., Flynn, E. M., Dietzel, K., Couture, J., Trievel, R. C., & Houtz, R. L. (2007) · Biochemistry · doi:10.1021/bi6023644 · Cited by 43 · see citing works

Strength of Cα−H···OC Hydrogen Bonds in Transmembrane Proteins

Park, H., Yoon, J.-K., & Seok, C. (2007) · The Journal of Physical Chemistry B · doi:10.1021/jp077285n · Cited by 40 · see citing works

Bisubstrate analogue structure?activity relationships for p300 histone acetyltransferase inhibitors

Sagar, V., Zheng, W., Thompson, P. R., & Cole, P. A. (2004) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2004.03.070 · Cited by 37 · see citing works

Mechanism of Product Specificity of AdoMet Methylation Catalyzed by Lysine Methyltransferases: Transcriptional Factor p53 Methylation by Histone Lysine Methyltransferase SET7/9

Zhang, X., & Bruice, T. C. (2008) · Biochemistry · doi:10.1021/bi702370p · Cited by 22 · see citing works

Use of Substrate Analogs and Mutagenesis to Study Substrate Binding and Catalysis in the Sir2 Family of NAD-dependent Protein Deacetylases

Khan, A. N., & Lewis, P. N. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511482200 · Cited by 22 · see citing works

Aberrant Forms of Histone Acetyltransferases in Human Disease

van Beekum, O., & Kalkhoven, E. (2007) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/1-4020-5466-1_11 · Cited by 16 · see citing works

Cellular Mechanisms of NETosis

Thiam, H. R., Wong, S. L., Wagner, D. D., & Waterman, C. M. (2020) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-020520-111016 · Cited by 624 · see citing works

Energetics, epigenetics, mitochondrial genetics

Wallace, D. C., & Fan, W. (2009) · Mitochondrion · doi:10.1016/j.mito.2009.09.006 · Cited by 507 · see citing works

Non-histone protein methylation as a regulator of cellular signalling and function

Biggar, K. K., & Li, S. S.-C. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3915 · Cited by 479 · see citing works

Protein methyltransferases as a target class for drug discovery

Copeland, R. A., Solomon, M. E., & Richon, V. M. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2974 · Cited by 467 · see citing works

Regulation of short-chain fatty acids in the immune system

Liu, X., Shao, J.-H., Liao, Y.-T., Wang, L., Yuan, J., Dong, P.-J., Liu, Z., He, D., Li, C., & Zhang, X. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1186892 · Cited by 435 · see citing works

Arginine: Its pKa value revisited

Fitch, C. A., Platzer, G., Okon, M., Bertrand García‐Moreno, E., & McIntosh, L. P. (2015) · Protein Science · doi:10.1002/pro.2647 · Cited by 386 · see citing works

Critical roles of non-histone protein lysine methylation in human tumorigenesis

Hamamoto, R., Saloura, V., & Nakamura, Y. (2015) · Nature Reviews Cancer · doi:10.1038/nrc3884 · Cited by 376 · see citing works

The Redox Basis of Epigenetic Modifications: From Mechanisms to Functional Consequences

Cyr, A. R., & Domann, F. E. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3492 · Cited by 294 · see citing works

Epigenome manipulation as a pathway to new natural product scaffolds and their congeners

Cichewicz, R. H. (2009) · Natural Product Reports · doi:10.1039/b920860g · Cited by 286 · see citing works

Extracellular Matrix Remodeling: The Common Denominator in Connective Tissue Diseases Possibilities for Evaluation and Current Understanding of the Matrix as More Than a Passive Architecture, but a Key Player in Tissue Failure

Karsdal, M. A., Nielsen, M. J., Sand, J. M. B., Henriksen, K., Genovese, F., Bay‐Jensen, A., Smith, V., Adamkewicz, J. I., Christiansen, C., & Leeming, D. J. (2012) · Assay and Drug Development Technologies · doi:10.1089/adt.2012.474 · Cited by 281 · see citing works

Iminoboronates: A New Strategy for Reversible Protein Modification

Cal, P. M. S. D., Vicente, J. B., Pires, E., Coelho, A. V., Veiros, L. F., CORDEIRO, C. A., & Góis, P. M. P. (2012) · Journal of the American Chemical Society · doi:10.1021/ja303436y · Cited by 279 · see citing works

Histone deacetylase inhibitors (HDACIs): multitargeted anticancer agents

Licciardi, P. V., Ververis, Hiong, & Karagiannis, T. C. (2013) · Biologics · doi:10.2147/btt.s29965 · Cited by 278 · see citing works

Tunable multiphase dynamics of arginine and lysine liquid condensates

Fisher, R. S., & Elbaum‐Garfinkle, S. (2020) · Nature Communications · doi:10.1038/s41467-020-18224-y · Cited by 278 · see citing works

A Novel Mammalian Flavin-dependent Histone Demethylase

Karytinos, A., Forneris, F., Profumo, A., Ciossani, G., Battaglioli, E., Binda, C., & Mattevi, A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.003087 · Cited by 274 · see citing works

Histone Methyl Transferases and Demethylases; Can They Link Metabolism and Transcription?

Teperino, R., Schoonjans, K., & Auwerx, J. H. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.09.004 · Cited by 270 · see citing works

Clinical and Experimental Applications of Sodium Phenylbutyrate

Iannitti, T., & Palmieri, B. (2011) · Drugs in R&D · doi:10.2165/11591280-000000000-00000 · Cited by 270 · see citing works

Structural Biology of Human H3K9 Methyltransferases

Wu, H., Min, J., Lunin, V. V., Antoshenko, T., Dombrovski, L., Zeng, H., Allali-Hassani, A., Campagna-Slater, V., Vedadi, M., Arrowsmith, C. H., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008570 · Cited by 268 · see citing works

Epigenetic phenomena linked to diabetic complications

Pirola, L., Balcerczyk, A., Okabe, J., & El-Osta, A. (2010) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2010.188 · Cited by 239 · see citing works

Trials with ‘epigenetic’ drugs: An update

Nebbioso, A., Carafa, V., Benedetti, R., & Altucci, L. (2012) · Molecular Oncology · doi:10.1016/j.molonc.2012.09.004 · Cited by 237 · see citing works

The protein arginine methyltransferase family: an update about function, new perspectives and the physiological role in humans

Wolf, S. S. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0010-x · Cited by 236 · see citing works

EZH2: biology, disease, and structure-based drug discovery

Tan, J., Yan, Y., Wang, X., Jiang, Y., & Xu, H. E. (2013) · Acta Pharmacologica Sinica · doi:10.1038/aps.2013.161 · Cited by 234 · see citing works

Epigenetic regulation in major depression and other stress-related disorders: molecular mechanisms, clinical relevance and therapeutic potential

Yuan, M., Yang, B., Rothschild, G., Mann, J. J., Sanford, L. D., Tang, X., Huang, C., Wang, C., & Zhang, W. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01519-z · Cited by 246 · see citing works

pH-dependent random coil 1H, 13C, and 15N chemical shifts of the ionizable amino acids: a guide for protein pK a measurements

Platzer, G., Okon, M., & McIntosh, L. P. (2014) · Journal of Biomolecular NMR · doi:10.1007/s10858-014-9862-y · Cited by 234 · see citing works

Coordinated Chromatin Control: Structural and Functional Linkage of DNA and Histone Methylation

Cheng, X., & Blumenthal, R. (2010) · Biochemistry · doi:10.1021/bi100213t · Cited by 217 · see citing works

Dietary Compounds as Epigenetic Modulating Agents in Cancer

Carlos‐Reyes, Á., López-González, J. S., Meneses-Flores, M., Gallardo‐Rincón, D., Ruíz‐García, E., Marchat, L. A., la Vega, H. A., la Cruz, O. N. H.-D., & López‐Camarillo, C. (2019) · Frontiers in Genetics · doi:10.3389/fgene.2019.00079 · Cited by 214 · see citing works

Targeting epigenetic and posttranslational modifications regulating ferroptosis for the treatment of diseases

Wang, Y., Hu, J., Wu, S., Fleishman, J. S., Li, Y., Xu, Y.-S., Zou, W., Wang, J., Feng, Y., Chen, J., et al. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01720-0 · Cited by 218 · see citing works

Antioxidants and HNE in redox homeostasis

Łuczaj, W., Gęgotek, A., & Skrzydlewska, E. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.11.033 · Cited by 197 · see citing works

Cell signaling, post-translational protein modifications and NMR spectroscopy

Theillet, F., Smet‐Nocca, C., Liokatis, S., Thongwichian, R., Kosten, J., Yoon, M., Kriwacki, R. W., Landrieu, I., Lippens, G. M., & Selenko, P. (2012) · Journal of Biomolecular NMR · doi:10.1007/s10858-012-9674-x · Cited by 188 · see citing works

Nicotinamide is an inhibitor of SIRT1 in vitro, but can be a stimulator in cells

Hwang, E. S., & Song, S. B. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2527-8 · Cited by 178 · see citing works

The Emerging Therapeutic Potential of Histone Methyltransferase and Demethylase Inhibitors

Spannhoff, A., Hauser, A., Heinke, R., Sippl, W., & Jung, M. (2009) · ChemMedChem · doi:10.1002/cmdc.200900301 · Cited by 172 · see citing works

Histone Deacetylases

Parbin, S., Kar, S., Shilpi, A., Sengupta, D., Deb, M., Rath, S. K., & Patra, S. K. (2013) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155413506582 · Cited by 172 · see citing works

Epigenetic modification of m6A regulator proteins in cancer

Wang, Y., Wang, Y., Patel, H. H., Chen, J., Wang, J., Chen, Z., & Wang, H. (2023) · Molecular Cancer · doi:10.1186/s12943-023-01810-1 · Cited by 170 · see citing works

Biological targets and mechanisms of action of natural products from marine cyanobacteria

Salvador‐Reyes, L. A., & Luesch, H. (2015) · Natural Product Reports · doi:10.1039/c4np00104d · Cited by 165 · see citing works

Targeting macrophage immunometabolism: Dawn in the darkness of sepsis

Kumar, V. (2018) · International Immunopharmacology · doi:10.1016/j.intimp.2018.03.005 · Cited by 149 · see citing works

Epigenetic polypharmacology: from combination therapy to multitargeted drugs

de Lera, Á. R., & Ganesan, A. (2016) · Clinical Epigenetics · doi:10.1186/s13148-016-0271-9 · Cited by 148 · see citing works

Protein acetylation affects acetate metabolism, motility and acid stress response in Escherichia coli

Castaño‐Cerezo, S., Bernal, V., Post, H., Fuhrer, T., Cappadona, S., Sánchez‐Díaz, N. C., Sauer, U., Heck, A. J. R., Altelaar, M. A. F., & Cánovas, M. (2014) · Molecular Systems Biology · doi:10.15252/msb.20145227 · Cited by 146 · see citing works

Peptidylarginine deiminase 4: a nuclear button triggering neutrophil extracellular traps in inflammatory diseases and aging

Wong, S. L., & Wagner, D. D. (2018) · The FASEB Journal · doi:10.1096/fj.201800691r · Cited by 145 · see citing works

Methylation multiplicity and its clinical values in cancer

Dai, X., Ren, T., Zhang, Y., & Nan, N. (2021) · Expert Reviews in Molecular Medicine · doi:10.1017/erm.2021.4 · Cited by 143 · see citing works

Effect of posttranslational modifications on enzyme function and assembly

Ryšlavá, H., Hýsková, V., Kavan, D., & Vaněk, O. (2013) · Journal of Proteomics · doi:10.1016/j.jprot.2013.03.025 · Cited by 142 · see citing works

The Search for Potent, Small‐Molecule HDACIs in Cancer Treatment: A Decade After Vorinostat

Zagni, C., Floresta, G., Monciino, G., & Rescifina, A. (2017) · Medicinal Research Reviews · doi:10.1002/med.21437 · Cited by 138 · see citing works

Histone Deacetylase Inhibition and Dietary Short-Chain Fatty Acids

Licciardi, P. V., Ververis, K., & Karagiannis, T. C. (2011) · ISRN Allergy · doi:10.5402/2011/869647 · Cited by 138 · see citing works

A Proton-Shuttle Reaction Mechanism for Histone Deacetylase 8 and the Catalytic Role of Metal Ions

Wu, R., Wang, S., Zhou, N., Cao, Z., & Zhang, Y. (2010) · Journal of the American Chemical Society · doi:10.1021/ja103932d · Cited by 135 · see citing works

PRDM9 Methyltransferase Activity Is Essential for Meiotic DNA Double-Strand Break Formation at Its Binding Sites

Diagouraga, B., Clément, J. A. J., Duret, L., Kadlec, J., de Massy, B., & Baudat, F. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.01.033 · Cited by 128 · see citing works

The histone methyltransferase Dot1/DOT1L as a critical regulator of the cell cycle

Kim, W., Choi, M., & Kim, J.-E. (2014) · Cell Cycle · doi:10.4161/cc.28104 · Cited by 121 · see citing works

Nothing Is Yet Set in (Hi)stone: Novel Post-Translational Modifications Regulating Chromatin Function

Chan, J. C., & Maze, I. S. (2020) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.05.009 · Cited by 119 · see citing works

Molecular Basis for the Regulation of the H3K4 Methyltransferase Activity of PRDM9

Wu, H. Y., Mathioudakis, N., Diagouraga, B., Dong, A., Dombrovski, L., Baudat, F., Cusack, S., de Massy, B., & Kadlec, J. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.08.035 · Cited by 118 · see citing works

Se-Adenosyl- l -selenomethionine Cofactor Analogue as a Reporter of Protein Methylation

Bothwell, I. R., Islam, K., Chen, Y., Zheng, W., Blum, G., Deng, H., & Luo, M. (2012) · Journal of the American Chemical Society · doi:10.1021/ja304782r · Cited by 109 · see citing works

Zinc Chelation with Hydroxamate in Histone Deacetylases Modulated by Water Access to the Linker Binding Channel

Wu, R., Lu, Z., Cao, Z., & Zhang, Y. (2011) · Journal of the American Chemical Society · doi:10.1021/ja111104p · Cited by 108 · see citing works

Expanding Cofactor Repertoire of Protein Lysine Methyltransferase for Substrate Labeling

Islam, K., Zheng, W., Yu, H., Deng, H., & Luo, M. (2011) · ACS Chemical Biology · doi:10.1021/cb2000567 · Cited by 107 · see citing works

Beyond histones – the expanding roles of protein lysine methylation

Wu, Z., Connolly, J., & Biggar, K. K. (2017) · FEBS Journal · doi:10.1111/febs.14056 · Cited by 105 · see citing works

A Method for Systematic Mapping of Protein Lysine Methylation Identifies Functions for HP1β in DNA Damage Response

Liu, H., Galka, M., Mori, E., Liu, X., Lin, Y., Wei, R., Pittock, P., Voss, C., Dhami, G. K., Li, X., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.04.025 · Cited by 107 · see citing works

A patent review of arginine methyltransferase inhibitors (2010–2018)

Xiao, L., Wang, C., Jiang, H., & Luo, C. (2019) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2019.1567711 · Cited by 106 · see citing works

Bioorthogonal Profiling of Protein Methylation Using Azido Derivative of S -Adenosyl- l -methionine

Islam, K., Bothwell, I. R., Chen, Y., Sengelaub, C. A., Wang, R. Y., Deng, H., & Luo, M. (2012) · Journal of the American Chemical Society · doi:10.1021/ja2118333 · Cited by 106 · see citing works

The emerging role of lysine methyltransferase SETD8 in human diseases

Milite, C., Feoli, A., Viviano, M., Rescigno, D., Cianciulli, A., Balzano, A. L., Mai, A., Castellano, S., & Sbardella, G. (2016) · Clinical Epigenetics · doi:10.1186/s13148-016-0268-4 · Cited by 105 · see citing works

Structural Chemistry of Human SET Domain Protein Methyltransferases

Schapira, M. (2011) · Current Chemical Genomics · doi:10.2174/1875397301005010085 · Cited by 104 · see citing works

The promise and failures of epigenetic therapies for cancer treatment

Bojang, P., & Ramos, K. S. (2013) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2013.05.009 · Cited by 100 · see citing works

Unfolding the pathogenesis of scleroderma through genomics and epigenomics

Tsou, P., & Sawalha, A. H. (2017) · Journal of Autoimmunity · doi:10.1016/j.jaut.2017.05.004 · Cited by 101 · see citing works

Novel HDAC inhibitor Chidamide synergizes with Rituximab to inhibit diffuse large B-cell lymphoma tumour growth by upregulating CD20

Guan, X., Wang, H., Ban, W.-W., Chang, Z., Chen, H., Jia, L., & Liu, F. (2020) · Cell Death and Disease · doi:10.1038/s41419-019-2210-0 · Cited by 98 · see citing works

Role of Histone-Modifying Enzymes and Their Complexes in Regulation of Chromatin Biology

DesJarlais, R. L., & Tummino, P. J. (2016) · Biochemistry · doi:10.1021/acs.biochem.5b01210 · Cited by 95 · see citing works

Transcriptional co-activators: emerging roles in signaling pathways and potential therapeutic targets for diseases

Talukdar, P. D., & Chatterji, U. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01651-w · Cited by 96 · see citing works

Vascular histone deacetylation by pharmacological HDAC inhibitionPreprint

Rafehi, H., Balcerczyk, A., Lunke, S., Kaspi, A., Ziemann, M., Kurup, H. K. N., Okabe, J., Khurana, I., Ooi, J. Y. Y., Khan, A. W., et al. (2014) · Genome Research · doi:10.1101/gr.168781.113 · Cited by 94 · see citing works

A chemical probe toolbox for dissecting the cancer epigenome

Shortt, J., Ott, C. J., Johnstone, R. W., & Bradner, J. E. (2017) · Nature reviews. Cancer · doi:10.1038/nrc.2016.148 · Cited by 94 · see citing works

Small Molecule Inhibitors of Histone Acetyltransferases as Epigenetic Tools and Drug Candidates

Furdas, S. D., Kannan, S., Sippl, W., & Jung, M. (2011) · Archiv der Pharmazie · doi:10.1002/ardp.201100209 · Cited by 91 · see citing works

The crucial role of epigenetic regulation in breast cancer anti-estrogen resistance: Current findings and future perspectives

Sukocheva, O. A., Lukina, E., Friedemann, M., Menschikowski, M., Hagelgans, A., & Aliev, G. M. (2020) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2020.12.004 · Cited by 91 · see citing works

Post-translational modifications of the extracellular matrix are key events in cancer progression: Opportunities for biochemical marker development

Leeming, D. J., Bay‐Jensen, A., Vassiliadis, E., Larsen, M. R., Henriksen, K., & Karsdal, M. A. (2011) · Biomarkers · doi:10.3109/1354750x.2011.557440 · Cited by 90 · see citing works

Novel 3,5-Bis(bromohydroxybenzylidene)piperidin-4-ones as Coactivator-Associated Arginine Methyltransferase 1 Inhibitors: Enzyme Selectivity and Cellular Activity

Cheng, D., Valente, S., Castellano, S., Sbardella, G., Santo, R. D., Costi, R., Bedford, M. T., & Mai, A. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm200453n · Cited by 88 · see citing works

New roles of flavoproteins in molecular cell biology: Histone demethylase LSD1 and chromatin

Forneris, F., Battaglioli, E., Mattevi, A., & Binda, C. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07142.x · Cited by 86 · see citing works

Perspectives on the interactions between metabolism, redox, and epigenetics in plants

Shen, Y., Issakidis‐Bourguet, E., & Zhou, D. (2016) · Journal of Experimental Botany · doi:10.1093/jxb/erw310 · Cited by 85 · see citing works

Updated review on green tea polyphenol epigallocatechin-3-gallate as a cancer epigenetic regulator

Li, F., Qasim, S., Li, D., & Dou, Q. P. (2021) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2020.11.018 · Cited by 85 · see citing works

PLMLA: prediction of lysine methylation and lysine acetylation by combining multiple features

Shi, S., Qiu, J., Sun, X., Suo, S., Huang, S., & Liang, R. (2012) · Molecular BioSystems · doi:10.1039/c2mb05502c · Cited by 82 · see citing works

Epidrug Repurposing: Discovering New Faces of Old Acquaintances in Cancer Therapy

Montalvo-Casimiro, M., González‐Barrios, R., Meraz-Rodríguez, M. A., Juárez-González, V. T., Arriaga-Canon, C., & Herrera, L. A. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.605386 · Cited by 80 · see citing works

Histone variants and modifications during abiotic stress response

Nunez-Vazquez, R., Desvoyes, B., & Gutiérrez, C. (2022) · Frontiers in Plant Science · doi:10.3389/fpls.2022.984702 · Cited by 80 · see citing works

OUP accepted manuscript

Xu, Y., Zhang, S., Lin, S., Guo, Y., Deng, W., Zhang, Y. W., & Xue, Y. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw1011 · Cited by 78 · see citing works

KATching-Up on Small Molecule Modulators of Lysine Acetyltransferases

Simon, R. P., Robaa, D., Alhalabi, Z., Sippl, W., & Jung, M. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01502 · Cited by 77 · see citing works

Chemical and functional aspects of posttranslational modification of proteins.

Knorre, D. G., Kudryashova, N. V., & Godovikova, T. S. (2009) · PubMed Central · Cited by 77 · see citing works

SIRT3 and SIRT4 are mitochondrial tumor suppressor proteins that connect mitochondrial metabolism and carcinogenesis

Zhu, Y., Yan, Y., Principe, D. R., Zou, X., Vassilopoulos, A., & Gius, D. R. (2014) · Cancer & Metabolism · doi:10.1186/2049-3002-2-15 · Cited by 76 · see citing works

Epigenetic regulation of endothelial‐cell‐mediated vascular repair

Fraineau, S., Palii, C. G., Allan, D., & Brand, M. (2014) · FEBS Journal · doi:10.1111/febs.13183 · Cited by 76 · see citing works

Clinical Presentation of Preeclampsia and the Diagnostic Value of Proteins and Their Methylation Products as Biomarkers in Pregnant Women with Preeclampsia and Their Newborns

Portelli, M., & Baron, B. (2018) · Journal of Pregnancy · doi:10.1155/2018/2632637 · Cited by 77 · see citing works

Epigenetics and psychoneuroimmunology: Mechanisms and models

Mathews, H. L., & Janusek, L. W. (2010) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2010.08.009 · Cited by 76 · see citing works

MicroRNA Regulation of Epigenetic Modifiers in Breast Cancer

Humphries, B. A., Wang, Z., & Yang, C. (2019) · Cancers · doi:10.3390/cancers11070897 · Cited by 73 · see citing works

Advances in Histone Demethylase KDM3A as a Cancer Therapeutic Target

Yoo, J. H., Jeon, Y. H., Cho, H. Y., Lee, S. W., Kim, G. W., Lee, D. H., & Kwon, S. H. (2020) · Cancers · doi:10.3390/cancers12051098 · Cited by 73 · see citing works

Chemical and biological methods to detect post‐translational modifications of arginine

Slade, D. J., Subramanian, V., Fuhrmann, J., & Thompson, P. R. (2013) · Biopolymers · doi:10.1002/bip.22256 · Cited by 73 · see citing works

NO sparks off chromatin: Tales of a multifaceted epigenetic regulator

Illi, B., Colussi, C., Grasselli, A., Farsetti, A., Capogrossi, M. C., & Gaetano, C. (2009) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2009.05.003 · Cited by 74 · see citing works

Effect of formaldehyde on cell proliferation and death

Szende, B., & Tyihák, E. (2010) · Cell Biology International · doi:10.1042/cbi20100532 · Cited by 72 · see citing works

Toward the development of potent and selective bisubstrate inhibitors of protein arginine methyltransferases

Dowden, J., Hong, W., Parry, R. V., Pike, R. A., & Ward, S. G. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.02.069 · Cited by 72 · see citing works

The Role of Histone Acetylation-/Methylation-Mediated Apoptotic Gene Regulation in Hepatocellular Carcinoma

Rajan, P. K., Udoh, U. S., Sanabria, J. D., Banerjee, M., Smith, G., Schade, M. S., Sanabria, J. A., Sodhi, K., Pierre, S. V., Xie, Z., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21238894 · Cited by 70 · see citing works

Apoptosis Induction byHistone Deacetylase Inhibitors in Cancer Cells: Role of Ku70

Gong, P., Wang, Y., & Jing, Y. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20071601 · Cited by 69 · see citing works

Chromatin and epigenetic determinants of estrogen receptor alpha (ESR1) signaling

Magnani, L., & Lupien, M. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2013.04.026 · Cited by 66 · see citing works

Structure-Based Design of a Novel SMYD3 Inhibitor that Bridges the SAM-and MEKK2-Binding Pockets

Aller, G. S. V., Graves, A. P., Elkins, P. A., Bonnette, W. G., McDevitt, P. J., Zappacosta, F., Annan, R. S., Dean, T. W., Su, D., Carpenter, C. L., et al. (2016) · Structure · doi:10.1016/j.str.2016.03.010 · Cited by 64 · see citing works

Discovery of a Novel Chemotype of Histone Lysine Methyltransferase EHMT1/2 (GLP/G9a) Inhibitors: Rational Design, Synthesis, Biological Evaluation, and Co-crystal Structure

Milite, C., Feoli, A., Horton, J. R., Rescigno, D., Cipriano, A., Pisapia, V., Viviano, M., Pepe, G., Amendola, G., Novellino, E., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b02008 · Cited by 65 · see citing works

Arginine methylation of REF/ALY promotes efficient handover of mRNA to TAP/NXF1

Hung, M., Hautbergue, G. M., Snijders, A. P., Dickman, M. J., & Wilson, S. A. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq033 · Cited by 63 · see citing works

SETDB1 Methylates MCT1 Promoting Tumor Progression by Enhancing the Lactate Shuttle

She, X., Wu, Q., Rao, Z., Song, D., Huang, C., Feng, S., Liu, A., Liu, L., Wan, K., Li, X., et al. (2023) · Advanced Science · doi:10.1002/advs.202301871 · Cited by 61 · see citing works

Targets in Epigenetics: Inhibiting the Methyl Writers of the Histone Code

Yost, J. M., Korboukh, I., Liu, F., Gao, C., & Jin, J. J. (2011) · Current Chemical Genomics · doi:10.2174/1875397301005010072 · Cited by 61 · see citing works

Histone Methylation Has Dynamics Distinct from Those of Histone Acetylation in Cell Cycle Reentry from Quiescence

Mews, P., Zee, B. M., Liu, S., Donahue, G., Garcia, B. A., & Berger, S. L. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00763-14 · Cited by 60 · see citing works

Epigenetics in Rheumatoid Arthritis

Trenkmann, M., Brock, M., Ospelt, C., & Gay, S. (2009) · Clinical Reviews in Allergy & Immunology · doi:10.1007/s12016-009-8166-6 · Cited by 60 · see citing works

Role of HDAC3 on p53 Expression and Apoptosis in T Cells of Patients with Multiple Sclerosis

Zhang, F., Shi, Y., Wang, L. H.-C., & Sriram, S. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016795 · Cited by 59 · see citing works

Therapeutic targets for endothelial dysfunction in vascular diseases

Huynh, D. T. N., & Heo, K. (2019) · Archives of Pharmacal Research · doi:10.1007/s12272-019-01180-7 · Cited by 59 · see citing works

A hitchhiker’s guide to the Arabidopsis ferrome

Schmidt, W., & Buckhout, T. J. (2010) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2010.12.001 · Cited by 57 · see citing works

Role of Histone Deacetylases (HDACs) in Epilepsy and Epileptogenesis

Citraro, R., Leo, A., Santoro, M., D’Agostino, G., Constanti, A., & Russo, E. (2018) · Current Pharmaceutical Design · doi:10.2174/1381612823666171024130001 · Cited by 58 · see citing works

Trimethyllysine: From Carnitine Biosynthesis to Epigenetics

Maas, M. N., Hintzen, J. C. J., Porzberg, M. R. B., & Mecinović, J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249451 · Cited by 58 · see citing works

Chemical probes for histone-modifying enzymes

Cole, P. A. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.111 · Cited by 249 · see citing works

Role of Protein Methylation in Regulation of Transcription

Lee, D. Y., Teyssier, C., Strahl, B. D., & Stallcup, M. R. (2005) · Endocrine Reviews · doi:10.1210/er.2004-0008 · Cited by 454 · see citing works

Arginine/lysine–methyl/methyl switches: biochemical role of histone arginine methylation in transcriptional regulation

Migliori, V., Phalke, S., Bezzi, M., & Guccione, E. (2010) · Epigenomics · doi:10.2217/epi.09.39 · Cited by 61 · see citing works

Histone Methyltransferase in Human Cancer

Das, M. (2011)

Histone H4 Acetylation Differentially Modulates Arginine Methylation by an in Cis Mechanism

Feng, Y., Wang, J., Asher, S., Hoang, L., Guardiani, C., Ivanov, I. N., & Zheng, Y. G. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.207258 · Cited by 78 · see citing works