Signaling to Chromatin through Histone Modifications

Crystal structure of the nucleosome core particle at 2.8 Å resolution

Luger, K., Mäder, A. W., Richmond, R. K., Sargent, D. F., & Richmond, T. J. (1997) · Nature · doi:10.1038/38444 · Cited by 9,466

DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139

Rogakou, E. P., Pilch, D. R., Orr, A. H., Ivanova, V. S., & Bonner, W. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.10.5858 · Cited by 5,438

Regulation of chromatin structure by site-specific histone H3 methyltransferases

Rea, S., Eisenhaber, F., O'Carroll, D., Strahl, B. D., Sun, Z.-W., Schmid, M., Opravil, S., Mechtler, K., Ponting, C. P., Allis, C. D., et al. (2000) · Nature · doi:10.1038/35020506 · Cited by 2,845

Chromatin Structure: A Repeating Unit of Histones and DNA

Kornberg, R. D. (1974) · Science · doi:10.1126/science.184.4139.868 · Cited by 2,662

Signaling—2000 and Beyond

Hunter, T. (2000) · Cell · doi:10.1016/s0092-8674(00)81688-8 · Cited by 2,586

IAP family proteins---suppressors of apoptosisPreprint

Deveraux, Q. L., & Reed, J. C. (1999) · Genes & Development · doi:10.1101/gad.13.3.239 · Cited by 2,535

Megabase Chromatin Domains Involved in DNA Double-Strand Breaks in Vivo

Rogakou, E. P., Boon, C., Redon, C., & Bonner, W. M. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.146.5.905 · Cited by 2,422

CREB: A Stimulus-Induced Transcription Factor Activated by A Diverse Array of Extracellular Signals

Shaywitz, A. J., & Greenberg, M. E. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.821 · Cited by 2,133

Phosphorylated CREB binds specifically to the nuclear protein CBP

Chrivia, J. C., Kwok, R. P. S., Lamb, N., Hagiwara, M., Montminy, M. R., & Goodman, R. H. (1993) · Nature · doi:10.1038/365855a0 · Cited by 2,052

Mitosis-specific phosphorylation of histone H3 initiates primarily within pericentromeric heterochromatin during G2 and spreads in an ordered fashion coincident with mitotic chromosome condensation

Hendzel, M. J., Wei, Y., Mancini, M. A., Hooser, A. A. V., Ranalli, T. A., Brinkley, B. R., Bazett‐Jones, D. P., & Allis, C. D. (1997) · Chromosoma · doi:10.1007/s004120050256 · Cited by 1,860

Translating the Histone Code

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

Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins

Lachner, M., O'Carroll, D., Rea, S., Mechtler, K., & Jenuwein, T. (2001) · Nature · doi:10.1038/35065132 · Cited by 2,868

Active Genes Are Tri-Methylated at K4 of Histone H3

Santos-Rosa, H., Schneider, R., Bannister, A. J., Sherriff, J., Bernstein, B. E., Emre, N. C. T., Schreiber, S. L., Mellor, J., & Kouzarides, T. (2002) · Nature · doi:10.1038/nature01080 · Cited by 2,138

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 1,906

The NAD+-dependent deacetylase SIRT1 modulates CLOCK-mediated chromatin remodeling and circadian control

Nakahata, Y., Kaluzova, M., Grimaldi, B., Sahar, S., Hirayama, J., Chen, D., Guarente, L. P., & Sassone-Corsi, P. (2008) · Cell · doi:10.1016/j.cell.2008.07.002 · Cited by 1,427

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 1,476

SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins

Schultz, D. C., Ayyanathan, K., Negorev, D., Maul, G. G., & Rauscher, F. J. (2002) · Genes & Development · doi:10.1101/gad.973302 · Cited by 1,313

Histone modifications in transcriptional regulation

Berger, S. L. (2002) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(02)00279-4 · Cited by 1,222

Histone and chromatin cross-talk

Fischle, W., Wang, Y., & Allis, C. D. (2003) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(03)00013-9 · Cited by 1,239

Extraction, purification and analysis of histones

Shechter, D., Dormann, H. L., Allis, C. D., & Hake, S. B. (2007) · Nature Protocols · doi:10.1038/nprot.2007.202 · Cited by 1,054

Multiple control of interleukin-8 gene expression

Hoffmann, E., Dittrich-Breiholz, O., Holtmann, H., & Kracht, M. (2002) · Journal of Leukocyte Biology · doi:10.1189/jlb.72.5.847 · Cited by 1,058

Histone acetylation: a switch between repressive and permissive chromatin

Eberharter, A., & Becker, P. B. (2002) · EMBO Reports · doi:10.1093/embo-reports/kvf053 · Cited by 944

The Interplay between the Glucocorticoid Receptor and Nuclear Factor-κB or Activator Protein-1: Molecular Mechanisms for Gene Repression

De Bosscher, K., Vanden Berghe, W., & Haegeman, G. (2003) · Endocrine Reviews · doi:10.1210/er.2002-0006 · Cited by 898

Circadian Regulator CLOCK Is a Histone Acetyltransferase

Doi, M., Hirayama, J., & Sassone‐Corsi, P. (2006) · Cell · doi:10.1016/j.cell.2006.03.033 · Cited by 910

Regulation of the INK4b–ARF–INK4a tumour suppressor locus: all for one or one for all

Gil, J., & Peters, G. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1987 · Cited by 843

Epigenetic Control of Smooth Muscle Cell Differentiation and Phenotypic Switching in Vascular Development and Disease

Alexander, M. R., & Owens, G. K. (2011) · Annual Review of Physiology · doi:10.1146/annurev-physiol-012110-142315 · Cited by 796

Nuclear retinoid receptors and the transcription of retinoid-target genes

Bastien, J., & Rochette-Egly, C. (2004) · Gene · doi:10.1016/j.gene.2003.12.005 · Cited by 773

Chromatin Remodeling Is a Key Mechanism Underlying Cocaine-Induced Plasticity in Striatum

Kumar, A., Choi, K.-H., Renthal, W., Tsankova, N. M., Theobald, D. E. H., Truong, H.-T., Russo, S. J., LaPlant, Q., Sasaki, T. S., Whistler, K. N., et al. (2005) · Neuron · doi:10.1016/j.neuron.2005.09.023 · Cited by 764

Essential function of histone deacetylase 1 in proliferation control and CDK inhibitor repression

Lagger, G., O'Carroll, D., Rembold, M., Khier, H., Tischler, J., Weitzer, G., Schuettengruber, B., Hauser, C., Brunmeir, R., Jenuwein, T., et al. (2002) · The EMBO Journal · doi:10.1093/emboj/21.11.2672 · Cited by 760

In vivo destabilization of dynamic microtubules by HDAC6‐mediated deacetylation

Matsuyama, A., Shimazu, T., Sumida, Y., Saito, A., Yoshimatsu, Y., Seigneurin‐Berny, D., Osada, H., Komatsu, Y., Nishino, N., Khochbin, S., et al. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf682 · Cited by 720

Phosphorylation of Histone H3 Is Required for Proper Chromosome Condensation and Segregation

Wei, Y., Yu, L., Bowen, J. K., Gorovsky, M. A., & Allis, C. D. (1999) · Cell · doi:10.1016/s0092-8674(00)80718-7 · Cited by 719

Aurora-A — A guardian of poles

Marumoto, T., Zhang, D., & Saya, H. (2005) · Nature reviews. Cancer · doi:10.1038/nrc1526 · Cited by 698

p38-dependent marking of inflammatory genes for increased NF-κB recruitment

Saccani, S., Pantano, S., & Natoli, G. (2001) · Nature Immunology · doi:10.1038/ni748 · Cited by 694

A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling

Blagoev, B., Kratchmarova, I., Ong, S., Nielsen, M. M., Foster, L. J., & Mann, M. (2003) · Nature Biotechnology · doi:10.1038/nbt790 · Cited by 691

The Nucleosome

Khorasanizadeh, S. (2004) · Cell · doi:10.1016/s0092-8674(04)00044-3 · Cited by 715

Mitotic Phosphorylation of Histone H3: Spatio-Temporal Regulation by Mammalian Aurora Kinases

Crosio, C., Fimia, G. M., Loury, R., Kimura, M., Okano, Y., Zhou, H., Sen, S., Allis, C. D., & Sassone‐Corsi, P. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.3.874-885.2002 · Cited by 668

Higher-order structure in pericentric heterochromatin involves a distinct pattern of histone modification and an RNA component

Maison, C., Bailly, D., Peters, A. H. F. M., Quivy, J., Roche, D. M. J., Taddei, A., Lachner, M., Jenuwein, T., & Almouzni, G. (2002) · Nature Genetics · doi:10.1038/ng843 · Cited by 688

IκB kinases: key regulators of the NF-κB pathway

Yamamoto, Y., & Gaynor, R. B. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2003.12.003 · Cited by 647

Lessons from the Genome Sequence ofNeurospora crassa: Tracing the Path from Genomic Blueprint to Multicellular Organism

Borkovich, K. A., Alex, L. A., Yarden, O., Freitag, M., Turner, G., Read, N. D., Seiler, S., Bell‐Pedersen, D., Paietta, J. V., Plesofsky, N. S., et al. (2004) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.68.1.1-108.2004 · Cited by 636

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 640

An epigenetic road map for histone lysine methylation

Lachner, M., O’Sullivan, R. J., & Jenuwein, T. (2003) · Journal of Cell Science · doi:10.1242/jcs.00493 · Cited by 641

SIRT1 Controls Endothelial Angiogenic Functions During Vascular Growth

Potente, M., Ghaeni, L., Baldessari, D., Mostoslavsky, R., Rossig, L., Dequiedt, F., Haendeler, J., Mione, M., Dejana, E., Alt, F. W., et al. (2007) · Genes & Development · doi:10.1101/gad.435107 · Cited by 608

p21-activated kinases in cancer

Kumar, R., Gururaj, A. E., & Barnes, C. J. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1892 · Cited by 609

What turns CREB on?

Johannessen, M., Delghandi, M. P., & Moens, U. L. (2004) · Cellular Signalling · doi:10.1016/j.cellsig.2004.05.001 · Cited by 586

Phosphorylation of Serine 10 in Histone H3 Is Functionally Linked In Vitro and In Vivo to Gcn5-Mediated Acetylation at Lysine 14

Lo, W., Trievel, R. C., Rojas, J. R., Duggan, L. J., Hsu, J.-Y., Allis, C. D., Marmorstein, R., & Berger, S. L. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80257-9 · Cited by 573

Histone H3 phosphorylation by IKK-α is critical for cytokine-induced gene expression

Yamamoto, Y., Verma, U. N., Prajapati, S., Kwak, Y.-T., & Gaynor, R. B. (2003) · Nature · doi:10.1038/nature01576 · Cited by 577

S-adenosylmethionine in Liver Health, Injury, and Cancer

Lu, S. C.-L., & Mato, J. M. (2012) · Physiological Reviews · doi:10.1152/physrev.00047.2011 · Cited by 565

Conformational Dynamics of the Chromatin Fiber in Solution: Determinants, Mechanisms, and Functions

Hansen, J. C. (2002) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.31.101101.140858 · Cited by 556

Mechanisms of Vascular Smooth Muscle Contraction and the Basis for Pharmacologic Treatment of Smooth Muscle Disorders

Brozovich, F. V., Nicholson, C., Degen, C. V., Gao, Y. Z., Aggarwal, M., & Morgan, K. G. (2016) · Pharmacological Reviews · doi:10.1124/pr.115.010652 · Cited by 568

Decoding the Epigenetic Language of Neuronal Plasticity

Borrelli, E., Nestler, E. J., Allis, C. D., & Sassone‐Corsi, P. (2008) · Neuron · doi:10.1016/j.neuron.2008.10.012 · Cited by 546

TH cell differentiation is accompanied by dynamic changes in histone acetylation of cytokine genes

Avni, O., Lee, D. H., Macián, F., Szabo, S. J., Glimcher, L. H., & Rao, A. (2002) · Nature Immunology · doi:10.1038/ni808 · Cited by 524

Histone H3 phosphorylation and cell division

Hans, F., & Dimitrov, S. I. (2001) · Oncogene · doi:10.1038/sj.onc.1204326 · Cited by 519

Methylation of Histone H3 at Lys-9 Is an Early Mark on the X Chromosome during X Inactivation

Heard, É., Rougeulle, C., Arnaud, D., Avner, P. R., Allis, C. D., & Spector, D. L. (2001) · Cell · doi:10.1016/s0092-8674(01)00598-0 · Cited by 520

Meiotic recombination hot spots and cold spots

Petes, T. D. (2001) · Nature Reviews Genetics · doi:10.1038/35072078 · Cited by 510

MSK2 and MSK1 mediate the mitogen‐ and stress‐induced phosphorylation of histone H3 and HMG‐14

Soloaga, A., Thomson, S., Wiggin, G. R., Rampersaud, N., Dyson, M. H., Hazzalin, C. A., Mahadevan, L. C., & Arthur, J. S. C. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg273 · Cited by 520

CBP and p300: HATs for different occasions

Kalkhoven, E. (2004) · Biochemical Pharmacology · doi:10.1016/j.bcp.2004.03.045 · Cited by 516

Phosphorylation of serine 10 in histone H3, what for?

Prigent, C., & Dimitrov, S. I. (2003) · Journal of Cell Science · doi:10.1242/jcs.00735 · Cited by 492

Apoptotic Phosphorylation of Histone H2B Is Mediated by Mammalian Sterile Twenty Kinase

Cheung, W. L., Ajiro, K., Samejima, K., Kloc, M., Cheung, P., Mizzen, C. A., Beeser, A. E., Etkin, L. D., Chernoff, J., Earnshaw, W. C., et al. (2003) · Cell · doi:10.1016/s0092-8674(03)00355-6 · Cited by 487

Unique Chromatin Remodeling and Transcriptional Regulation in Spermatogenesis

Sassone‐Corsi, P. (2002) · Science · doi:10.1126/science.1070963 · Cited by 474

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

Strahl, B. D., Briggs, S. D., Brame, C. J., Caldwell, J., Koh, S. S., Ma, H., Cook, R. G., Shabanowitz, J., Hunt, D. F., Stallcup, M. R., et al. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00294-9 · Cited by 457

Chromatin remodelling and epigenetic features of germ cells

Kimmins, S., & Sassone‐Corsi, P. (2005) · Nature · doi:10.1038/nature03368 · Cited by 465

S-nitrosylation of histone deacetylase 2 induces chromatin remodelling in neurons

Nott, A., Watson, P. M., Robinson, J. D., Crepaldi, L., & Riccio, A. (2008) · Nature · doi:10.1038/nature07238 · Cited by 434

Functional Analysis of Kinetochore Assembly in Caenorhabditis elegans

Oegema, K., Desai, A. B., Rybina, S., Kirkham, M., & Hyman, A. A. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.6.1209 · Cited by 428

S‐Adenosylmethionine: a control switch that regulates liver function

Mato, J. M., Corrales, F. J., Lu, S. C.-L., & Avila, M. A. (2002) · The FASEB Journal · doi:10.1096/fj.01-0401rev · Cited by 427

Transcriptional regulation by histone ubiquitination and deubiquitinationPreprint

Zhang, Y. (2003) · Genes & Development · doi:10.1101/gad.1156403 · Cited by 425

Signaling Network Model of Chromatin

Schreiber, S. L., & Bernstein, B. (2002) · Cell · doi:10.1016/s0092-8674(02)01196-0 · Cited by 399

Chromatin crosstalk in development and disease: lessons from REST

Ooi, L., & Wood, I. C. (2007) · Nature Reviews Genetics · doi:10.1038/nrg2100 · Cited by 405

Structure of the histone deacetylase SIRT2.

Finnin, M. S., Donigian, J. R., & Pavletich, N. P. (2001) · Nature Structural Biology · doi:10.1038/89668 · Cited by 376

Modifications of DNA by platinum complexes

Brabec, V., & Kašpárková, J. (2005) · Drug Resistance Updates · doi:10.1016/j.drup.2005.04.006 · Cited by 374

Functional significance of histone deacetylase diversity

Khochbin, S., Verdel, A., Lemercier, C., & Seigneurin-Berny, D. (2001) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(00)00174-x · Cited by 366

Histone Modifications and Nuclear Architecture: A Review

Bártová, E., Krejčí, J., Harničarová, A., Galiová, G., & Kozubek, S. (2008) · Journal of Histochemistry & Cytochemistry · doi:10.1369/jhc.2008.951251 · Cited by 381

Epigenetic regulation of memory formation and maintenancePreprint

Zovkic, I. B., Karlsson, M. G., & Sweatt, J. D. (2013) · Learning & Memory · doi:10.1101/lm.026575.112 · Cited by 371

Polycomb Group Protein Ezh2 Controls Actin Polymerization and Cell Signaling

Su, I.-H., Dobenecker, M.-W., Dickinson, E., Oser, M., Basavaraj, A., Marqueron, R., Viale, A., Reinberg, D., Wülfing, C., & Tarakhovsky, A. (2005) · Cell · doi:10.1016/j.cell.2005.02.029 · Cited by 365

Cell geometric constraints induce modular gene-expression patterns via redistribution of HDAC3 regulated by actomyosin contractility

Jain, N., Iyer, K. V., Kumar, A., & Shivashankar, G. V. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1300801110 · Cited by 362

Cell Apoptosis: Requirement of H2AX in DNA Ladder Formation, but Not for the Activation of Caspase-3

Lu, C., Zhu, F., Cho, Y., Tang, F., Zykova, T. A., Ma, W., Bode, A. M., & Dong, Z. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.05.023 · Cited by 363

Novel Linear Quadrupole Ion Trap/FT Mass Spectrometer: Performance Characterization and Use in the Comparative Analysis of Histone H3 Post-translational Modifications

Syka, J. E. P., Marto, J. A., Bai, D. L., Horning, S. R., Senko, M. W., Schwartz, J. C., Ueberheide, B. M., Garcia, B. A., Busby, S. A., Muratore‐Schroeder, T. L., et al. (2004) · Journal of Proteome Research · doi:10.1021/pr0499794 · Cited by 349

Epigenetic Regulation by Histone Methylation and Histone Variants

Cheung, P., & Lau, P. N. I. (2005) · Molecular Endocrinology · doi:10.1210/me.2004-0496 · Cited by 340

Circadian Programs of Transcriptional Activation, Signaling, and Protein Turnover Revealed by Microarray Analysis of Mammalian Cells

Duffield, G. E., Best, J. D., Meurers, B. H., Bittner, A., Loros, J., & Dunlap, J. (2002) · Current Biology · doi:10.1016/s0960-9822(02)00765-0 · Cited by 329

Histone H2A.Z Regulates Transcription and Is Partially Redundant with Nucleosome Remodeling Complexes

Santisteban, M. S., Kalashnikova, T. I., & Smith, M. M. (2000) · Cell · doi:10.1016/s0092-8674(00)00133-1 · Cited by 329

Haematopoietic cell-fate decisions, chromatin regulation and ikaros

Georgopoulos, K. (2002) · Nature reviews. Immunology · doi:10.1038/nri747 · Cited by 324

T Helper Cell Differentiation: Regulation by cis Elements and Epigenetics

Lee, G. R., Kim, S. T., Spilianakis, C. G., Fields, P. E., & Flavell, R. A. (2006) · Immunity · doi:10.1016/j.immuni.2006.03.007 · Cited by 320

Epigenetics—An Epicenter of Gene Regulation: Histones and Histone‐Modifying Enzymes

Biel, M., Wascholowski, V., & Giannis, A. (2005) · Angewandte Chemie International Edition · doi:10.1002/anie.200461346 · Cited by 324

H2AX: functional roles and potential applications

Dickey, J. S., Redon, C. E., Nakamura, A. J., Baird, B. J., Sedelnikova, O. A., & Bonner, W. M. (2009) · Chromosoma · doi:10.1007/s00412-009-0234-4 · Cited by 320

Bop encodes a muscle-restricted protein containing MYND and SET domains and is essential for cardiac differentiation and morphogenesis

Gottlieb, P. D., Pierce, S. A., Sims, R. J., Yamagishi, H., Weihe, E., Harriss, J. V., Maika, S. D., Kuziel, W. A., King, H. L., Olson, E. N., et al. (2002) · Nature Genetics · doi:10.1038/ng866 · Cited by 320

Environmental Epigenetics and Its Implication on Disease Risk and Health Outcomes

Ho, S., Johnson, A. D., Tarapore, P., Janakiram, V., Zhang, X., & Leung, Y. (2012) · ILAR Journal · doi:10.1093/ilar.53.3-4.289 · Cited by 327

Organismal Differences in Post-translational Modifications in Histones H3 and H4

Garcia, B. A., Hake, S. B., Diaz, R. L., Kauer, M., Morris, S. A., Recht, J., Shabanowitz, J., Mishra, N., Strahl, B. D., Allis, C. D., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607900200 · Cited by 314

Crosstalk between CARM1 Methylation and CBP Acetylation on Histone H3

Daujat, S., Bauer, U., Shah, V., Turner, B. M., Berger, S. L., & Kouzarides, T. (2002) · Current Biology · doi:10.1016/s0960-9822(02)01387-8 · Cited by 314

Epigenetic codes in cognition and behaviour

Gräff, J., & Mansuy, I. M. (2008) · Behavioural Brain Research · doi:10.1016/j.bbr.2008.01.021 · Cited by 328

Regulation of the transcriptional activity of the nuclear factor-κB p65 subunit

Vermeulen, L., Wilde, G. D., Notebaert, S., Berghe, W. V., & Haegeman, G. (2002) · Biochemical Pharmacology · doi:10.1016/s0006-2952(02)01161-9 · Cited by 303

Transcription Corepressor CtBP Is an NAD+-Regulated Dehydrogenase

Kumar, V., Carlson, J. E., Ohgi, K. A., Edwards, T. A., Rose, D. W., Escalante, C. R., Rosenfeld, M. G., & Aggarwal, A. K. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00650-0 · Cited by 299

Critical loss of CBP/p300 histone acetylase activity by caspase‐6 during neurodegeneration

Rouaux, C., Jokic, N., Mbebi, C., Boutillier, S., Loeffler, J., & Boutillier, A. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg615 · Cited by 302

Re-SET-ting heterochromatin by histone methyltransferases

Jenuwein, T. (2001) · Trends in Cell Biology · doi:10.1016/s0962-8924(01)02001-3 · Cited by 304

Cigarette Smoke Alters Chromatin Remodeling and Induces Proinflammatory Genes in Rat Lungs

Marwick, J. A., Kirkham, P., Stevenson, C. S., Danahay, H. L., Giddings, J., Butler, K. D., Donaldson, K., MacNee, W., & Rahman, I. (2004) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2004-0006oc · Cited by 301

Higher-order structure of chromatin and chromosomes

Woodcock, C. L. F., & Dimitrov, S. I. (2001) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(00)00169-6 · Cited by 300

Epigenetics meets endocrinology

Zhang, X., & Ho, S. (2010) · Journal of Molecular Endocrinology · doi:10.1677/jme-10-0053 · Cited by 300

The histone methyltransferase MLL1 permits the oscillation of circadian gene expression

Katada, S., & Sassone‐Corsi, P. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1961 · Cited by 302

Molecular sequelae of histone deacetylase inhibition in human malignant B cells

Mitsiades, N., Mitsiades, C. S., Richardson, P. G. G., McMullan, C. J., Poulaki, V., Fanourakis, G., Schlossman, R. L., Chauhan, D., Munshi, N. C., Hideshima, T., et al. (2003) · Blood · doi:10.1182/blood-2002-11-3514 · Cited by 292

Emerging roles for chromatin as a signal integration and storage platform

Badeaux, A. I., & Shi, Y. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3545 · Cited by 291

Tribute to P. L. Lutz: putting life on `pause' – molecular regulation of hypometabolism

Storey, K. B., & Storey, J. M. (2007) · Journal of Experimental Biology · doi:10.1242/jeb.02716 · Cited by 279

Epigenetic Mechanisms of Depression and Antidepressant Action

Vialou, V., Feng, J., Robison, A. J., & Nestler, E. J. (2013) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010611-134540 · Cited by 277

PIM1-dependent phosphorylation of Histone H3 at Serine 10 is required for MYC-dependent transcriptional activation and oncogenic transformation.Preprint

Zippo, A., Robertis, A. D., Serafini, R., & Oliviero, S. (2007) · Nature Precedings · doi:10.1038/ncb1618 · Cited by 284

Distinctive Core Histone Post-Translational Modification Patterns in Arabidopsis thaliana

Zhang, K., Sridhar, V. V., Zhu, J., Kapoor, A., & Zhu, J. (2007) · PLoS ONE · doi:10.1371/journal.pone.0001210 · Cited by 271

Light induces chromatin modification in cells of the mammalian circadian clock

Crosio, C., Cermakian, N., Allis, C. D., & Sassone‐Corsi, P. (2000) · Nature Neuroscience · doi:10.1038/81767 · Cited by 264

Methylation of histone H4 by arginine methyltransferase PRMT1 is essential in vivo for many subsequent histone modificationsPreprint

Huang, S., Litt, M. D., & Felsenfeld, G. (2005) · Genes & Development · doi:10.1101/gad.1333905 · Cited by 273

Chromatin modifications in the germinal vesicle (GV) of mammalian oocytes

Fuente, R. D. L. (2006) · Developmental Biology · doi:10.1016/j.ydbio.2006.01.008 · Cited by 262

Histone deacetylase inhibitors: from target to clinical trials

Kelly, W. K., O’Connor, O. A., & Marks, P. A. (2002) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.11.12.1695 · Cited by 256

Fragmentation and Dispersal of the Pericentriolar Golgi Complex Is Required for Entry into Mitosis in Mammalian Cells

Sütterlin, C., Hsu, P., Mallabiabarrena, A., & Malhotra, V. (2002) · Cell · doi:10.1016/s0092-8674(02)00720-1 · Cited by 252

Chromatin-associated Protein Phosphatase 1 Regulates Aurora-B and Histone H3 Phosphorylation

Murnion, M. E., Adams, R. R., Callister, D. M., Allis, C. D., Earnshaw, W. C., & Swedlow, J. R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102288200 · Cited by 250

CENP-A Phosphorylation by Aurora-A in Prophase Is Required for Enrichment of Aurora-B at Inner Centromeres and for Kinetochore Function

Kunitoku, N., Sasayama, T., Marumoto, T., Zhang, D., Honda, S., Kobayashi, O., Hatakeyama, K., Ushio, Y., Saya, H., & Hirota, T. (2003) · Developmental Cell · doi:10.1016/s1534-5807(03)00364-2 · Cited by 248

Chromatin remodeling and neuronal response: multiple signaling pathways induce specific histone H3 modifications and early gene expression in hippocampal neurons

Crosio, C., Heitz, E., Allis, C. D., Borrelli, E., & Sassone‐Corsi, P. (2003) · Journal of Cell Science · doi:10.1242/jcs.00804 · Cited by 247

Signal transduction from cell surface to nucleus in development and disease

Karin, M. (1992) · The FASEB Journal · doi:10.1096/fasebj.6.8.1317309 · Cited by 243

Transcriptional Regulation by Extracellular signals: Mechanisms and Specificity

Hill, C. S., & Treisman, R. (1995) · Cell · doi:10.1016/0092-8674(95)90403-4 · Cited by 1,012

Signal transduction and gene control

Karin, M. (1991) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(91)90075-a · Cited by 94

Histone Phosphorylation

Lau, P. N. I., & Cheung, P. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00288-6 · Cited by 3

Signal transduction from the cell surface to the nucleus through the phosphorylation of transcription factors

Karin, M. (1994) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(94)90035-3 · Cited by 389