HDACs, histone deacetylation and gene transcription: from molecular biology to cancer therapeutics
Abstract
Histone deacetylases (HDACs) and histone acetyl transferases (HATs) are two counteracting enzyme families whose enzymatic activity controls the acetylation state of protein lysine residues, notably those contained in the N-terminal extensions of the core histones. Acetylation of histones affects gene expression through its influence on chromatin conformation. In addition, several non-histone proteins are regulated in their stability or biological function by the acetylation state of specific lysine residues. HDACs intervene in a multitude of biological processes and are part of a multiprotein family in which each member has its specialized functions. In addition, HDAC activity is tightly controlled through targeted recruitment, protein-protein interactions and post-translational modifications. Control of cell cycle progression, cell survival and differentiation are among the most important roles of these enzymes. Since these processes are affected by malignant transformation, HDAC inhibitors were developed as antineoplastic drugs and are showing encouraging efficacy in cancer patients.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The mammalian HDAC family consists of 18 isoforms categorized into four major classes (Classes I-IV).
“The mammalian HDAC family consists of 18 isoforms categorized into four major classes (Classes I–IV) (Zhang et al., 2024; Glozak et al., 2005; Gallinari et al., 2007; Yang and Grégoire, 2005), as summarized in Table 1 (Vanaja et al., 2018; Johnstone, 2002; Gao et al., 2002; Tong et al., 2002; Hubbert et al., 2002).”
From Histone modifications and depression: epigenetic mechanisms, therapeutic targets, and translational outlook (2026) · cites this paper as Gallinari et al., 2007
Cites
Jenuwein, T., & Allis, C. D. (2001) · Science · doi:10.1126/science.1063127 · Cited by 9,756 · 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
Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain
Bannister, A. J., Zegerman, P., Partridge, J. F., Miska, E. A., Thomas, J. O., Allshire, R. C., & Kouzarides, T. (2001) · Nature · doi:10.1038/35065138 · Cited by 2,903 · see citing works
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 · see citing works
DNA methylation and human disease
Robertson, K. D. (2005) · Nature Reviews Genetics · doi:10.1038/nrg1655 · Cited by 2,864 · 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
HDAC6 is a microtubule-associated deacetylase
Hubbert, C., Guardiola, A., Shao, R., Kawaguchi, Y., Ito, A., Nixon, A., Yoshida, M., Wang, X.-F., & Yao, T.-P. (2002) · Nature · doi:10.1038/417455a · Cited by 2,403 · see citing works
Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
Minucci, S., & Pelicci, P. G. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1779 · Cited by 2,211 · see citing works
The diverse functions of histone lysine methylation
Martin, C., & Zhang, Y. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1761 · Cited by 2,066 · see citing works
Yoshida, M., Kijima, M., Akita, M., & Beppu, T. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44885-x · Cited by 1,856 · see citing works
Dent, S., Denu, J. M., & Allis, C. D. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.81 · Cited by 1,844 · see citing works
Role of Histone H3 Lysine 9 Methylation in Epigenetic Control of Heterochromatin Assembly
Nakayama, J.-I., Rice, J. C., Strahl, B. D., Allis, C. D., & Grewal, S. I. S. (2001) · Science · doi:10.1126/science.1060118 · Cited by 1,739 · 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
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
Kawaguchi, Y., Kovacs, J. J., McLaurin, A. C., Vance, J. M., Ito, A., & Yao, T. (2003) · Cell · doi:10.1016/s0092-8674(03)00939-5 · Cited by 1,529 · see citing works
The Sir2 Family of Protein Deacetylases
Blander, G., & Guarente, L. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073651 · Cited by 1,496 · see citing works
One‐thousand‐and‐one substrates of protein kinase CK2?
Meggio, F., & Pinna, L. A. (2003) · The FASEB Journal · doi:10.1096/fj.02-0473rev · Cited by 1,315 · see citing works
Duration of Nuclear NF-κB Action Regulated by Reversible Acetylation
Chen, L., Fischle, W., Verdin, E. M., & Greene, W. C. (2001) · Science · doi:10.1126/science.1062374 · Cited by 1,231 · see citing works
HDAC6 Regulates Hsp90 Acetylation and Chaperone-Dependent Activation of Glucocorticoid Receptor
Kovacs, J. J., Murphy, P. J. M., Gaillard, S., Zhao, X., Wu, J.-T., Nicchitta, C. V., Yoshida, M., Toft, D. O., Pratt, W. B., & Yao, T.-P. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.021 · Cited by 1,153 · see citing works
Zhang, Y., Ng, H.-H., Erdjument-Bromage, H., Tempst, P., Bird, A., & Reinberg, D. (1999) · Genes & Development · doi:10.1101/gad.13.15.1924 · Cited by 1,103 · see citing works
Haggarty, S. J., Koeller, K. M., Wong, J. C., Grozinger, C. M., & Schreiber, S. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0430973100 · Cited by 1,066 · 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
Class II Histone Deacetylases Act as Signal-Responsive Repressors of Cardiac Hypertrophy
Zhang, C. L., McKinsey, T. A., Chang, S., Antos, C. L., Hill, J. A., & Olson, E. N. (2002) · Cell · doi:10.1016/s0092-8674(02)00861-9 · Cited by 973 · see citing works
Kelly, W. K., O’Connor, O. A., Krug, L. M., Chiao, J. H., Heaney, M. L., Curley, T., MacGregor‐Cortelli, B., Tong, W. P., Secrist, J. P., Schwartz, L. B., et al. (2005) · Journal of Clinical Oncology · doi:10.1200/jco.2005.14.167 · Cited by 906 · see citing works
The many faces of histone lysine methylation
Lachner, M., & Jenuwein, T. (2002) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(02)00335-6 · Cited by 814 · see citing works
Histone Deacetylase 4 Controls Chondrocyte Hypertrophy during Skeletogenesis
Vega, R. B., Matsuda, K., Oh, J., Barbosa, A. C. C., Yang, X., Meadows, E., McAnally, J., Pomajzl, C., Shelton, J. M., Richardson, J. A., et al. (2004) · Cell · doi:10.1016/j.cell.2004.10.024 · Cited by 805 · see citing works
Stat3 Dimerization Regulated by Reversible Acetylation of a Single Lysine Residue
Yuan, Z.-L., Guan, Y.-J., Chatterjee, D., & Chin, Y. E. (2005) · Science · doi:10.1126/science.1105166 · Cited by 790 · see citing works
n-Butyrate causes histone modification in HeLa and Friend erythroleukaemia cells
Riggs, M. G., WHITTAKER, R. G., Neumann, J. R., & Ingram, V. M. (1977) · Nature · doi:10.1038/268462a0 · Cited by 777 · see citing works
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 · see citing works
Bali, P., Pranpat, M., Bradner, J., Balasis, M., Fiskus, W., Guo, F., Rocha, K., Kumaraswamy, S., Boyapalle, S., Atadja, P., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500186200 · Cited by 755 · see citing works
Gao, L., Cueto, M. A., Asselbergs, F., & Atadja, P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111871200 · Cited by 744 · see citing works
Histone Deacetylase Activity Is Required for Full Transcriptional Repression by mSin3A
Hassig, C. A., Fleischer, T. C., Billin, A. N., Schreiber, S. L., & Ayer, D. E. (1997) · Cell · doi:10.1016/s0092-8674(00)80214-7 · Cited by 740 · see citing works
(2002) · PubMed · Cited by 732 · see citing works
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 · see citing works
Structural Snapshots of Human HDAC8 Provide Insights into the Class I Histone Deacetylases
Somoza, J. R., Skene, R. J., Katz, B. A., Mol, C., Ho, J. D., Jennings, A. J., Luong, C., Arvai, A., Buggy, J. J., Chi, E., et al. (2004) · Structure · doi:10.1016/j.str.2004.04.012 · Cited by 710 · see citing works
Saito, A., Yamashita, T., Mariko, Y., Nosaka, Y., Tsuchiya, K., Ando, T., Suzuki, T., Tsuruo, T., & Nakanishi, O. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.8.4592 · Cited by 696 · see citing works
Zlokarnik, G., Negulescu, P. A., Knapp, T. E., Mere, L., Burres, N. S., Feng, L., Whitney, M. A., Roemer, K., & Tsien, R. Y. (1998) · Science · doi:10.1126/science.279.5347.84 · Cited by 691 · see citing works
Class II histone deacetylases: versatile regulators
Verdin, E., Dequiedt, F., & Kasler, H. G. (2003) · Trends in Genetics · doi:10.1016/s0168-9525(03)00073-8 · Cited by 664 · see citing works
(1996) · Europe PMC (PubMed Central) · Cited by 659 · see citing works
Butyric acid, a potent inducer of erythroid differentiation in cultured erythroleukemic cells
Leder, A., & Leder, P. (1975) · Cell · doi:10.1016/0092-8674(75)90107-5 · Cited by 659 · see citing works
Vannini, A., Volpari, C., Filocamo, G., Casavola, E. C., Brunetti, M., Renzoni, D., Chakravarty, P., Paolini, C., De Francesco, R., Gallinari, P., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404603101 · Cited by 638 · see citing works
Self-citationNowak, S. J., & Corces, V. G. (2004) · Trends in Genetics · doi:10.1016/j.tig.2004.02.007 · Cited by 622 · see citing works
Chang, S., McKinsey, T. A., Zhang, C. L., Richardson, J. A., Hill, J. A., & Olson, E. N. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.19.8467-8476.2004 · Cited by 612 · see citing works
The SMRT and N-CoR Corepressors Are Activating Cofactors for Histone Deacetylase 3
Guenther, M. G., Barak, O., & Lazar, M. A. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.18.6091-6101.2001 · Cited by 611 · see citing works
The diverse functions of histone acetyltransferase complexes
Carrozza, M. J., Utley, R. T., Workman, J. L., & Côté, J. (2003) · Trends in Genetics · doi:10.1016/s0168-9525(03)00115-x · Cited by 576 · see citing works
Apicidin: A novel antiprotozoal agent that inhibits parasite histone deacetylase
Darkin‐Rattray, S. J., Gurnett, A. M., Myers, R. W., Dulski, P. M., Crumley, T. M., Allocco, J., Cannova, C., Meinke, P. T., Colletti, S. L., Bednarek, M. A., et al. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.23.13143 · Cited by 575 · see citing works
Wilson, A. J., Byun, D.-S., Popova, N., Murray, L. B., L'Italien, K., Sowa, Y., Arango, D., Velcich, A., Augenlicht, L. H., & Mariadason, J. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m510023200 · Cited by 575 · see citing works
Gui, C., Ngo, L., Xu, W., Richon, V. M., & Marks, P. A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307708100 · Cited by 550 · see citing works
Post-activation Turn-off of NF-κB-dependent Transcription Is Regulated by Acetylation of p65
Kiernan, R. E., Brès, V., Ng, R. W. M., Coudart, M.-P., Messaoudi, S. E., Sardet, C., Jin, D., Emiliani, S., & Benkirane, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209572200 · Cited by 536 · see citing works
Mitsiades, C. S., Mitsiades, N., McMullan, C. J., Poulaki, V., Shringarpure, R., Hideshima, T., Akiyama, M., Chauhan, D., Munshi, N. C., Gu, X., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2536759100 · Cited by 532 · see citing works
Induction of HDAC2 expression upon loss of APC in colorectal tumorigenesis
Zhu, P., Martin, E., Mengwasser, J., Schlag, P., Janssen, K., & Göttlicher, M. (2004) · Cancer Cell · doi:10.1016/s1535-6108(04)00114-x · Cited by 524 · see citing works
McKinsey, T. A., Zhang, C. L., & Olson, E. N. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.260501497 · Cited by 520 · see citing works
Kijima, M., Yoshida, M., Sugita, K., Horinouchi, S., & Beppu, T. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41547-5 · Cited by 516 · see citing works
Vega, R. B., Harrison, B. C., Meadows, E., Roberts, C. R., Papst, P. J., Olson, E. N., & McKinsey, T. A. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.19.8374-8385.2004 · Cited by 512 · see citing works
CoREST is an integral component of the CoREST- human histone deacetylase complex
You, A., Tong, J. K., Grozinger, C. M., & Schreiber, S. L. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.4.1454 · Cited by 500 · see citing works
Microarray Deacetylation Maps Determine Genome-Wide Functions for Yeast Histone Deacetylases
Robyr, D., Suka, Y., Xénarios, I., Kurdistani, S. K., Wang, A., Suka, N., & Grunstein, M. R. (2002) · Cell · doi:10.1016/s0092-8674(02)00746-8 · Cited by 468 · see citing works
Wang, D., Westerheide, S. D., Ostrander, J. H., & Baldwin, A. S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001358200 · Cited by 454 · see citing works
Histone Deacetylase 7 Maintains Vascular Integrity by Repressing Matrix Metalloproteinase 10
Chang, S., Young, B. D., Li, S., Qi, X., Richardson, J. A., & Olson, E. N. (2006) · Cell · doi:10.1016/j.cell.2006.05.040 · Cited by 454 · see citing works
p300 Transcriptional Repression Is Mediated by SUMO Modification
Girdwood, D., Bumpass, D. C., Vaughan, O. A., Thain, A., Anderson, L. A., Snowden, A. W., Garcia-Wilson, E., Perkins, N. D., & Hay, R. T. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00141-2 · Cited by 448 · see citing works
Active-site zinc ligands and activated H2O of zinc enzymes.
Vallée, B. L., & Auld, D. S. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.1.220 · Cited by 434 · see citing works
Second generation hybrid polar compounds are potent inducers of transformed cell differentiation.
Richon, V. M., Webb, Y., Merger, R., Sheppard, T. L., Jursic, B., Ngo, L., Civoli, F., Breslow, R., Rifkind, R. A., & Marks, P. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.12.5705 · Cited by 420 · see citing works
Genomewide studies of histone deacetylase function in yeast
Bernstein, B., Tong, J. K., & Schreiber, S. L. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.250477697 · Cited by 419 · see citing works
Class II Histone Deacetylases: from Sequence to Function, Regulation, and Clinical Implication
Yang, X., & Grégoire, S. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.8.2873-2884.2005 · Cited by 419 · see citing works
Zhang, J., Kalkum, M., Chait, B. T., & Roeder, R. G. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00468-9 · Cited by 414 · see citing works
Modulation of p53, ErbB1, ErbB2, and Raf-1 Expression in Lung Cancer Cells by Depsipeptide FR901228
Yu, X. (2002) · CancerSpectrum Knowledge Environment · doi:10.1093/jnci/94.7.504 · Cited by 360 · see citing works
Lysine acetylation and the bromodomain: a new partnership for signaling
Yang, X. (2004) · BioEssays · doi:10.1002/bies.20104 · Cited by 359 · see citing works
SUMO Promotes HDAC-Mediated Transcriptional Repression
Yang, S., & Sharrocks, A. D. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00060-7 · Cited by 351 · see citing works
Regulation of histone deacetylase activities
Sengupta, N., & Seto, E. (2004) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20179 · Cited by 347 · see citing works
Marks, P. A. (2003) · Current Opinion in Pharmacology · doi:10.1016/s1471-4892(03)00084-5 · Cited by 344 · see citing works
A new antifungal antibiotic, trichostatin.
Tsuji, N., Kobayashi, M., NAGASHIMA, K., Wakisaka, Y., & Koizumi, K. (1976) · The Journal of Antibiotics · doi:10.7164/antibiotics.29.1 · Cited by 341 · see citing works
Kelly, W. K., & Marks, P. A. (2005) · Nature Clinical Practice Oncology · doi:10.1038/ncponc0106 · Cited by 330 · see citing works
The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase
Kirsh, O., Seeler, J.-S., Pichler, A., Gast, A., Müller, S. P., Miska, E. A., Marion, M., Harel‐Bellan, A., Kouzarides, T., Melchior, F., et al. (2002) · The EMBO Journal · doi:10.1093/emboj/21.11.2682 · Cited by 328 · see citing works
Plumb, J. A., Finn, P. W., Williams, R. J., Bandara, M. J., Romero, M., Watkins, C. J., Thangue, N. B. L., & Brown, R. E. (2003) · PubMed · Cited by 312 · see citing works
Hu, E., Chen, Z., Fredrickson, T., Zhu, Y., Kirkpatrick, R., Zhang, G.-F., Johanson, K., Sung, C.-M., Liu, R., & Winkler, J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m908988199 · Cited by 309 · see citing works
Identification of a Signal-Responsive Nuclear Export Sequence in Class II Histone Deacetylases
McKinsey, T. A., Zhang, C. L., & Olson, E. N. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.18.6312-6321.2001 · Cited by 285 · see citing works
Genome-wide binding map of the histone deacetylase Rpd3 in yeast
Kurdistani, S. K., Robyr, D., Tavazoie, S., & Grunstein, M. (2002) · Nature Genetics · doi:10.1038/ng907 · Cited by 279 · see citing works
Requirement of Hos2 Histone Deacetylase for Gene Activity in Yeast
Wang, A., Kurdistani, S. K., & Grunstein, M. R. (2002) · Science · doi:10.1126/science.1077790 · Cited by 272 · see citing works
Regulation of MEF2 by Histone Deacetylase 4- and SIRT1 Deacetylase-Mediated Lysine Modifications
Zhao, X., Sternsdorf, T., Bolger, T. A., Evans, R. M., & Yao, T.-P. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.19.8456-8464.2005 · Cited by 264 · see citing works
Negative and Positive Regulation of Gene Expression by Mouse Histone Deacetylase 1
Zupkovitz, G., Tischler, J., Posch, M., Sadzak, I., Ramsauer, K., Egger, G., Grausenburger, R., Schweifer, N., Chiocca, S., Decker, T., et al. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01220-06 · Cited by 262 · see citing works
The Retinoblastoma-Histone Deacetylase 3 Complex Inhibits PPARγ and Adipocyte Differentiation
Lluis Fajas, A., Egler, V., Reiter, R. J., Hansen, J. B., Kristiansen, K., Debril, M.-B., Miard, S., & Auwerx, J. H. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00360-x · Cited by 258 · see citing works
Histone Deacetylase 1 Phosphorylation Promotes Enzymatic Activity and Complex Formation
Pflum, M. K. H., Tong, J. K., Lane, W. S., & Schreiber, S. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105590200 · Cited by 253 · see citing works
Functional Domains of Histone Deacetylase-3
Yang, W., Tsai, S., Wen, Y., Fejér, G., & Seto, E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m105993200 · Cited by 247 · see citing works
Global Position and Recruitment of HATs and HDACs in the Yeast Genome
Robert, F., Pokholok, D., Hannett, N. M., Rinaldi, N. J., Chandy, M., Rolfe, A., Workman, J. L., Gifford, D. K., & Young, R. A. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.09.021 · Cited by 242 · see citing works
Momparler, R. L. (2003) · Oncogene · doi:10.1038/sj.onc.1206774 · Cited by 242 · see citing works
Collaborative spirit of histone deacetylases in regulating chromatin structure and gene expression
Yang, X., & Seto, E. (2003) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(03)00015-7 · Cited by 241 · see citing works
SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities
David, G., Neptune, M. A., & DePinho, R. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203690200 · Cited by 236 · see citing works
Chen, C., Weng, S., Tseng, P., Lin, H.-P., & Chen, C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505733200 · Cited by 232 · see citing works
Somech, R., Shaklai, S., Geller, O., Amariglio, N., Simon, A. J., Rechavi, G., & Gal-Yam, E. N. (2005) · Journal of Cell Science · doi:10.1242/jcs.02521 · Cited by 223 · see citing works
Zhang, X. M., Ozawa, Y., Lee, H., Wen, Y., Tan, T., Wadzinski, B. E., & Seto, E. (2005) · Genes & Development · doi:10.1101/gad.1286005 · Cited by 222 · see citing works
Egger, G., Doetzlhofer, A., Schuettengruber, B., Haidweger, E., Simboeck, E., Tischler, J., Chiocca, S., Suske, G., Rotheneder, H., Wintersberger, E., et al. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.8.2669-2679.2003 · Cited by 214 · see citing works
Dequiedt, F., Kasler, H. G., Fischle, W., Kiermer, V., Weinstein, M., HERNDIER, B. G., & Verdin, E. M. (2003) · Immunity · doi:10.1016/s1074-7613(03)00109-2 · Cited by 212 · see citing works
Grégoire, S., & Yang, X. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.6.2273-2287.2005 · Cited by 207 · see citing works
Protein kinase CK2 and protein kinase D are associated with the COP9 signalosome
Uhle, S., Medalia, O., Waldron, R. T., Dumdey, R., Henklein, P., Bech‐Otschir, D., Huang, X., Berse, M., Sperling, J. M., Schade, R., et al. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg127 · Cited by 202 · see citing works
Haggarty, S. J., Koeller, K. M., Wong, J. C., Butcher, R. A., & Schreiber, S. L. (2003) · Chemistry & Biology · doi:10.1016/s1074-5521(03)00095-4 · Cited by 201 · see citing works
Itazaki, H., NAGASHIMA, K., Sugita, K., Yoshida, H., Kawamura, Y., YASUDA, Y., Matsumoto, K., ISHII, K., UOTANI, N., Nakai, H., et al. (1990) · The Journal of Antibiotics · doi:10.7164/antibiotics.43.1524 · Cited by 198 · see citing works
Waltregny, D., Glénisson, W., Tran, S. L., North, B. J., Verdin, E. M., Colige, A., & Castronovo, V. (2005) · The FASEB Journal · doi:10.1096/fj.04-2303fje · Cited by 197 · see citing works
Regulation of histone deacetylase 2 by protein kinase CK2
Tsai, S.-C., & Seto, E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204149200 · Cited by 196 · see citing works
Isolierung und Strukturaufklärung von Chlamydocin
Closse, A., & Huguenin, R. (1974) · Helvetica Chimica Acta · doi:10.1002/hlca.19740570306 · Cited by 190 · see citing works
Intracellular Trafficking of Histone Deacetylase 4 Regulates Neuronal Cell Death
Bolger, T. A., & Yao, T. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.1826-05.2005 · Cited by 190 · see citing works
Attenuation of a phosphorylation-dependent activator by an HDAC–PP1 complex
Canettieri, G., Morantte, I. G., Guzmán, E., Asahara, H., Herzig, S., Anderson, S., Yates, J. R., & Montminy, M. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb895 · Cited by 188 · see citing works
Xu, W., Ngo, L., Perez, G., Dokmanovic, M., & Marks, P. A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607518103 · Cited by 179 · see citing works
Li, D., Yea, S., Li, S., Zhu, C. X., Narla, G., Banck, M. S., Laborda, J., Tan, S., Friedman, J. M., Friedman, S. L., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500463200 · Cited by 177 · see citing works
A novel histone deacetylase pathway regulates mitosis by modulating Aurora B kinase activityPreprint
Li, Y., Kao, G. D., Garcia, B. A., Shabanowitz, J., Hunt, D. F., Qin, J., Phelan, C. A., & Lazar, M. A. (2006) · Genes & Development · doi:10.1101/gad.1455006 · Cited by 175 · see citing works
Control of MEF2 Transcriptional Activity by Coordinated Phosphorylation and Sumoylation
Grégoire, S., Tremblay, A., Xiao, L., Yang, Q., Ma, K., Nie, J., Mao, Z., Wu, Z., Giguère, V., & Yang, X. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509471200 · Cited by 171 · see citing works
Dequiedt, F., Lint, J. V., Lecomte, E., Duppen, V. V., Seufferlein, T. T. W., Vandenheede, J. R., Wattiez, R., & Kettmann, R. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20042034 · Cited by 171 · 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
Histone ubiquitination: a tagging tail unfolds?
Jason, L. J. M., Moore, S. C., Lewis, J. D., Lindsey, G. G., & Ausió, J. (2002) · BioEssays · doi:10.1002/bies.10038 · Cited by 164 · see citing works
Durst, K. L., Lutterbach, B., Kummalue, T., Friedman, A. D., & Hiebert, S. W. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.2.607-619.2003 · Cited by 161 · see citing works
Galasinski, S. C., Resing, K. A., Goodrich, J. A., & Ahn, N. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201174200 · Cited by 157 · see citing works
Crystal Structure of a Bacterial Class 2 Histone Deacetylase Homologue
Nielsen, T. K., Hildmann, C., Dickmanns, A., Schwienhorst, A., & Ficner, R. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.09.065 · Cited by 157 · see citing works
Regulation of Cardiac Stress Signaling by Protein Kinase D1
Harrison, B. C., Kim, M.-S., van Rooij, E., Plato, C. F., Papst, P. J., Vega, R. B., McAnally, J., Richardson, J. A., Bassel‐Duby, R., Olson, E. N., et al. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.10.3875-3888.2006 · Cited by 155 · see citing works
Ling, Y. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh195 · Cited by 155 · see citing works
Negative regulation of histone deacetylase 8 activity by cyclic AMP-dependent protein kinase A
Lee, H., Rezai-Zadeh, N., & Seto, E. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.2.765-773.2004 · Cited by 153 · see citing works
Zhao, X., Ito, A., Kane, C. D., Liao, T.-S., Bolger, T. A., Lemrow, S. M., Means, A. R., & Yao, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105086200 · Cited by 151 · see citing works
Liu, Y., Randall, W. R., & Schneider, M. F. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200408128 · Cited by 150 · see citing works
Trifluoromethyl ketones as inhibitors of histone deacetylase
Frey, R. R., Wada, C. K., Garland, R. B., Curtin, M. L., Michaelides, M. R., Li, J., Pease, L. J., Glaser, K. B., Marcotte, P. A., Bouska, J. J., et al. (2002) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(02)00754-0 · Cited by 149 · see citing works
Histone deacetylase inhibitors: insights into mechanisms of lethality
Rosato, R. R., & Grant, S. (2005) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.9.4.809 · Cited by 138 · see citing works
Chronic Oral Administration of CI-994: A Phase I Study
Prakash, S., Foster, B. J., Meyer, M., Wozniak, A., Heilbrun, L. K., Flaherty, L. E., Zalupski, M. M., Radulovic, L. L., Valdivieso, M., & LoRusso, P. M. (2001) · Investigational New Drugs · doi:10.1023/a:1006489328324 · Cited by 136 · see citing works
Isolation and Characterization of a Novel Class II Histone Deacetylase, HDAC10
Fischer, D. D., Cai, R. L., Bhatia, U., Asselbergs, F. A. M., Song, C., Terry, R., Trogani, N., Widmer, R., Atadja, P. W., & Cohen, D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108055200 · Cited by 133 · see citing works
Davis, F. J., Gupta, M., Camoretti-Mercado, B., Schwartz, R. J., & Gupta, M. P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209998200 · Cited by 132 · see citing works
Remiszewski, S., Sambucetti, L. C., Bair, K. W., Bontempo, J., Cesarz, D., Chandramouli, N., Chen, R., Cheung, M., Cornell-Kennon, S., Dean, K., et al. (2003) · Journal of Medicinal Chemistry · doi:10.1021/jm030235w · Cited by 130 · see citing works
Deactylase Inhibitors Disrupt Cellular Complexes Containing Protein Phosphatases and Deacetylases
Brush, M., Guardiola, A. R., Connor, J. H., Yao, T., & Shenolikar, S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310997200 · Cited by 128 · see citing works
Buggy, J. J., Cao, Z. A., Bass, K. E., Verner, E., Balasubramanian, S., Liu, L., Schultz, B. E., Young, P. R., & Dalrymple, S. A. (2006) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-05-0442 · Cited by 127 · see citing works
Protein Kinase CK2 as Regulator of Cell Survival: Implications for Cancer Therapy
Unger, G. M., Davis, A. R., Slaton, J. W., & Ahmed, K. (2004) · Current Cancer Drug Targets · doi:10.2174/1568009043481687 · Cited by 120 · see citing works
Histone deacetylase inhibitors and cancer: from cell biology to the clinic
Hess‐Stumpp, H. (2005) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2004.12.010 · Cited by 117 · see citing works
Histone modifications: Now summoning sumoylation
Nathan, D., Sterner, D. E., & Berger, S. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2436173100 · Cited by 116 · see citing works
Histone deacetylase 3 associates with and represses the transcription factor GATA-2
Ozawa, Y., Towatari, M., Tsuzuki, S., Hayakawa, F., Maeda, T., Miyata, Y., Tanimoto, M., & Saito, H. (2001) · Blood · doi:10.1182/blood.v98.7.2116 · Cited by 113 · see citing works
Alland, L., David, G., Shen-Li, H., Potes, J., Muhle, R., Lee, H.-C., Hou, H., Chen, K., & DePinho, R. A. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.8.2743-2750.2002 · Cited by 113 · see citing works
Histone deacetylase 3 localizes to the plasma membrane and is a substrate of Src
Longworth, M. S., & Laimins, L. A. (2006) · Oncogene · doi:10.1038/sj.onc.1209473 · Cited by 110 · see citing works
Lechner, T., Carrozza, M. J., Yu, Y., Grant, P. A., Eberharter, A., Vannier, D., Brosch, G., Stillman, D. J., Shore, D., & Workman, J. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005730200 · Cited by 97 · see citing works
Foglietti, C., Filocamo, G., Cundari, E., de Rinaldis, E., Lahm, A., Cortese, R., & Steinkühler, C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511945200 · Cited by 90 · see citing works
Self-citationThe Transcriptional Repressor Sp3 Is Associated with CK2-phosphorylated Histone Deacetylase 2
Sun, J.-M., Chen, H. Y., Moniwa, M., Litchfield, D. W., Seto, E., & Davie, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200378200 · Cited by 89 · see citing works
Kinetics and Comparative Reactivity of Human Class I and Class IIb Histone Deacetylases
Schultz, B. E., Misialek, S., Wu, J., Tang, J., Conn, M. T., Tahilramani, R., & Wong, L. (2004) · Biochemistry · doi:10.1021/bi0494471 · Cited by 88 · see citing works
The adenovirus protein Gam1 interferes with sumoylation of histone deacetylase 1
Colombo, R., Boggio, R., Seiser, C., Draetta, G. F., & Chiocca, S. (2002) · EMBO Reports · doi:10.1093/embo-reports/kvf213 · Cited by 87 · see citing works
Lee, H., Sengupta, N., Villagra, A., Rezai‐Zadeh, N., & Seto, E. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01971-05 · Cited by 86 · see citing works
The SIN3 Deacetylase Complex Represses Genes Encoding Mitochondrial Proteins
Pile, L. A., Spellman, P. T., Katzenberger, R. J., & Wassarman, D. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305996200 · Cited by 85 · see citing works
α-Keto amides as inhibitors of histone deacetylase
Wada, C. K., Frey, R. R., Ji, Z., Curtin, M. L., Garland, R. B., Holms, J. H., Li, J., Pease, L. J., Guo, J., Glaser, K. B., et al. (2003) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(03)00685-1 · Cited by 83 · see citing works
Hartman, H. B., Yu, J., Alenghat, T., Ishizuka, T., & Lazar, M. A. (2005) · EMBO Reports · doi:10.1038/sj.embor.7400391 · Cited by 82 · see citing works
Silence of the genes — mechanisms of long-term repression
Lande‐Diner, L., & Cedar, H. (2005) · Nature Reviews Genetics · doi:10.1038/nrg1639 · Cited by 80 · see citing works
Davis, A. P. (1999) · Nature · doi:10.1038/43576 · Cited by 77 · see citing works
Genome-wide expression screens indicate a global role for protein kinase CK2 in chromatin remodeling
Barz, T., Ackermann, K., Dubois, G., Eils, R., & Pyerin, W. G. (2003) · Journal of Cell Science · doi:10.1242/jcs.00352 · Cited by 72 · see citing works
Riester, D., Wegener, D., Hildmann, C., & Schwienhorst, A. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.09.155 · Cited by 68 · see citing works
He, X., Gonzalez-Pena, V., Tsang, A. H., Thompson, J., Tsang, T. C., & Harris, D. T. (2005) · Stem Cells and Development · doi:10.1089/scd.2005.14.188 · Cited by 68 · see citing works
A series of novel, potent, and selective histone deacetylase inhibitors
JONES, P. G., Altamura, S., Chakravarty, P. K., Cecchetti, O., Francesco, R. D., Gallinari, P., Ingenito, R., Meinke, P. T., Petrocchi, A., Rowley, M., et al. (2006) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2006.09.002 · Cited by 67 · see citing works
Self-citationKraker, A. J., Mizzen, C. A., Hartl, B. G., Miin, J., Allis, C. D., & Merriman, R. L. (2003) · PubMed · Cited by 64 · see citing works
Mammalian Histone Deacetylase 1 Protein Is Posttranslationally Modified by Phosphorylation
Cai, R. L., Kwon, P. O., Yan‐Neale, Y., Sambuccetti, L., Fischer, D. D., & Cohen, D. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.4786 · Cited by 62 · see citing works
The SMRT corepressor is a target of phosphorylation by protein kinase CK2 (casein kinase II)
Zhou, Y.-Y., Gross, W., Hong, S.-H., & Privalsky, M. (2001) · Molecular and Cellular Biochemistry · doi:10.1023/a:1011087910699 · Cited by 61 · see citing works
Goodwin, W. J., Lane, H. W., Bradford, K., Marshall, M. V., Griffin, A. C., Geopfert, H., & Jesse, R. H. (1983) · Cancer · doi:10.1002/1097-0142(19830101)51:1 · Cited by 52 · see citing works
Heterocyclic ketones as inhibitors of histone deacetylase
Vasudevan, A., Ji, Z., Frey, R. R., Wada, C. K., Steinman, D. H., Heyman, H. R., Guo, Y. P., Curtin, M. L., Guo, J., Li, J., et al. (2003) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2003.09.007 · Cited by 52 · see citing works
Expression and functional characterization of recombinant human HDAC1 and HDAC3
Li, J., Staver, M. J., Curtin, M. L., Holms, J. H., Frey, R. R., Edalji, R. P., Smith, R. A., Michaelides, M. R., Davidsen, S. K., & Glaser, K. B. (2004) · Life Sciences · doi:10.1016/j.lfs.2003.09.070 · Cited by 45 · see citing works
Sun, J.-M. (2003) · Methods · doi:10.1016/s1046-2023(03)00083-5 · Cited by 44 · see citing works
Olsen, E. A., Kim, Y. H., Kuzel, T. M., Pacheco, T. R., Foss, F. M., Parker, S. R. S., Wang, J. G., Frankel, S., Lis, J., & Duvic, M. A. (2006) · Journal of Clinical Oncology · doi:10.1200/jco.2006.24.18_suppl.7500 · Cited by 42 · see citing works
Chemical Constitution of the Host-Specific Toxin of Helminthosporium carbonum
Pringle, R. B. (1970) · PLANT PHYSIOLOGY · doi:10.1104/pp.46.1.45 · Cited by 35 · see citing works
Dynamics of Protein Kinase CK2 Association with Nucleosomes in Relation to Transcriptional Activity
Guo, C., Davis, A. T., & Ahmed, K. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.22.13675 · Cited by 33 · see citing works
Kim, S. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki985 · Cited by 32 · see citing works
Franco, P. J., Farooqui, M., Seto, E., & Wei, L. (2001) · Molecular Endocrinology · doi:10.1210/mend.15.8.0682 · Cited by 29 · see citing works
Guo, C., Davis, A. T., Yu, S., Tawfic, S. H., & Ahmed, K. (1999) · Springer eBooks · doi:10.1007/978-1-4419-8624-5_17 · Cited by 21 · see citing works
Guo, C., Davis, A. T., Yu, S., Tawfic, S. H., & Ahmed, K. (1999) · Molecular and Cellular Biochemistry · doi:10.1023/a:1006881405383 · Cited by 21 · see citing works
Hauschild, A., Trefzer, U., Garbe, C., Kaehler, K. C., Ugurel, S., Kiecker, F., Eigentler, T., Krissel, H., & Schadendorf, D. (2006) · Journal of Clinical Oncology · doi:10.1200/jco.2006.24.18_suppl.8044 · Cited by 20 · see citing works
Steele, N. L., Vidal, L., Plumb, J., Attard, G., Rasmussen, A., Buhl-Jensen, P., Brown, R. E., Blagden, S. P., Evans, J. A., & Bono, J. S. D. (2005) · Journal of Clinical Oncology · doi:10.1200/jco.2005.23.16_suppl.3035 · Cited by 19 · see citing works
Development of a melatonin-based formulation for the treatment of insomnia in the elderly
Zisapel, N. (2000) · Drug Development Research · doi:10.1002/1098-2299(200007/08)50:3/4 · Cited by 16 · see citing works
Ottmann, O. G., DeAngelo, D. J., Stone, R. M., Pfeifer, R., Löwenberg, B., Atadja, P. W., Peng, B., Scott, J. W., Dugan, M. H., & Sonneveld, P. (2004) · Journal of Clinical Oncology · doi:10.1200/jco.2004.22.14_suppl.3024 · Cited by 14 · see citing works
Whittaker, S. J., McCulloch, W. F., Robak, T., & Baran, E. (2006) · Journal of Clinical Oncology · doi:10.1200/jco.2006.24.18_suppl.3063 · Cited by 13 · see citing works
Identification of histone deacetylase-3 domains that interact with the orphan nuclear receptor TR2
Li, G., Franco, P. J., & Wei, L. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.08.145 · Cited by 9 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
The world of protein acetylation
Drazic, A., Myklebust, L. M., Ree, R., & Arnesen, T. (2016) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2016.06.007 · Cited by 798 · see citing works
SCFAs strongly stimulate PYY production in human enteroendocrine cells
Larraufie, P., Martin‐Gallausiaux, C., Lapaque, N., Dore, J. M., Gribble, F. M., Reimann, F. M., & Blottière, H. M. (2018) · Scientific Reports · doi:10.1038/s41598-017-18259-0 · Cited by 455 · see citing works
The emerging role of epigenetic therapeutics in immuno-oncology
Topper, M. J., Vaz, M., Marrone, K. A., Brahmer, J. R., & Baylin, S. B. (2020) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-019-0266-5 · Cited by 433 · see citing works
Novel histone deacetylase inhibitors in clinical trials as anti-cancer agents
Tan, J., Cang, S., Ma, Y., Petrillo, R. L., & Liu, D. (2010) · Journal of Hematology & Oncology · doi:10.1186/1756-8722-3-5 · Cited by 425 · see citing works
Jares, P., Colomer, D., & Campo, E. (2007) · Nature Reviews Cancer · doi:10.1038/nrc2230 · Cited by 466 · see citing works
Bhaskara, S., Chyla, B., Amann, J. M., Knutson, S. K., Cortez, D., Sun, Z., & Hiebert, S. W. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.02.030 · Cited by 369 · see citing works
Histone Deacetylase Inhibitors: From Bench to Clinic
Paris, M., Porcelloni, M., Binaschi, M., & Fattori, D. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm7011408 · Cited by 373 · see citing works
Epigenetic modulation and understanding of HDAC inhibitors in cancer therapy
Ramaiah, M. J., Tangutur, A. D., & Manyam, R. R. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119504 · Cited by 358 · see citing works
Hdac3 is essential for the maintenance of chromatin structure and genome stability
Bhaskara, S., Knutson, S. K., Jiang, G., Chandrasekharan, M. B., Wilson, A. J., Zheng, S., Yenamandra, A., Locke, K., Yuan, J.-L., Bonine-Summers, A. R., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.10.022 · Cited by 353 · see citing works
Dadashpour, S., & Emami, S. (2018) · European journal of medicinal chemistry · doi:10.1016/j.ejmech.2018.02.065 · Cited by 280 · see citing works
Bottomley, M. J., Surdo, P. L., Giovine, P. D., Cirillo, A., Scarpelli, R., Ferrigno, F., JONES, P. G., Neddermann, P., Francesco, R. D., Steinkühler, C., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803514200 · Cited by 319 · see citing works
Self-citationThe role of histone modifications: from neurodevelopment to neurodiseases
Park, J., Lee, K., Kim, K., & Yi, S.-J. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01078-9 · Cited by 321 · see citing works
Hodawadekar, S. C., & Marmorstein, R. (2007) · Oncogene · doi:10.1038/sj.onc.1210619 · Cited by 271 · see citing works
Liver-specific deletion of histone deacetylase 3 disrupts metabolic transcriptional networks
Knutson, S. K., Chyla, B. J., Amann, J. M., Bhaskara, S., Huppert, S. S., & Hiebert, S. W. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.51 · Cited by 271 · see citing works
Liu, R., Wu, J., Guo, H., Yao, W., Li, S., Lu, Y., Jia, Y., Liang, X., Tang, J., & Zhang, H. (2023) · MedComm · doi:10.1002/mco2.292 · Cited by 287 · see citing works
Vannini, A., Volpari, C., Gallinari, P., Jones, P., Mattu, M., Carfí, A., De Francesco, R., Steinkühler, C., & Di Marco, S. (2007) · The EMBO Reports · doi:10.1038/sj.embor.7401047 · Cited by 256 · see citing works
Self-citationThe Cytoplasmic Deacetylase HDAC6 Is Required for Efficient Oncogenic Tumorigenesis
Lee, Y.-S., Lim, K.-H., Guo, X., Kawaguchi, Y., Gao, Y., Barrientos, T., Ordentlich, P., Wang, X.-F., Counter, C. M., & Yao, T.-P. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-0188 · Cited by 260 · see citing works
Histone acetylation dynamics regulating plant development and stress responses
Kumar, V., Thakur, J. K., & Prasad, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03794-x · Cited by 244 · see citing works
Quinoline-based antimalarial hybrid compounds
Vandekerckhove, S., & D’hooghe, M. (2014) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2014.12.018 · Cited by 232 · see citing works
Isoform-specific histone deacetylase inhibitors: The next step?
Balasubramanian, S., Verner, E. J., & Buggy, J. J. (2009) · Cancer Letters · doi:10.1016/j.canlet.2009.02.013 · Cited by 224 · see citing works
Dietary phytochemicals, HDAC inhibition, and DNA damage/repair defects in cancer cells
Rajendran, P., Ho, E., Williams, D. E., & Dashwood, R. H. (2011) · Clinical Epigenetics · doi:10.1186/1868-7083-3-4 · Cited by 219 · see citing works
Martin‐Gallausiaux, C., Béguet-Crespel, F., Marinelli, L., Jamet, A., Ledue, F., Blottière, H. M., & Lapaque, N. (2018) · Scientific Reports · doi:10.1038/s41598-018-28048-y · Cited by 215 · see citing works
Moreno, D. A., Scrideli, C. A., Cortez, M. A. A., De Paula Queiroz, R., Valera, E. T., Da Silva Silveira, V., Yunes, J. A., Brandalise, S. R., & Tone, L. G. (2010) · British Journal of Haematology · doi:10.1111/j.1365-2141.2010.08301.x · Cited by 208 · see citing works
Chemical modifier screen identifies HDAC inhibitors as suppressors of PKD models
Cao, Y., Semanchik, N., Lee, S. H., Somlo, S., Barbano, P. E., Coifman, R. R., & Sun, Z. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911987106 · Cited by 201 · see citing works
Keedy, K. S., Archin, N. M., Gates, A. T., Espeseth, A. S., Hazuda, D. J., & Margolis, D. M. (2009) · Journal of Virology · doi:10.1128/jvi.02585-08 · Cited by 199 · see citing works
Small molecule inhibitors targeting the cancers
Liu, G., Chen, T., Zhang, X., Ma, X., & Shi, H. (2022) · MedComm · doi:10.1002/mco2.181 · Cited by 198 · see citing works
Identification of the novel role of butyrate as AhR ligand in human intestinal epithelial cells
Marinelli, L., Martin‐Gallausiaux, C., Bourhis, J., Béguet-Crespel, F., Blottière, H. M., & Lapaque, N. (2019) · Scientific Reports · doi:10.1038/s41598-018-37019-2 · Cited by 190 · see citing works
Mikhed, Y., Görlach, A., Knaus, U. G., & Daiber, A. (2015) · Redox Biology · doi:10.1016/j.redox.2015.05.008 · Cited by 181 · see citing works
Mysteries of Metals in Metalloenzymes
Valdez, C. E., Smith, Q. A., Nechay, M. R., & Alexandrova, A. N. (2014) · Accounts of Chemical Research · doi:10.1021/ar500227u · Cited by 179 · see citing works
HDAC inhibitors: Targets for tumor therapy, immune modulation and lung diseases
Shanmugam, G., Rakshit, S., & Sarkar, K. (2021) · Translational Oncology · doi:10.1016/j.tranon.2021.101312 · Cited by 178 · see citing works
Mechanisms of Oocyte Maturation and Related Epigenetic Regulation
He, M., Zhang, T., Yang, Y., & Wang, C. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.654028 · Cited by 173 · see citing works
Martin‐Gallausiaux, C., Larraufie, P., Jarry, A., Béguet-Crespel, F., Marinelli, L., Ledue, F., Reimann, F. M., Blottière, H. M., & Lapaque, N. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02838 · Cited by 170 · see citing works
LSD1: oxidative chemistry for multifaceted functions in chromatin regulation
Forneris, F., Binda, C., Battaglioli, E., & Mattevi, A. (2008) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2008.01.003 · Cited by 166 · see citing works
Suzuki, T., Ota, Y., Ri, M., Bando, M., Gotoh, A., Itoh, Y., Tsumoto, H., Tatum, P. R., Mizukami, T., Nakagawa, H., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300837y · Cited by 165 · see citing works
Gupta, M., Ansell, S. M., Novak, A. J., Kumar, S. K., Kaufmann, S. H., & Witzig, T. E. (2009) · Blood · doi:10.1182/blood-2009-05-220889 · Cited by 163 · see citing works
Lucio-Eterovic, A. K., Cortez, M. A. A., Valera, E. T., Motta, F., Queiróz, R. G. D. P., Machado, H. R., Carlotti, C. G., Neder, L., Scrideli, C. A., & Tone, L. G. (2008) · BMC Cancer · doi:10.1186/1471-2407-8-243 · Cited by 156 · see citing works
Thakur, V. S., Gupta, K., & Gupta, S. (2011) · Carcinogenesis · doi:10.1093/carcin/bgr277 · Cited by 152 · see citing works
Greenblatt, D. Y., Vaccaro, A. M., Jaskula‐Sztul, R., Li, N., Haymart, M. R., Kunnimalaiyaan, M., & Chen, H. (2007) · The Oncologist · doi:10.1634/theoncologist.12-8-942 · Cited by 145 · see citing works
Next-generation of selective histone deacetylase inhibitors
Yang, F., Zhao, N., Ge, D., & Chen, Y. (2019) · RSC Advances · doi:10.1039/c9ra02985k · Cited by 144 · see citing works
Xia, C., Tao, Y., Li, M., Che, T., & Qu, J. (2020) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2020.9073 · Cited by 136 · see citing works
Fiegler, N., Textor, S., Arnold, A., Rölle, A., Oehme, I., Breuhahn, K., Moldenhauer, G., Witzens‐Harig, M., & Cerwenka, A. (2013) · Blood · doi:10.1182/blood-2013-02-482513 · Cited by 135 · see citing works
A Proton-Shuttle Reaction Mechanism for Histone Deacetylase 8 and the Catalytic Role of Metal Ions
Wu, R., Wang, S., Zhou, N., Cao, Z., & Zhang, Y. (2010) · Journal of the American Chemical Society · doi:10.1021/ja103932d · Cited by 135 · see citing works
HDAC inhibitors as antifibrotic drugs in cardiac and pulmonary fibrosis
Lyu, X., Hu, M., Peng, J., Zhang, X.-Y., & Sanders, Y. (2019) · Therapeutic Advances in Chronic Disease · doi:10.1177/2040622319862697 · Cited by 121 · see citing works
Targeting Histone Deacetylases in Diseases: Where Are We?
Benedetti, R., Conte, M., & Altucci, L. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5776 · Cited by 127 · see citing works
Chemical regulation of epigenetic modifications: Opportunities for new cancer therapy
Zheng, Y. G., Wu, J., Chen, Z., & Goodman, M. (2008) · Medicinal Research Reviews · doi:10.1002/med.20120 · Cited by 124 · see citing works
Fraczek, J., Bolleyn, J., Vanhaecke, T., Rogiers, V., & Vinken, M. (2013) · Archives of Toxicology · doi:10.1007/s00204-012-0983-3 · Cited by 119 · see citing works
Histone deacetylase 2 expression predicts poorer prognosis in oral cancer patients
Chang, H., Chiang, C., Hung, H.-C., Lin, C., Deng, Y., & Kuo, M. Y. (2008) · Oral Oncology · doi:10.1016/j.oraloncology.2008.08.011 · Cited by 119 · see citing works
Epigenetic regulation in fibrosis progress
Xue, T., Qiu, X., Liu, H., Gan, C., Tan, Z., Xie, Y., Wang, D., & Ye, T. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105910 · Cited by 109 · see citing works
Concepts of epigenetics in prostate cancer development
Cooper, C. S., & Foster, C. S. (2008) · British Journal of Cancer · doi:10.1038/sj.bjc.6604771 · Cited by 107 · see citing works
Godmann, M., Lambrot, R., & Kimmins, S. (2009) · Microscopy Research and Technique · doi:10.1002/jemt.20715 · Cited by 109 · see citing works
McClure, J. J., Zhang, C., Inks, E. S., Peterson, Y. K., Li, J., & Chou, C. J. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01385 · Cited by 108 · see citing works
The Role of Extracellular Vesicles: An Epigenetic View of the Cancer Microenvironment
Qian, Z., Shen, Q., Yang, X., Qiu, Y., & Zhang, W. (2015) · BioMed Research International · doi:10.1155/2015/649161 · Cited by 106 · see citing works
Ferroptosis and Its Multifaceted Roles in Cerebral Stroke
Zhang, Y., Lu, X., Tai, B., Li, W., & Li, T. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.615372 · Cited by 108 · see citing works
Epigenomics of leukemia: from mechanisms to therapeutic applications
Florean, C., Schnekenburger, M., Grandjenette, C., Dicato, M. A., & Diederich, M. F. (2011) · Epigenomics · doi:10.2217/epi.11.73 · Cited by 105 · see citing works
Bonfils, C., Kalita, A., Dubay, M., Siu, L. L., Carducci, M. A., Reid, G. K., Martell, R. E., Besterman, J. M., & Li, Z. (2008) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-07-4427 · Cited by 105 · see citing works
Inhibition of Histone Deacetylase 3 Causes Replication Stress in Cutaneous T Cell Lymphoma
Wells, C. E., Bhaskara, S., Stengel, K. R., Zhao, Y., Sirbu, B. M., Chagot, B., Cortez, D., Khabele, D., Chazin, W., Cooper, A. C., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0068915 · Cited by 101 · see citing works
Mathew, O. P., Ranganna, K., & Yatsu, F. M. (2010) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2010.09.017 · Cited by 98 · see citing works
Epigenetics and pancreatic cancer: Pathophysiology and novel treatment aspects
Neureiter, D. (2014) · World Journal of Gastroenterology · doi:10.3748/wjg.v20.i24.7830 · Cited by 98 · see citing works
Epigenetic Regulation of HIV-1 Latency in Astrocytes
Narasipura, S. D., Kim, S. H., & Al‐Harthi, L. (2013) · Journal of Virology · doi:10.1128/jvi.03333-13 · Cited by 96 · see citing works
HDAC1 and HDAC2 in mouse oocytes and preimplantation embryos: Specificity versus compensation
Ma, P., & Schultz, R. M. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2016.31 · Cited by 95 · see citing works
Noh, J. H., Jung, K. H., Kim, J. K., Eun, J. W., Bae, H. J., Xie, H. J., Chang, Y. G., Kim, M., Park, W. S., Lee, J. Y., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0028103 · Cited by 95 · see citing works
Global analysis of DNA methylation in early-stage liver fibrosis
Komatsu, Y., Waku, T., Iwasaki, N., Ono, W., Yamaguchi, C., & Yanagisawa, J. (2012) · BMC Medical Genomics · doi:10.1186/1755-8794-5-5 · Cited by 95 · see citing works
HDAC3 Deficiency Promotes Liver Cancer through a Defect in H3K9ac/H3K9me3 Transition
Ji, H., Zhou, Y., Zhuang, X., Zhu, Y., Wu, Z., Lu, Y., Li, S., Zeng, Y., Lu, Q. R., Huo, Y., et al. (2019) · Cancer Research · doi:10.1158/0008-5472.can-18-3767 · Cited by 94 · see citing works
Howell, P., Liu, S., Ren, S., Behlen, C., Fodstad, Ø., & Riker, A. I. (2009) · Cancer Control · doi:10.1177/107327480901600302 · Cited by 93 · see citing works
Jeong, Y., Du, R., Zhu, X., Yin, S., Wang, J., Cui, H., Cao, W., & Lowenstein, C. J. (2013) · Journal of Leukocyte Biology · doi:10.1189/jlb.1013565 · Cited by 93 · see citing works
Gatla, H. R., Muniraj, N., Thevkar, P., Yavvari, S., Sukhavasi, S., & Makena, M. R. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20051110 · Cited by 91 · see citing works
Strategies to enhance CAR-T persistence
Liu, Y., An, L., Huang, R., Xiong, J., Yang, H., Wang, X., & Zhang, X. (2022) · Biomarker Research · doi:10.1186/s40364-022-00434-9 · Cited by 97 · see citing works
Epigenetic alterations underlying autoimmune diseases
Aslani, S., Mahmoudi, M., Karami, J., Jamshidi, A., Malekshahi, Z., & Nicknam, M. H. (2016) · Autoimmunity · doi:10.3109/08916934.2015.1134511 · Cited by 90 · see citing works
Zhao, Y., Jia, X., Yang, X., Bai, X., Lu, Y., Zhu, L., Cheng, W., Shu, M., Zhu, Y., Du, X., et al. (2022) · Metabolism · doi:10.1016/j.metabol.2022.155162 · Cited by 90 · see citing works
Zhong, Y., Huang, T., Huang, J., Quan, J., Su, G., Xiong, Z., Lv, Y., Li, S., Lai, X., Xiang, Y., et al. (2023) · Theranostics · doi:10.7150/thno.82535 · Cited by 89 · see citing works
Pontiki, E. A., & Hadjipavlou‐Litina, D. (2010) · Medicinal Research Reviews · doi:10.1002/med.20200 · Cited by 89 · see citing works
Current advances of carbene-mediated photoaffinity labeling in medicinal chemistry
Ge, S.-S., Chen, B., Wu, Y., Long, Q.-S., Zhao, Y., Wang, P., & Yang, S. (2018) · RSC Advances · doi:10.1039/c8ra03538e · Cited by 87 · see citing works
Choo, M., Yeo, H., & Zayzafoon, M. (2009) · Bone · doi:10.1016/j.bone.2009.05.009 · Cited by 87 · see citing works
Baba, R., Hori, Y., Mizukami, S., & Kikuchi, K. (2012) · Journal of the American Chemical Society · doi:10.1021/ja306045j · Cited by 86 · see citing works
Role of histone deacetylases and their inhibitors in neurological diseases
Zhang, L.-Y., Zhang, S.-Y., Wen, R., Zhang, T.-N., & Yang, N. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107410 · Cited by 84 · see citing works
MTA2 promotes gastric cancer cells invasion and is transcriptionally regulated by Sp1
Zhou, C., Ji, J., Cai, Q., Shi, M., Chen, X., Yu, Y., Liu, B., Zhu, Z., & Zhang, J. (2013) · Molecular Cancer · doi:10.1186/1476-4598-12-102 · Cited by 79 · see citing works
Development of a Potent and Selective HDAC8 Inhibitor
Ingham, O. J., Paranal, R. M., Smith, W. B., Escobar, R. A., Yueh, H., Snyder, T., Porco, J. A. J., Bradner, J. E., & Beeler, A. B. (2016) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.6b00239 · Cited by 79 · see citing works
The use of novel agents in the treatment of relapsed and refractory multiple myeloma
Laubach, J. P., Mahindra, A. K., Mitsiades, C. S., Schlossman, R. L., Munshi, N. C., Ghobrial, I. M., Carreau, N. A., Hideshima, T., Anderson, K. C., & Richardson, P. G. G. (2009) · Leukemia · doi:10.1038/leu.2009.179 · Cited by 78 · see citing works
Histone Acetylation and Plant Development
Liu, X., Yang, S., Yu, C.-W., Chen, C.-Y., & Wu, K. (2016) · The Enzymes · doi:10.1016/bs.enz.2016.08.001 · Cited by 78 · see citing works
Fiskus, W. C., Rao, R., Fernandez, P., Herger, B. E., Yang, Y., Chen, J., Kolhe, R. B., Mandawat, A., Wang, Y., Joshi, R., et al. (2008) · Blood · doi:10.1182/blood-2007-10-116319 · Cited by 77 · see citing works
Qiao, Z., Ren, S., Li, W., Wang, X., He, M., Guo, Y., Sun, L., He, Y., Ge, Y., & Yu, Q. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.03.059 · Cited by 77 · see citing works
The Histone Deacetylase HDAC4 Regulates Long-Term Memory in Drosophila
Fitzsimons, H. L., Schwartz, S., Given, F. M., & Scott, M. J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0083903 · Cited by 77 · see citing works
Microbiome as an immune regulator in health, disease, and therapeutics
Juarez, V. M., Montalbine, A. N., & Singh, A. K. (2022) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2022.114400 · Cited by 76 · see citing works
Fluorescent Probes for Single-Step Detection and Proteomic Profiling of Histone Deacetylases
Xie, Y., Ge, J., Lei, J. H., Peng, B., Zhang, H., Wang, D., Pan, S., Chen, G., Chen, L., Wang, Y., et al. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b07334 · Cited by 73 · see citing works
Acetylation of αA-crystallin in the human lens: Effects on structure and chaperone function
Nagaraj, R. H., Nahomi, R. B., Shanthakumar, S., Linetsky, M. D., Padmanabha, S., Pasupuleti, N., Wang, B., Santhoshkumar, P., Panda, A. K., & Biswas, A. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.11.011 · Cited by 72 · see citing works
Lai, M.-J., Huang, H.-L., Pan, S., Liu, Y.-M., Peng, C.-Y., Lee, H., Yeh, T., Huang, P.-H., Teng, C., Chen, C., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300197a · Cited by 72 · see citing works
Histone deacetylases 1 and 2 maintain S-phase chromatin and DNA replication fork progression
Bhaskara, S., Jacques, V., Rusche, J. R., Olson, E. N., Cairns, B. R., & Chandrasekharan, M. B. (2013) · Epigenetics & Chromatin · doi:10.1186/1756-8935-6-27 · Cited by 71 · see citing works
Borbone, E., Berlingieri, M. T., Bellis, F. D., Nebbioso, A., Chiappetta, G., Mai, A., Altucci, L., & Fusco, A. (2009) · Oncogene · doi:10.1038/onc.2009.306 · Cited by 71 · see citing works
Identification of novel quinazoline derivatives as potent antiplasmodial agents
Bouchut, A., Rotili, D., Pierrot, C., Valente, S., Lafitte, S., Schultz, J., Höglund, U., Mazzone, R., Lucidi, A., Fabrizi, G., et al. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.10.041 · Cited by 70 · see citing works
Valproic Acid Activates Notch1 Signaling and Induces Apoptosis in Medullary Thyroid Cancer Cells
Greenblatt, D. Y., Cayo, M. A., Adler, J. T., Ning, L., Haymart, M. R., Kunnimalaiyaan, M., & Chen, H. (2008) · Annals of Surgery · doi:10.1097/sla.0b013e3181758d0e · Cited by 70 · see citing works
Malinen, M., Saramäki, A., Ropponen, A., Degenhardt, T., Vaïsänen, S., & Carlberg, C. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm913 · Cited by 70 · see citing works
Chronic stress and antidepressant induced changes in Hdac5 and Sirt2 affect synaptic plasticity
Erburu, M. M., Muñoz-Cobo, I., Domínguez‐Andrés, J., Beltrán, E., Suzuki, T., Mai, A., Valente, S., Puerta, E., & Tordera, R. M. (2015) · European Neuropsychopharmacology · doi:10.1016/j.euroneuro.2015.08.016 · Cited by 71 · see citing works
Epigenetics of Huntington’s Disease
Bassi, S., Tripathi, T., Monziani, A., Leva, F. D., & Biagioli, M. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-53889-1_15 · Cited by 66 · see citing works
MYCN Impact on High-Risk Neuroblastoma: From Diagnosis and Prognosis to Targeted Treatment
Bartolucci, D., Montemurro, L., Raieli, S., Lampis, S., Pession, A., Hrelia, P., & Tonelli, R. (2022) · Cancers · doi:10.3390/cancers14184421 · Cited by 65 · see citing works
Singh, T., Prasad, R., & Katiyar, S. K. (2012) · Epigenetics · doi:10.4161/epi.23078 · Cited by 67 · see citing works
Yang, F., Gao, Z., Xu, J., Wang, H., Guo, Q., Li, B., Li, M., Xu, H., Qi, Y., Zhao, S., et al. (2023) · Theranostics · doi:10.7150/thno.82590 · Cited by 66 · see citing works
Benn, C., Butler, R. K., Mariner, L., Nixon, J., Moffitt, H., Mielcarek, M., Woodman, B., & Bates, G. P. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005747 · Cited by 66 · see citing works
Metal Ion Signaling in Biomedicine
Rodriguez, R., Müller, S., Colombeau, L., Solier, S., Sindikubwabo, F., & Cañeque, T. (2025) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00577 · Cited by 66 · see citing works
The Chromatin Landscape of Kaposi’s Sarcoma-Associated Herpesvirus
Tóth, Z., Brulois, K., & Jung, J. U. (2013) · Viruses · doi:10.3390/v5051346 · Cited by 65 · see citing works
Photoreceptor rescue and toxicity induced by different calpain inhibitors
Paquet‐Durand, F., Sanges, D., McCall, J., Silva, J., Veen, T. V., Marigo, V., & Ekström, P. A. R. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06983.x · Cited by 64 · see citing works
- Authors
- Gallinari, P., Marco, S. D., Jones, P., Pallaoro, M., & Steinkühler, C.
- Affiliations
- Institute of Molecular Biology and Pathology (IT)
- Corresponding author
- Steinkühler, Christian
- Venue
- Cell Research
- Published
- 2007-02-27
- Volume
- 17
- Issue
- 3
- Pages
- 195-211
- ISSN
- 1001-0602 (ISSN-L)
- 1748-7838
- OpenAlex
- W2031954417
- Semantic Scholar
- 755cb3e836171a20f267d47b6677a035efcf7c22
- Cited by
- 678
- References
- 165
- Citations by year
- 2026: 47 · 2025: 87 · 2024: 38 · 2023: 37 · 2022: 52 · 2021: 58 · 2020: 30 · 2019: 29 · 2018: 28 · 2017: 20 · 2016: 29 · 2015: 22 · 2014: 27 · 2013: 38 · 2012: 20
- FWCI
- 2.44
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Cell Research (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Keywords
- histone deacetylase, histone acetyltransferase, histone acetylation, gene transcription, chromatin conformation, histone deacetylase inhibitors, cancer therapeutics, non-histone protein acetylation, post-translational modification, cell cycle regulation, cell differentiation, malignant transformation
- MeSH terms
- Acetylation, Animals, Histone Deacetylases, Histones, Humans, Models, Biological, Models, Molecular, Molecular Biology, Neoplasms, Transcription, Genetic, Histone Deacetylase Inhibitors
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review