Structure of Histone Deacetylases

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

ACETYLATION AND METHYLATION OF HISTONES AND THEIR POSSIBLE ROLE IN THE REGULATION OF RNA SYNTHESIS

Allfrey, V. G., Faulkner, R. D., & Mirsky, A. E. (1964) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.51.5.786 · Cited by 2,649 · see citing works

A Mammalian Histone Deacetylase Related to the Yeast Transcriptional Regulator Rpd3p

Taunton, J., Hassig, C. A., & Schreiber, S. L. (1996) · Science · doi:10.1126/science.272.5260.408 · Cited by 1,829 · see citing works

The CBP co-activator is a histone acetyltransferase

Bannister, A. J., & Kouzarides, T. (1996) · Nature · doi:10.1038/384641a0 · Cited by 1,824 · see citing works

Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors

Finnin, M. S., Donigian, J. R., Cohen, A., Richon, V. M., Rifkind, R. A., Marks, P. A., Breslow, R., & Pavletich, N. P. (1999) · Nature · doi:10.1038/43710 · Cited by 1,714 · see citing works

Tetrahymena Histone Acetyltransferase A: A Homolog to Yeast Gcn5p Linking Histone Acetylation to Gene Activation

Brownell, J. E., Zhou, J., Ranalli, T. A., Kobayashi, R., Edmondson, D. G., Dent, S., & Allis, C. D. (1996) · Cell · doi:10.1016/s0092-8674(00)81063-6 · Cited by 1,636 · 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

Steroid receptor coactivator-1 is a histone acetyltransferase

Spencer, T. E., Jenster, G. W., Burcin, M. M., Allis, C. D., Zhou, J., Mizzen, C. A., McKenna, N. J., Oñate, S. A., Tsai, S. Y., Tsai, M., et al. (1997) · Nature · doi:10.1038/38304 · Cited by 1,242 · see citing works

Role of the histone deacetylase complex in acute promyelocytic leukaemia

Lin, R. J., Nagy, L., Inoue, S., Shao, W., Miller, W. H., & Evans, R. M. (1998) · Nature · doi:10.1038/35895 · Cited by 1,060 · see citing works

Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation

McKinsey, T. A., Zhang, C., Lu, J., & Olson, E. N. (2000) · Nature · doi:10.1038/35040593 · Cited by 1,051 · see citing works

Fusion proteins of the retinoic acid receptor-α recruit histone deacetylase in promyelocytic leukaemia

Grignani, F., Matteis, S. D., Nervi, C., Tomassoni, L., Gelmetti, V., Cioce, M., Fanelli, M., Ruthardt, M., Ferrara, F. F., Zamir, I., et al. (1998) · Nature · doi:10.1038/35901 · Cited by 1,004 · 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

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

Three proteins define a class of human histone deacetylases related to yeast Hda1p

Grozinger, C. M., Hassig, C. A., & Schreiber, S. L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.9.4868 · Cited by 770 · see citing works

The TAFII250 Subunit of TFIID Has Histone Acetyltransferase Activity

Mizzen, C. A., Yang, X., Kokubo, T., Brownell, J. E., Bannister, A. J., Owen‐Hughes, T., Workman, J. L., Wang, L., Berger, S. L., Kouzarides, T., et al. (1996) · Cell · doi:10.1016/s0092-8674(00)81821-8 · Cited by 724 · see citing works

HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription

Rundlett, S. E., Carmen, A. A., Kobayashi, R., Bavykin, S. G., Turner, B. M., & Grunstein, M. R. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.25.14503 · Cited by 618 · see citing works

Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3- 3-dependent cellular localization

Grozinger, C. M., & Schreiber, S. L. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.140199597 · Cited by 587 · 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

The Human Histone Deacetylase Family

Gray, S. G., & Ekström, T. J. (2001) · Experimental Cell Research · doi:10.1006/excr.2000.5080 · Cited by 544 · see citing works

The p300/CBP family: integrating signals with transcription factors and chromatin

Shiama, N. (1997) · Trends in Cell Biology · doi:10.1016/s0962-8924(97)01048-9 · Cited by 481 · see citing works

Structure of a unique binuclear manganese cluster in arginase

Kanyo, Z. F., Scolnick, L. R., Ash, D. E., & Christianson, D. W. (1996) · Nature · doi:10.1038/383554a0 · Cited by 441 · see citing works

Genetic isolation of ADA2: A potential transcriptional adaptor required for function of certain acidic activation domains

Berger, S. L., Piña, B., Silverman, N., Marcus, G. A., Agapite, J., Regier, J. L., Triezenberg, S. J., & Guarente, L. (1992) · Cell · doi:10.1016/0092-8674(92)90100-q · Cited by 435 · see citing works

Untitled work

Ng (2000) · doi:10.1016/s0968-0004(00)01551-6 · Cited by 427 · see citing works

RING domains: master builders of molecular scaffolds?

Borden, K. L. B. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3429 · Cited by 410 · see citing works

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 · see citing works

A role for histone deacetylase activity in HDAC1-mediated transcriptional repression

Hassig, C. A., Tong, J. K., Fleischer, T. C., Owa, T., Grable, P. G., Ayer, D. E., & Schreiber, S. L. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.7.3519 · Cited by 365 · see citing works

Sin Meets NuRD and Other Tails of Repression

Knoepfler, P. S., & Eisenman, R. N. (1999) · Cell · doi:10.1016/s0092-8674(00)81531-7 · Cited by 356 · see citing works

Crystal Structure of a SIR2 Homolog–NAD Complex

Min, J., Landry, J. W., Sternglanz, R., & Xu, R.-M. (2001) · Cell · doi:10.1016/s0092-8674(01)00317-8 · Cited by 326 · see citing works

Transcriptional control at regulatory checkpoints by histone deacetylases: molecular connections between cancer and chromatin

Wade, P. A. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.7.693 · Cited by 319 · see citing works

Two distinct yeast transcriptional activators require the function of the GCN5 protein to promote normal levels of transcription.

Georgakopoulos, T., & Thireos, G. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05507.x · Cited by 306 · see citing works

HDAC4, a Human Histone Deacetylase Related to Yeast HDA1, Is a Transcriptional Corepressor

Wang, A. H., Bertos, N. R., Vezmar, M., Pelletier, N., Crosato, M., Heng, H. H., Th’ng, J., Han, J., & Yang, X.-J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.11.7816 · Cited by 294 · see citing works

The nicotinamide dinucleotide binding motif: a comparison of nucleotide binding proteins

Bellamacina, C. R. (1996) · The FASEB Journal · doi:10.1096/fasebj.10.11.8836039 · Cited by 249 · see citing works

Coupling of histone deacetylation to NAD breakdown by the yeast silencing protein Sir2: Evidence for acetyl transfer from substrate to an NAD breakdown product

Tanny, J. C., & Moazed, D. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.2.415 · Cited by 242 · see citing works

Histone deacetylase activity of Rpd3 is important for transcriptional repression in vivo

Kadosh, D., & Struhl, K. (1998) · Genes & Development · doi:10.1101/gad.12.6.797 · Cited by 234 · see citing works

Active maintenance of mHDA2/mHDAC6 histone-deacetylase in the cytoplasm

Verdel, A., Curtet, S., Brocard, M.-P., Rousseaux, S., Lemercier, C., Yoshida, M., & Khochbin, S. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00542-x · Cited by 224 · see citing works

HDA1 and HDA3 Are Components of a Yeast Histone Deacetylase (HDA) Complex

Carmen, A. A., Rundlett, S. E., & Grunstein, M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.26.15837 · Cited by 188 · see citing works

A cytosolic NAD‐dependent deacetylase, Hst2p, can modulate nucleolar and telomeric silencing in yeast

Perrod, S., Cockell, M. M., Laroche, T., Renauld, H., Ducrest, A., Bonnard, C., & Gasser, S. M. (2001) · The EMBO Journal · doi:10.1093/emboj/20.1.197 · Cited by 165 · see citing works

Human mesenchymal stem cells support megakaryocyte and pro-platelet formation from CD34+ hematopoietic progenitor cells

Cheng, L., Qasba, P., Vanguri, P., & Thiede, M. A. (2000) · Journal of Cellular Physiology · doi:10.1002/(sici)1097-4652(200007)184:1 · Cited by 136 · see citing works

The N-terminal domain of TFIIB from Pyrococcus furiosus forms a zinc ribbon

Zhu, W., Zeng, Q., Colangelo, C. M., Lewis, L. M., Summers, M. F., & Scott, R. A. (1996) · Nature Structural Biology · doi:10.1038/nsb0296-122 · Cited by 134 · see citing works

Inhibition of histone deacetylases: a new strategy to target epigenetic modifications for anticancer treatment.

Weidle, U. H., & Grossmann, A. (2000) · PubMed · Cited by 129 · see citing works

Histone deacetylase 4 associates with extracellular signal-regulated kinases 1 and 2, and its cellular localization is regulated by oncogenic Ras

Zhou, X., Richon, V. M., Wang, A. H., Yang, X., Rifkind, R. A., & Marks, P. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.250494697 · Cited by 123 · see citing works

The charge relay system in chymotrypsin and chymotrypsinogen

Fersht, A. R., & Sperling, J. M. (1973) · Journal of Molecular Biology · doi:10.1016/0022-2836(73)90103-4 · Cited by 107 · see citing works

The Conserved Core of a HumanSIR2Homologue Functions in Yeast Silencing

Sherman, J. M., Stone, E. M., Freeman-Cook, L. L., Brachmann, C. B., Boeke, J. D., & Pillus, L. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.9.3045 · Cited by 94 · see citing works

Histone acetylation: plants and fungi as model systems for the investigation of histone deacetylases

Graessle, S., Loidl, P., & Brosch, G. (2001) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000894 · Cited by 45 · see citing works

Inhibition of Histone Deacetylases

Liu, C., & Xu, D. (2004) · Humana Press eBooks · doi:10.1385/1-59259-828-5:087 · Cited by 12 · see citing works

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

RUIJTER, A. J. M. D., GENNIP, A. H. V., CARON, H. N., KEMP, S., & KUILENBURG, A. B. P. V. (2003) · Biochemical Journal · doi:10.1042/bj20021321 · Cited by 3,114 · 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

The biochemistry of sirtuins

Sauve, A. A., Wolberger, C., Schramm, V. L., & Boeke, J. D. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133500 · Cited by 763 · see citing works

The Nucleosome

Khorasanizadeh, S. (2004) · Cell · doi:10.1016/s0092-8674(04)00044-3 · Cited by 672 · see citing works

Boron Containing Compounds as Protease Inhibitors

Smoum, R., Rubinstein, A., Dembitsky, V. M., & Srebnik, M. (2012) · Chemical Reviews · doi:10.1021/cr608202m · Cited by 451 · see citing works

Inside HDAC with HDAC inhibitors

Bertrand, P. (2010) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2010.02.030 · Cited by 363 · see citing works

A Fluorogenic Histone Deacetylase Assay Well Suited for High-Throughput Activity Screening

Wegener, D., Wirsching, F., Riester, D., & Schwienhorst, A. (2003) · Chemistry & Biology · doi:10.1016/s1074-5521(02)00305-8 · Cited by 283 · 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

Dose-dependent Blockade to Cardiomyocyte Hypertrophy by Histone Deacetylase Inhibitors

Antos, C. L., McKinsey, T. A., Dreitz, M., Hollingsworth, L. M., Zhang, C., Schreiber, K. L., Rindt, H., Gorczynski, R. J., & Olson, E. N. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303113200 · Cited by 269 · see citing works

The Substrate Specificity of Sirtuins

Bheda, P., Jing, H., Wolberger, C., & Lin, H. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014537 · Cited by 247 · see citing works

Mitochondrial sirtuins

Huang, J.-Y., Hirschey, M. D., Shimazu, T., Ho, L., & Verdin, E. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.12.021 · Cited by 231 · see citing works

The sirtuin pathway in ageing and Alzheimer disease: mechanistic and therapeutic considerations

Bonda, D., Lee, H., Camins, A., Pallàs, M., Casadesús, G., Smith, M. A., & Zhu, X. (2011) · The Lancet Neurology · doi:10.1016/s1474-4422(11)70013-8 · Cited by 221 · see citing works

The Interactome of the Glucocorticoid Receptor and Its Influence on the Actions of Glucocorticoids in Combatting Inflammatory and Infectious Diseases

Πέττα, Ι., Dejager, L., Ballegeer, M., Lievens, S., Tavernier, J. H., Bosscher, K. D., & Libert, C. (2016) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00064-15 · Cited by 202 · see citing works

Structural Studies of Human Histone Deacetylase 8 and Its Site-Specific Variants Complexed with Substrate and Inhibitors^,

Dowling, D. P., Gantt, S. L., Gattis, S. G., Fierke, C. A., & Christianson, D. W. (2008) · Biochemistry · doi:10.1021/bi801610c · Cited by 200 · see citing works

Cancer Drug Discovery and Development

Humphrey, J. S., Price, K., Gupta, E., Baxter, A. R. W., Bird, J., Sonnichsen, D. S., & Naglich, J. G. (2003) · Humana Press eBooks · doi:10.1007/978-1-59259-325-5_21 · Cited by 195 · see citing works

Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress

Hentchel, K. L., & Escalante‐Semerena, J. C. (2015) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00020-15 · Cited by 190 · see citing works

Functional Proteomics Establishes the Interaction of SIRT7 with Chromatin Remodeling Complexes and Expands Its Role in Regulation of RNA Polymerase I Transcription

Tsai, Y.-C., Greco, T. M., Boonmee, A., Miteva, Y., & Cristea, I. M. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.a111.015156 · Cited by 198 · see citing works

Post-translational Protein Acetylation: An Elegant Mechanism for Bacteria to Dynamically Regulate Metabolic Functions

Christensen, D. G., Xie, X., Basisty, N., Byrnes, J., McSweeney, S. M., Schilling, B., & Wolfe, A. J. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.01604 · Cited by 179 · see citing works

Melatonin and sirtuins: A “not-so unexpected” relationship

Mayo, J. C., Sainz, R. M., González Menéndez, P., Cepas, V., Tan, D., & Reiter, R. J. (2017) · Journal of Pineal Research · doi:10.1111/jpi.12391 · Cited by 175 · see citing works

Inhibition of class I histone deacetylase with an apicidin derivative prevents cardiac hypertrophy and failure

Gallo, P., Latronico, M. V. G., Gallo, P., Grimaldi, S., Borgia, F., Todaro, M., JONES, P. G., Gallinari, P., Francesco, R. D., Ciliberto, G., et al. (2008) · Cardiovascular Research · doi:10.1093/cvr/cvn215 · Cited by 170 · see citing works

Arginase: Structure, Mechanism, and Physiological Role in Male and Female Sexual Arousal

Christianson, D. W. (2005) · Accounts of Chemical Research · doi:10.1021/ar040183k · Cited by 168 · see citing works

Epigenetics in Cardiac Hypertrophy and Heart Failure

Liu, C., & Tang, W. H. W. (2019) · JACC Basic to Translational Science · doi:10.1016/j.jacbts.2019.05.011 · Cited by 150 · see citing works

Histone deacetylase 11 is an ε-N-Myristoyllysine hydrolase

Moreno-Yruela, C., Galleano, I., Madsen, A. S., & Olsen, C. A. (2018) · Cell Chemical Biology · doi:10.1016/j.chembiol.2018.04.007 · Cited by 149 · see citing works

The human SIRT3 protein deacetylase is exclusively mitochondrial

Cooper, H. M., & Spelbrink, J. N. (2008) · Biochemical Journal · doi:10.1042/bj20071624 · Cited by 133 · see citing works

Improved fluorogenic histone deacetylase assay for high-throughput-screening applications

Wegener, D., Hildmann, C., Riester, D., & Schwienhorst, A. (2003) · Analytical Biochemistry · doi:10.1016/s0003-2697(03)00426-3 · Cited by 112 · see citing works

Structure of the Yeast Hst2 Protein Deacetylase in Ternary Complex with 2′-O-Acetyl ADP Ribose and Histone Peptide

Zhao, K., Chai, X., & Marmorstein, R. (2003) · Structure · doi:10.1016/j.str.2003.09.016 · Cited by 110 · see citing works

Structure and autoregulation of the yeast Hst2 homolog of Sir2

Zhao, K., Chai, X., Clements, A. M., & Marmorstein, R. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb978 · Cited by 109 · see citing works

Circulating Nucleosomes and Nucleosome Modifications as Biomarkers in Cancer

McAnena, P. F., Brown, J. A. L., & Kerin, M. J. (2017) · Cancers · doi:10.3390/cancers9010005 · Cited by 107 · see citing works

Chemical and structural biology of protein lysine deacetylases

Yoshida, M., Kudo, N., Kosono, S., & Ito, A. (2017) · Proceedings of the Japan Academy Series B · doi:10.2183/pjab.93.019 · Cited by 102 · see citing works

Structure and chemistry of the Sir2 family of NAD+-dependent histone/protein deactylases

Marmorstein, R. (2004) · Biochemical Society Transactions · doi:10.1042/bst0320904 · Cited by 84 · see citing works

Sirtuins: Novel targets for metabolic disease in drug development

Jiang, W. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.06.048 · Cited by 82 · see citing works

Mechanism‐Based Inhibitors of the Human Sirtuin 5 Deacylase: Structure–Activity Relationship, Biostructural, and Kinetic Insight

Rajabi, N., Auth, M., Troelsen, K. R., Pannek, M., Bhatt, D. P., Fontenas, M., Hirschey, M. D., Steegborn, C., Madsen, A. S., & Olsen, C. A. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201709050 · Cited by 75 · see citing works

HDAC1/2/3 are major histone desuccinylases critical for promoter desuccinylation

Li, J., Lu, L., Liu, L., Ren, X., Chen, J., Yin, X., Xiao, Y., Li, J., Wei, G., Huang, H., et al. (2023) · Cell Discovery · doi:10.1038/s41421-023-00573-9 · Cited by 76 · see citing works

Evolution of the arginase fold and functional diversity

Dowling, D., Costanzo, L. D., Gennadios, H. A., & Christianson, D. W. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-7554-z · Cited by 73 · see citing works

Histone deacetylase 2 selective inhibitors: A versatile therapeutic strategy as next generation drug target in cancer therapy

Shetty, M. G., Pai, P., Deaver, R. E., Satyamoorthy, K., & Babitha, K. S. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105695 · Cited by 73 · see citing works

Aryl Fluorosulfate Based Inhibitors That Covalently Target the SIRT5 Lysine Deacylase**

Bolding, J. E., Martín‐Gago, P., Rajabi, N., Gamon, L. F., Hansen, T. N., Bartling, C. R. O., Strømgaard, K., Davies, M. J., & Olsen, C. A. (2022) · Angewandte Chemie International Edition · doi:10.1002/anie.202204565 · Cited by 52 · see citing works

Targeting Sirtuins: Substrate Specificity and Inhibitor Design

Rajabi, N., Galleano, I., Madsen, A. S., & Olsen, C. A. (2018) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2017.11.003 · Cited by 52 · see citing works

A New Amidohydrolase from Bordetella or Alcaligenes Strain FB188 with Similarities to Histone Deacetylases

Hildmann, C., Ninković, M., Dietrich, R., Wegener, D., Riester, D., Zimmermann, T. P., Birch, O. M., Bernegger, C., Loidl, P., & Schwienhorst, A. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.8.2328-2339.2004 · Cited by 52 · see citing works

Biochemical and Mutational Analyses of AcuA, the Acetyltransferase Enzyme That Controls the Activity of the Acetyl Coenzyme A Synthetase (AcsA) in Bacillus subtilis

Gardner, J. G., & Escalante‐Semerena, J. C. (2008) · Journal of Bacteriology · doi:10.1128/jb.00340-08 · Cited by 49 · see citing works

Assays for the Determination of Structure and Dynamics of the Interaction of the Chromodomain with Histone Peptides

Jacobs, S. A., Fischle, W., & Khorasanizadeh, S. (2003) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(03)76009-1 · Cited by 47 · see citing works

Sirtuin 3 enhanced drug sensitivity of human hepatoma cells through glutathione S-transferase pi 1/JNK signaling pathway

Tao, N., Zhou, H., Tang, H., Cai, X.-F., Zhang, W., Ren, J., Zhou, L., Chen, X., Chen, K., Li, W., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.10319 · Cited by 44 · see citing works

Overexpression of Cytoplasmic TcSIR2RP1 and Mitochondrial TcSIR2RP3 Impacts on Trypanosoma cruzi Growth and Cell Invasion

Ritagliati, C., Alonso, V. L., Manarin, R., Cribb, P., & Serra, E. C. (2015) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0003725 · Cited by 42 · see citing works

Zn2+-Dependent Histone Deacetylases in Plants: Structure and Evolution

Yruela, I., Moreno–Yruela, C., & Olsen, C. A. (2021) · Trends in Plant Science · doi:10.1016/j.tplants.2020.12.011 · Cited by 41 · see citing works

Recent progress in the development of assays suited for histone deacetylase inhibitor screening

Wegener, D., Hildmann, C., & Schwienhorst, A. (2003) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2003.08.008 · Cited by 41 · see citing works

Post-translational Lysine Ac(et)ylation in Bacteria: A Biochemical, Structural, and Synthetic Biological Perspective

Lammers, M. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.757179 · Cited by 41 · see citing works

Histone acetyltransferases and deacetylase in Entamoeba histolytica

Ramakrishnan, G., Gilchrist, C. A., Musa, H., Torok, M. S., Grant, P. A., Mann, B. J., & Petri, W. A. (2004) · Molecular and Biochemical Parasitology · doi:10.1016/j.molbiopara.2004.09.002 · Cited by 40 · see citing works

Functional Proteomics Establishes the Interaction of SIRT7 with Chromatin Remodeling Complexes and Expands Its Role in Regulation of RNA Polymerase I Transcription

Tsai, Y.-C., Greco, T. M., Boonmee, A., Miteva, Y., & Cristea, I. M. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.015156 · Cited by 36 · see citing works

Identification of HDAC Inhibitors Using a Cell-Based HDAC I/II Assay

Hsu, C.-W., Shou, D., Huang, R., Khuc, T., Dai, S., Zheng, W., Klumpp-Thomas, C. A., & Xia, M. (2016) · SLAS DISCOVERY · doi:10.1177/1087057116629381 · Cited by 35 · see citing works

Rational Drug Design of Antineoplastic Agents Using 3D-QSAR, Cheminformatic, and Virtual Screening Approaches

Vučićević, J., Nikolic, K. M., & Mitchell, J. B. O. (2019) · Current Medicinal Chemistry · doi:10.2174/0929867324666170712115411 · Cited by 35 · see citing works

Ecdysone Induced Gene Expression Is Associated with Acetylation of Histone H3 Lysine 23 in Drosophila melanogaster

Bodai, L., Zsindely, N., Gáspár, R., Kristó, I., Komonyi, O., & Boros, I. (2012) · PLoS ONE · doi:10.1371/journal.pone.0040565 · Cited by 31 · see citing works

Structural basis for the regulation of nucleosome recognition and HDAC activity by histone deacetylase assemblies

Lee, J., Bollschweiler, D., Schäfer, T., & Huber, R. (2021) · Science Advances · doi:10.1126/sciadv.abd4413 · Cited by 29 · see citing works

Antiproliferative and Phenotype-Transforming Antitumor Agents Derived from Cysteine

Glenn, M. P., Kahnberg, P., Boyle, G. M., Hansford, K. A., Hans, D., Martyn, A. C., Parsons, P. G., & Fairlie, D. P. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm030222i · Cited by 29 · see citing works

Nuclear import and activity of histone deacetylase in Xenopus oocytes is regulated by phosphorylation

Smillie, D. A., Llinas, A. J., Ryan, J. T. P., Kemp, G. D., & Sommerville, J. (2004) · Journal of Cell Science · doi:10.1242/jcs.01008 · Cited by 29 · see citing works

Chromatin Modification and Senescence: Linkage by Tumor Suppressors?

Han, X., Berardi, P., & Riabowol, K. T. (2006) · Rejuvenation Research · doi:10.1089/rej.2006.9.69 · Cited by 20 · see citing works

The Crystal Structure of CCG1/TAFII250-interacting Factor B (CIB)

Padmanabhan, B., Kuzuhara, T., Adachi, N., & Horikoshi, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312165200 · Cited by 19 · see citing works

Epigenetic Regulation of Resistance to Emotional Stress: Possible Involvement of 5-HT1A Receptor–Mediated Histone Acetylation

Tsuji, M., Miyagawa, K., & Takeda, H. (2014) · Journal of Pharmacological Sciences · doi:10.1254/jphs.14r07cp · Cited by 19 · see citing works

Histone acetyltransferase CBP-related H3K23 acetylation contributes to courtship learning in Drosophila

Li, K.-L., Zhang, L., Yang, X., Fang, Q., Yin, X.-F., Wei, H.-M., Zhou, T., Li, Y., Chen, X., Tang, F., et al. (2018) · BMC Developmental Biology · doi:10.1186/s12861-018-0179-z · Cited by 19 · see citing works

Chromatin Acetylation Status in the Manifestation of Neurodegenerative Diseases

Boutillier, A., Rouaux, C., Panteleeva, I., & Loeffler, J. (2007) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/1-4020-5466-1_12 · Cited by 19 · see citing works

Exceptionally versatile take II: post-translational modifications of lysine and their impact on bacterial physiology

Lassak, J., Sieber, A., & Hellwig, M. (2022) · Biological Chemistry · doi:10.1515/hsz-2021-0382 · Cited by 17 · see citing works

Histone Deacetylases Function in the Control of Early Hematopoiesis and Erythropoiesis

Vong, P., Ouled‐Haddou, H., & Garçon, L. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23179790 · Cited by 17 · see citing works

Effects of tyroservatide on histone acetylation in lung carcinoma cells

Xu, Q., Lu, R., Zhu, Z., Lv, J., Wang, L., Zhang, W., Hu, J., Meng, J., Lin, G., & Yao, Z. Q. (2010) · International Journal of Cancer · doi:10.1002/ijc.25346 · Cited by 16 · see citing works

Mechanism‐Based Inhibitors of the Human Sirtuin 5 Deacylase: Structure–Activity Relationship, Biostructural, and Kinetic Insight

Rajabi, N., Auth, M., Troelsen, K. R., Pannek, M., Bhatt, D. P., Fontenas, M., Hirschey, M. D., Steegborn, C., Madsen, A. S., & Olsen, C. A. (2017) · Angewandte Chemie · doi:10.1002/ange.201709050 · Cited by 14 · see citing works

Structural genomics of histone tail recognition

Wang, M., Mok, M. W., Harper, H., Lee, W. H., Min, J., Knapp, S., Oppermann, U. C. T., Marsden, B. D., & Schapira, M. (2010) · Bioinformatics · doi:10.1093/bioinformatics/btq491 · Cited by 12 · see citing works

Trichostatin A reduced phospholipase C gamma-1 transcript and protein contents in MCF-7 breast cancer cells

Drzewiecka, H., & Jagodziński, P. P. (2011) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2011.09.005 · Cited by 10 · see citing works

A novel method for purification of polymerizable tubulin with a high content of the acetylated isotype

Carbajal, A., Chesta, M. E., Bisig, C. G., & Arce, C. A. (2012) · Biochemical Journal · doi:10.1042/bj20121439 · Cited by 9 · see citing works

Epigenetic Therapy as a Putative Molecular Target to Modulate B Cell Biology and Behavior in the Context of Immunological Disorders

da Costa, T. P., El-Cheikh, M. C., & Carneiro, K. (2020) · Journal of Immunology Research · doi:10.1155/2020/1589191 · Cited by 8 · see citing works

A novel hydroxysuberamide derivative potentiates MG132‐mediated anticancer activity against human hormone refractory prostate cancers—the role of histone deacetylase and endoplasmic reticulum stress

Chen, Y., Huang, W., Hsu, J., Yu, C., Wang, W., & Guh, J. (2013) · The Prostate · doi:10.1002/pros.22641 · Cited by 6 · see citing works

Histone Deacetylase 1

Meunier, D., & Seiser, C. (2006) · Humana Press eBooks · doi:10.1385/1-59745-024-3:3 · Cited by 5 · see citing works

Cloning and expression analysis of PtHDT903, a HD2-type histone deacetylase gene in Populus trichocarpa

Tong, B., Xia, D., Lv, S., & Ma, X. (2018) · Biotechnology & Biotechnological Equipment · doi:10.1080/13102818.2018.1478749 · Cited by 5 · see citing works

Therapeutic Aspects of Melatonin-sirtuin Crosstalk: An Updated Review of Current Data Based on Cellular Mechanisms

Hosseinzadeh, A., Seirafianpour, F., Sheibani, M., Taheri, M., Naeini, A. J., Reiter, R. J., & Mehrzadi, S. (2025) · Current Drug Targets · doi:10.2174/0113894501360934250512052503 · Cited by 4 · see citing works

Temporal perturbation of histone deacetylase activity reveals a requirement for HDAC1–3 in mesendoderm cell differentiation

Sinniah, E., Wu, Z., Shen, S., Naval-Sánchez, M., Chen, X., Lim, J., Helfer, A., Iyer, A., Tng, J., Lucke, A. J., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110818 · Cited by 4 · see citing works

Cloning, expression, and biochemical characterization of a new histone deacetylase-like protein from Thermus caldophilus GK24

Song, Y., Kim, Y. S., Kim, D., Lee, D., & Kwon, H. J. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.06.147 · Cited by 4 · see citing works

Ion mobility-mass spectrometry reveals evidence of specific complex formation between human histone deacetylase 8 and poly-r(C)-binding protein 1

Niu, S., Kim, B. C., Fierke, C. A., & Ruotolo, B. T. (2016) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2016.12.017 · Cited by 4 · see citing works

Determination and stress studies on YK-1101, a potential histone deacetylase, by HPLC–UV and HPLC–TOF/MS methods

Zhou, C., Liu, W., Feng, F., Hai, Y., & Wu, C. (2013) · Journal of Pharmaceutical Analysis · doi:10.1016/j.jpha.2013.01.003 · Cited by 3 · see citing works

Post-translational Modification

Wang, J., & Schwartz, R. J. (2015) · Springer eBooks · doi:10.1007/978-3-7091-1883-2_14 · Cited by 3 · see citing works

Systematic Analysis of Lysine Acetylation Reveals Diverse Functions in Azorhizobium caulinodans Strain ORS571

Liu, Y., Liu, X., Dong, X., Yin, Z., Xie, Z., & Luo, Y. (2022) · Microbiology Spectrum · doi:10.1128/spectrum.03539-22 · Cited by 2 · see citing works

Histone Deacetylases in Vascular Pathophysiology: Regulation by Vasoactive Peptides and Growth Factors

Pietruczuk, P., & Srivastava, A. K. (2017) · Springer eBooks · doi:10.1007/978-3-319-60324-7_14 · Cited by 2 · see citing works

Caloric Restriction and Oxidative Stress

Škrha, J. (2011) · doi:10.1002/9781118148143.ch6 · Cited by 2 · see citing works

In vitro characterization of the catalytic domain of human histone deacetylase 5

Mammen, C., Hornung, F. M., Anzenhofer, C., Schumacher, J., Reiners, J., Li, J., Mazzone, F., Bilsing, F. L., Kassack, M. U., Kurz, T., et al. (2026) · Scientific Reports · doi:10.1038/s41598-026-37633-5 · Cited by 1 · see citing works

Understanding the Posttranslational Regulation of the Response Regulator Rcsb and Acetyl Phosphate as an Acetyl Group Donor in E. Coli

Hu, L. I. (2013) · Loyola eCommons (Loyola University of Chicago) · Cited by 1 · see citing works

Association Between a Sirtuin 5 SNP (rs SIRT5 SNP, rs9382222) and Three Functional Markers of Brain Health

Velazquez, E. I. (2011) · D-Scholarship@Pitt (University of Pittsburgh) · Cited by 1 · see citing works

A Review of Sirtuin Inhibitors in Therapeutics, Pharmaceutics, and Plant Research

Lee, Y. (2020) · Journal of Life Science · Cited by 1 · see citing works

A synthetic lethal screen identifies HDAC4 as a potential target in MELK overexpressing cancers

Zhou, L., Zheng, S., Bringas, F. R. R., Bakker, B., Simon, J. E., Bakker, P. L., Kazemier, H. G., Schubert, M., Roorda, M., van Vugt, M. A. T. M., et al. (2021) · G3 Genes Genomes Genetics · doi:10.1093/g3journal/jkab335 · Cited by 1 · see citing works

Aryl Fluorosulfate Based Inhibitors That Covalently Target the SIRT5 Lysine Deacylase**

Bolding, J. E., Martín‐Gago, P., Rajabi, N., Gamon, L. F., Hansen, T. N., Bartling, C. R. O., Strømgaard, K., Davies, M. J., & Olsen, C. A. (2022) · Angewandte Chemie · doi:10.1002/ange.202204565 · Cited by 2 · see citing works

Integrative Structural Modeling of Intrinsically Disordered Regions in a Human HDAC2 Chromatin Remodeling ComplexPreprint

Nde, J., Kempf, C. G., Zimmermann, R. C., Cesare, J., Zhang, Y., Workman, J. L., Florens, L. A., & Washburn, M. P. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.08.08.669391 · Cited by 2 · see citing works

Application of a Drosophila model to study Huntington's disease pathogenesis in vivo

Bodai, L. (2004) · SZTE Repository of Dissertations (University of Szeged)

Histone deacetylases and their co-regulators in Schizosaccharomyces pombe

Silverstein, R. A. (2007) · Figshare

The Anaphase-Promoting Complex Interacts with Histone Modification Proteins and Chromatin Assembly Factors

Turner, E. L. (2011) · University Library - University of Saskatchewan (University of Saskatchewan)

In Vitro Histone Deacetylase Activity Screening

Sodji, Q. H., Kornacki, J. R., Mrksich, M., & Oyelere, A. K. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-801080-8.00015-6

Promiscuous gene expression in the thymic medulla – on regulation at the epigenetic and single cell level

Sinemus, A. (2009) · heiDOK (Heidelberg University) · doi:10.11588/heidok.00009968

NEW AND EMERGING HDAC INHIBITORS FOR THE TREATMENT OF DISEASES

Mahajan, S., & Chavan, A. B. (2014) · INDIAN DRUGS · doi:10.53879/id.51.06.10115

Interplay of histone acetylation and transcription factors in cardiac hypertrophy

Ramachandran, G., Sf, Q., Anantapur, & Nallari, P. (2011) · DOAJ (DOAJ: Directory of Open Access Journals)

Peptide molecular glues select between BET paralogues by exploiting allosteric sites and conformational dynamicsPreprint

Patel, K., Mohanty, B., Norman, A. R., Franck, C., Pachl, P., Yang, L., Jing, X., Reid, X. J., Walshe, J. L., Solomon, P. D., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.24.678353

ETUDE DE LA DEACETYLASE HDAC6 : UNE ENZYME MULTIFONCTIONNELLE

Gilquin, B. (2005) · OpenGrey (Institut de l'Information Scientifique et Technique)

Rôle de l'histone désacétylase HDAC6 au cours de l'érythropoïèse humaine

Vong, P. (2022) · doi:10.70675/699e8d9bz5404z43f6zabe7zdd0f0b6c8c42

Investigation of the classical histone deacetylases and sirtuins using peptide technologies

Rogers, J. M., & Olsen, C. A. (2026) · Cell chemical biology · doi:10.1016/j.chembiol.2026.08.009

Integrative Structural Modeling of Intrinsically Disordered Regions in a Human HDAC2 Chromatin Remodeling Complex

Nde, J., Kempf, C. G., Zimmermann, R. C., Cesare, J., Zhang, Y., Workman, J. L., Florens, L. A., & Washburn, M. P. (2026) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6c00256

BindingDB Entry 50031855: Inside HDAC with HDAC inhibitors.

BindingDB (2010) · UC San Diego · doi:10.7270/q2br8scs

BindingDB Entry 50014813: Antiproliferative and phenotype-transforming antitumor agents derived from cysteine.

BindingDB (2009) · UC San Diego · doi:10.7270/q2g44pr0

Histone Deacetylase

(2015) · Springer eBooks · doi:10.1007/978-3-642-36172-2_200668

Histone Deacetylases

(2001) · Springer eBooks · doi:10.1007/3-540-30683-8_769

Second Family of Histone Deacetylases

Aravind, L., & Koonin, E. V. (1998) · Science · doi:10.1126/science.280.5367.1167a · Cited by 52 · see citing works

the histone deacetylase

Tate, R. R., Rhodes, L. V., Segar, H. C., Driver, J. L., Pounder, F. N., Burow, M. E., & Collins‐Burow, B. M. (2016)

Structure, mechanism, and inhibition of histone deacetylases and related metalloenzymes

Lombardi, P. M., Cole, K., Dowling, D., & Christianson, D. W. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.08.004 · Cited by 279 · see citing works