Cited by 697Histone Deacetylase Inhibitors ResearchGenomics and Chromatin DynamicsEpigenetics and DNA Methylation

The DOI matches its Crossref record; 165 of the 165 references it cites were found in a registry or an index.

HDACs, histone deacetylation and gene transcription: from molecular biology to cancer therapeutics

Gallinari, Paola, Marco, Stefania Di, Jones, Phillip, Pallaoro, Michele, Steinkühler, Christian·2007·Cell Research

Open this paper in CoChat — free account

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

Crossref · 10.1038/sj.cr.7310149

Cites

165 of 165 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Translating the Histone Code
Jenuwein, T., & Allis, C. D. (2001) · Science · doi:10.1126/science.1063127 · Cited by 9,756
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
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
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
DNA methylation and human disease
Robertson, K. D. (2005) · Nature Reviews Genetics · doi:10.1038/nrg1655 · Cited by 2,864
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 2,788
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
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 2,234
The diverse functions of histone lysine methylation
Martin, C., & Zhang, Y. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1761 · Cited by 2,157
Histone Acetyltransferases
Dent, S., Denu, J. M., & Allis, C. D. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.81 · Cited by 1,906
Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A.
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
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
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
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
The Deacetylase HDAC6 Regulates Aggresome Formation and Cell Viability in Response to Misfolded Protein Stress
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
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 1,497
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 1,329
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
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
Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation
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
Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation
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
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
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
Phase I Study of an Oral Histone Deacetylase Inhibitor, Suberoylanilide Hydroxamic Acid, in Patients With Advanced Cancer
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
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 832
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
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
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
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
Inhibition of Histone Deacetylase 6 Acetylates and Disrupts the Chaperone Function of Heat Shock Protein 90
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
Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family
Gao, L., Cueto, M. A., Asselbergs, F., & Atadja, P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111871200 · Cited by 744
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
Untitled work
(2002) · PubMed · Cited by 732
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
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
A synthetic inhibitor of histone deacetylase, MS-27-275, with marked in vivo antitumor activity against human tumors
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
Quantitation of Transcription and Clonal Selection of Single Living Cells with β-Lactamase as Reporter
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
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
The expression of a small fraction of cellular genes is changed in response to histone hyperacetylation.
(1996) · Europe PMC (PubMed Central) · Cited by 659
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
Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor
Vannini, A., Volpari, C., Filocamo, G., Casavola, E. C., Brunetti, M., Renzoni, D., Chakravarty, P., Paolini, C., De Francesco, R., Gallinari, P., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404603101 · Cited by 638
Self-citation
Phosphorylation of histone H3: a balancing act between chromosome condensation and transcriptional activation
Nowak, S. J., & Corces, V. G. (2004) · Trends in Genetics · doi:10.1016/j.tig.2004.02.007 · Cited by 622
Histone Deacetylases 5 and 9 Govern Responsiveness of the Heart to a Subset of Stress Signals and Play Redundant Roles in Heart Development
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
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
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
Histone deacetylase 3 (HDAC3) and other class I HDACs regulate colon cell maturation and p21 expression and are deregulated in human colon cancer
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
Histone deacetylase (HDAC) inhibitor activation of p21 WAF1 involves changes in promoter-associated proteins, including HDAC1
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
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 545
Transcriptional signature of histone deacetylase inhibition in multiple myeloma: Biological and clinical implications
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 537
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 529
Activation of the myocyte enhancer factor-2 transcription factor by calcium/calmodulin-dependent protein kinase-stimulated binding of 14-3-3 to histone deacetylase 5
McKinsey, T. A., Zhang, C. L., & Olson, E. N. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.260501497 · Cited by 526
Trapoxin, an antitumor cyclic tetrapeptide, is an irreversible inhibitor of mammalian histone deacetylase.
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
Protein Kinases C and D Mediate Agonist-Dependent Cardiac Hypertrophy through Nuclear Export of Histone Deacetylase 5
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
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
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 487
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
Tumor Necrosis Factor α-induced Phosphorylation of RelA/p65 on Ser529 Is Controlled by Casein Kinase II
Wang, D., Westerheide, S. D., Ostrander, J. H., & Baldwin, A. S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001358200 · Cited by 454
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
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
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
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 428
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
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
The N-CoR-HDAC3 Nuclear Receptor Corepressor Complex Inhibits the JNK Pathway through the Integral Subunit GPS2
Zhang, J., Kalkum, M., Chait, B. T., & Roeder, R. G. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00468-9 · Cited by 414
Lysine acetylation and the bromodomain: a new partnership for signaling
Yang, X. (2004) · BioEssays · doi:10.1002/bies.20104 · Cited by 371
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
SUMO Promotes HDAC-Mediated Transcriptional Repression
Yang, S., & Sharrocks, A. D. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00060-7 · Cited by 358
Regulation of histone deacetylase activities
Sengupta, N., & Seto, E. (2004) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20179 · Cited by 357
Histone deacetylases
Marks, P. A. (2003) · Current Opinion in Pharmacology · doi:10.1016/s1471-4892(03)00084-5 · Cited by 350
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
Drug Insight: histone deacetylase inhibitors—development of the new targeted anticancer agent suberoylanilide hydroxamic acid
Kelly, W. K., & Marks, P. A. (2005) · Nature Clinical Practice Oncology · doi:10.1038/ncponc0106 · Cited by 338
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
Pharmacodynamic response and inhibition of growth of human tumor xenografts by the novel histone deacetylase inhibitor PXD101.
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
Cloning and Characterization of a Novel Human Class I Histone Deacetylase That Functions as a Transcription Repressor
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
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 287
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
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
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 265
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
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
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
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 256
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 246
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 245
Cancer epigenetics
Momparler, R. L. (2003) · Oncogene · doi:10.1038/sj.onc.1206774 · Cited by 242
Histone Acetylation-independent Effect of Histone Deacetylase Inhibitors on Akt through the Reshuffling of Protein Phosphatase 1 Complexes
Chen, C., Weng, S., Tseng, P., Lin, H.-P., & Chen, C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505733200 · Cited by 236
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
The nuclear-envelope protein and transcriptional repressor LAP2β interacts with HDAC3 at the nuclear periphery, and induces histone H4 deacetylation
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
Histone deacetylase 3 (HDAC3) activity is regulated by interaction with protein serine/threonine phosphatase 4Preprint
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
HDAC7, a Thymus-Specific Class II Histone Deacetylase, Regulates Nur77 Transcription and TCR-Mediated Apoptosis
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 218
The Tumor Suppressor p53 and Histone Deacetylase 1 Are Antagonistic Regulators of the Cyclin-Dependent Kinase Inhibitor p21/WAF1/CIP1 Gene
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
Association with Class IIa Histone Deacetylases Upregulates the Sumoylation of MEF2 Transcription Factors
Grégoire, S., & Yang, X. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.6.2273-2287.2005 · Cited by 207
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
Multidimensional Chemical Genetic Analysis of Diversity-Oriented Synthesis-Derived Deacetylase Inhibitors Using Cell-Based Assays
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
Isolation and structural elucidation of new cyclotetrapeptides, trapoxins A and B, having detransformation activities as antitumor agents.
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
Histone deacetylase HDAC8 associates with smooth muscle α‐actin and is essential for smooth muscle cell contractility
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
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
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 194
Isolierung und Strukturaufklärung von Chlamydocin
Closse, A., & Huguenin, R. (1974) · Helvetica Chimica Acta · doi:10.1002/hlca.19740570306 · Cited by 190
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
Intrinsic apoptotic and thioredoxin pathways in human prostate cancer cell response to histone deacetylase inhibitor
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
Krüppel-like Factor-6 Promotes Preadipocyte Differentiation through Histone Deacetylase 3-dependent Repression of DLK1
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
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
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
Phosphorylation of histone deacetylase 7 by protein kinase D mediates T cell receptor–induced Nur77 expression and apoptosis
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
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
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
Modification of de novo DNA methyltransferase 3a (Dnmt3a) by SUMO-1 modulates its interaction with histone deacetylases (HDACs) and its capacity to repress transcription
Ling, Y. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh195 · Cited by 164
The inv(16) fusion protein associates with corepressors via a smooth muscle myosin heavy-chain domain
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
Phosphatase Inhibition Leads to Histone Deacetylases 1 and 2 Phosphorylation and Disruption of Corepressor Interactions
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
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
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
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
The Modular Nature of Histone Deacetylase HDAC4 Confers Phosphorylation-dependent Intracellular Trafficking
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
Activity-dependent and -independent nuclear fluxes of HDAC4 mediated by different kinases in adult skeletal muscle
Liu, Y., Randall, W. R., & Schneider, M. F. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200408128 · Cited by 150
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
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
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
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
Calcium/Calmodulin-dependent Protein Kinase Activates Serum Response Factor Transcription Activity by Its Dissociation from Histone Deacetylase, HDAC4
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
N-Hydroxy-3-phenyl-2-propenamides as Novel Inhibitors of Human Histone Deacetylase with in Vivo Antitumor Activity: Discovery of (2E)-N-Hydroxy-3-[4-[[(2-hydroxyethyl)[2-(1H-indol-3-yl)ethyl]amino]methyl]phenyl]-2-propenamide (NVP-LAQ824)
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
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
CRA-024781: a novel synthetic inhibitor of histone deacetylase enzymes with antitumor activity in vitro and in vivo
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
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
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
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
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 115
Identification of Mammalian Sds3 as an Integral Component of the Sin3/Histone Deacetylase Corepressor Complex
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
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
Sds3 (Suppressor of Defective Silencing 3) Is an Integral Component of the Yeast Sin3·Rpd3 Histone Deacetylase Complex and Is Required for Histone Deacetylase Activity
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
Dissecting the Biological Functions of Drosophila Histone Deacetylases by RNA Interference and Transcriptional Profiling
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
Self-citation
The 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
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
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
Histone Deacetylase 8 Safeguards the Human Ever-Shorter Telomeres 1B (hEST1B) Protein from Ubiquitin-Mediated Degradation
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
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
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
Silence of the genes — mechanisms of long-term repression
Lande‐Diner, L., & Cedar, H. (2005) · Nature Reviews Genetics · doi:10.1038/nrg1639 · Cited by 82
The histone‐binding code of nuclear receptor co‐repressors matches the substrate specificity of histone deacetylase 3
Hartman, H. B., Yu, J., Alenghat, T., Ishizuka, T., & Lazar, M. A. (2005) · EMBO Reports · doi:10.1038/sj.embor.7400391 · Cited by 82
Synthetic molecular motors
Davis, A. P. (1999) · Nature · doi:10.1038/43576 · Cited by 77
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
Members of the histone deacetylase superfamily differ in substrate specificity towards small synthetic substrates
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
Differential Gene Expression Profiling of CD34 + CD133 + Umbilical Cord Blood Hematopoietic Stem Progenitor Cells
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
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
Self-citation
Modulation of histone acetylation by [4-(acetylamino)-N-(2-amino-phenyl) benzamide] in HCT-8 colon carcinoma.
Kraker, A. J., Mizzen, C. A., Hartl, B. G., Miin, J., Allis, C. D., & Merriman, R. L. (2003) · PubMed · Cited by 64
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
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
Selenium and glutathione peroxidase levels in patients with epidermoid carcinoma of the oral cavity and oropharynx
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
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
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
Measurement of histone acetyltransferase and histone deacetylase activities and kinetics of histone acetylation
Sun, J.-M. (2003) · Methods · doi:10.1016/s1046-2023(03)00083-5 · Cited by 44
Vorinostat (suberoylanilide hydroxamic acid, SAHA) is clinically active in advanced cutaneous T-cell lymphoma (CTCL): Results of a phase IIb trial
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
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
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
Kruppel-like zinc finger protein Gli-similar 2 (Glis2) represses transcription through interaction with C-terminal binding protein 1 (CtBP1)
Kim, S. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki985 · Cited by 32
The Orphan Nuclear Receptor TR2 Interacts Directly with Both Class I and Class II Histone Deacetylases
Franco, P. J., Farooqui, M., Seto, E., & Wei, L. (2001) · Molecular Endocrinology · doi:10.1210/mend.15.8.0682 · Cited by 29
Role of protein kinase CK2 in phosphorylation of nucleosomal proteins in relation to transcriptional activity
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
Role of protein kinase CK2 in phosphorylation of nucleosomal proteins in relation to transcriptional activity
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
A phase II multicenter study on the histone deacetylase (HDAC) inhibitor MS-275, comparing two dosage schedules in metastatic melanoma
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
A phase 1 pharmacokinetic (PK) and pharmacodynamic (PD) study of the histone deacetylase (HDAC) inhibitor PXD101 in patients (pts) with advanced solid tumours
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
A Phase I, pharmacokinetic (PK) and pharmacodynamic (PD) study of a novel histone deacetylase inhibitor LAQ824 in patients with hematologic malignancies
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
International multicenter phase II study of the HDAC inhibitor (HDACi) depsipeptide (FK228) in cutaneous T-cell lymphoma (CTCL): Interim report
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
Peptidyl epoxides as selective protease inactivators
Albeck, A. (2000) · Drug Development Research · doi:10.1002/1098-2299(200007/08)50:3/4 · Cited by 12
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
Biologists abandon Popper at their peril
(2000) · doi:10.1002/(sici)1521-1878(200002)22:2

Research works printed but not linked: 1

Vaisburg A . Discovery and development of MGCD0103 – an orally active HDAC inhibitor in human clinical trials. XIXth International Symposium on Medical Chemistry, Istanbul, Aug 29-Sep 2, 2006.

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 847
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 484
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
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
Genetic and molecular pathogenesis of mantle cell lymphoma: perspectives for new targeted therapeutics
Jares, P., Colomer, D., & Campo, E. (2007) · Nature Reviews Cancer · doi:10.1038/nrc2230 · Cited by 466

See all 697

Authors: Gallinari, P., Marco, S. D., Jones, P., Pallaoro, M., & Steinkühler, C.
Affiliations: Institute of Molecular Biology and Pathology (IT)
Corresponding author: Steinkühler, Christian
ORCID: Gallinari, Paola
Steinkühler, Christian
Venue: Cell Research
Publisher: Springer Science and Business Media LLC
Published: 2007-02-27
Volume: 17
Issue: 3
Pages: 195-211
ISSN: 1001-0602 (ISSN-L)
1748-7838
DOI: 10.1038/sj.cr.7310149
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

HDACs, histone deacetylation and gene transcription: from molecular biology to cancer therapeutics

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks