Is there a code embedded in proteins that is based on post-translational modifications?

Translating the Histone Code

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

Surfing the p53 network

Vogelstein, B., Lane, D., & Levine, A. J. (2000) · Nature · doi:10.1038/35042675 · Cited by 6,607 · see citing works

Structure and ligand of a histone acetyltransferase bromodomain

Dhalluin, C., Carlson, J. E., Zeng, L., He, C., Aggarwal, A. K., Zhou, M.-M., & Zhou, M.-M. (1999) · Nature · doi:10.1038/20974 · Cited by 1,732 · see citing works

Acetylation and deacetylation of non-histone proteins

Glozak, M. A., Sengupta, N., Zhang, X., & Seto, E. (2005) · Gene · doi:10.1016/j.gene.2005.09.010 · Cited by 1,584 · see citing works

How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers

Taverna, 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

Heterochromatin revisited

Grewal, S. I. S., & Jia, S. (2007) · Nature Reviews Genetics · doi:10.1038/nrg2008 · Cited by 1,263 · 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

Methylation of lysine 4 on histone H3: intricacy of writing and reading a single epigenetic mark

Ruthenburg, A. J., Allis, C. D., & Wysocka, J. (2007) · Molecular Cell · doi:10.1016/j.molcel.2006.12.014 · Cited by 1,147 · see citing works

Regulation of HP1–chromatin binding by histone H3 methylation and phosphorylation

Fischle, W., Tseng, B. S., Dormann, H. L., Ueberheide, B. M., Garcia, B. A., Shabanowitz, J., Hunt, D. F., Funabiki, H., & Allis, C. D. (2005) · Nature · doi:10.1038/nature04219 · Cited by 996 · 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

Structure and Function of a Human TAF II 250 Double Bromodomain Module

Jacobson, R. H., Ladurner, A. G., King, D., & Tjian, R. (2000) · Science · doi:10.1126/science.288.5470.1422 · Cited by 845 · see citing works

Regulation of p53 activity through lysine methylation

Chuikov, S., Kurash, J. K., Wilson, J. R., Xiao, B., Justin, N., Ivanov, G. S., McKinney, K. M., Tempst, P., Prives, C. L., Gamblin, S. J., et al. (2004) · Nature · doi:10.1038/nature03117 · Cited by 820 · see citing works

p53 is regulated by the lysine demethylase LSD1

Huang, J. L., Sengupta, R., Espejo, A. B., Lee, M. G., Dorsey, J. A., Richter, M., Opravil, S., Shiekhattar, R., Bedford, M. T., Jenuwein, T., et al. (2007) · Nature · doi:10.1038/nature06092 · Cited by 820 · see citing works

Phosphorylation and functions of the RNA polymerase II CTDPreprint

Phatnani, H. P., & Greenleaf, A. L. (2006) · Genes & Development · doi:10.1101/gad.1477006 · Cited by 752 · see citing works

Histone H3 Lysine 9 Methylation and HP1γ Are Associated with Transcription Elongation through Mammalian Chromatin

Vakoc, C. R., Mandat, S. A., Olenchock, B. A., & Blobel, G. A. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.06.011 · Cited by 698 · see citing works

Binary switches and modification cassettes in histone biology and beyond

Fischle, W., Wang, Y., & Allis, C. D. (2003) · Nature · doi:10.1038/nature02017 · Cited by 627 · see citing works

Repression of p53 activity by Smyd2-mediated methylation

Huang, J. L., Perez-Burgos, L., Placek, B. J., Sengupta, R., Richter, M., Dorsey, J. A., Kubicek, S., Opravil, S., Jenuwein, T., & Berger, S. L. (2006) · Nature · doi:10.1038/nature05287 · Cited by 626 · see citing works

Facultative Heterochromatin: Is There a Distinctive Molecular Signature?

Trojer, P., & Reinberg, D. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.09.011 · Cited by 609 · see citing works

Recognition of Trimethylated Histone H3 Lysine 4 Facilitates the Recruitment of Transcription Postinitiation Factors and Pre-mRNA Splicing

Sims, R. J., Millhouse, S., Chen, C.-F., Lewis, B. A., Erdjument‐Bromage, H., Tempst, P., Manley, J. L., & Reinberg, D. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.11.010 · Cited by 581 · see citing works

PR-Set7 Is a Nucleosome-Specific Methyltransferase that Modifies Lysine 20 of Histone H4 and Is Associated with Silent Chromatin

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

Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formationPreprint

Nishioka, K., Chuikov, S., Sarma, K., Erdjument‐Bromage, H., Allis, C. D., Tempst, P., & Reinberg, D. (2002) · Genes & Development · doi:10.1101/gad.967202 · Cited by 558 · 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

Function and Selectivity of Bromodomains in Anchoring Chromatin-Modifying Complexes to Promoter Nucleosomes

Hassan, A. H., Prochasson, P., Neely, K. E., Galasinski, S. C., Chandy, M., Carrozza, M. J., & Workman, J. L. (2002) · Cell · doi:10.1016/s0092-8674(02)01005-x · Cited by 533 · see citing works

Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive

Guccione, E., Bassi, C., Casadio, F., Martinato, F., Cesaroni, M., Schuchlautz, H., Lüscher, B., & Amati, B. B. (2007) · Nature · doi:10.1038/nature06166 · Cited by 495 · see citing works

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

Recognition of unmethylated histone H3 lysine 4 links BHC80 to LSD1-mediated gene repression

Lan, F., Collins, R. E., Cegli, R. D., Alpatov, R., Horton, J. R., Shi, X., Gozani, O., Cheng, X., & Shi, Y. (2007) · Nature · doi:10.1038/nature06034 · Cited by 432 · see citing works

Acetylation of p53 augments its site-specific DNA binding both in vitro and in vivo

Luo, J., Li, M., Tang, Y., Laszkowska, M., Roeder, R. G., & Gu, W. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308762101 · Cited by 419 · see citing works

Defining an epigenetic code

Turner, B. M. (2007) · Nature Cell Biology · doi:10.1038/ncb0107-2 · Cited by 392 · see citing works

Protein lysine methyltransferase G9a acts on non-histone targets

Rathert, P., Dhayalan, A., Murakami, M., Zhang, X., Tamas, R., Jurkowska, R., Komatsu, Y., Shinkai, Y., Cheng, X., & Jeltsch, A. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.88 · Cited by 347 · see citing works

Arginine methylation at a glance

Bedford, M. T. (2007) · Journal of Cell Science · doi:10.1242/jcs.019885 · Cited by 342 · see citing works

Yng1 PHD Finger Binding to H3 Trimethylated at K4 Promotes NuA3 HAT Activity at K14 of H3 and Transcription at a Subset of Targeted ORFs

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

Identification and characterization of Smyd2: a split SET/MYND domain-containing histone H3 lysine 36-specific methyltransferase that interacts with the Sin3 histone deacetylase complex

Brown, M. A., Sims, R. J., Gottlieb, P. D., & Tucker, P. W. (2006) · Molecular Cancer · doi:10.1186/1476-4598-5-26 · Cited by 314 · see citing works

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

The emerging field of dynamic lysine methylation of non-histone proteins

Huang, J. L., & Berger, S. L. (2008) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2008.01.012 · Cited by 288 · see citing works

Multisite protein modification and intramolecular signaling

Yang, X. (2004) · Oncogene · doi:10.1038/sj.onc.1208173 · Cited by 267 · see citing works

Methylation of a Histone Mimic within the Histone Methyltransferase G9a Regulates Protein Complex Assembly

Sampath, S. C., Marazzi, I., Yap, K. L., Sampath, S. C., Krutchinsky, A. N., Mecklenbräuker, I., Viale, A. J., Rudensky, E., Zhou, M., Chait, B. T., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.06.026 · Cited by 246 · 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 distribution and turnover of labeled methyl groups in histone fractions of cultured mammalian cells

Byvoet, P., Shepherd, G. R., Hardin, J. M., & Noland, B. J. (1972) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(72)90174-9 · Cited by 238 · see citing works

Methylation of p53 by Set7/9 Mediates p53 Acetylation and Activity In Vivo

Kurash, J. K., Lei, H., Shen, Q. “., Marston, W. L., Granda, B. W., Fan, H. X., Wall, D., Li, E., & Gaudet, F. (2008) · Molecular Cell · doi:10.1016/j.molcel.2007.12.025 · Cited by 215 · see citing works

Histone Lysine Demethylases and Their Impact on Epigenetics

Trojer, P., & Reinberg, D. (2006) · Cell · doi:10.1016/j.cell.2006.04.003 · Cited by 212 · see citing works

Why Is p53 Acetylated?

Prives, C. L., & Manley, J. L. (2001) · Cell · doi:10.1016/s0092-8674(01)00619-5 · Cited by 210 · see citing works

Arginine Methylation of the Histone H3 Tail Impedes Effector Binding

Iberg, A. N., Espejo, A. B., Cheng, D., Kim, D., Michaud‐Levesque, J., Richard, S., & Bedford, M. T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.c700192200 · Cited by 203 · see citing works

Studies of Histone Methylation during the HeLa S-3 Cell Cycle

Borun, T. W., Pearson, D., & Paik, W. K. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45074-6 · Cited by 141 · see citing works

Autoregulation of the Rsc4 Tandem Bromodomain by Gcn5 Acetylation

VanDemark, A. P., Kasten, M. M., Ferris, E., Heroux, A., Hill, C. P., & Cairns, B. R. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.08.018 · Cited by 130 · see citing works

Inactivating Chromosomes

Ladurner, A. G. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00284-3 · Cited by 108 · see citing works

Simultaneous induction of stimulatory and inhibitory signals by PDGF

Heldin, C. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00318-9 · Cited by 87 · see citing works

IN VIVO METHYLATION AND TURNOVER OF RAT BRAIN HISTONES

Duerre, J. A., & Lee, C. T. (1974) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1974.tb06057.x · Cited by 80 · see citing works

Relationship between Methylation and Acetylation of Arginine-Rich Histones in Cycling and Arrested HeLa Cells

Annunziato, A. T., Eason, M. B., & Perry, C. A. (1995) · Biochemistry · doi:10.1021/bi00009a023 · Cited by 70 · see citing works

p53–RNA interactions: New clues in an old mystery

Riley, K. J.-L., & Maher, L. J. (2007) · RNA · doi:10.1261/rna.673407 · Cited by 65 · 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

Histones: annotating chromatin

Campos, E. I., & Reinberg, D. (2009) · Annual Review of Genetics · doi:10.1146/annurev.genet.032608.103928 · Cited by 852 · see citing works

Integrative epigenomic mapping defines four main chromatin states in Arabidopsis

Roudier, F., Ahmed, I., Bérard, C., Sarazin, A., Mary‐Huard, T., Cortijo, S., Bouyer, D., Caillieux, E., Duvernois‐Berthet, E., Al-Shikhley, L., et al. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.103 · Cited by 707 · see citing works

p53 post-translational modification: deregulated in tumorigenesis

Dai, C., & Gu, W. J. (2010) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2010.09.002 · Cited by 523 · see citing works

N‐Methylation of Peptides and Proteins: An Important Element for Modulating Biological Functions

Chatterjee, J., Rechenmacher, F., & Kessler, H. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201205674 · Cited by 500 · see citing works

Regulating tumor suppressor genes: post-translational modifications

Chen, L., Liu, S., & Tao, Y. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-0196-9 · Cited by 449 · see citing works

Paternal DNA packaging in spermatozoa: more than the sum of its parts? DNA, histones, protamines and epigenetics

Miller, D., Brinkworth, M. H., & Iles, D. (2009) · Reproduction · doi:10.1530/rep-09-0281 · Cited by 416 · see citing works

Retinoic acid receptors: From molecular mechanisms to cancer therapy

di Masi, A., Leboffe, L., De Marinis, E., Pagano, F., Cicconi, L., Rochette-Egly, C., Lo-Coco, F., Ascenzi, P., & Nervi, C. (2015) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2014.12.003 · Cited by 403 · see citing works

Vitamin A and retinoid signaling: genomic and nongenomic effects

Al Tanoury, Z., Piskunov, A., & Rochette-Egly, C. (2013) · Journal of Lipid Research · doi:10.1194/jlr.r030833 · Cited by 408 · see citing works

β- N -acetylglucosamine (O-GlcNAc) is part of the histone code

Sakabe, K., Wang, Z., & Hart, G. W. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009023107 · 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

The structural and functional signatures of proteins that undergo multiple events of post‐translational modification

Pejaver, V., Hsu, W., Xin, F., Dunker, A. K., Uversky, V. N., & Radivojac, P. (2014) · Protein Science · doi:10.1002/pro.2494 · Cited by 349 · see citing works

Posttranslational modifications of NF-κB: Another layer of regulation for NF-κB signaling pathway

Huang, B., Yang, X., Lamb, A., & Chen, L. F. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.03.017 · Cited by 345 · see citing works

Post‐translational modification: nature's escape from genetic imprisonment and the basis for dynamic information encoding

Prabakaran, S., Lippens, G., Steen, H., & Gunawardena, J. (2012) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.1185 · Cited by 335 · see citing works

The next level of complexity: Crosstalk of posttranslational modifications

Venne, A. S., Kollipara, L., & Zahedi, R. P. (2013) · PROTEOMICS · doi:10.1002/pmic.201300344 · Cited by 325 · see citing works

High Throughput Characterization of Combinatorial Histone Codes

Young, N. L., DiMaggio, P. A., Plazas-Mayorca, M. D., Baliban, R. C., Floudas, C. A., & Garcia, B. A. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m900238-mcp200 · Cited by 312 · see citing works

Genetics and epigenetics: stability and plasticity during cellular differentiation

Mohn, F., & Schübeler, D. (2009) · Trends in Genetics · doi:10.1016/j.tig.2008.12.005 · Cited by 299 · see citing works

Brd4 maintains constitutively active NF-κB in cancer cells by binding to acetylated RelA

Zou, Z., Huang, B., Wu, X., Zhang, H., Qi, J., Bradner, J. E., Nair, S. K., & Chen, L.-F. (2013) · Oncogene · doi:10.1038/onc.2013.179 · Cited by 260 · see citing works

Finding one's way in proteomics: a protein species nomenclature

Schlüter, H., Apweiler, R., Holzhütter, H., & Jungblut, P. (2009) · Chemistry Central Journal · doi:10.1186/1752-153x-3-11 · Cited by 254 · see citing works

Unlimited multistability in multisite phosphorylation systems

Thomson, M., & Gunawardena, J. (2009) · Nature · doi:10.1038/nature08102 · Cited by 238 · see citing works

The ups and downs of p53: understanding protein dynamics in single cells

Batchelor, E., Loewer, A., & Lahav, G. (2009) · Nature reviews. Cancer · doi:10.1038/nrc2604 · Cited by 242 · see citing works

Dynamic and combinatorial control of gene expression by nuclear retinoic acid receptors (RARs)

Rochette‐Egly, C., & Germain, P. (2009) · Nuclear Receptor Signaling · doi:10.1621/nrs.07005 · Cited by 244 · see citing works

Crosstalk between Arg 1175 methylation and Tyr 1173 phosphorylation negatively modulates EGFR-mediated ERK activation

Hsu, J.-M., Chen, C., Chou, C., Kuo, H.-P., Li, L., Lin, C.-Y., Lee, H.-J., Wang, Y., Liu, M., Liao, H.-W., et al. (2011) · Nature Cell Biology · doi:10.1038/ncb2158 · Cited by 240 · see citing works

The Chromatin Signaling Pathway: Diverse Mechanisms of Recruitment of Histone-Modifying Enzymes and Varied Biological Outcomes

Smith, E. R., & Shilatifard, A. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.11.031 · Cited by 234 · see citing works

Surf the Post-translational Modification Network of p53 Regulation

Gu, B., & Zhu, W. (2012) · International Journal of Biological Sciences · doi:10.7150/ijbs.4283 · Cited by 234 · see citing works

Carm1 Regulates Pax7 Transcriptional Activity through MLL1/2 Recruitment during Asymmetric Satellite Stem Cell Divisions

Kawabe, Y.-I., Wang, Y. X., McKinnell, I. W., Bedford, M. T., & Rudnicki, M. A. (2012) · Cell stem cell · doi:10.1016/j.stem.2012.07.001 · Cited by 220 · see citing works

Epigenetic regulation of the neural transcriptome: the meaning of the marks

Meaney, M. J., & Ferguson-Smith, A. C. (2010) · Nature Neuroscience · doi:10.1038/nn1110-1313 · Cited by 216 · see citing works

Allosteric post-translational modification codes

Nussinov, R., Tsai, C.-J., Xin, F., & Radivojac, P. (2012) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.07.001 · Cited by 211 · see citing works

THE CROSSTALK BETWEEN PHYSIOLOGY AND CIRCADIAN CLOCK PROTEINS

Duguay, D., & Cermakian, N. (2009) · Chronobiology International · doi:10.3109/07420520903497575 · Cited by 201 · see citing works

RNA templating the epigenome

Spitale, R. C., Tsai, M.-C., & Chang, H. Y. (2011) · Epigenetics · doi:10.4161/epi.6.5.15221 · Cited by 194 · see citing works

Structure and function of the nucleosome-binding PWWP domain

Su, Q., & Min, J. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2014.09.001 · Cited by 191 · see citing works

Deciphering post‐translational modification codes

Lothrop, A. P., Torres, M. P., & Fuchs, S. M. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.01.047 · Cited by 182 · see citing works

Influence of Combinatorial Histone Modifications on Antibody and Effector Protein Recognition

Fuchs, S. M., Krajewski, K., Baker, R. W., Miller, V. L., & Strahl, B. D. (2010) · Current Biology · doi:10.1016/j.cub.2010.11.058 · Cited by 182 · see citing works

Interrogating the Function of Metazoan Histones using Engineered Gene Clusters

McKay, D. J., Klusza, S., Penke, T. J. R., Meers, M. P., Curry, K. P., McDaniel, S. L., Malek, P. Y., Cooper, S. W., Tatomer, D. C., Lieb, J. D., et al. (2015) · Developmental Cell · doi:10.1016/j.devcel.2014.12.025 · Cited by 169 · see citing works

Smyd2 controls cytoplasmic lysine methylation of Hsp90 and myofilament organizationPreprint

Donlin, L. T., Andresen, C., Just, S., Rudensky, E., Pappas, C. T., Krüger, M., Jacobs, E. Y., Unger, A., Zieseniß, A., Dobenecker, M., et al. (2012) · Genes & Development · doi:10.1101/gad.177758.111 · Cited by 169 · see citing works

The Interplay of Cofactor Interactions and Post-translational Modifications in the Regulation of the AAA+ ATPase p97

Hänzelmann, P., & Schindelin, H. (2017) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2017.00021 · Cited by 152 · see citing works

Epigenetic cancer therapy: rationales, targets and drugs

Rius, M., & Lyko, F. (2012) · Oncogene · doi:10.1038/onc.2011.601 · Cited by 157 · see citing works

The non‐apoptotic role of p53 in neuronal biology: enlightening the dark side of the moon

Tedeschi, A., & Giovanni, S. D. (2009) · EMBO Reports · doi:10.1038/embor.2009.89 · Cited by 159 · see citing works

A histone chaperone, DEK, transcriptionally coactivates a nuclear receptorPreprint

Sawatsubashi, S., Murata, T., Lim, J., Fujiki, R., Ito, S., Suzuki, E., Tanabe, M., Zhao, Y., Kimura, S., Fujiyama, S., et al. (2009) · Genes & Development · doi:10.1101/gad.1857410 · Cited by 157 · see citing works

Uncovering post-translational modification-associated protein–protein interactions

Wang, S., Osgood, A. O., & Chatterjee, A. (2022) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2022.102352 · Cited by 153 · see citing works

When Signaling Kinases Meet Histones and Histone Modifiers in the Nucleus

Baek, S. H. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.03.022 · Cited by 147 · see citing works

Functional Interplay between Acetylation and Methylation of the RelA Subunit of NF-κB

Yang, X., Tajkhorshid, E., & Chen, L. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01343-09 · Cited by 143 · see citing works

PAX6: 25th anniversary and more to learn

Cvekl, A., & Callaerts, P. (2016) · Experimental Eye Research · doi:10.1016/j.exer.2016.04.017 · Cited by 142 · see citing works

Extensive Crosstalk between O-GlcNAcylation and Phosphorylation Regulates Akt Signaling

Wang, S., Huang, X., Sun, D., Xin, X., Pan, Q., Peng, S., Liang, Z. T., Luo, C., Yang, Y., Jiang, H., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0037427 · Cited by 140 · see citing works

Role of Hepatocyte Nuclear Factor 4α (HNF4α) in Cell Proliferation and Cancer

Walesky, C. M., & Apte, U. M. (2015) · Gene Expression · doi:10.3727/105221615x14181438356292 · Cited by 138 · see citing works

Two Distinct Repressive Mechanisms for Histone 3 Lysine 4 Methylation through Promoting 3′-End Antisense Transcription

Margaritis, T., Oréal, V., Brabers, N. A. C. H., Maestroni, L., Vitaliano-Prunier, A., Benschop, J. J., van Hooff, S. R., van Leenen, D., Dargemont, C., Géli, V., et al. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002952 · Cited by 134 · see citing works

A statistical framework for modeling gene expression using chromatin features and application to modENCODE datasets

Cheng, C., Yan, K., Yip, K. Y.-L., Rozowsky, J. S., Alexander, R. P., Shou, C., & Gerstein, M. (2011) · Genome biology · doi:10.1186/gb-2011-12-2-r15 · Cited by 137 · see citing works

Clinical significance of estrogen receptor phosphorylation

Murphy, L. C., Seekallu, S. V., & Watson, P. H. (2010) · Endocrine Related Cancer · doi:10.1677/erc-10-0070 · Cited by 133 · see citing works

Phospho‐MED1‐enhanced UBE2C locus looping drives castration‐resistant prostate cancer growth

Chen, Z., Zhang, C., Wu, D., Chen, H., Rorick, A. M., Zhang, X., & Wang, Q. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.154 · Cited by 128 · see citing works

Enzymatic Site‐Specific Functionalization of Protein Methyltransferase Substrates with Alkynes for Click Labeling

Peters, W., Willnow, S., Duisken, M., Kleine, H. O., Macherey, T., Duncan, K., Litchfield, D. W., Lüscher, B., & Weinhold, E. G. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.201001240 · Cited by 130 · see citing works

Reconsidering the evidence for learning in single cells

Gershman, S. J., Balbi, P. E., Gallistel, C. R., & Gunawardena, J. (2021) · eLife · doi:10.7554/elife.61907 · Cited by 125 · see citing works

A post-translational modification code for transcription factors: sorting through a sea of signals

Benayoun, B. A., & Veitia, R. A. (2009) · Trends in Cell Biology · doi:10.1016/j.tcb.2009.02.003 · Cited by 121 · see citing works

Structural Basis and Specificity of Acetylated Transcription Factor GATA1 Recognition by BET Family Bromodomain Protein Brd3

Gamsjaeger, R., Webb, S. R., Lamonica, J. M., Billin, A. N., Blobel, G. A., & Mackay, J. P. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05413-11 · Cited by 121 · see citing works

Epigenetic regulation: methylation of histone and non-histone proteins

Lan, F., & Shi, Y. (2009) · Science in China Series C Life Sciences · doi:10.1007/s11427-009-0054-z · Cited by 120 · see citing works

Dynamic interactions of proteins in complex networks: a more structured view

Stein, A., Pache, R. A., Bernadó, P., Pons, M., & Aloy, P. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07251.x · Cited by 118 · see citing works

Lysine Methylation Regulators Moonlighting outside the Epigenome

Cornett, E. M., Ferry, L., Defossez, P., & Rothbart, S. B. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.08.026 · Cited by 113 · see citing works

A Selenium‐Based Click AdoMet Analogue for Versatile Substrate Labeling with Wild‐Type Protein Methyltransferases

Willnow, S., Martin, M., Lüscher, B., & Weinhold, E. G. (2012) · ChemBioChem · doi:10.1002/cbic.201100781 · Cited by 110 · see citing works

EZH2: Not EZHY (Easy) to Deal

Deb, G., Singh, A. K., & Gupta, S. (2014) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-13-0546 · Cited by 105 · see citing works

100% protein sequence coverage: a modern form of surrealism in proteomics

Meyer, B., Papasotiriou, D. G., & Karas, M. (2010) · Amino Acids · doi:10.1007/s00726-010-0680-6 · Cited by 104 · see citing works

Crosstalk between C/EBPβ phosphorylation, arginine methylation, and SWI/SNF/Mediator implies an indexing transcription factor code

Kowenz‐Leutz, E., Pleß, O., Dittmar, G. A. G., Knoblich, M., & Leutz, A. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.3 · Cited by 103 · see citing works

Comparative proteomic analysis of the plant–virus interaction in resistant and susceptible ecotypes of maize infected with sugarcane mosaic virus

Wu, L., Han, Z., Wang, S., Wang, X., Sun, A., Zu, X., & Chen, Y. (2013) · Journal of Proteomics · doi:10.1016/j.jprot.2013.06.005 · Cited by 101 · see citing works

Post-translational modification networks regulating FOXP3 function

van Loosdregt, J., & Coffer, P. J. (2014) · Trends in Immunology · doi:10.1016/j.it.2014.06.005 · Cited by 100 · see citing works

Methylation of the Tumor Suppressor Protein, BRCA1, Influences Its Transcriptional Cofactor Function

Guendel, I., Carpio, L., Pedati, C., Schwartz, A. M., Teal, C. B., Kashanchi, F., & Kehn‐Hall, K. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011379 · Cited by 100 · see citing works

Cell fate regulation governed by p53: Friends or reversible foes in cancer therapy

Song, B., Yang, P., & Zhang, S. (2024) · 癌症：英文版 · doi:10.1002/cac2.12520 · Cited by 97 · see citing works

Epigenetic Dysregulation in Cancer

Muntean, A. G., & Hess, J. L. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2009.081142 · Cited by 93 · see citing works

Chromatin Affinity Purification and Quantitative Mass Spectrometry Defining the Interactome of Histone Modification Patterns

Nikolov, M., Stützer, A., Mosch, K., Krasauskas, A., Soeroes, S., Stark, H., Urlaub, H., & Fischle, W. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m110.005371 · Cited by 93 · see citing works

Proteoglycomics: Recent Progress and Future Challenges

Ly, M., Laremore, T. N., & Linhardt, R. J. (2010) · OMICS A Journal of Integrative Biology · doi:10.1089/omi.2009.0123 · Cited by 93 · see citing works

The solution structure of the first PHD finger of autoimmune regulator in complex with non-modified histone H3 tail reveals the antagonistic role of H3R2 methylation

Chignola, F., Gaetani, M., Rebane, A., Org, T., Mollica, L., Zucchelli, C., Spitaleri, A., Mannella, V., Peterson, P., & Musco, G. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp166 · Cited by 90 · see citing works

Diversity within the pRb pathway: is there a code of conduct?

Munro, S., Carr, S. M., & Thangue, N. B. L. (2012) · Oncogene · doi:10.1038/onc.2011.603 · Cited by 88 · see citing works

From structural to functional glycomics: core substitutions as molecular switches for shape and lectin affinity of N-glycans

André, S., Kožár, T., Kojima, S., Unverzagt, C., & Gabius, H. (2009) · Biological Chemistry · doi:10.1515/bc.2009.072 · Cited by 88 · see citing works

Mass spectrometric analysis of mono- and multi-phosphopeptides by selective binding with NiZnFe2O4 magnetic nanoparticles

Zhong, H., Xiao, X., Zheng, S. J., Zhang, W., Ding, M., Jiang, H., Huang, L., & Kang, J. (2013) · Nature Communications · doi:10.1038/ncomms2662 · Cited by 85 · see citing works

Computational studies of protein regulation by post-translational phosphorylation

Narayanan, A., & Jacobson, M. P. (2009) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2009.02.007 · Cited by 81 · see citing works

Alcohol-induced protein hyperacetylation: Mechanisms and consequences

Shepard, B. D. (2009) · World Journal of Gastroenterology · doi:10.3748/wjg.15.1219 · Cited by 83 · see citing works

Epigenetic mechanisms facilitating oligodendrocyte development, maturation, and aging

Copray, S. C. V. M., Huynh, J. L., Sher, F., Casaccia‐Bonnefil, P., & Boddeke, E. (2009) · Glia · doi:10.1002/glia.20881 · Cited by 82 · see citing works

Lysine-specific modifications of p53: a matter of life and death?

Marouco, D. M., Garabadgiu, A. V., Melino, G., & Barlev, N. A. (2013) · Oncotarget · doi:10.18632/oncotarget.1436 · Cited by 81 · see citing works

Histone H3 phosphorylation: Universal code or lineage specific dialects?

Cerutti, H. D., & Casas-Mollano, J. A. (2009) · Epigenetics · doi:10.4161/epi.4.2.7781 · Cited by 81 · see citing works

Cardiac Deletion of Smyd2 Is Dispensable for Mouse Heart Development

Diehl, F., Brown, M. A., van Amerongen, M. J., Novoyatleva, T., Wietelmann, A., Harriss, J. V., Ferrazzi, F., Boettger, T., Harvey, R. P., Tucker, P. W., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009748 · Cited by 81 · see citing works

Targeted large‐scale analysis of protein acetylation

Mischerikow, N., & Heck, A. J. R. (2010) · PROTEOMICS · doi:10.1002/pmic.201000397 · Cited by 78 · see citing works

Application of Celluspots peptide arrays for the analysis of the binding specificity of epigenetic reading domains to modified histone tails

Bock, I., Kudithipudi, S., Tamas, R., Kungulovski, G., Dhayalan, A., & Jeltsch, A. (2011) · BMC Biochemistry · doi:10.1186/1471-2091-12-48 · Cited by 78 · see citing works

N‐Methylierung von Peptiden und Proteinen: ein wichtiges Element für die Regulation biologischer Funktionen

Chatterjee, J., Rechenmacher, F., & Kessler, H. (2012) · Angewandte Chemie · doi:10.1002/ange.201205674 · Cited by 78 · see citing works

Epigenetic regulatory mechanisms in vertebrate eye development and disease

Cvekl, A., & Mitton, K. P. (2010) · Heredity · doi:10.1038/hdy.2010.16 · Cited by 77 · see citing works

On your histone mark, SET, methylate!

Binda, O. (2013) · Epigenetics · doi:10.4161/epi.24451 · Cited by 75 · see citing works

A Gene-Specific Requirement of RNA Polymerase II CTD Phosphorylation for Sexual Differentiation in S. pombe

Coudreuse, D. Y. M., van Bakel, H., Dewez, M., Soutourina, J., Parnell, T. J., Vandenhaute, J., Cairns, B., Werner, M., & Hermand, D. (2010) · Current Biology · doi:10.1016/j.cub.2010.04.054 · Cited by 76 · see citing works

Haspin: a newly discovered regulator of mitotic chromosome behavior

Higgins, J. M. G. (2009) · Chromosoma · doi:10.1007/s00412-009-0250-4 · Cited by 76 · see citing works

Can changes in histone acetylation contribute to memory formation?

López‐Atalaya, J. P., & Barco, Á. (2014) · Trends in Genetics · doi:10.1016/j.tig.2014.09.003 · Cited by 74 · see citing works

Direct interrogation of the role of H3K9 in metazoan heterochromatin function

Penke, T. J. R., McKay, D. J., Strahl, B. D., Matera, A. G., & Duronio, R. J. (2016) · Genes & Development · doi:10.1101/gad.286278.116 · Cited by 74 · see citing works

Polycomb repressive complex’s evolutionary conserved function: the role of EZH2 status and cellular background

Gall‐Tros̆elj, K., Kujundžić, R. N., & Ugarkovic, D. (2016) · Clinical Epigenetics · doi:10.1186/s13148-016-0226-1 · Cited by 73 · see citing works

The biology of lysine acetylation integrates transcriptional programming and metabolism

Patel, J. A., Pathak, R. R., & Mujtaba, S. (2011) · Nutrition & Metabolism · doi:10.1186/1743-7075-8-12 · Cited by 72 · see citing works

Extensive Post-translational Modification of Active and Inactivated Forms of Endogenous p53

DeHart, C. J., Chahal, J. S., Flint, S. J., & Perlman, D. H. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.030254 · Cited by 70 · see citing works

Peptide Microarrays to Interrogate the “Histone Code”

Rothbart, S. B., Krajewski, K., Strahl, B. D., & Fuchs, S. M. (2012) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-391940-3.00006-8 · Cited by 70 · see citing works

Posttranslational Modifications of the Retinoblastoma Tumor Suppressor Protein as Determinants of Function

MacDonald, J. I., & Dick, F. A. (2012) · Genes & Cancer · doi:10.1177/1947601912473305 · Cited by 69 · see citing works

NEDDylation regulates E2F‐1‐dependent transcription

Loftus, S. J., Liu, G., Carr, S. M., Munro, S., & Thangue, N. B. L. (2012) · EMBO Reports · doi:10.1038/embor.2012.113 · Cited by 67 · see citing works

The Fission Yeast HIRA Histone Chaperone Is Required for Promoter Silencing and the Suppression of Cryptic Antisense Transcripts

Anderson, H. E., Wardle, J., Korkut, Ş. V., Murton, H. E., López‐Maury, L., Bähler, J., & Whitehall, S. K. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00698-09 · Cited by 64 · see citing works

Capturing Post-Translational Modification-Triggered Protein–Protein Interactions Using Dual Noncanonical Amino Acid Mutagenesis

Zheng, Y., Gilgenast, M. J., Hauc, S. C., & Chatterjee, A. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.8b00021 · Cited by 64 · see citing works

Mechanisms of noncanonical binding dynamics in multivalent protein–protein interactions

Errington, W. J., Bruncsics, B., & Sarkar, C. A. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1902909116 · Cited by 63 · see citing works

Post-translational modification of nucleoid-associated proteins: an extra layer of functional modulation in bacteria?

Dilweg, I. W., & Dame, R. T. (2018) · Biochemical Society Transactions · doi:10.1042/bst20180488 · Cited by 59 · see citing works

p53 Interaction with JMJD3 Results in Its Nuclear Distribution during Mouse Neural Stem Cell Differentiation

Solá, S., Xavier, J. M., dos Santos, D. M., Aranha, M. M., Morgado, A. L., Jepsen, K., & Rodrigues, C. M. P. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018421 · Cited by 59 · see citing works

Histone Variants: The Nexus of Developmental Decisions and Epigenetic Memory

Loppin, B., & Berger, F. (2020) · Annual Review of Genetics · doi:10.1146/annurev-genet-022620-100039 · Cited by 56 · see citing works

Histone arginine methylation keeps RUNX1 target genes in an intermediate state

Herglotz, J., Kuvardina, O. N., Kolodziej, S., Kumar, A., Hussong, H., Grez, M., & Lausen, J. (2012) · Oncogene · doi:10.1038/onc.2012.274 · Cited by 59 · see citing works

Chromatin dynamics associated with HIV-1 Tat-activated transcription

Easley, R. L., Duyne, R. V., Coley, W., Guendel, I., Dadgar, S., Kehn‐Hall, K., & Kashanchi, F. (2009) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2009.08.008 · Cited by 58 · see citing works

In This Issue

(2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1777

The language of covalent histone modifications

Strahl, B. D., & Allis, C. D. (2000) · Nature · doi:10.1038/47412 · Cited by 8,679 · see citing works

PTMcode: a database of known and predicted functional associations between post-translational modifications in proteins

Mínguez, P., Letunić, I., Parca, L., & Bork, P. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1230 · Cited by 138 · see citing works

Deciphering post‐translational modification codes

Lothrop, A. P., Torres, M. P., & Fuchs, S. M. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.01.047 · Cited by 182 · see citing works

Lysine methylation: beyond histones

Zhang, X., Wen, H., & Shi, X. (2011) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmr100 · Cited by 233 · see citing works